A cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.
A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.
A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.
A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.
An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).
A serine protease found in the azurophil granules of NEUTROPHILS. It has an enzyme specificity similar to that of chymotrypsin C.
An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.
An aspartic endopeptidase that is similar in structure to CATHEPSIN D. It is found primarily in the cells of the immune system where it may play a role in processing of CELL SURFACE ANTIGENS.
A papain-like cysteine protease that has specificity for amino terminal dipeptides. The enzyme plays a role in the activation of several pro-inflammatory serine proteases by removal of their aminoterminal inhibitory dipeptides. Genetic mutations that cause loss of cathepsin C activity in humans are associated with PAPILLON-LEFEVRE DISEASE.
A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.
ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
A large multinuclear cell associated with the BONE RESORPTION. An odontoclast, also called cementoclast, is cytomorphologically the same as an osteoclast and is involved in CEMENTUM resorption.
A ubiquitously-expressed cysteine peptidase that exhibits carboxypeptidase activity. It is highly expressed in a variety of immune cell types and may play a role in inflammatory processes and immune responses.
Bone loss due to osteoclastic activity.
Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.
A cysteine endopeptidase found in NATURAL KILLER CELLS and CYTOTOXIC T-LYMPHOCYTES. It may have a specific function in the mechanism or regulation of cytolytic activity of immune cells.
A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
An ERYTHROLEUKEMIA cell line derived from a CHRONIC MYELOID LEUKEMIA patient in BLAST CRISIS.
Defective bone formation involving individual bones, singly or in combination.
A homologous group of endogenous CYSTEINE PROTEINASE INHIBITORS. The cystatins inhibit most CYSTEINE ENDOPEPTIDASES such as PAPAIN, and other peptidases which have a sulfhydryl group at the active site.
A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by protecting BETA-GALACTOSIDASE and NEURAMINIDASE from degradation. It was formerly classified as EC 3.4.12.1 and EC 3.4.21.13.
A transmembrane protein belonging to the tumor necrosis factor superfamily that specifically binds RECEPTOR ACTIVATOR OF NUCLEAR FACTOR-KAPPA B and OSTEOPROTEGERIN. It plays an important role in regulating OSTEOCLAST differentiation and activation.
A variety of rare sarcoma having a reticulated fibrous stroma enclosing groups of sarcoma cells, which resemble epithelial cells and are enclosed in alveoli walled with connective tissue. It is a rare tumor, usually occurring between 15 and 35 years of age. It appears in the muscles of the extremities in adults and most commonly in the head and neck regions of children. Though slow-growing, it commonly metastasizes to the lungs, brain, bones, and lymph nodes. (DeVita Jr et al., Cancer: Principles & Practice of Oncology, 3d ed, p1365)
N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.
An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2.
Excessive formation of dense trabecular bone leading to pathological fractures; OSTEITIS; SPLENOMEGALY with infarct; ANEMIA; and extramedullary hemopoiesis (HEMATOPOIESIS, EXTRAMEDULLARY).
Rare autosomal recessive syndrome characterized by delayed closing of CRANIAL SUTURES, short stature, ACRO-OSTEOLYSIS of distal phalanges, dental and MAXILLOFACIAL ABNORMALITIES and an increase in bone density that results in frequent BONE FRACTURES. It is associated with BONE RESORPTION defect due to mutations in the lysosomal cysteine protease CATHEPSIN K.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
Peptides composed of two amino acid units.
Resorption of calcified dental tissue, involving demineralization due to reversal of the cation exchange and lacunar resorption by osteoclasts. There are two types: external (as a result of tooth pathology) and internal (apparently initiated by a peculiar inflammatory hyperplasia of the pulp). (From Jablonski, Dictionary of Dentistry, 1992, p676)
A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 3.4.22.2.
Distinctive neoplastic disorders of histiocytes. Included are malignant neoplasms of MACROPHAGES and DENDRITIC CELLS.
Physiologically inactive substances that can be converted to active enzymes.
Diazomethane is an extremely hazardous and unstable organic compound, (CH2)N=N=O, with a methane substituted diazo group, that is highly explosive when heated, shocked or contaminated, and used as a powerful methylating agent in chemical syntheses, but its production and handling require special expertise and equipment due to the high risks involved.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Hydrolytic enzyme activity used as a histocytochemical test for the presence of esterases in tissue. Substrate used is 3-hydroxy-4'-nitro-2-naphthanilide chloroacetate (naphthol AS-D).
A single-pass type I membrane protein. It is cleaved by AMYLOID PRECURSOR PROTEIN SECRETASES to produce peptides of varying amino acid lengths. A 39-42 amino acid peptide, AMYLOID BETA-PEPTIDES is a principal component of the extracellular amyloid in SENILE PLAQUES.
An extracellular cystatin subtype that is abundantly expressed in bodily fluids. It may play a role in the inhibition of interstitial CYSTEINE PROTEASES.
A degenerative disease of the BRAIN characterized by the insidious onset of DEMENTIA. Impairment of MEMORY, judgment, attention span, and problem solving skills are followed by severe APRAXIAS and a global loss of cognitive abilities. The condition primarily occurs after age 60, and is marked pathologically by severe cortical atrophy and the triad of SENILE PLAQUES; NEUROFIBRILLARY TANGLES; and NEUROPIL THREADS. (From Adams et al., Principles of Neurology, 6th ed, pp1049-57)
Laboratory mice that have been produced from a genetically manipulated EGG or EMBRYO, MAMMALIAN.

Crystal structure of wild-type human procathepsin K. (1/284)

Cathepsin K is a lysosomal cysteine protease belonging to the papain superfamily. It has been implicated as a major mediator of osteoclastic bone resorption. Wild-type human procathepsin K has been crystallized in a glycosylated and a deglycosylated form. The latter crystals diffract better, to 3.2 A resolution, and contain four molecules in the asymmetric unit. The structure was solved by molecular replacement and refined to an R-factor of 0.194. The N-terminal fragment of the proregion forms a globular domain while the C-terminal segment is extended and shows substantial flexibility. The proregion interacts with the enzyme along the substrate binding groove and along the proregion binding loop (residues Ser138-Asn156). It binds to the active site in the opposite direction to that of natural substrates. The overall binding mode of the proregion to cathepsin K is similar to that observed in cathepsin L, caricain, and cathepsin B, but there are local differences that likely contribute to the specificity of these proregions for their cognate enzymes. The main observed difference is in the position of the short helix alpha3p (67p-75p), which occupies the S' subsites. As in the other proenzymes, the proregion utilizes the S2 subsite for anchoring by placing a leucine side chain there, according to the specificity of cathepsin K toward its substrate.  (+info)

Characterization of novel cathepsin K mutations in the pro and mature polypeptide regions causing pycnodysostosis. (2/284)

Cathepsin K, a lysosomal cysteine protease critical for bone remodeling by osteoclasts, was recently identified as the deficient enzyme causing pycnodysostosis, an autosomal recessive osteosclerotic skeletal dysplasia. To investigate the nature of molecular lesions causing this disease, mutations in the cathepsin K gene from eight families were determined, identifying seven novel mutations (K52X, G79E, Q190X, Y212C, A277E, A277V, and R312G). Expression of the first pro region missense mutation in a cysteine protease, G79E, in Pichia pastoris resulted in an unstable precursor protein, consistent with misfolding of the proenzyme. Expression of five mature region missense defects revealed that G146R, A277E, A277V, and R312G precursors were unstable, and no mature proteins or protease activity were detected. The Y212C precursor was activated to its mature form in a manner similar to that of the wild-type cathepsin K. The mature Y212C enzyme retained its dipeptide substrate specificity and gelatinolytic activity, but it had markedly decreased activity toward type I collagen and a cathepsin K-specific tripeptide substrate, indicating that it was unable to bind collagen triple helix. These studies demonstrated the molecular heterogeneity of mutations causing pycnodysostosis, indicated that pro region conformation directs proper folding of the proenzyme, and suggested that the cathepsin K active site contains a critical collagen-binding domain.  (+info)

Expression of cathepsin K messenger RNA in giant cells and their precursors in human osteoarthritic synovial tissues. (3/284)

OBJECTIVE: To investigate the expression of cathepsin K messenger RNA (mRNA) in the giant cells found in human osteoarthritic (OA) synovium and associated reparative connective tissues, and to compare this with mRNA expression of cathepsins B, L, and S, which are cysteine proteases known to be highly expressed by cells of the monocyte/macrophage lineage. METHODS: Sections of human OA synovium were processed for in situ hybridization and probed for cathepsins K, B, L, and S. Serial sections were reacted for tartrate-resistant acid phosphatase (TRAP) and nonspecific esterase (NSE) activity, which are selective markers for the osteoclast and cells of the macrophage/monocyte lineage, respectively. RESULTS: At 3 sites of monocyte infiltration/giant cell formation (granulation tissue, the intimal and subintimal synovial layers, and deep stroma extending to the periphery of osteophytic tissue), both TRAP-positive mono- and multinucleated cells and TRAP-negative, NSE-positive mononuclear precursors were identified. Cells containing both enzyme activities were also found, potentially indicating an intermediate stage of differentiation. The TRAP-positive mononuclear/giant cells, and the occasional NSE-positive precursor, expressed an intense signal for cathepsin K mRNA, but did not express cathepsins B, L, and S. In contrast, the deep zone of phagocytic-like cells adjacent to sites of ossification expressed high levels of mRNA for cathepsins L, B, and S as well as cathepsin K mRNA. CONCLUSION: Giant cells that form within OA synovial tissue express high levels of cathepsin K mRNA. It appears that cathepsin K acts principally to digest the bone (and cartilage) fragments sheered from the joint surface during OA. The high TRAP activity and the undetectable expression of the macrophage-associated degradative proteases (cathepsins B, L, and S) by synovial giant cells strengthens the hypothesis that cathepsin K is the primary protease involved in bone degradation. At sites of synovial osteogenesis, a population of phagocytic-like cells expressed TRAP and cathepsins B, L, S, and K, and may represent blood-derived macrophages pushed toward an osteoclast phenotype.  (+info)

Osteopetrosis and osteoporosis: two sides of the same coin. (4/284)

Together, osteoporosis and osteopetrosis comprise a substantial proportion of the bone diseases that severely affect humans. In order to understand and effectively treat these disorders, an understanding of the mechanisms controlling bone remodelling is essential. While numerous animal models of bone disease have been generated, the lack of correlation between these animal models and human disease has limited their utility in terms of defining therapeutic strategies. The generation and analysis of cathepsin K knockout mice has resulted in a model for pycnodysostosis, a rare human osteopetrotic disease, and is now providing considerable insights into both osteoclast function and potential therapeutic strategies for the treatment of bone disease. This review highlights the importance of genes such as cathepsin K in understanding bone remodelling and illustrates a new trend towards understanding bone disease as a complete entity rather than as a series of unrelated disorders.  (+info)

Cathepsin P, a novel protease in mouse placenta. (5/284)

The complete cDNA nucleotide sequence of a novel cathepsin derived from mouse placenta, termed cathepsin P, was determined. mRNA for cathepsin P was expressed in placenta and at lower levels in visceral yolk sac, but could not be detected in a range of adult tissues. The expression pattern of this protease indicates that it probably plays an important role during implantation and fetal development.  (+info)

Expression of cathepsin K in the human embryo and fetus. (6/284)

Cathepsin K is a protease with high collagenolytic and elastinolytic activity. Its cellular expression was previously thought to be restricted to osteoclasts and osteoclast-mediated bone resorption. In this study, the expression of cathepsin K in the human embryo and fetus was demonstrated by immunohistochemistry, in situ hybridization, and by Northern blotting of fetal tissue extracts. Besides osteoclasts and chondroclasts and their precursors, epithelial cells of various organ systems expressed significant amounts of this enzyme. Respiratory and gastrointestinal mucosa, including bile duct epithelia and urothelia, showed high levels of cathepsin K expression. With the exception of the urothelium, showing a more homogenous expression pattern, the protease was usually accentuated in the surface cell layers of pithelia. In summary, these findings in the human embryo and early fetus demonstrated a significant expression of cathepsin K in different epithelial cell types besides osteoclasts. The functional aspects of cathepsin K expression in nonosteoclastic cells and potential conclusions on physiological and pathological conditions in the embryo-fetal or adult organism remain to be investigated. Dev Dyn 1999;216:89-95.  (+info)

