Immunoglobulin Variable Region
Immunoglobulin Heavy Chains
Somatic Hypermutation, Immunoglobulin
Genes, Immunoglobulin
Immunoglobulin Light Chains
Binding Sites, Antibody
B-Lymphocytes
Hybridomas
Base Sequence
Molecular Sequence Data
Amino Acid Sequence
Immunoglobulins
Immunoglobulin G
Immunoglobulin kappa-Chains
Leukemia, Lymphocytic, Chronic, B-Cell
Gene Rearrangement, B-Lymphocyte, Heavy Chain
Genes, Immunoglobulin Heavy Chain
Gene Rearrangement, B-Lymphocyte
Immunoglobulin M
Immunoglobulin A
Immunoglobulin Idiotypes
Gene Rearrangement
Cytidine Deaminase
Complementarity Determining Regions
Mutation
Antibody Specificity
Clone Cells
Immunoglobulins, Intravenous
Polymerase Chain Reaction
Cloning, Molecular
Immunoglobulin Constant Regions
Immunoglobulin lambda-Chains
Immunoglobulin Fragments
DNA
Mice, Inbred BALB C
Immunoglobulin mu-Chains
Immunoglobulin E
Immunoglobulin Isotypes
Immunoglobulin A, Secretory
Immunoglobulin D
Immunoglobulin Allotypes
Immunoglobulin J-Chains
Immunoglobulin Fab Fragments
Plasmacytoma
Immunoglobulin Fc Fragments
Immunoglobulin gamma-Chains
Immunoglobulin Joining Region
Immunoglobulin Class Switching
Antibody Diversity
Repertoire of human antibodies against the polysaccharide capsule of Streptococcus pneumoniae serotype 6B. (1/3058)
We examined the repertoire of antibodies to Streptococcus pneumoniae 6B capsular polysaccharide induced with the conventional polysaccharide vaccine in adults at the molecular level two ways. In the first, we purified from the sera of seven vaccinees antipneumococcal antibodies and determined their amino acid sequences. Their VH regions are mainly the products of VH3 family genes (candidate genes, 3-23, 3-07, 3-66, and 3-74), but the product of a VH1 family gene (candidate gene, 1-03) is occasionally used. All seven individuals have small amounts of polyclonal kappa+ antibodies (Vkappa1 to Vkappa4 families), although kappa+ antibodies are occasionally dominated by antibodies formed with the product of the A27 Vkappa gene. In contrast, lambda+ anti-6B antibodies are dominated by the antibodies derived from one of 3 very similar Vlambda2 family genes (candidate genes, 2c, 2e, and 2a2) and Clambda1 gene product. The Vlambda2(+) antibodies express the 8.12 idiotype, which is expressed on anti-double-stranded-DNA antibodies. In one case, Vlambda is derived from a rarely expressed Vlambda gene, 10a. In the second approach, we studied a human hybridoma (Dob1) producing anti-6B antibody. Its VH region sequence is closely related to those of the 3-15 VH gene (88% nucleotide homology) and JH4 (92% homology). Its VL region is homologous to the 2a2 Vlambda2 gene (91%) and Jlambda1/Clambda1. Taken together, the V region of human anti-6B antibodies is commonly formed by a VH3 and a Vlambda2 family gene product. (+info)Analysis of V(H)-D-J(H) gene transcripts in B cells infiltrating the salivary glands and lymph node tissues of patients with Sjogren's syndrome. (2/3058)
OBJECTIVE: In patients with Sjogren's syndrome (SS), B lymphocytes have been found to infiltrate salivary glands, resulting in sialadenitis and keratoconjunctivitis. The disease is frequently associated with benign and neoplastic lymphoproliferation. The present study was undertaken to investigate whether clonal B cell expansion takes place in lymphocytic infiltrations of salivary glands under (auto- [?]) antigen stimulation, by analyzing in more detail the variable part (V(H)-D-J(H)) of the immunoglobulin heavy chain genes expressed in these B cells. METHODS: Biopsies of the labial salivary glands and lymph nodes were performed on 2 female patients with SS. The Ig gene rearrangements in these tissues were amplified by reverse transcriptase-polymerase chain reaction using specific primers. RESULTS: A total of 94 V(H)-D-J(H) transcripts were cloned and sequenced. Our data suggest a polyclonal origin of the B cell infiltrates. In 92 of the transcripts, V(H) genes were modified by somatic mutation. Further analysis showed counterselection for replacement mutations within the framework regions, suggesting that those B cells were stimulated and selected for functional expression of a surface Ig. In labial salivary glands from both patients, clonally related B cells became evident. Members of 1 particular clone were found in both the lip and lymph node material. CONCLUSION: These data provide evidence, on the nucleotide sequence level, that an antigen-triggered clonal B cell expansion takes place in the salivary glands of patients with SS who do not have histologic evidence of developing lymphoma. It may be speculated that those B cell clones expand during disease progression, resulting in lymphomagenesis. (+info)The role of homophilic binding in anti-tumor antibody R24 recognition of molecular surfaces. Demonstration of an intermolecular beta-sheet interaction between vh domains. (3/3058)