Synovial tissue in rheumatoid arthritis is a source of osteoclast differentiation factor. (7/284)

OBJECTIVE: Osteoclast differentiation factor (ODF; also known as osteoprotegerin ligand, receptor activator of nuclear factor kappaB ligand, and tumor necrosis factor-related activation-induced cytokine) is a recently described cytokine known to be critical in inducing the differentiation of cells of the monocyte/macrophage lineage into osteoclasts. The role of osteoclasts in bone erosion in rheumatoid arthritis (RA) has been demonstrated, but the exact mechanisms involved in the formation and activation of osteoclasts in RA are not known. These studies address the potential role of ODF and the bone and marrow microenvironment in the pathogenesis of osteoclast-mediated bone erosion in RA. METHODS: Tissue sections from the bone-pannus interface at sites of bone erosion were examined for the presence of osteoclast precursors by the colocalization of messenger RNA (mRNA) for tartrate-resistant acid phosphatase (TRAP) and cathepsin K in mononuclear cells. Reverse transcriptase-polymerase chain reaction (RT-PCR) was used to identify mRNA for ODF in synovial tissues, adherent synovial fibroblasts, and activated T lymphocytes derived from patients with RA. RESULTS: Multinucleated cells expressing both TRAP and cathepsin K mRNA were identified in bone resorption lacunae in areas of pannus invasion into bone in RA patients. In addition, mononuclear cells expressing both TRAP and cathepsin K mRNA (preosteoclasts) were identified in bone marrow in and adjacent to areas of pannus invasion in RA erosions. ODF mRNA was detected by RT-PCR in whole synovial tissues from patients with RA but not in normal synovial tissues. In addition, ODF mRNA was detected in cultured adherent synovial fibroblasts and in activated T lymphocytes derived from RA synovial tissue, which were expanded by exposure to anti-CD3. CONCLUSION: TRAP-positive, cathepsin K-positive osteoclast precursor cells are identified in areas of pannus invasion into bone in RA. ODF is expressed by both synovial fibroblasts and by activated T lymphocytes derived from synovial tissues from patients with RA. These synovial cells may contribute directly to the expansion of osteoclast precursors and to the formation and activation of osteoclasts at sites of bone erosion in RA.  (+info)

Cloning and function of rabbit peroxisome proliferator-activated receptor delta/beta in mature osteoclasts. (8/284)

Osteoclasts modulate bone resorption under physiological and pathological conditions. Previously, we showed that both estrogens and retinoids regulated osteoclastic bone resorption and postulated that such regulation was directly mediated through their cognate receptors expressed in mature osteoclasts. In this study, we searched for expression of other members of the nuclear hormone receptor superfamily in osteoclasts. Using the low stringency homologous hybridization method, we isolated the peroxisome proliferator-activated receptor delta/beta (PPARdelta/beta) cDNA from mature rabbit osteoclasts. Northern blot analysis showed that PPARdelta/beta mRNA was highly expressed in highly enriched rabbit osteoclasts. Carbaprostacyclin, a prostacyclin analogue known to be a ligand for PPARdelta/beta, significantly induced both bone-resorbing activities of isolated mature rabbit osteoclasts and mRNA expression of the cathepsin K, carbonic anhydrase type II, and tartrate-resistant acid phosphatase genes in these cells. Moreover, the carbaprostacyclin-induced bone resorption was completely blocked by an antisense phosphothiorate oligodeoxynucleotide of PPARdelta/beta but not by the sense phosphothiorate oligodeoxynucleotide of the same DNA sequence. Our results suggest that PPARdelta/beta may be involved in direct modulation of osteoclastic bone resorption.  (+info)

Cathepsin K is a proteolytic enzyme, which belongs to the family of papain-like cysteine proteases. It is primarily produced by osteoclasts, which are specialized cells responsible for bone resorption. Cathepsin K plays a crucial role in the degradation and remodeling of the extracellular matrix, particularly in bone tissue.

This enzyme is capable of breaking down various proteins, including collagen, elastin, and proteoglycans, which are major components of the bone matrix. By doing so, cathepsin K helps osteoclasts to dissolve and remove mineralized and non-mineralized bone matrix during the process of bone resorption.

Apart from its function in bone metabolism, cathepsin K has also been implicated in several pathological conditions, such as osteoporosis, rheumatoid arthritis, and tumor metastasis to bones. Inhibitors of cathepsin K are being investigated as potential therapeutic agents for the treatment of these disorders.

Cathepsins are a type of proteolytic enzymes, which are found in lysosomes and are responsible for breaking down proteins inside the cell. They are classified as papain-like cysteine proteases and play important roles in various physiological processes, including tissue remodeling, antigen presentation, and apoptosis (programmed cell death). There are several different types of cathepsins, including cathepsin B, C, D, F, H, K, L, S, V, and X/Z, each with distinct substrate specificities and functions.

Dysregulation of cathepsins has been implicated in various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders. For example, overexpression or hyperactivation of certain cathepsins has been shown to contribute to tumor invasion and metastasis, while their inhibition has been explored as a potential therapeutic strategy in cancer treatment. Similarly, abnormal levels of cathepsins have been linked to the progression of neurodegenerative diseases like Alzheimer's and Parkinson's, making them attractive targets for drug development.

Cathepsin B is a lysosomal cysteine protease that plays a role in various physiological processes, including intracellular protein degradation, antigen presentation, and extracellular matrix remodeling. It is produced as an inactive precursor (procathepsin B) and activated upon cleavage of the propeptide by other proteases or autocatalytically. Cathepsin B has a wide range of substrates, including collagen, elastin, and various intracellular proteins. Its dysregulation has been implicated in several pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders.

Cathepsin L is a lysosomal cysteine protease that plays a role in various physiological processes, including protein degradation, antigen presentation, and extracellular matrix remodeling. It is produced as an inactive precursor and activated by cleavage of its propeptide domain. Cathepsin L has a broad specificity for peptide bonds and can cleave both intracellular and extracellular proteins, making it an important player in various pathological conditions such as cancer, neurodegenerative diseases, and infectious diseases. Inhibition of cathepsin L has been explored as a potential therapeutic strategy for these conditions.

Cathepsin D is a lysosomal aspartic protease that plays a role in intracellular protein degradation and turnover. It is produced as an inactive precursor and is activated by cleavage into two subunits within the acidic environment of the lysosome. Cathepsin D is also known to be secreted by certain cells, where it can contribute to extracellular matrix remodeling and tissue degradation. In addition, abnormal levels or activity of cathepsin D have been implicated in various diseases, including cancer, neurodegenerative disorders, and infectious diseases.

Cathepsin G is a serine protease, which is a type of enzyme that breaks down other proteins. It is produced and released by neutrophils, a type of white blood cell that plays an important role in the body's immune response to infection. Cathepsin G helps to digest and kill microorganisms that have invaded the body. It can also contribute to tissue damage and inflammation in certain diseases, such as rheumatoid arthritis and cystic fibrosis.

Cathepsin H is a lysosomal cysteine protease that plays a role in intracellular protein degradation and turnover. It is expressed in various tissues, including the spleen, thymus, lungs, and immune cells. Cathepsin H has been implicated in several physiological processes, such as antigen presentation, bone resorption, and extracellular matrix remodeling. Additionally, its dysregulation has been associated with various pathological conditions, including cancer, neurodegenerative disorders, and infectious diseases.

The enzyme's active site contains a catalytic triad composed of cysteine, histidine, and aspartic acid residues, which facilitates the proteolytic activity. Cathepsin H exhibits specificity for peptide bonds containing hydrophobic or aromatic amino acids, making it an important player in processing and degrading various cellular proteins.

In summary, Cathepsin H is a lysosomal cysteine protease involved in protein turnover and degradation with potential implications in several pathological conditions when dysregulated.

Cathepsin E is a type of proteolytic enzyme, which belongs to the family of papain-like cysteine proteases. It is primarily located in the lysosomes of cells and plays a role in intracellular protein degradation. Cathepsin E is unique among the cathepsins because it is predominantly expressed in immune cells, such as macrophages and dendritic cells, where it functions as a protease involved in antigen presentation.

The enzyme has a molecular weight of approximately 42 kDa and is synthesized as an inactive precursor that undergoes proteolytic processing to generate the mature, active enzyme. Cathepsin E can cleave various substrates, including peptides and proteins, and has been implicated in several physiological and pathological processes, such as inflammation, immune response, and cancer.

In summary, Cathepsin E is a lysosomal cysteine protease that plays a crucial role in antigen presentation and protein degradation, primarily expressed in immune cells.

Cathepsin C is a lysosomal cysteine protease that plays a role in intracellular protein degradation and activation of other proteases. It is also known as dipeptidyl peptidase I (DPP I) because of its ability to remove dipeptides from the N-terminus of polypeptides. Cathepsin C is widely expressed in many tissues, including immune cells, and has been implicated in various physiological and pathological processes such as antigen presentation, bone resorption, and tumor cell invasion. Defects in the gene encoding cathepsin C have been associated with several genetic disorders, including Papillon-Lefèvre syndrome and Haim-Munk syndrome, which are characterized by severe periodontal disease and skin abnormalities.

Cathepsin F is a lysosomal cysteine protease that belongs to the papain family. It is primarily expressed in hematopoietic cells, including monocytes, macrophages, and dendritic cells. Cathepsin F plays a role in various physiological processes, such as antigen presentation, bone remodeling, and extracellular matrix degradation. It is also implicated in several pathological conditions, such as cancer, neurodegenerative disorders, and infectious diseases.

Cathepsin F has a broad substrate specificity and can cleave various proteins, including collagen, elastin, and casein. Its activity is tightly regulated by endogenous inhibitors, such as cystatins and stefins, to prevent excessive protein degradation and tissue damage.

In summary, Cathepsin F is a lysosomal enzyme involved in various physiological and pathological processes, with a broad substrate specificity and regulatory mechanisms.

Cysteine endopeptidases are a type of enzymes that cleave peptide bonds within proteins. They are also known as cysteine proteases or cysteine proteinases. These enzymes contain a catalytic triad consisting of three amino acids: cysteine, histidine, and aspartate. The thiol group (-SH) of the cysteine residue acts as a nucleophile and attacks the carbonyl carbon of the peptide bond, leading to its cleavage.

Cysteine endopeptidases play important roles in various biological processes, including protein degradation, cell signaling, and inflammation. They are involved in many physiological and pathological conditions, such as apoptosis, immune response, and cancer. Some examples of cysteine endopeptidases include cathepsins, caspases, and calpains.

It is important to note that these enzymes require a reducing environment to maintain the reduced state of their active site cysteine residue. Therefore, they are sensitive to oxidizing agents and inhibitors that target the thiol group. Understanding the structure and function of cysteine endopeptidases is crucial for developing therapeutic strategies that target these enzymes in various diseases.

Osteoclasts are large, multinucleated cells that are primarily responsible for bone resorption, a process in which they break down and dissolve the mineralized matrix of bones. They are derived from monocyte-macrophage precursor cells of hematopoietic origin and play a crucial role in maintaining bone homeostasis by balancing bone formation and bone resorption.

Osteoclasts adhere to the bone surface and create an isolated microenvironment, called the "resorption lacuna," between their cell membrane and the bone surface. Here, they release hydrogen ions into the lacuna through a process called proton pumping, which lowers the pH and dissolves the mineral component of the bone matrix. Additionally, osteoclasts secrete proteolytic enzymes, such as cathepsin K, that degrade the organic components, like collagen, in the bone matrix.

An imbalance in osteoclast activity can lead to various bone diseases, including osteoporosis and Paget's disease, where excessive bone resorption results in weakened and fragile bones.

Cathepsin Z is a lysosomal protease, also known as cathepsin X or peptidyl-dipeptidase I. It is a cysteine proteinase that plays a role in intracellular protein degradation and turnover. Cathepsin Z is expressed in various tissues, including the spleen, thymus, liver, and lungs. It has been found to be involved in several physiological processes, such as antigen presentation, bone resorption, and extracellular matrix remodeling. Additionally, cathepsin Z may contribute to some pathological conditions, like cancer, atherosclerosis, and neurodegenerative disorders.

The enzyme's primary function is to cleave peptide bonds, particularly after hydrophobic residues, in the process of protein degradation. Cathepsin Z has an optimal pH range between 5.0 and 6.5, which is typical for lysosomal enzymes. Its activity can be regulated by endogenous inhibitors, such as cystatins, to maintain a balance in proteolytic processes within the cell.

In summary, Cathepsin Z is a lysosomal cysteine protease involved in intracellular protein degradation and turnover, with potential roles in various physiological and pathological conditions.

Bone resorption is the process by which bone tissue is broken down and absorbed into the body. It is a normal part of bone remodeling, in which old or damaged bone tissue is removed and new tissue is formed. However, excessive bone resorption can lead to conditions such as osteoporosis, in which bones become weak and fragile due to a loss of density. This process is carried out by cells called osteoclasts, which break down the bone tissue and release minerals such as calcium into the bloodstream.

Cysteine proteinase inhibitors are a type of molecule that bind to and inhibit the activity of cysteine proteases, which are enzymes that cleave proteins at specific sites containing the amino acid cysteine. These inhibitors play important roles in regulating various biological processes, including inflammation, immune response, and programmed cell death (apoptosis). They can also have potential therapeutic applications in diseases where excessive protease activity contributes to pathology, such as cancer, arthritis, and neurodegenerative disorders. Examples of cysteine proteinase inhibitors include cystatins, kininogens, and serpins.

Cathepsin W is a lysosomal cysteine protease that is primarily expressed in cells of the immune system, such as natural killer (NK) cells and cytotoxic T lymphocytes (CTLs). It is also known as lysosomal thiol protease or NK-lysin.

Cathepsin W plays a role in the immune response by contributing to the destruction of target cells during the process of cell-mediated cytotoxicity. It is stored in the lysosomes of NK cells and CTLs, and upon activation, it is released into the immunological synapse between the effector and target cells.

Once released, cathepsin W can cleave various proteins, including cytoskeletal components, adhesion molecules, and signaling proteins, leading to the disruption of the target cell's membrane and ultimately its death. Dysregulation of cathepsin W has been implicated in several diseases, including autoimmune disorders, neurodegenerative diseases, and cancer.

Lysosomes are membrane-bound organelles found in the cytoplasm of eukaryotic cells. They are responsible for breaking down and recycling various materials, such as waste products, foreign substances, and damaged cellular components, through a process called autophagy or phagocytosis. Lysosomes contain hydrolytic enzymes that can break down biomolecules like proteins, nucleic acids, lipids, and carbohydrates into their basic building blocks, which can then be reused by the cell. They play a crucial role in maintaining cellular homeostasis and are often referred to as the "garbage disposal system" of the cell.

Endopeptidases are a type of enzyme that breaks down proteins by cleaving peptide bonds inside the polypeptide chain. They are also known as proteinases or endoproteinases. These enzymes work within the interior of the protein molecule, cutting it at specific points along its length, as opposed to exopeptidases, which remove individual amino acids from the ends of the protein chain.

Endopeptidases play a crucial role in various biological processes, such as digestion, blood coagulation, and programmed cell death (apoptosis). They are classified based on their catalytic mechanism and the structure of their active site. Some examples of endopeptidase families include serine proteases, cysteine proteases, aspartic proteases, and metalloproteases.

It is important to note that while endopeptidases are essential for normal physiological functions, they can also contribute to disease processes when their activity is unregulated or misdirected. For instance, excessive endopeptidase activity has been implicated in the pathogenesis of neurodegenerative disorders, cancer, and inflammatory conditions.

K562 cells are a type of human cancer cell that are commonly used in scientific research. They are derived from a patient with chronic myelogenous leukemia (CML), a type of cancer that affects the blood and bone marrow.

K562 cells are often used as a model system to study various biological processes, including cell signaling, gene expression, differentiation, and apoptosis (programmed cell death). They are also commonly used in drug discovery and development, as they can be used to test the effectiveness of potential new therapies against cancer.

K562 cells have several characteristics that make them useful for research purposes. They are easy to grow and maintain in culture, and they can be manipulated genetically to express or knock down specific genes. Additionally, K562 cells are capable of differentiating into various cell types, such as red blood cells and megakaryocytes, which allows researchers to study the mechanisms of cell differentiation.

It's important to note that while K562 cells are a valuable tool for research, they do not fully recapitulate the complexity of human CML or other cancers. Therefore, findings from studies using K562 cells should be validated in more complex model systems or in clinical trials before they can be translated into treatments for patients.

Dysostosis is a term used to describe a group of genetic disorders that are characterized by abnormal development and formation of one or more bones in the body. The condition is typically present at birth (congenital) and can affect any bone, but it most commonly involves the bones of the skull, face, hands, and feet.

The term "dysostosis" comes from the Greek words "dys," meaning difficult or abnormal, and "osteon," meaning bone. Dysostoses are usually caused by mutations in specific genes that regulate bone development. These genetic changes can be inherited from one or both parents or can occur spontaneously during fetal development.

There are many different types of dysostoses, each with its own set of symptoms and characteristics. Some common examples include:

1. Cleidocranial Dysplasia: This is a rare genetic disorder that affects the development of the skull and collarbones (cleido). People with cleidocranial dysplasia may have a larger than normal head, wide-set eyes, a prominent forehead, and underdeveloped or missing collarbones.
2. Acrocephalopolysyndactyly Type II: Also known as ACPS II or Greig cephalopolysyndactyly syndrome, this disorder is characterized by a pointed skull (acrocephaly), extra fingers and toes (polydactyly), and wide-set eyes.
3. Osteogenesis Imperfecta: This is a group of genetic disorders that affect the body's production of collagen, a protein that helps to strengthen bones. People with osteogenesis imperfecta have fragile bones that break easily, often as a result of minor trauma.
4. Diastrophic Dysplasia: This is a rare genetic disorder that affects the development of the bones and cartilage in the body. People with diastrophic dysplasia may have short limbs, a deformed spine, and a characteristic "hitchhiker's thumb" appearance.
5. Thanatophoric Dysplasia: This is a severe genetic disorder that affects the development of the bones in the body. People with thanatophoric dysplasia have very short limbs, a small chest, and a deformed skull. The condition is often fatal in infancy or early childhood.

These are just a few examples of the many different types of skeletal dysplasias that exist. While some forms of these disorders can be managed with medical treatment and therapy, others may require surgery or other interventions to help improve quality of life. In some cases, genetic counseling and testing may be recommended for individuals who are considering starting a family and have a history of skeletal dysplasia in their family.

Cystatins are a group of proteins that inhibit cysteine proteases, which are enzymes that break down other proteins. Cystatins are found in various biological fluids and tissues, including tears, saliva, seminal plasma, and urine. They play an important role in regulating protein catabolism and protecting cells from excessive protease activity. There are three main types of cystatins: type 1 (cystatin C), type 2 (cystatin M, cystatin N, and fetuin), and type 3 (kininogens). Abnormal levels of cystatins have been associated with various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders.

Cathepsin A is a lysosomal protein that belongs to the peptidase family. It plays a role in various biological processes, including protein degradation and activation, cell signaling, and inflammation. Cathepsin A has both endopeptidase and exopeptidase activities, which allow it to cleave and process a wide range of substrates.

In addition to its enzymatic functions, cathepsin A also plays a structural role in the formation and stability of the protective protein complex called the "serglycin-cathepsin A proteoglycan complex." This complex protects certain proteases from degradation and helps regulate their activity within the lysosome.

Deficiencies or mutations in cathepsin A have been linked to several diseases, including a rare genetic disorder called galactosialidosis, which is characterized by developmental delays, coarse facial features, and progressive neurological deterioration.

REceptor Activator of NF-kB (RANK) Ligand is a type of protein that plays a crucial role in the immune system and bone metabolism. It belongs to the tumor necrosis factor (TNF) superfamily and is primarily produced by osteoblasts, which are cells responsible for bone formation.

RANK Ligand binds to its receptor RANK, which is found on the surface of osteoclasts, a type of cell involved in bone resorption or breakdown. The binding of RANK Ligand to RANK activates signaling pathways that promote the differentiation, activation, and survival of osteoclasts, thereby increasing bone resorption.

Abnormalities in the RANKL-RANK signaling pathway have been implicated in various bone diseases, such as osteoporosis, rheumatoid arthritis, and certain types of cancer that metastasize to bones. Therefore, targeting this pathway with therapeutic agents has emerged as a promising approach for the treatment of these conditions.

Alveolar Soft Part Sarcoma (ASPS) is a rare type of sarcoma, which is a cancer that develops in the body's connective or supportive tissues such as muscles, tendons, ligaments, cartilage, nerves, and blood vessels. ASPS typically arises in deep soft tissues, often in the legs or arms, but can also occur in other parts of the body like the head and neck region.

ASPS is called "alveolar" because the cancer cells sometimes form structures that look like the air sacs (alveoli) found in the lungs. The term "soft part" indicates that this type of sarcoma usually arises in the soft tissues of the body.

Histologically, ASPS is characterized by the presence of distinctive organoid nests or alveolar structures composed of large polygonal cells with eosinophilic cytoplasm and distinct cell borders. The nuclei are round to oval, with finely dispersed chromatin and prominent nucleoli. Immunohistochemically, ASPS cells typically express TFE3, a transcription factor that can be used in the diagnosis of this tumor type.

ASPS tends to grow slowly but can metastasize (spread) to other parts of the body, such as the lungs, brain, and bones. It primarily affects adolescents and young adults, with a slight female predominance. Treatment usually involves surgical resection, radiation therapy, and/or systemic treatment like targeted therapy or chemotherapy. The prognosis for ASPS is variable, depending on factors such as the tumor's size, location, and extent of metastasis at diagnosis.

Pepstatins are a group of naturally occurring cyclic peptides that inhibit aspartic proteases, a type of enzyme that breaks down proteins. They are isolated from various actinomycete species of Streptomyces and Actinosynnema. Pepstatins are often used in laboratory research to study the function of aspartic proteases and as tools to probe the mechanism of action of these enzymes. In addition, pepstatins have been explored for their potential therapeutic use in various diseases, including cancer, viral infections, and cardiovascular disease. However, they have not yet been approved for clinical use.

Acid phosphatase is a type of enzyme that is found in various tissues and organs throughout the body, including the prostate gland, red blood cells, bone, liver, spleen, and kidneys. This enzyme plays a role in several biological processes, such as bone metabolism and the breakdown of molecules like nucleotides and proteins.

Acid phosphatase is classified based on its optimum pH level for activity. Acid phosphatases have an optimal activity at acidic pH levels (below 7.0), while alkaline phosphatases have an optimal activity at basic or alkaline pH levels (above 7.0).

In clinical settings, measuring the level of acid phosphatase in the blood can be useful as a tumor marker for prostate cancer. Elevated acid phosphatase levels may indicate the presence of metastatic prostate cancer or disease progression. However, it is important to note that acid phosphatase is not specific to prostate cancer and can also be elevated in other conditions, such as bone diseases, liver disorders, and some benign conditions. Therefore, acid phosphatase should be interpreted in conjunction with other diagnostic tests and clinical findings for a more accurate diagnosis.

Osteopetrosis, also known as Albers-Schönberg disease or marble bone disease, is a group of rare genetic disorders characterized by increased bone density due to impaired bone resorption by osteoclasts. This results in brittle bones that are more susceptible to fractures and can also lead to various complications such as anemia, hearing loss, and vision problems. There are several types of osteopetrosis, which vary in severity and age of onset.

The medical definition of osteopetrosis is:

A genetic disorder characterized by defective bone resorption due to impaired osteoclast function, resulting in increased bone density, susceptibility to fractures, and potential complications such as anemia, hearing loss, and vision problems.