The murine antibody R24 and mouse-human Fv-IgG1(kappa) chimeric antibody chR24 are specific for the cell-surface tumor antigen disialoganglioside GD3. X-ray diffraction and surface plasmon resonance experiments have been employed to study the mechanism of "homophilic binding," in which molecules of R24 recognize and bind to other molecules of R24 though their heavy chain variable domains. R24 exhibits strong binding to liposomes containing disialoganglioside GD3; however, the kinetics are unusual in that saturation of binding is not observed. The binding of chR24 to GD3-bearing liposomes is significantly weaker, suggesting that cooperative interactions involving antibody constant regions contribute to R24 binding of membrane-bound GD3. The crystal structures of the Fabs from R24 and chR24 reveal the mechanism for homophilic binding and confirm that the homophilic and antigen-binding idiotopes are distinct. The homophilic binding idiotope is formed largely by an anti-parallel beta-sheet dimerization between the H2 complementarity determining region (CDR) loops of two Fabs, while the antigen-binding idiotope is a pocket formed by the three CDR loops on the heavy chain. The formation of homophilic dimers requires the presence of a canonical conformation for the H2 CDR in conjunction with participation of side chains. The relative positions of the homophilic and antigen-binding sites allows for a lattice of GD3-specific antibodies to be constructed, which is stabilized by the presence of the cell membrane. This model provides for the selective recognition by R24 of cells that overexpress GD3 on the cell surface. (+info)Immune response to the immunodominant epitope of mouse hepatitis virus is polyclonal, but functionally monospecific in C57Bl/6 mice. (4/3058)
Mutations in an immunodominant CD8 CTL epitope (S-510-518) are selected in mice persistently infected with the neurotropic JHM strain of mouse hepatitis virus. These mutations abrogate recognition by T cells harvested from the infected CNS in direct ex vivo cytotoxicity assays. Previous reports have suggested that, in general, an oligoclonal, monospecific T cell response contributes to the selection of CTL escape mutants. Herein, we show that, in MHV-JHM-infected mice, the CD8 T cell response after intraperitoneal infection is polyclonal and diverse. This diverse response was shown to include both polyclonal and oligoclonal components. The polyclonal data were shown to fit a logarithmic distribution. With regard to specificity, we used a panel of peptide analogues of epitope S-510-518 and spleen-derived CD8 T cell lines to determine why only a subset of possible mutations was selected in persistently infected mice. At a given position in the epitope, the mutations identified in in vivo isolates were among those that resulted in the greatest loss of recognition. However, not all such mutations were selected, suggesting that additional factors must contribute to selection in vivo. By extrapolation of these results to the persistently infected CNS, they suggest that the selection of CTL escape mutants requires the presence of a monospecific T cell response but also show that this response need not be oligoclonal. (+info)Induction of Ig light chain gene rearrangement in heavy chain-deficient B cells by activated Ras. (5/3058)
During B cell development, rearrangement and expression of Ig heavy chain (HC) genes promote development and expansion of pre-B cells accompanied by the onset of Ig light chain (LC) variable region gene assembly. To elucidate the signaling pathways that control these events, we have tested the ability of activated Ras expression to promote B cell differentiation to the stage of LC gene rearrangement in the absence of Ig HC gene expression. For this purpose, we introduced an activated Ras expression construct into JH-deleted embryonic stem cells that lack the ability to assemble HC variable region genes and assayed differentiation potential by recombination activating gene (RAG) 2-deficient blastocyst complementation. We found that activated Ras expression induces the progression of B lineage cells beyond the developmental checkpoint ordinarily controlled by mu HC. Such Ras/JH-deleted B cells accumulate in the periphery but continue to express markers associated with precursor B cells including RAG gene products. These peripheral Ras/JH-deleted B cell populations show extensive Ig LC gene rearrangement but maintain an extent of kappa LC gene rearrangement and a preference for kappa over lambda LC gene rearrangement similar to that of wild-type B cells. We discuss these findings in the context of potential mechanisms that may regulate Ig LC gene rearrangement. (+info)Predominant VH genes expressed in innate antibodies are associated with distinctive antigen-binding sites. (6/3058)
Antibodies to phosphatidylcholine (PtC), a common constituent of mammalian and bacterial cell membranes, represent a large proportion of the natural antibody repertoire in mice. Previous studies of several mouse strains (e.g., C57BL/6) have shown that anti-PtC antibodies are mainly encoded by the VH11 and VH12 immunoglobulin heavy chain variable region gene families. We show here, however, that VH11 and VH12 encode only a small proportion of the anti-PtC antibodies in BALB/c mice. Instead, VHQ52-encoded antibodies predominate in this strain. In addition, two-thirds of the cells expressing VHQ52 family genes use a single gene (which, interestingly, has been previously shown to predominate in the anti-oxazolone response). We also show here that in anti-PtC antibodies from all strains, the distinctive antigen-binding sites associated