Pycnodysostosis is a rare genetic disorder characterized by skeletal dysplasia (abnormal development of the bones) and distinctive facial features. The condition is caused by mutations in the CTSK gene, which provides instructions for making an enzyme called cathepsin K. This enzyme is responsible for breaking down collagen, a protein that provides structure and strength to connective tissues throughout the body.

In people with pycnodysostosis, the lack of functional cathepsin K leads to the accumulation of abnormal bone matrix, which results in bones that are dense but fragile and prone to fractures. The condition is also associated with a number of other skeletal abnormalities, including:

* Short stature
* A prominent forehead (frontal bossing)
* A broad, flat nasal bridge
* A small chin (micrognathia)
* A narrow mouth
* A high-arched palate
* Dental abnormalities, such as delayed tooth eruption and thickened dental enamel
* Hypoplastic or aplastic clavicles (collarbones)
* Short fingers and toes
* Multiple fractures, particularly in the long bones of the arms and legs

Pycnodysostosis is typically diagnosed in childhood based on clinical features and confirmed with genetic testing. There is no cure for the condition, but treatment is focused on managing symptoms and preventing complications. This may include:

* Orthopedic interventions to correct skeletal abnormalities or treat fractures
* Dental care to address dental abnormalities and prevent tooth decay
* Speech therapy to help with any speech difficulties caused by the narrow mouth and high-arched palate
* Genetic counseling for affected individuals and their families.

Protease inhibitors are a class of antiviral drugs that are used to treat infections caused by retroviruses, such as the human immunodeficiency virus (HIV), which is responsible for causing AIDS. These drugs work by blocking the activity of protease enzymes, which are necessary for the replication and multiplication of the virus within infected cells.

Protease enzymes play a crucial role in the life cycle of retroviruses by cleaving viral polyproteins into functional units that are required for the assembly of new viral particles. By inhibiting the activity of these enzymes, protease inhibitors prevent the virus from replicating and spreading to other cells, thereby slowing down the progression of the infection.

Protease inhibitors are often used in combination with other antiretroviral drugs as part of highly active antiretroviral therapy (HAART) for the treatment of HIV/AIDS. Common examples of protease inhibitors include saquinavir, ritonavir, indinavir, and atazanavir. While these drugs have been successful in improving the outcomes of people living with HIV/AIDS, they can also cause side effects such as nausea, diarrhea, headaches, and lipodystrophy (changes in body fat distribution).

A dipeptide is a type of molecule that is formed by the condensation of two amino acids. In this process, the carboxyl group (-COOH) of one amino acid combines with the amino group (-NH2) of another amino acid, releasing a water molecule and forming a peptide bond.

The resulting molecule contains two amino acids joined together by a single peptide bond, which is a type of covalent bond that forms between the carboxyl group of one amino acid and the amino group of another. Dipeptides are relatively simple molecules compared to larger polypeptides or proteins, which can contain hundreds or even thousands of amino acids linked together by multiple peptide bonds.

Dipeptides have a variety of biological functions in the body, including serving as building blocks for larger proteins and playing important roles in various physiological processes. Some dipeptides also have potential therapeutic uses, such as in the treatment of hypertension or muscle wasting disorders.

Tooth resorption is a process in which there is an abnormal loss or breakdown of tooth structure, either internally (internal resorption) or externally (external resorption), due to the action of specialized cells called odontoclasts. This can lead to weakening and destruction of the tooth, potentially causing sensitivity, pain, or even tooth loss if left untreated. The causes of tooth resorption can vary, including trauma, orthodontic treatment, periodontal disease, and certain systemic conditions. It is important to diagnose and treat tooth resorption early to prevent further damage and preserve the tooth structure.

Papain is defined as a proteolytic enzyme that is derived from the latex of the papaya tree (Carica papaya). It has the ability to break down other proteins into smaller peptides or individual amino acids. Papain is widely used in various industries, including the food industry for tenderizing meat and brewing beer, as well as in the medical field for its digestive and anti-inflammatory properties.

In medicine, papain is sometimes used topically to help heal burns, wounds, and skin ulcers. It can also be taken orally to treat indigestion, parasitic infections, and other gastrointestinal disorders. However, its use as a medical treatment is not widely accepted and more research is needed to establish its safety and efficacy.

Malignant histiocytic disorders are a group of rare and aggressive cancers that affect the mononuclear phagocyte system, which includes histiocytes or cells that originate from bone marrow precursors called monoblasts. These disorders are characterized by the uncontrolled proliferation of malignant histiocytes, leading to tissue invasion and damage.

There are several types of malignant histiocytic disorders, including:

1. Acute Monocytic Leukemia (AML-M5): This is a subtype of acute myeloid leukemia that affects the monocyte cell lineage and can involve the skin, lymph nodes, and other organs.
2. Langerhans Cell Histiocytosis (LCH): Although primarily considered a benign histiocytic disorder, some cases of LCH can progress to a malignant form with aggressive behavior and poor prognosis.
3. Malignant Histiocytosis (MH): This is a rare and aggressive disorder characterized by the infiltration of malignant histiocytes into various organs, including the liver, spleen, and lymph nodes.
4. Histiocytic Sarcoma (HS): This is a highly aggressive cancer that arises from malignant histiocytes and can affect various organs, such as the skin, lymph nodes, and soft tissues.

Symptoms of malignant histiocytic disorders depend on the type and extent of organ involvement but may include fever, fatigue, weight loss, anemia, and enlarged lymph nodes or organs. Treatment typically involves a combination of chemotherapy, radiation therapy, and/or stem cell transplantation. The prognosis for malignant histiocytic disorders is generally poor, with a high risk of relapse and a low overall survival rate.

Enzyme precursors are typically referred to as zymogens or proenzymes. These are inactive forms of enzymes that can be activated under specific conditions. When the need for the enzyme's function arises, the proenzyme is converted into its active form through a process called proteolysis, where it is cleaved by another enzyme. This mechanism helps control and regulate the activation of certain enzymes in the body, preventing unwanted or premature reactions. A well-known example of an enzyme precursor is trypsinogen, which is converted into its active form, trypsin, in the digestive system.

Diazomethane is a highly reactive, explosive organic compound with the chemical formula CH2N2. It is a colorless gas or pale yellow liquid that is used as a methylating agent in organic synthesis. Diazomethane is prepared by the reaction of nitrosomethane with a base such as potassium hydroxide.

It is important to handle diazomethane with care, as it can be explosive and toxic. It should only be used in well-ventilated areas, and protective equipment such as gloves and safety glasses should be worn. Diazomethane should not be stored for long periods of time, as it can decompose spontaneously and release nitrogen gas.

Diazomethane is used to introduce methyl groups into organic molecules in a process called methylation. It reacts with carboxylic acids to form methyl esters, and with phenols to form methyl ethers. Diazomethane is also used to synthesize other organic compounds such as pyrazoles and triazoles.

It is important to note that the use of diazomethane in the laboratory has declined due to its hazardous nature, and safer alternatives are now available for many of its applications.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Naphthol AS-D esterase is an enzyme that catalyzes the hydrolysis of Naphthol AS-D esters to produce phenol and naphthoic acids. It is commonly found in various tissues, including the liver, kidney, and intestine, and is used as a marker for neutrophil activation in diagnostic tests.

In medical terms, Naphthol AS-D esterase is often referred to as a "non-specific esterase" because it can hydrolyze various types of esters, not just those containing the Naphthol AS-D group. It is also known as "alkaline phosphatase" because it has optimal activity at alkaline pH levels and contains phosphate groups in its active site.

Naphthol AS-D esterase is often used in histological staining techniques to identify and differentiate various types of cells, such as neutrophils, monocytes, and macrophages, based on their enzymatic activity. The presence and intensity of the enzyme activity can provide valuable information about the type, location, and severity of inflammation or tissue damage in various pathological conditions.

The Amyloid Beta-Protein Precursor (AβPP) is a type of transmembrane protein that is widely expressed in various tissues and organs, including the brain. It plays a crucial role in normal physiological processes, such as neuronal development, synaptic plasticity, and repair.

AβPP undergoes proteolytic processing by enzymes called secretases, resulting in the production of several protein fragments, including the amyloid-beta (Aβ) peptide. Aβ is a small peptide that can aggregate and form insoluble fibrils, which are the main component of amyloid plaques found in the brains of patients with Alzheimer's disease (AD).

The accumulation of Aβ plaques is believed to contribute to the neurodegeneration and cognitive decline observed in AD. Therefore, AβPP and its proteolytic processing have been the focus of extensive research aimed at understanding the pathogenesis of AD and developing potential therapies.

Cystatin C is a protein produced by many cells in the body, including all types of nucleated cells. It is a member of the cysteine protease inhibitor family and functions as an endogenous inhibitor of cathepsins, which are proteases involved in various physiological and pathological processes such as extracellular matrix degradation, antigen presentation, and cell death.

Cystatin C is freely filtered by the glomeruli in the kidneys and almost completely reabsorbed and catabolized by the proximal tubules. Therefore, its serum concentration is a reliable marker of glomerular filtration rate (GFR) and can be used to estimate kidney function.

Increased levels of cystatin C in the blood may indicate impaired kidney function or kidney disease, while decreased levels are less common and may be associated with hyperfiltration or overproduction of cystatin C. Measuring cystatin C levels can complement or supplement traditional methods for assessing kidney function, such as estimating GFR based on serum creatinine levels.

Alzheimer's disease is a progressive disorder that causes brain cells to waste away (degenerate) and die. It's the most common cause of dementia — a continuous decline in thinking, behavioral and social skills that disrupts a person's ability to function independently.

The early signs of the disease include forgetting recent events or conversations. As the disease progresses, a person with Alzheimer's disease will develop severe memory impairment and lose the ability to carry out everyday tasks.

Currently, there's no cure for Alzheimer's disease. However, treatments can temporarily slow the worsening of dementia symptoms and improve quality of life.

Transgenic mice are genetically modified rodents that have incorporated foreign DNA (exogenous DNA) into their own genome. This is typically done through the use of recombinant DNA technology, where a specific gene or genetic sequence of interest is isolated and then introduced into the mouse embryo. The resulting transgenic mice can then express the protein encoded by the foreign gene, allowing researchers to study its function in a living organism.

The process of creating transgenic mice usually involves microinjecting the exogenous DNA into the pronucleus of a fertilized egg, which is then implanted into a surrogate mother. The offspring that result from this procedure are screened for the presence of the foreign DNA, and those that carry the desired genetic modification are used to establish a transgenic mouse line.

Transgenic mice have been widely used in biomedical research to model human diseases, study gene function, and test new therapies. They provide a valuable tool for understanding complex biological processes and developing new treatments for a variety of medical conditions.

... A (serine protease) Cathepsin B (cysteine protease) Cathepsin C (cysteine protease) Cathepsin D (aspartyl protease) ... Cathepsin H (cysteine protease) Cathepsin K (cysteine protease) Cathepsin L1 (cysteine protease) Cathepsin L2 (or V) (cysteine ... Cathepsin S (cysteine protease) Cathepsin W (cysteine proteinase) Cathepsin Z (or X) (cysteine protease) Cathepsins are ... Cathepsin K has also been shown to play a role in arthritis. Mouse cathepsin L is homologous to human cathepsin V. Mouse ...
Cathepsin+T at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.22). ... Cathepsin T (EC 3.4.22.24) is an enzyme. This enzyme catalyses the following chemical reaction: Interconversion of the three ... Cathepsin Gohda E, Pitot HC (May 1981). "Purification and characterization of a new thiol proteinase from rat kidney". ... Pitot HC, Gohda E (1987). Cathepsin T. Methods in Enzymology. Vol. 142. pp. 279-89. doi:10.1016/s0076-6879(87)42038-7. PMID ...
... is a protein that in humans is encoded by the CTSF gene. Cysteine cathepsins are a family of cysteine proteases ... The cathepsin F gene is ubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. ... Wex T, Levy B, Wex H, Brömme D (1999). "Human cathepsins F and W: A new subgroup of cathepsins". Biochem. Biophys. Res. Commun ... Wex T, Wex H, Brömme D (2000). "The human cathepsin F gene--a fusion product between an ancestral cathepsin and cystatin gene ...
... may refer to: Cathepsin L1, a human protease enzyme encoded by the CTSL gene and known for its role in viral entry ... Cathepsin L2, a human protease enzyme encoded by the CTSV gene and also known as cathepsin V This disambiguation page lists ... articles associated with the title Cathepsin L. If an internal link led you here, you may wish to change the link to point ...
"Human cathepsins W and F form a new subgroup of cathepsins that is evolutionary separated from the cathepsin B- and L-like ... Wex T, Levy B, Wex H, Brömme D (1999). "Human cathepsins F and W: A new subgroup of cathepsins". Biochem. Biophys. Res. Commun ... The protein encoded by this gene, a member of the peptidase C1 family of cysteine cathepsins, is a cysteine protease cathepsin ... 2003). "Characterization of novel anti-cathepsin W antibodies and cellular distribution of cathepsin W in the gastrointestinal ...
... cathepsin S can be replaced by cathepsin F. Secreted cathepsin S cleaves some extracellular matrix (ECM) proteins. Cathepsin S ... In vitro, cathepsin S retains some enzyme activity in the presence of 3M urea. Cathepsin S is produced as a zymogen and is ... Cathepsin S can function as an elastase over a broad pH range in alveolar macrophages. Cathepsin S is a lysosomal enzyme that ... Cathepsin S is a member of the peptidase C1 family of cysteine cathepsins, a lysosomal cysteine protease that may participate ...
... (EC 3.4.18.1, cathepsin B2, cysteine-type carboxypeptidase, cathepsin IV, cathepsin Z, acid carboxypeptidase, ... Shows weak endopeptidase activity Cathepsin X is a cysteine cathepsin, a lysosomal cysteine peptidase of family C1 (papain ... Otto K, Riesenkönig H (February 1975). "Improved purification of cathepsin B1 and cathepsin B2". Biochimica et Biophysica Acta ... "On the substrate specificity of cathepsins B1 and B2 including a new fluorogenic substrate for cathepsin B1". Life Sciences. 17 ...
... can also be found in the extracellular space and it is one of the few cathepsins, that shows some activity at ... Cathepsin D is an aspartic endo-protease that is ubiquitously distributed in lysosomes. The main function of cathepsin D is to ... "Entrez Gene: CTSD cathepsin D". Barrett AJ (April 1970). "Cathepsin D. Purification of isoenzymes from human and chicken liver ... The optimum pH for cathepsin D in vitro is 4.5-5.0. Cathepsin-D is an aspartic protease that depends critically on protonation ...
... is degraded by Cathepsin S, in a process referred to as Controlled Cathepsin Cannibalism. Cathepsin K expression is ... Cathepsin K has also been found to be over-expressed in glioblastoma. That the expression of cathepsin K is characteristic for ... Cathepsin K antibodies are marketed for research into expression of this enzyme by various cells. Merck had a cathepsin K ... Other cathepsin K inhibitors are in various stages of development. Medivir has a cathepsin K inhibitor, MIV-711 (L-006235), in ...
... cathepsin C, cathepsin F, cathepsin H, cathepsin K, cathepsin L, cathepsin L2 or V, cathepsin O, cathepsin S, cathepsin Z, and ... Cathepsin Z, also called cathepsin X or cathepsin P, is a protein that in humans is encoded by the CTSZ gene. It is a member of ... As one of the 11 cathepsins, cathepsin Z contains distinctive features from others. Cathepsin Z has been reported involved in ... Cathepsin Z has an exposed integrin-binding Arg-Gly-Asp motif within the propeptide of the enzyme, through which cathepsin Z ...
"Entrez Gene: CTSL1 cathepsin L1". Barrett AJ, Kirschke H (1981). Cathepsin B, Cathepsin H, and cathepsin L. Methods in ... or by cathepsins (primarily cathepsin L) in endolysosomes. Hydroxychloroquine inhibits the action of cathepsin L in ... Cathepsin L1 is a protein that in humans is encoded by the CTSL1 gene. The protein is a cysteine cathepsin, a lysosomal ... Cathepsin L1 is a member of the Peptidase C1 (cathepsin) MEROPS family, which plays an important role in diverse processes ...
... is a protein that in humans is encoded by the CTSH gene. The protein encoded by this gene is a cysteine cathepsin, ... "Entrez Gene: CTSH cathepsin H". Sawicki G, Warwas M (1990). "Cathepsin H from human placenta". Acta Biochim. Pol. 36 (3-4): 343 ... 2003). "Expression of cathepsins B, H, K, L, and S during human fetal lung development". Dev. Dyn. 225 (1): 14-21. doi:10.1002/ ... 2001). "Expression of cathepsins B, H, K, L, and S and matrix metalloproteinases 9 and 13 during chondrocyte hypertrophy and ...
... is one of those homologous protease that evolved from a common ancestor by gene duplication. Cathepsin G is a 255- ... An upregulation of cathepsin G was reported in studies of keratoconus. Cathepsin G has been found to interact with: SERPINB1 ... "Entrez Gene: CTSG cathepsin G". Shafer WM, Pohl J, Onunka VC, Bangalore N, Travis J (January 1991). "Human lysosomal cathepsin ... "Generation of the neutrophil-activating peptide-2 by cathepsin G and cathepsin G-treated human platelets". The American Journal ...
... prepro-cathepsin C) comprising signal peptides of 24 residues, pro-regions of 205 (rat cathepsin C) or 206 (human cathepsin C) ... Cathepsin C appears to be a central coordinator for activation of many serine proteases in immune/inflammatory cells. Cathepsin ... identical to the mature amino acid sequences of papain and a number of other cathepsins including cathepsins, B, H, K, L, and S ... "Entrez Gene: CTSC cathepsin C". Paris A, Strukelj B, Pungercar J, Renko M, Dolenc I, Turk V (Aug 1995). "Molecular cloning and ...
Cathepsin K detection by zymography Zymographic techniques for detection of cathepsins K, L, S, and V Zymography for detection ... Cathepsin zymography is a technique for quantifying enzymatic activity of the cathepsin family of cysteine proteases. It is ... While the proform of cathepsins are generally stable, once activated, proteases such as cathepsin K are vulnerable to ... After the renaturing period, the gel is then incubated in assay buffer to allow the now active cathepsins to proteolyze the ...
... (EC 3.4.22.43, also known as cathepsin V or cathepsin U) is a protein encoded in humans by the CTSV gene. The ... "Entrez Gene: CTSL2 cathepsin L2". Brömme D, Li Z, Barnes M, Mehler E (February 1999). "Human cathepsin V functional expression ... 2006). "Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the ... 2007). "Inhibition of cathepsin L-like proteases by cathepsin V propeptide". Biol. Chem. 388 (5): 541-5. doi:10.1515/BC. ...
... is an enzyme that is classified both as a cathepsin and a carboxypeptidase. In humans, it is encoded by the CTSA ... Cathepsin+A at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e (Genes on human ... "Entrez Gene: CTSA cathepsin A". Mitchell, Richard Sheppard; Kumar, Vinay; Robbins, Stanley L.; Abbas, Abul K.; Fausto, Nelson ( ... Cathepsin A has been shown to interact with NEU1. GRCh38: Ensembl release 89: ENSG00000064601 - Ensembl, May 2017 GRCm38: ...
... is an enzyme that in humans is encoded by the CTSO gene. Cathepsin O is a cysteine cathepsin, a cysteine protease ... "Entrez Gene: cathepsin O". Shi GP, Chapman HA, Bhairi SM, et al. (1995). "Molecular cloning of human cathepsin O, a novel ... 1994). "Human cathepsin O. Molecular cloning from a breast carcinoma, production of the active enzyme in Escherichia coli, and ... "Genomic structure and chromosomal localization of the human cathepsin O gene (CTSO)". Genomics. 53 (2): 231-4. doi:10.1006/geno ...
... cathepsin D-like acid proteinase, cathepsin E-like acid proteinase, cathepsin D-type proteinase) is an enzyme. Cathepsin E is a ... The structure of Cathepsin E is very similar to those of Cathepsin D and BACE1, and all 3 have almost identical active site ... Along with renin and Cathepsin D, Cathepsin E is one of the only few aspartic proteases known to be made in human tissues other ... A distinguishing factor of Cathepsin E in comparison with the structure of Cathepsin D and BACE1 can be seen at the formation ...
In humans, cathepsin B is encoded by the CTSB gene. Cathepsin B is upregulated in certain cancers, in pre-malignant lesions, ... Cathepsin B belongs to a family of lysosomal cysteine proteases known as the cysteine cathepsins and plays an important role in ... Cathepsin B has been shown to interact with: CTSD CSTA, CSTB, and S100A10. Cathepsin B is inhibited by: Nitroxoline CA-074 ... Cathepsin B has been proposed as a potentially effective biomarker for a variety of cancers. Overexpression of cathepsin B is ...
... , Histones & Cathepsin; PMAP The Proteolysis Map-animation Nature journal: recent chromatin publications and news ...
... collagenases such as cathepsin B1; and hyaluronidase. PSGAG inhibits the synthesis of prostaglandin E2, which is released upon ...
Cathepsin A Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51: 83-128. doi:10.1007/bf02907561 ... Miller JJ, Changaris DG, Levy RS (December 1992). "Purification, subunit structure and inhibitor profile of cathepsin A". ... Carboxypeptidase C (EC 3.4.16.5, carboxypeptidase Y, serine carboxypeptidase I, cathepsin A, lysosomal protective protein, ...
Cathepsin E. TALE homeodomain transcription factors. Hydrocortisone. Since keratinocyte differentiation inhibits keratinocyte ... "The role of cathepsin E in terminal differentiation of keratinocytes". Biological Chemistry. 392 (6): 571-85. doi:10.1515/BC. ...
Cathepsin D is involved in CLN10. DNA analysis can be used to help confirm the diagnosis of Batten disease. When the mutation ...
Miv-711 Cathepsin K inhibitor for osteoarthritis. Fast track (FDA) MALT1 "Swedish pharma firm Medivir partners Aragen Life ...
Her research has examined cathepsins and proteases associated with cancer. She has also used imaging with fluorescent probes to ... Sloane, Bonnie F.; Dunn, John R.; Honn, Kenneth V. (1981-06-05). "Lysosomal Cathepsin B: Correlation with Metastatic Potential ... Sloane, Bonnie F.; Dunn, John R.; Honn, Kenneth V. (1981-06-05). "Lysosomal Cathepsin B: Correlation with Metastatic Potential ... Mohamed, Mona Mostafa; Sloane, Bonnie F. (2006). "Cysteine cathepsins: multifunctional enzymes in cancer". Nature Reviews ...
... these include cathepsin L, papain, and procaricain. It forms an alpha-helical domain that runs through the substrate-binding ...
"Cathepsins as transcriptional activators? Developmental Cell 2004, 6(5):610-1. Goulet B, and Nepveu A. "Complete and Limited ...
Lushbaugh WB, Hofbauer AF, Pittman FE (June 1985). "Entamoeba histolytica: purification of cathepsin B". Experimental ...