with VHQ52 differ substantially from those associated with VH11 and VH12. That is, VHQ52-containing transcripts preferentially use the joining region JH4 rather than JH1 and exhibit more diverse complementarity-determining region 3 (CDR3) junctions with more N-region nucleotide additions at the gene segment junctions. Thus, the VH gene family that predominates in the anti-PtC repertoire differs among mouse strains, whereas the distinctive VHDJH rearrangements (CDR3, JH) associated with each VH gene family are similar in all strains. We discuss these findings in the context of a recent hypothesis suggesting that CDR3 structure, independent of VH framework, is sufficient to define the specificity of an antibody. (+info)Evidence of T cell receptor beta-chain patterns in inflammatory and noninflammatory bowel disease states. (7/3058)
T cell activation, as defined by expression of relevant cell surface molecules, such as the interleukin-2 receptor (CD25), is increased in many chronic relapsing diseases, including inflammatory bowel disease (IBD). These T cells are generally activated through contact of their clonotypic T cell receptor (TCR) with a peptide antigen presented by a major histocompatibility complex molecule. One of the putative antigenic contact sites for the TCR is the third complementarity determining region (CDR3) of the TCR beta-chain variable region (TCRBV). Therefore, analysis of the TCRBV CDR3 provides insight into the diversity of antigens encountered by a given T cell population. This study evaluated the TCRBV CDR3 usage of the activated intestinal lymphocytes from human subjects with IBD, diverticulitis (inflammatory control), and a normal tissue control. Public patterns, as demonstrated by shared TCRBV CDR3 amino acid sequences of activated intestinal T cell subpopulations, were observed. In particular, a public pattern of TCRBV22, a conserved valine in the fifth position, and use of TCRBJ2S1 or TCRBJ2S5 was present in three of four Crohn's disease subjects while not present in the ulcerative colitis subjects. However, the private patterns of TCRBV CDR3 region amino acid sequences were far more striking and easily demonstrated in all individuals studied, including a normal noninflammatory control. Thus we conclude that selective antigenic pressures are prevalent among an individual's activated intestinal lymphocytes. (+info)Plasma cell development in synovial germinal centers in patients with rheumatoid and reactive arthritis. (8/3058)
Plasma cells are found surrounding the inflammatory infiltrates of macrophages, T, and B cells in the synovial tissue of patients with rheumatoid and reactive arthritis. This characteristic arrangement suggests that in the synovial tissue CD20+ B cells differentiate into plasma cells. To examine clonal relationships, we have used micromanipulation to separately isolate CD20+ B cells and plasma cells from single infiltrates. DNA was extracted, and from both populations the VH/VL gene repertoires was determined. The data show that in the inflamed synovial tissue activated B cells are clonally expanded. During proliferation in the network of follicular dendritic cells, V gene variants are generated by the hypermutation mechanism. Surprisingly, we do not find identical rearrangements between CD20+ B cells and plasma cells. Nevertheless, the finding of clonally related plasma cells within single infiltrates suggests that these cells underwent terminal differentiation in the synovial tissue. These results indicate that B cell differentiation in the synovial tissue is a dynamic process. Whereas CD20+ B cells may turnover rapidly, plasma cells may well be long lived and thus accumulate in the synovial tissue. The analysis of individual B cells recovered from synovial tissue opens a new way to determine the specificity of those cells that take part in the local immune reaction. This will provide new insights into the pathogenesis of chronic inflammatory diseases like rheumatoid or reactive arthritis. (+info)The Immunoglobulin (Ig) variable region is the antigen-binding part of an antibody, which is highly variable in its amino acid sequence and therefore specific to a particular epitope (the site on an antigen that is recognized by the antigen-binding site of an antibody). This variability is generated during the process of V(D)J recombination in the maturation of B cells, allowing for a diverse repertoire of antibodies to be produced and recognizing a wide range of potential pathogens.
The variable region is composed of several sub-regions including:
1. The heavy chain variable region (VH)
2. The light chain variable region (VL)
3. The heavy chain joining region (JH)
4. The light chain joining region (JL)
These regions are further divided into framework regions and complementarity-determining regions (CDRs). The CDRs, particularly CDR3, contain the most variability and are primarily responsible for antigen recognition.
Immunoglobulin heavy chains are proteins that make up the framework of antibodies, which are Y-shaped immune proteins. These heavy chains, along with light chains, form the antigen-binding sites of an antibody, which recognize and bind to specific foreign substances (antigens) in order to neutralize or remove them from the body.