Cathepsin A (serine protease) Cathepsin B (cysteine protease) Cathepsin C (cysteine protease) Cathepsin D (aspartyl protease) ... Cathepsin H (cysteine protease) Cathepsin K (cysteine protease) Cathepsin L1 (cysteine protease) Cathepsin L2 (or V) (cysteine ... Cathepsin S (cysteine protease) Cathepsin W (cysteine proteinase) Cathepsin Z (or X) (cysteine protease) Cathepsins are ... Cathepsin K has also been shown to play a role in arthritis. Mouse cathepsin L is homologous to human cathepsin V. Mouse ...
Directed screening of nitrile compounds revealed 3 as a highly potent cathepsin K inhibitor but with cathepsin S activity and ... Directed screening of nitrile compounds revealed 3 as a highly potent cathepsin K inhibitor but with cathepsin S activity and ... a potent and highly selective cathepsin K inhibitor for the treatment of osteoarthritis.. Dossetter, A.G., Beeley, H., Bowyer, ...
This procedure applies to all products that have a specification for Cathepsin B activity determined by the liberation of 7- ... Cathepsin B Enzyme Solution (Enzyme). Immediately before use, prepare a solution containing 5-10 units/mL of Cathepsin B in ... Lysosomal Cathepsin B has also been shown to degrade soluble monomeric collagen and insoluble polymeric collagen in vitro. ... Cathepsin B is a lysosomal cysteine proteinase that will hydrolyze proteins with a broad specificity for peptide bonds, but ...
CATHEPSIN D (human). Find diseases associated with this biological target and compounds tested against it in bioassay ...
Ausgesuchte Qualitäts-Hersteller für Cathepsin G Antikörper. Hier bestellen. ... Monoklonale und polyklonale Cathepsin G Antikörper für viele Methoden. ... Aliase für Cathepsin G Antikörper. cathepsin G (CTSG) Antikörper. cathepsin G (Ctsg) Antikörper. cathepsin G (LOC505658) ... cathepsin G (LOC509956) Antikörper. cathepsin G (ctsg) Antikörper. cathepsin G (LOC100053921) Antikörper. cathepsin G ( ...
Cathepsin E mRNA was detected in enalapril-treated aorta and kidney, and cathepsin D mRNA was detected in all tissues examined ... Cathepsin E and cathepsin S, endosomal/lysosomal proteases, have been shown to play important roles in the major ... While significant amounts of cathepsin D were found in both the hippocampus and the neostriatum of normal rats, cathepsin E was ... Cathepsin E in follicle associated epithelium of intestine and tonsils: localization to M cells and possible role in antigen ...
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"If cathepsin Bs activity is to chew back at the C-terminus of Aβ, particularly Aβ42, then a mouse with increased Aβ42 ... The enzyme, cathepsin B (CatB), caught the attention of Li Gan at the Gladstone Institute of Neurological Disease in San ... Cystatin Cs Naughty Side-Slowing Aβ Degradation by Cathepsin B. Quick Links. *Article ... production (the APP-J20 mouse) will show the greatest effects when cathepsin B activity is increased," he said. "I think that ...
One of the less explored is the milk enzyme cathepsin D, proteolytic enzyme located in the lysosomes, which are an integral ... Detection of cathepsin D in ewes milk by Western Blotting method. Iva Dolenčić Špehar orcid.org/0000-0002-8036-583X ; ... 2013). Detection of cathepsin D in ewes milk by Western Blotting method, Mljekarstvo, 63(1), str. 36-41. Preuzeto s: https ... Dolenčić Špehar I, Martinković F, Havranek J, Marinculić A, Tudor Kalit M, Kalit S. Detection of cathepsin D in ewes milk by ...
The cysteinal lysosomal proteases, cathepsin L (CL) and cathepsin S (CS), have been shown to process invariant chain, thereby ... A role for cathepsin L and cathepsin S in peptide generation for MHC class II presentation J Immunol. 2002 Mar 15;168(6):2618- ... The cysteinal lysosomal proteases, cathepsin L (CL) and cathepsin S (CS), have been shown to process invariant chain, thereby ...
Cathepsin B, also known as CTSB, is a lysosomal cysteine protease. ... Cathepsin B Activity Protocol: 1. Dilute the recombinant mouse Cathepsin B to 10 μg/ml in activation buffer (25 mM MES, 1 mM ... Cathepsin B, also known as CTSB, is a lysosomal cysteine protease. While most cathepsins are exclusively endopeptidases, CTSB ... CTSB, CPSB, APP secretase, APPS, Cathepsin B1, CB Ave. Rating Submit a Review Product Citations publications Mouse CTSB enzyme ...
Cathepsin B activity was selectively elevated early in the course of illness. Luepeptin, a cathepsin B inhibitor, and ... Inhibitors of prostaglandin synthesis or cathepsin B prevent muscle wasting due to sepsis in the rat.. ... Inhibitors of prostaglandin synthesis or cathepsin B prevent muscle wasting due to sepsis in the rat.. ... Muscle wasting and impaired contractility associated with sepsis may involve selective prostaglandin stimulation of cathepsin B ...
Pharmacological inhibition of cathepsin activity with CA074-Me resulted in a substantial reduction of both mature IL-1β ... Pharmacological inhibition of cathepsin activity with CA074-Me resulted in a substantial reduction of both mature IL-1β ... Moreover, cathepsin inhibition abolished the interaction between NLRP3 and ASC, measured by co-immunoprecipitation and by ... Moreover, cathepsin inhibition abolished the interaction between NLRP3 and ASC, measured by immunofluorescence imaging in H37Rv ...
Verschiedene Studien weisen auf eine Beteiligung von Cathepsin D an Apoptose hin. In manchen Systemen ist die durch Cathepsin D ... Proteinolyse-unabhaengige proapoptotische Wirkung von Cathepsin D und Procathepsin D ... Übergangszustandsmimetika zur selektiven Inhibition der HIV-1 Protease und Cathepsin D by: Specker, Edgar Published: (2004) ... mediierte Apoptose durch seinen Inhibitor Pepstatin A hemmbar, in anderen ist die enzymatische Aktivität des Cathepsin D für ...
Cathepsins are a class of globular lysosomal proteases, playing a vital role in mammalian cellular turnover. They degrade ... The cathepsin family consists of 12 cysteine proteases with broad exo- and endopeptidase activity, of which Cathepsin B is a ... Cathepsin B enzyme, human liver: 5 µL Component D: Assay Buffer: 20 mL Component E: Cathepsin B inhibitor Ac-LVK-CHO: 100 µM, ... Component A: Cathepsin B substrate, Ex/Em=354 nm/442 nm upon cleavage: 1 mM, 50 µL Component B: AMC, Fluorescence Reference ...
Western blot analysis of PARP-1 cleavage patterns in mutant lysates suggests that increases in pH dependent cathepsin activity ... Consistently, treatment with ALLM and Bafilomycin A1 (cathepsin/calpain and vacuolar-type H+-ATPase inhibitors, respectively), ... Taken together, these data suggest that vps11 promotes normal melanophore morphology and survival by inhibiting cathepsin ...
Tatò, Maia Lucia (2019): Untersuchungen zur Rolle von Cathepsin S beim experimentellen und humanen Systemischen Lupus ... Untersuchungen zur Rolle von Cathepsin S beim experimentellen und humanen Systemischen Lupus Erythematodes ... Untersuchungen zur Rolle von Cathepsin S beim experimentellen und humanen Systemischen Lupus Erythematodes ...
Cathepsin D was assayed with a Dako set. Keratin was measured by the Kreyberg method. Normal skin from behind the ear was taken ... There were trace amounts of cathepsin D within the dermis. In the control group (the skin samples), there were trace amounts of ... The aim of the present study was to evaluate the activity of cathepsin D in the structures of cholesteatoma.Material/Methods: ... cathepsin D within the corneous layer of the epithelium.Conclusions: Cathepsin D places a major role in bone tissue destruction ...
Serum cathepsin B activity was significantly higher in both the BRT-treated group (27.8±4.1 U/I,p<0.01) and the tumor- ... Serum cathepsin B activity was determined, tumor volumes were measured, and histological examinations of the tumor tissues were ... The aim of this study was to assess serum cathepsin activity during tumor progression and regression.Material/Methods: Of 60 ... bearing group (19.9±2.5 U/l, p<0.05), as compared to the controls (13.3±3.4U/l).Conclusions:Cathepsin B may play an ...
Recombinant Autographa californica nuclear polyhedrosis virus Viral cathepsin (VCATH) from Cusabio. Cat Number: CSB-EP340730ARA ... Recombinant Autographa californica nuclear polyhedrosis virus Viral cathepsin (VCATH) , CSB-EP340730ARA. (No reviews yet) Write ... Recombinant Autographa californica nuclear polyhedrosis virus Viral cathepsin (VCATH) , CSB-EP340730ARA Cusabio Other Organism ... Recombinant Autographa californica nuclear polyhedrosis virus Viral cathepsin (VCATH) , CSB-EP340730ARA. Rating Required Select ...
Mutations of the cathepsin C gene are responsible for Papillon-Lefèvre syndrome ... Mutations of the cathepsin C gene are responsible for Papillon-Lefèvre syndrome ...
Cathepsin L might be an efficient way to reduce the spread & severity of COVID-19 - Learn how. ... In addition, a broad range of other Cathepsin Assays, Cathepsin Inhibitors as well as recombinant Cathepsins, Cathepsin ... Furin Inhibitor Screening Kit as well as Cathepsin L Activity Assay Kit & Cathepsin L Inhibitor Screening Kit as tools to ... Cathepsin Inhibitors. Product Info Related Resources Cell Analysis Brochure. For cutting-edge research, you need the best cell- ...
Haim-Munk syndrome and Papillon-Lefèvre syndrome are allelic mutations in cathepsin C ... Haim-Munk syndrome and Papillon-Lefèvre syndrome are allelic mutations in cathepsin C ...
Submit a product review for Human Cathepsin L Biotinylated Antibody BAF952 ...
Aspartic proteinase, Cathepsin D, Endopeptidase, Hordeum (proteinase). in Planta. volume. 186. issue. 3. pages. 7 pages. ... Aspartic proteinase from barley grains is related to mammalian lysosomal cathepsin D. *Mark ... Cathepsin D; Endopeptidase; Hordeum (proteinase)}}, language = {{eng}}, number = {{3}}, pages = {{317--323}}, publisher = {{ ... sequence alignment and inhibition studies showed that the barley aspartic proteinase resembles mammalian lysosomal cathepsin D ...
cathepsin L - C1: Papain. Detailed annotation on the structure, function, physiology, pharmacology and clinical relevance of ... Cathepsins B, H and L have become important therapeutic targets as their proteolytic activity has been implicated in several ... cathepsin L1 , fs , furless , MEP , nackt , nkt , Cat L , p39 cysteine proteinase ... 2010) Identification and pre-clinical testing of a reversible cathepsin protease inhibitor reveals anti-tumor efficacy in a ...
Synthetic peptide surrounding aa 140 of mouse cathepsins D.. Activity cross reaction. Reacts with mouse CTSD / Cathepsin D. ... CTSD / Cathepsin D antibody CTSD, CPSD, CLN10, Lysosomal aspartyl peptidase, Lysosomal aspartyl protease, ProCathepsin D, CatD ...
Assessment of cathepsin D and L-like proteinases of poultry red mite, Dermanyssus gallinae (De Geer), as potential vaccine ... Assessment of cathepsin D and L-like proteinases of poultry red mite, Dermanyssus gallinae (De Geer), as potential vaccine ... Printed from /publications/assessment-cathepsin-d-and-l-proteinases-poultry-red-mite-dermanyssus-gallinae-de-geer on 07/12/23 ... assessment-cathepsin-d-and-l-proteinases-poultry-red-mite-dermanyssus-gallinae-de-geer ...
The encoded protein is also known as cathepsin X and cathepsin P. This gene is ubiquitously expressed in cancer cell lines and ... Ortholog to human CTSZ (cathepsin Z); INTERACTS WITH 1-naphthyl isothiocyanate; 2,3,7,8-tetrachlorodibenzodioxin; 3,3,5,5- ...
The Role of Cathepsin B in Pathophysiologies of Non-tumor and Tumor tissues: A Systematic Review. J Cancer. 14(12):2344-2358. ... The Role of Cathepsin B in Pathophysiologies of Non-tumor and Tumor tissues: A Systematic Review Jiangping Wang1#, Minying ... Wang J, Zheng M, Yang X, Zhou X, Zhang S. The Role of Cathepsin B in Pathophysiologies of Non-tumor and Tumor tissues: A ... Wang J, Zheng M, Yang X, Zhou X, Zhang S. The Role of Cathepsin B in Pathophysiologies of Non-tumor and Tumor tissues: A ...
  • SAR114137, a Cathepsin S inhibitor, did not progress past phase I for chronic pain. (wikipedia.org)
  • In 2022, STI-1558, a Cathepsin L inhibitor, received FDA clearance to begin phase I studies to treat COVID-19. (wikipedia.org)
  • Directed screening of nitrile compounds revealed 3 as a highly potent cathepsin K inhibitor but with cathepsin S activity and very poor stability to microsomes. (rcsb.org)
  • In manchen Systemen ist die durch Cathepsin D mediierte Apoptose durch seinen Inhibitor Pepstatin A hemmbar, in anderen ist die enzymatische Aktivität des Cathepsin D für seine apoptotische Involvierung entbehrlich. (uni-marburg.de)
  • In addition to our assays for studying binding of SARS-CoV-2 to the ACE2 receptor and screening for respective inhibitors/drugs (see below), we offer the Furin Activity Assay Kit & Furin Inhibitor Screening Kit as well as Cathepsin L Activity Assay Kit & Cathepsin L Inhibitor Screening Kit as tools to develop new targeted therapeutics for Covid-19. (promocell.com)
  • 2010) Identification and pre-clinical testing of a reversible cathepsin protease inhibitor reveals anti-tumor efficacy in a pancreatic cancer model. (guidetopharmacology.org)
  • 4. Méthot N, Rubin J, Guay D, Beaulieu C, Ethier D, Reddy TJ, Riendeau D, Percival MD. (2007) Inhibition of the activation of multiple serine proteases with a cathepsin C inhibitor requires sustained exposure to prevent pro-enzyme processing. (guidetopharmacology.org)
  • 5. Takahashi K, Ueno T, Tanida I, Minematsu-Ikeguchi N, Murata M, Kominami E. (2009) Characterization of CAA0225, a novel inhibitor specific for cathepsin L, as a probe for autophagic proteolysis. (guidetopharmacology.org)
  • Roche's cathepsin S inhibitor petesicatib (RO5459072 or RG7625) completed Phase 2 clinical evaluation in Sjögren's syndrome ( NCT02701985 ) and Phase 1 in celiac disease ( NCT02679014 ), but there are no active clinical trials registered with ClinicalTrials.gov . (guidetoimmunopharmacology.org)
  • 2008) The discovery of odanacatib (MK-0822), a selective inhibitor of cathepsin K. Bioorg Med Chem Lett , 18 (3): 923-8. (guidetoimmunopharmacology.org)
  • Pharmacological inhibition of cathepsin activity with CA074-Me resulted in a substantial reduction of both mature IL-1β production and caspase-1 activation in infected macrophages. (frontiersin.org)
  • Moreover, cathepsin inhibition abolished the interaction between NLRP3 and ASC, measured by immunofluorescence imaging in H37Rv-infected macrophages, demonstrating a critical role of the enzyme in NLRP3-inflammasome activation. (frontiersin.org)
  • Inhibition of the Furin protease and Cathepsin L might therefore be an efficient way to attenuate the infection process and reduce the spread and severity of COVID-19. (promocell.com)
  • Amino-acid sequence alignment and inhibition studies showed that the barley aspartic proteinase resembles mammalian lysosomal cathepsin D (EC 3.4.23.5). (lu.se)
  • SerpinB1 is critical for neutrophil survival through cell-autonomous inhibition of cathepsin G." Blood 121, no. 19 (2013): 3900-3907 van den Berg, Carmen W., et al. (athensresearch.com)
  • By screening a combinatorial pentapeptide amide collection in an inhibition assay, we systematically evaluated the potential of 19 proteinogenic amino acids and seven nonproteinogenic amino acids to serve as building blocks for inhibitors of human cathepsin L. Particularly efficient were aromatic, bulky, hydrophobic amino-acid residues, especially leucine, and positively charged residues, especially arginine. (uni-bielefeld.de)
  • RNAi mediated depletion of CD44 and MT1-MMP expression and pharmacological inhibition of cathepsin K attenuated CD44 promoted invasion through a collagen I matrix. (biomedcentral.com)
  • 2017) Cathepsin S inhibition combines control of systemic and peripheral pathomechanisms of autoimmune tissue injury. (guidetoimmunopharmacology.org)
  • 2010) Functionalized benzophenone, thiophene, pyridine, and fluorene thiosemicarbazone derivatives as inhibitors of cathepsin L. Bioorg Med Chem Lett , 20 (22): 6610-5. (guidetopharmacology.org)
  • Cathepsin B may function as a beta-secretase 1, cleaving amyloid precursor protein to produce amyloid beta. (wikipedia.org)
  • Osteoclasts are the bone resorbing cells of the body, and they secrete cathepsin K in order to break down collagen, the major component of the non-mineral protein matrix of the bone. (wikipedia.org)
  • The enzyme, cathepsin B (CatB), caught the attention of Li Gan at the Gladstone Institute of Neurological Disease in San Francisco several years ago when it appeared to prevent buildup of amyloid plaques in the brains of AD mice overexpressing mutant human amyloid precursor protein (APP). (alzforum.org)
  • 1. Dilute the recombinant mouse Cathepsin B to 10 μg/ml in activation buffer (25 mM MES, 1 mM DTT, pH 5.0) and incubate the protein at 25°C for 3 min. (biolegend.com)
  • This protein mediates either fusion of the virus membrane with the host cell membrane (TMPRSS2 activated mediation) or endocytosis of the virus particle (Cathepsin-activated mediation) and its entry into the cell. (promocell.com)
  • A further host protease required for activation of the S Protein is Cathepsin L which also facilitates SARS-CoV-2 entry into target cells through an alternative route. (promocell.com)
  • The S Protein is then processed/activated by the lysosomal Cathepsin L in the late endosomes (endo-lysosomes) following endocytosis of the virus. (promocell.com)
  • Specific Furin and Cathepsin L inhibitors which block proteolytic activation of the S Protein , and thus SARS-CoV-2 virus entry and replication, are potential antiviral agents to counteract SARS-CoV-2 infection and pathogenesis. (promocell.com)
  • Reacts with mouse CTSD / Cathepsin D. Cross reacts with human and rat protein. (covalab.com)
  • The encoded protein is also known as cathepsin X and cathepsin P. This gene is ubiquitously expressed in cancer cell lines and primary tumors and, like other members of this family, may be involved in tumorigenesis. (enigmadiagnostics.com)
  • The deduced amino acid sequence between the primers was identical to that reported for neutrophil cathepsin G, indicating that the protein of cutaneous mast cells previously shown to be immunologically cross-reactive with neutrophil cathepsin G has a comparable amino acid sequence. (duke.edu)
  • Quantitative real-time PCR, immuno-blotting and ELISA-based experiments have demonstrated that the transcript and protein expression of cathepsin K and MT1MMP increase in response to CD44/HA signalling in a panel of CD44-expressing breast cancer cell lines (MDA231, MDA157 and MCF7F). (biomedcentral.com)
  • Furthermore, CD44/HA signalling was shown to increase cathepsin K and MT1MMP mRNA and protein expression in the MDAMB231BO cells. (biomedcentral.com)
  • Cathepsin E Protein, Human (HEK293, His) is an approximately 46.0 kDa mouse cathepsin Dwith a His tag. (medchemexpress.com)
  • Human Cathepsin E is synthesized as a precursor protein, consisting of a signal peptide (residues 1 17), a propeptide (residues 18 53), and a mature chain (residues 54 396) [3] . (medchemexpress.com)
  • Furthermore, the discovery of Cathepsin B secretion and function as an extracellular matrix protein has broadened our appreciation for the impact of Cathepsin B on cancer progression. (edu.rs)
  • Cathepsin S is expressed in the lysosome of antigen presenting cells (dendritic cells, B-cells and macrophages) where it processes the invariant chain-MHC-II complex (a chaperone protein that prevents premature peptide loading) inside antigen presenting cells and in this way controls antigen presentation. (guidetoimmunopharmacology.org)
  • This invention relates to a compound of formula I and their use as inhibitors of Cathepsin C, pharmaceutical compositions containing the same, and methods of using the same as agents for treatment and/or prevention of diseases connected with dipeptidyl peptidase I activity, e.g. respiratory diseases. (justia.com)
  • Thus, inhibitors of Cathepsin C could potentially be useful therapeutics for the treatment of neutrophil-dominated inflammatory diseases such as chronic obstructive pulmonary disease (COPD), pulmonary emphysema, asthma, multiple sclerosis, and cystic fibrosis (Guay et al. (justia.com)
  • The cysteinal lysosomal proteases, cathepsin L (CL) and cathepsin S (CS), have been shown to process invariant chain, thereby facilitating MHC class II maturation. (nih.gov)
  • Cathepsins are a class of globular lysosomal proteases playing a vital role in mammalian cellular turnover. (eurogentec.com)
  • The cathepsin family consists of 12 cysteine proteases with broad exo- and endopeptidase activity, of which Cathepsin B is a member. (eurogentec.com)
  • Neutrophils are recruited to the site of joint inflammation and release Cathepsin G, elastase and proteinase 3, proteases which are believed to be responsible for cartilage destruction associated with rheumatoid arthritis. (justia.com)
  • Cathepsin E is an aspartic protease and a member of the peptidase A1 family of proteases. (medchemexpress.com)
  • Cathepsins represent a group of such proteases aimed at maintenance of cellular homeostasis. (edu.rs)
  • Cathepsin K is the most potent mammalian collagenase. (wikipedia.org)
  • It has been surprisingly found that the bicyclic compounds of the present invention possess potent Cathepsin C activity, high selectivity against other Cathepsins, e.g. (justia.com)
  • Among the most potent novel inhibitors, one peptide, RKLLW-NH2, shares the amphiphilic character of the nonamer fragment VMNGLQNRK of the autoinhibitory, substrate-like, but reverse-binding prosegment of human cathepsin L which blocks the active center of the enzyme. (uni-bielefeld.de)
  • Highly potent inhibitors of human cathepsin L identified by screening combinatorial pentapeptide amide collections", EUROPEAN JOURNAL OF BIOCHEMISTRY , vol. 267, 2000, pp. 5085-5092. (uni-bielefeld.de)
  • Cathepsins have a vital role in mammalian cellular turnover. (wikipedia.org)
  • Finally, we discuss how insights from yeast cathepsin D and its role in regulated cell death can unveil novel functions of mammalian cathepsin D in apoptosis and cancer . (bvsalud.org)
  • Cathepsin B is a lysosomal cysteine proteinase that will hydrolyze proteins with a broad specificity for peptide bonds, but will preferentially cleave at the carboxyl side of Arg-Arg bonds in small molecule substrates. (sigmaaldrich.com)
  • The activity of Cathepsin B is determined by its ability to cleave the fluorogenic peptide substrate, Z-Leu-Arg-AMC (Z=Benzyloxycarbonyl, and AMC=7-amino-4-methylcoumarin) after activation. (biolegend.com)
  • The SensoLyte® 440 Cathepsin B Assay Kit provides a fluorogenic peptide for measurement of enzyme activity. (eurogentec.com)
  • This peptide releases the AMC (7-amino-4-methylcoumarin) fluorophore upon cathepsin B cleavage and can be detected with excitation at 354 nm and emission at 442 nm. (eurogentec.com)
  • Synthetic peptide surrounding aa 140 of mouse cathepsins D. (covalab.com)
  • Cathepsin E functions by breaking down proteins through the hydrolysis of peptide bonds at a specific peptide sequence site. (medchemexpress.com)
  • One of the less explored is the milk enzyme cathepsin D, proteolytic enzyme located in the lysosomes, which are an integral part of the somatic cells whose number varies depending on the animal's health. (srce.hr)
  • Cathepsins B, H and L have become important therapeutic targets as their proteolytic activity has been implicated in several pathological inflammatory conditions, such as arthritis and periodontitis. (guidetopharmacology.org)
  • 2. Frizler M, Schmitz J, Schulz-Fincke AC, Gütschow M. (2012) Selective nitrile inhibitors to modulate the proteolytic synergism of cathepsins S and F. J Med Chem , 55 (12): 5982-6. (guidetoimmunopharmacology.org)
  • However, cathepsin D can have both anti- and pro- survival functions depending on its proteolytic activity, cellular context and stress stimulus. (bvsalud.org)
  • Cathepsin zymography separates different cathepsins based on their migration through a polyacrylamide gel co-polymerized with a gelatin substrate. (wikipedia.org)
  • The substrate Nα-CBZ-Arg-Arg-7-amido-4-methylcoumarin is used for the fluorometric detection of Cathepsin B activity. (sigmaaldrich.com)
  • Add 50 μl of the diluted, activated Cathepsin B (0.0025 µg/well) to a black well and start the reaction by adding 50 μl of 40 μM substrate. (biolegend.com)
  • Sensitive fluorogenic substrate for the quantitative determination of cathepsin B activity. (emdmillipore.com)