The heavy chain is composed of a variable region, which contains the antigen-binding site, and constant regions that determine the class and function of the antibody. There are five classes of immunoglobulins (IgA, IgD, IgE, IgG, and IgM) that differ in their heavy chain constant regions and therefore have different functions in the immune response.
Immunoglobulin heavy chains are synthesized by B cells, a type of white blood cell involved in the adaptive immune response. The genetic rearrangement of immunoglobulin heavy chain genes during B cell development results in the production of a vast array of different antibodies with unique antigen-binding sites, allowing for the recognition and elimination of a wide variety of pathogens.
Somatic hypermutation is a process that occurs in the immune system, specifically within B cells, which are a type of white blood cell responsible for producing antibodies. This process involves the introduction of point mutations into the immunoglobulin (Ig) genes, which encode for the variable regions of antibodies.
Somatic hypermutation occurs in the germinal centers of lymphoid follicles in response to antigen stimulation. The activation-induced cytidine deaminase (AID) enzyme is responsible for initiating this process by deaminating cytosines to uracils in the Ig genes. This leads to the introduction of point mutations during DNA replication and repair, which can result in changes to the antibody's binding affinity for the antigen.
The somatic hypermutation process allows for the selection of B cells with higher affinity antibodies that can better recognize and neutralize pathogens. This is an important mechanism for the development of humoral immunity and the generation of long-lived memory B cells. However, excessive or aberrant somatic hypermutation can also contribute to the development of certain types of B cell malignancies, such as lymphomas and leukemias.
Immunoglobulins (Igs), also known as antibodies, are proteins produced by the immune system to recognize and neutralize foreign substances such as pathogens or toxins. They are composed of four polypeptide chains: two heavy chains and two light chains, which are held together by disulfide bonds. The variable regions of the heavy and light chains contain loops that form the antigen-binding site, allowing each Ig molecule to recognize a specific epitope (antigenic determinant) on an antigen.
Genes encoding immunoglobulins are located on chromosome 14 (light chain genes) and chromosomes 22 and 2 (heavy chain genes). The diversity of the immune system is generated through a process called V(D)J recombination, where variable (V), diversity (D), and joining (J) gene segments are randomly selected and assembled to form the variable regions of the heavy and light chains. This results in an enormous number of possible combinations, allowing the immune system to recognize and respond to a vast array of potential threats.
There are five classes of immunoglobulins: IgA, IgD, IgE, IgG, and IgM, each with distinct functions and structures. For example, IgG is the most abundant class in serum and provides long-term protection against pathogens, while IgA is found on mucosal surfaces and helps prevent the entry of pathogens into the body.
Immunoglobulin light chains are the smaller protein subunits of an immunoglobulin, also known as an antibody. They are composed of two polypeptide chains, called kappa (κ) and lambda (λ), which are produced by B cells during the immune response. Each immunoglobulin molecule contains either two kappa or two lambda light chains, in association with two heavy chains.
Light chains play a crucial role in the antigen-binding site of an antibody, where they contribute to the specificity and affinity of the interaction between the antibody and its target antigen. In addition to their role in immune function, abnormal production or accumulation of light chains can lead to various diseases, such as multiple myeloma and amyloidosis.
A binding site on an antibody refers to the specific region on the surface of the antibody molecule that can recognize and bind to a specific antigen. Antibodies are proteins produced by the immune system in response to the presence of foreign substances called antigens. They have two main functions: to neutralize the harmful effects of antigens and to help eliminate them from the body.
The binding site of an antibody is located at the tips of its Y-shaped structure, formed by the variable regions of the heavy and light chains of the antibody molecule. These regions contain unique amino acid sequences that determine the specificity of the antibody for a particular antigen. The binding site can recognize and bind to a specific epitope or region on the antigen, forming an antigen-antibody complex.
The binding between the antibody and antigen is highly specific and depends on non-covalent interactions such as hydrogen bonds, van der Waals forces, and electrostatic attractions. This interaction plays a crucial role in the immune response, as it allows the immune system to recognize and eliminate pathogens and other foreign substances from the body.
B-lymphocytes, also known as B-cells, are a type of white blood cell that plays a key role in the immune system's response to infection. They are responsible for producing antibodies, which are proteins that help to neutralize or destroy pathogens such as bacteria and viruses.
When a B-lymphocyte encounters a pathogen, it becomes activated and begins to divide and differentiate into plasma cells, which produce and secrete large amounts of antibodies specific to the antigens on the surface of the pathogen. These antibodies bind to the pathogen, marking it for destruction by other immune cells such as neutrophils and macrophages.
B-lymphocytes also have a role in presenting antigens to T-lymphocytes, another type of white blood cell involved in the immune response. This helps to stimulate the activation and proliferation of T-lymphocytes, which can then go on to destroy infected cells or help to coordinate the overall immune response.
Overall, B-lymphocytes are an essential part of the adaptive immune system, providing long-lasting immunity to previously encountered pathogens and helping to protect against future infections.
A hybridoma is a type of hybrid cell that is created in a laboratory by fusing a cancer cell (usually a B cell) with a normal immune cell. The resulting hybrid cell combines the ability of the cancer cell to grow and divide indefinitely with the ability of the immune cell to produce antibodies, which are proteins that help the body fight infection.
Hybridomas are commonly used to produce monoclonal antibodies, which are identical copies of a single antibody produced by a single clone of cells. These antibodies can be used for a variety of purposes, including diagnostic tests and treatments for diseases such as cancer and autoimmune disorders.
To create hybridomas, B cells are first isolated from the spleen or blood of an animal that has been immunized with a specific antigen (a substance that triggers an immune response). The B cells are then fused with cancer cells using a chemical agent such as polyethylene glycol. The resulting hybrid cells are called hybridomas and are grown in culture medium, where they can be selected for their ability to produce antibodies specific to the antigen of interest. These antibody-producing hybridomas can then be cloned to produce large quantities of monoclonal antibodies.
A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.
Immunoglobulins (Igs), also known as antibodies, are glycoprotein molecules produced by the immune system's B cells in response to the presence of foreign substances, such as bacteria, viruses, and toxins. These Y-shaped proteins play a crucial role in identifying and neutralizing pathogens and other antigens, thereby protecting the body against infection and disease.
Immunoglobulins are composed of four polypeptide chains: two identical heavy chains and two identical light chains, held together by disulfide bonds. The variable regions of these chains form the antigen-binding sites, which recognize and bind to specific epitopes on antigens. Based on their heavy chain type, immunoglobulins are classified into five main isotypes or classes: IgA, IgD, IgE, IgG, and IgM. Each class has distinct functions in the immune response, such as providing protection in different body fluids and tissues, mediating hypersensitivity reactions, and aiding in the development of immunological memory.
In medical settings, immunoglobulins can be administered therapeutically to provide passive immunity against certain diseases or to treat immune deficiencies, autoimmune disorders, and other conditions that may benefit from immunomodulation.
Immunoglobulin G (IgG) is a type of antibody, which is a protective protein produced by the immune system in response to foreign substances like bacteria or viruses. IgG is the most abundant type of antibody in human blood, making up about 75-80% of all antibodies. It is found in all body fluids and plays a crucial role in fighting infections caused by bacteria, viruses, and toxins.
IgG has several important functions:
1. Neutralization: IgG can bind to the surface of bacteria or viruses, preventing them from attaching to and infecting human cells.
2. Opsonization: IgG coats the surface of pathogens, making them more recognizable and easier for immune cells like neutrophils and macrophages to phagocytose (engulf and destroy) them.
3. Complement activation: IgG can activate the complement system, a group of proteins that work together to help eliminate pathogens from the body. Activation of the complement system leads to the formation of the membrane attack complex, which creates holes in the cell membranes of bacteria, leading to their lysis (destruction).
4. Antibody-dependent cellular cytotoxicity (ADCC): IgG can bind to immune cells like natural killer (NK) cells and trigger them to release substances that cause target cells (such as virus-infected or cancerous cells) to undergo apoptosis (programmed cell death).
5. Immune complex formation: IgG can form immune complexes with antigens, which can then be removed from the body through various mechanisms, such as phagocytosis by immune cells or excretion in urine.
IgG is a critical component of adaptive immunity and provides long-lasting protection against reinfection with many pathogens. It has four subclasses (IgG1, IgG2, IgG3, and IgG4) that differ in their structure, function, and distribution in the body.
Immunoglobulin kappa-chains are one of the two types of light chains (the other being lambda-chains) that make up an immunoglobulin molecule, also known as an antibody. These light chains combine with heavy chains to form the antigen-binding site of an antibody, which is responsible for recognizing and binding to specific antigens or foreign substances in the body.
Kappa-chains contain a variable region that differs between different antibodies and contributes to the diversity of the immune system's response to various antigens. They also have a constant region, which is consistent across all kappa-chains. Approximately 60% of all human antibodies contain kappa-chains, while the remaining 40% contain lambda-chains. The relative proportions of kappa and lambda chains can be used in diagnostic tests to identify clonal expansions of B cells, which may indicate a malignancy such as multiple myeloma or lymphoma.
Chronic lymphocytic leukemia (CLL) is a type of cancer that starts from cells that become certain white blood cells (called lymphocytes) in the bone marrow. The cancer (leukemia) cells start in the bone marrow but then go into the blood.