  • There are, however, exceptions such as cathepsin K, which works extracellularly after secretion by osteoclasts in bone resorption. (wikipedia.org)
  • Objectives: To investigate serum biomarkers, tartrate resistant acid phosphatase 5b (TRAcP5b) and cathepsin K, indicative of osteoclastic bone resorption, and their relationship to pain and pain change in knee osteoarthritis (OA). (nottingham.ac.uk)
  • Unlike some of the other cathepsins, cathepsin D has some protease activity at neutral pH. (wikipedia.org)
  • CTS protease activity also measured by zymograph electrophoresis of Cathepsins. (histoready.com)
  • Cathepsin B, also known as CTSB, is a lysosomal cysteine protease. (biolegend.com)
  • While most cathepsins are exclusively endopeptidases, CTSB exhibits both carboxypeptidase and endopeptidase activities. (biolegend.com)
  • Lysosomal cathepsin B (CTSB) has been proposed to play a role in the induction of acute inflammation. (frontiersin.org)
  • These observations suggest that during Mtb infection, lysosomal release of activated CTSB and possibly other cathepsins inhibitable by CA07-Me is critical for the induction of inflammasome-mediated IL-1β processing by regulating NLRP3-inflammasome assembly in the cytosol. (frontiersin.org)
  • Cathepsin B (CTSB), a lysosomal cysteine protease, plays an important role in human physiology and pathology. (jcancer.org)
  • This study establishes the primary structure of human skin chymase and provides further evidence for the presence of a cathepsin G-like proteinase within human mast cells. (duke.edu)
  • 2. Dilute the recombinant mouse Cathepsin B to 0.05 μg/ml in assay buffer (25 mM MES, pH 5.0). (biolegend.com)
  • In addition, a broad range of other Cathepsin Assays , Cathepsin Inhibitors as well as recombinant Cathepsins , Cathepsin antibodies & ELISAs also useful to study SARS-CoV infections (e.g. (promocell.com)
  • Cathepsin D (an aspartyl protease) appears to cleave a variety of substrates such as fibronectin and laminin. (wikipedia.org)
  • Cathepsin K, among other cathepsins, plays a role in cancer metastasis through the degradation of the extracellular matrix. (wikipedia.org)
  • Background:Serum cathepsin B activity has been considered a potential marker of tumor progression. (medscimonit.com)
  • The aim of this study was to assess serum cathepsin activity during tumor progression and regression.Material/Methods: Of 60 female rats inoculated with Morris hepatoma cells, 45 were treated with BRT, and the remaining 15 were left without treatment. (medscimonit.com)
  • Serum cathepsin B activity was determined, tumor volumes were measured, and histological examinations of the tumor tissues were performed.Results: Of the 45 BRT-treated rats, tumor regression was observed in 31 rats, and serum cathepsin activity was analyzed in these rats. (medscimonit.com)
  • Conclusions: Cathepsin B may play an important role, not only in tumor expansion, but also during the processes of cancer cell death and resorption. (medscimonit.com)
  • Wang J, Zheng M, Yang X, Zhou X, Zhang S. The Role of Cathepsin B in Pathophysiologies of Non-tumor and Tumor tissues: A Systematic Review. (jcancer.org)
  • Nevertheless, recent reports suggest that Cathepsin B executes other cellular programs such as controlling tumor growth, migration, invasion, angiogenesis, and metastases development. (edu.rs)
  • Underneath a façade of an intracellular protease with limited therapeutic potential hides a central role of cathepsins in extracellular functions. (edu.rs)
  • Here we discuss the role of Cathepsin B in the oncogenic process and perspective the use of Cathepsin B for diagnostic and therapeutic applications. (edu.rs)
  • In particular, cathepsin D is often overexpressed and hypersecreted in cancer cells , implying it may constitute a therapeutic target. (bvsalud.org)
  • The cathepsin A activity in lysates of metastatic lesions of malignant melanoma is significantly higher than in primary focus lysates. (wikipedia.org)
  • Five cyclic peptides show inhibitory activity towards human cathepsins L, B, H, and K. Several inhibitors have reached clinical trials, targeting cathepsins K and S as promising therapeutics for osteoporosis, osteoarthritis, and chronic pain. (wikipedia.org)
  • This procedure applies to all products that have a specification for Cathepsin B activity, such as product numbers C0150 and C8571 , determined by the liberation of 7-amino-4-methylcoumarin from Z-Arg-Arg 7-amido-4-methylcoumarin. (sigmaaldrich.com)
  • Cathepsin B activity was selectively elevated early in the course of illness. (jci.org)
  • Muscle wasting and impaired contractility associated with sepsis may involve selective prostaglandin stimulation of cathepsin B activity. (jci.org)
  • Immunohistochemical investigations on cathepsin D activity in structures of cholesteatoma. (medscimonit.com)
  • Results: Serum TRAcP5b activity, but not cathepsin K-immunoreactivity, was associated with density of TRAcP-positive osteoclasts in the subchondral bone of medial tibia plateaux. (nottingham.ac.uk)
  • Cathepsin G Protease Assay for compound screening and profiling via fluorescence-based quantification of enzyme activity. (reactionbiology.com)
  • Cathepsins B and L are involved in matrix degradation and cell invasion. (wikipedia.org)
  • And Cathepsin E plays an important role in the degradation of proteins, the generation of bioactive proteins, and antigen processing [2] . (medchemexpress.com)
  • Cathepsin L-deficient mice were shown to have less adipose tissue, lower serum glucose and insulin levels, more insulin receptor subunits, more glucose transporter (GLUT4) and more fibronectin than wild type controls. (wikipedia.org)
  • To compare the levels of Dynamin and Cathepsin L in serum and urine of participants with proteinuric kidney disease to those of normal controls. (wits.ac.za)
  • Methods A prospective study of 37 patients with proteinuric kidney disease versus a healthy control group of 40 individuals, where the serum and urine levels of Cathepsin L and Dynamin were determined using an Enzyme Linked immunosorbent assay and the levels compared between the two groups. (wits.ac.za)
  • An independent sample t-test was used to assess whether the mean serum Dynamin, urine Dynamin, serum Cathepsin L and urine Cathepsin L differed for the control group compared with kidney disease group. (wits.ac.za)
  • There was no difference in the levels of serum Cathepsin L between the renal disease and the control groups (p= 0.23). (wits.ac.za)
  • Intracellular electrolyte changes may involve prostaglandin synthesis but do not require cathepsin B activation. (jci.org)
  • As an intracellular, hydrolytic aspartic protease, Cathepsin E is mainly expressed in cells of the immune and gastrointestinal systems, lymphoid tissues, erythrocytes, and cancer cells [1] . (medchemexpress.com)
  • UP-cDNA demonstrating amplification products for cathepsin G did not demonstrate amplification products for human neutrophil elastase, suggesting that the cathepsin G PCR amplification product was not derived from neutrophils or monocytes possibly contaminating the lesion. (duke.edu)
  • Cathepsin B has also been implicated in the progression of various human tumors including ovarian cancer. (wikipedia.org)
  • Mouse cathepsin L is homologous to human cathepsin V. Mouse cathepsin L has been shown to play a role in adipogenesis and glucose intolerance in mice. (wikipedia.org)
  • Hier sind Cathepsin G Antikörper für eine Vielzahl von Species wie anti-Human Cathepsin G, anti-Rat Cathepsin G, anti-Mouse Cathepsin G zu finden. (antikoerper-online.de)
  • Buy Purified Native Human Cathepsin G (CatG), Human Neutrophil. (athensresearch.com)
  • This random approach for the design of inhibitors was introduced to compensate for the inaccuracy induced by shifted docking of combinatorial compound collections at the active center of cathepsin L. Thereby, we obtained structurally defined pentapeptide amides which inhibited human cathepsin L at nanomolar concentrations. (uni-bielefeld.de)
  • Scholars@Duke publication: Determination of the primary structures of human skin chymase and cathepsin G from cutaneous mast cells of urticaria pigmentosa lesions. (duke.edu)
  • Amplification of the same UP-cDNA with primers coding for the NH2- and COOH-terminal sequences of human neutrophil cathepsin G also produced a specific amplification product which was sequenced. (duke.edu)
  • Cathepsin D has garnered increased attention in recent years, mainly since it has been associated with several human pathologies . (bvsalud.org)
  • Cathepsin L levels were elevated in the urine of the renal disease group, in keeping with the notion that Cathepsin L proteolysis plays a critical role in the various forms of proteinuria. (wits.ac.za)
  • In this review , we provide an overview of the role of cathepsin D in physiological and pathological scenarios. (bvsalud.org)
  • Mouse Cathepsin B, amino acids (His18-Phe339) (Accession# P10605), with C-terminal 10x His tag, was expressed in CHO cells. (biolegend.com)
  • Cathepsin K has also been shown to play a role in arthritis. (wikipedia.org)
  • Emphasis is given to the role of the yeast protease Pep4p, the vacuolar counterpart of cathepsin D , in life and death . (bvsalud.org)
  • Role of engineered metal oxide nanoparticle agglomeration in reactive oxygen species generation and cathepsin B release in NLRP3 inflammasome activation and pulmonary toxicity. (cdc.gov)
  • Therefore, specific particle parameters, i.e. preexposure dispersion status and particle surface area, of two ENM (NiO and CeO2) were used to evaluate the role of ROS generation and cathepsin B release during ENM-induced toxicity. (cdc.gov)
  • The cysteine cathepsins have attracted significant research effort as drug targets. (wikipedia.org)
  • Hier sind Cathepsin G Antikörper zu finden, welche für eine bestimmte Anwendung wie WB, FACS, ELISA, IHC validiert wurde. (antikoerper-online.de)
  • In fact, elevated levels of Cathepsins are found under different pathological conditions including inflammation, infection, neurodegenerative disease, and cancer. (edu.rs)
  • Therefore, a more detailed understanding of cathepsin D regulation and how to modulate its apoptotic functions is clearly needed. (bvsalud.org)
  • Elevated levels of cathepsin B were detected in metastases and neurological disorders including Alzheimer's disease (AD). (eurogentec.com)
  • Stroke Traumatic brain injury Alzheimer's disease Arthritis Ebola, Cathepsin B and to a lesser extent cathepsin L have been found to be necessary for the virus to enter host cells. (wikipedia.org)
  • 1) You stated that there is a lack of information on other SNPs of cathepsin, after a few minutes in Clarivate's Web of Science a paper was found (10.1016/j.jpeds.2017.08.063) describing an extra cathepsin mutation (Q334P) possibly involved in pancreatitis, though not tropical calcific pancreatitis. (peerj.com)
  • A New Analytical Method for Determination of Cathepsin L Based on the Surface Plasmon Resonance Imaging Biosensor. (uni-bielefeld.de)
  • The expression of cathepsin K in cultured endothelial cells is regulated by shear stress. (wikipedia.org)
  • Further experiments conducted using a parental and bone-homing subclone of the MDAMB231 cell line (MDAMB213BO) have shown that the expression of CD44, cathepsin K and MT1MMP is elevated in the MDAMB231BO cells relative to their parental counterparts. (biomedcentral.com)
  • CpG DNA inhibits the proliferation of pro-B, but not pre-B, cells by inducing caspase-independent cell death through a pathway that requires the expression of cathepsin B. This pathway is operative in Rag-deficient mice carrying an SP6 transgene, in which B lymphopoiesis is compromised, to reduce the size of the B lymphocyte precursor compartments in the bone marrow. (pasteur.fr)
  • The genetic knockout for cathepsin S and K in mice with atherosclerosis was shown to reduce the size of atherosclerotic lesions. (wikipedia.org)
  • Tatò, Maia Lucia (2019): Untersuchungen zur Rolle von Cathepsin S beim experimentellen und humanen Systemischen Lupus Erythematodes. (uni-muenchen.de)