In CLL, the leukemia cells often build up slowly. Many people don't have any symptoms for at least a few years. But over time, the cells can spread to other parts of the body, including the lymph nodes, liver, and spleen.
The "B-cell" part of the name refers to the fact that the cancer starts in a type of white blood cell called a B lymphocyte or B cell. The "chronic" part means that this leukemia usually progresses more slowly than other types of leukemia.
It's important to note that chronic lymphocytic leukemia is different from chronic myelogenous leukemia (CML). Although both are cancers of the white blood cells, they start in different types of white blood cells and progress differently.
'Gene rearrangement in B-lymphocytes, heavy chain' refers to the biological process that occurs during the development of B-lymphocytes (a type of white blood cell) in the bone marrow. This process involves the rearrangement of genetic material on chromosome 14, specifically within the immunoglobulin heavy chain gene locus.
During B-cell maturation, the variable region of the heavy chain gene is assembled from several gene segments, including the variable (V), diversity (D), and joining (J) segments. Through a series of genetic recombination events, these segments are randomly selected and joined together to form a unique V(D)J exon that encodes the variable region of the immunoglobulin heavy chain protein.
This gene rearrangement process allows for the generation of a diverse repertoire of antibodies with different specificities, enabling B-lymphocytes to recognize and respond to a wide range of foreign antigens. However, if errors occur during this process, it can lead to the production of autoantibodies that target the body's own cells and tissues, contributing to the development of certain immune disorders such as autoimmune diseases.
Immunoglobulin heavy chains (IgH) are proteins that make up the framework of antibodies, which are crucial components of the adaptive immune system. These heavy chains are produced by B cells and plasma cells, and they contain variable regions that can bind to specific antigens, as well as constant regions that determine the effector functions of the antibody.
The genes that encode for immunoglobulin heavy chains are located on chromosome 14 in humans, within a region known as the IgH locus. These genes undergo a complex process of rearrangement during B cell development, whereby different gene segments (V, D, and J) are joined together to create a unique variable region that can recognize a specific antigen. This process of gene rearrangement is critical for the diversity and specificity of the antibody response.
Therefore, the medical definition of 'Genes, Immunoglobulin Heavy Chain' refers to the set of genetic elements that encode for the immunoglobulin heavy chain proteins, and their complex process of rearrangement during B cell development.
B-lymphocyte gene rearrangement is a fundamental biological process that occurs during the development of B-lymphocytes (also known as B cells), which are a type of white blood cell responsible for producing antibodies to help fight infections. This process involves the rearrangement of genetic material within the B-lymphocyte's immunoglobulin genes, specifically the heavy chain (IgH) and light chain (IgL) genes, to create a diverse repertoire of antibodies with unique specificities.
During B-lymphocyte gene rearrangement, large segments of DNA are cut, deleted, or inverted, and then rejoined to form a functional IgH or IgL gene that encodes an antigen-binding site on the antibody molecule. The process occurs in two main steps:
1. Variable (V), diversity (D), and joining (J) gene segments are rearranged to form the heavy chain gene, which is located on chromosome 14. This results in a vast array of possible combinations, allowing for the generation of a diverse set of antibody molecules.
2. A separate variable (V) and joining (J) gene segment rearrangement occurs to form the light chain gene, which can be either kappa or lambda type, located on chromosomes 2 and 22, respectively.
Once the heavy and light chain genes are successfully rearranged, they are transcribed into mRNA and translated into immunoglobulin proteins, forming a functional antibody molecule. If the initial gene rearrangement fails to produce a functional antibody, additional attempts at rearrangement can occur, involving different combinations of V, D, and J segments or the use of alternative reading frames.
Errors in B-lymphocyte gene rearrangement can lead to various genetic disorders, such as lymphomas and leukemias, due to the production of aberrant antibodies or uncontrolled cell growth.
Immunoglobulin M (IgM) is a type of antibody that is primarily found in the blood and lymph fluid. It is the first antibody to be produced in response to an initial exposure to an antigen, making it an important part of the body's primary immune response. IgM antibodies are large molecules that are composed of five basic units, giving them a pentameric structure. They are primarily found on the surface of B cells as membrane-bound immunoglobulins (mlgM), where they function as receptors for antigens. Once an mlgM receptor binds to an antigen, it triggers the activation and differentiation of the B cell into a plasma cell that produces and secretes large amounts of soluble IgM antibodies.
IgM antibodies are particularly effective at agglutination (clumping) and complement activation, which makes them important in the early stages of an immune response to help clear pathogens from the bloodstream. However, they are not as stable or long-lived as other types of antibodies, such as IgG, and their levels tend to decline after the initial immune response has occurred.
In summary, Immunoglobulin M (IgM) is a type of antibody that plays a crucial role in the primary immune response to antigens by agglutination and complement activation. It is primarily found in the blood and lymph fluid, and it is produced by B cells after they are activated by an antigen.
Immunoglobulin A (IgA) is a type of antibody that plays a crucial role in the immune function of the human body. It is primarily found in external secretions, such as saliva, tears, breast milk, and sweat, as well as in mucous membranes lining the respiratory and gastrointestinal tracts. IgA exists in two forms: a monomeric form found in serum and a polymeric form found in secretions.
The primary function of IgA is to provide immune protection at mucosal surfaces, which are exposed to various environmental antigens, such as bacteria, viruses, parasites, and allergens. By doing so, it helps prevent the entry and colonization of pathogens into the body, reducing the risk of infections and inflammation.
IgA functions by binding to antigens present on the surface of pathogens or allergens, forming immune complexes that can neutralize their activity. These complexes are then transported across the epithelial cells lining mucosal surfaces and released into the lumen, where they prevent the adherence and invasion of pathogens.
In summary, Immunoglobulin A (IgA) is a vital antibody that provides immune defense at mucosal surfaces by neutralizing and preventing the entry of harmful antigens into the body.
Immunoglobulin idiotypes refer to the unique antigenic determinants found on the variable regions of an immunoglobulin (antibody) molecule. These determinants are specific to each individual antibody and can be used to distinguish between different antibodies produced by a single individual or between antibodies produced by different individuals.
The variable region of an antibody is responsible for recognizing and binding to a specific antigen. The amino acid sequence in this region varies between different antibodies, and it is these variations that give rise to the unique idiotypes. Idiotypes can be used as markers to study the immune response, including the clonal selection and affinity maturation of B cells during an immune response.
Immunoglobulin idiotypes are also important in the development of monoclonal antibodies for therapeutic use. By identifying and isolating a specific antibody with the desired idiotype, it is possible to produce large quantities of identical antibodies that can be used to treat various diseases, including cancer and autoimmune disorders.
"Gene rearrangement" is a process that involves the alteration of the order, orientation, or copy number of genes or gene segments within an organism's genome. This natural mechanism plays a crucial role in generating diversity and specificity in the immune system, particularly in vertebrates.
In the context of the immune system, gene rearrangement occurs during the development of B-cells and T-cells, which are responsible for adaptive immunity. The process involves breaking and rejoining DNA segments that encode antigen recognition sites, resulting in a unique combination of gene segments and creating a vast array of possible antigen receptors.
There are two main types of gene rearrangement:
1. V(D)J recombination: This process occurs in both B-cells and T-cells. It involves the recombination of variable (V), diversity (D), and joining (J) gene segments to form a functional antigen receptor gene. In humans, there are multiple copies of V, D, and J segments for each antigen receptor gene, allowing for a vast number of possible combinations.
2. Class switch recombination: This process occurs only in mature B-cells after antigen exposure. It involves the replacement of the constant (C) region of the immunoglobulin heavy chain gene with another C region, resulting in the production of different isotypes of antibodies (IgG, IgA, or IgE) that have distinct effector functions while maintaining the same antigen specificity.
These processes contribute to the generation of a diverse repertoire of antigen receptors, allowing the immune system to recognize and respond effectively to a wide range of pathogens.
Cytidine deaminase is an enzyme that catalyzes the removal of an amino group from cytidine, converting it to uridine. This reaction is part of the process of RNA degradation and also plays a role in the immune response to viral infections.
Cytidine deaminase can be found in various organisms, including bacteria, humans, and other mammals. In humans, cytidine deaminase is encoded by the APOBEC3 gene family, which consists of several different enzymes that have distinct functions and expression patterns. Some members of this gene family are involved in the restriction of retroviruses, such as HIV-1, while others play a role in the regulation of endogenous retroelements and the modification of cellular RNA.
Mutations in cytidine deaminase genes have been associated with various diseases, including cancer and autoimmune disorders. For example, mutations in the APOBEC3B gene have been linked to an increased risk of breast cancer, while mutations in other members of the APOBEC3 family have been implicated in the development of lymphoma and other malignancies. Additionally, aberrant expression of cytidine deaminase enzymes has been observed in some autoimmune diseases, such as rheumatoid arthritis and systemic lupus erythematosus, suggesting a potential role for these enzymes in the pathogenesis of these conditions.
Complementarity Determining Regions (CDRs) are the portions of an antibody that recognize and bind to a specific antigen. These regions are located in the variable domains of both the heavy and light chains of the antibody molecule. The CDRs are formed by the hypervariable loops within these domains, which have unique sequences that allow them to bind specifically to a particular epitope on an antigen. There are three CDRs in each variable domain, for a total of six CDRs per antibody. The CDRs are primarily responsible for the antigen-binding specificity and affinity of an antibody.
A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.
Antibody specificity refers to the ability of an antibody to bind to a specific epitope or antigenic determinant on an antigen. Each antibody has a unique structure that allows it to recognize and bind to a specific region of an antigen, typically a small portion of the antigen's surface made up of amino acids or sugar residues. This highly specific binding is mediated by the variable regions of the antibody's heavy and light chains, which form a pocket that recognizes and binds to the epitope.
The specificity of an antibody is determined by its unique complementarity-determining regions (CDRs), which are loops of amino acids located in the variable domains of both the heavy and light chains. The CDRs form a binding site that recognizes and interacts with the epitope on the antigen. The precise fit between the antibody's binding site and the epitope is critical for specificity, as even small changes in the structure of either can prevent binding.
Antibody specificity is important in immune responses because it allows the immune system to distinguish between self and non-self antigens. This helps to prevent autoimmune reactions where the immune system attacks the body's own cells and tissues. Antibody specificity also plays a crucial role in diagnostic tests, such as ELISA assays, where antibodies are used to detect the presence of specific antigens in biological samples.
Monoclonal antibodies are a type of antibody that are identical because they are produced by a single clone of cells. They are laboratory-produced molecules that act like human antibodies in the immune system. They can be designed to attach to specific proteins found on the surface of cancer cells, making them useful for targeting and treating cancer. Monoclonal antibodies can also be used as a therapy for other diseases, such as autoimmune disorders and inflammatory conditions.
Monoclonal antibodies are produced by fusing a single type of immune cell, called a B cell, with a tumor cell to create a hybrid cell, or hybridoma. This hybrid cell is then able to replicate indefinitely, producing a large number of identical copies of the original antibody. These antibodies can be further modified and engineered to enhance their ability to bind to specific targets, increase their stability, and improve their effectiveness as therapeutic agents.
Monoclonal antibodies have several mechanisms of action in cancer therapy. They can directly kill cancer cells by binding to them and triggering an immune response. They can also block the signals that promote cancer growth and survival. Additionally, monoclonal antibodies can be used to deliver drugs or radiation directly to cancer cells, increasing the effectiveness of these treatments while minimizing their side effects on healthy tissues.
Monoclonal antibodies have become an important tool in modern medicine, with several approved for use in cancer therapy and other diseases. They are continuing to be studied and developed as a promising approach to treating a wide range of medical conditions.
A clone is a group of cells that are genetically identical to each other because they are derived from a common ancestor cell through processes such as mitosis or asexual reproduction. Therefore, the term "clone cells" refers to a population of cells that are genetic copies of a single parent cell.
In the context of laboratory research, cells can be cloned by isolating a single cell and allowing it to divide in culture, creating a population of genetically identical cells. This is useful for studying the behavior and characteristics of individual cell types, as well as for generating large quantities of cells for use in experiments.
It's important to note that while clone cells are genetically identical, they may still exhibit differences in their phenotype (physical traits) due to epigenetic factors or environmental influences.
Intravenous Immunoglobulins (IVIG) are a preparation of antibodies, specifically immunoglobulins, that are derived from the plasma of healthy donors. They are administered intravenously to provide passive immunity and help boost the immune system's response in individuals with weakened or compromised immune systems. IVIG can be used for various medical conditions such as primary immunodeficiency disorders, secondary immunodeficiencies, autoimmune diseases, and some infectious diseases. The administration of IVIG can help prevent infections, reduce the severity and frequency of infections, and manage the symptoms of certain autoimmune disorders. It is important to note that while IVIG provides temporary immunity, it does not replace a person's own immune system.
Polymerase Chain Reaction (PCR) is a laboratory technique used to amplify specific regions of DNA. It enables the production of thousands to millions of copies of a particular DNA sequence in a rapid and efficient manner, making it an essential tool in various fields such as molecular biology, medical diagnostics, forensic science, and research.
The PCR process involves repeated cycles of heating and cooling to separate the DNA strands, allow primers (short sequences of single-stranded DNA) to attach to the target regions, and extend these primers using an enzyme called Taq polymerase, resulting in the exponential amplification of the desired DNA segment.
In a medical context, PCR is often used for detecting and quantifying specific pathogens (viruses, bacteria, fungi, or parasites) in clinical samples, identifying genetic mutations or polymorphisms associated with diseases, monitoring disease progression, and evaluating treatment effectiveness.
Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:
1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.
Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.
Immunoglobulin constant regions are the invariant portions of antibody molecules (immunoglobulins) that are identical in all antibodies of the same isotype. These regions are responsible for effector functions such as complement activation, binding to Fc receptors, and initiating immune responses. They are composed of amino acid sequences that remain unchanged during antigen-driven somatic hypermutation, allowing them to interact with various components of the immune system. The constant regions are found in the heavy chains (CH) and light chains (CL) of an immunoglobulin molecule. In contrast, the variable regions are responsible for recognizing and binding to specific antigens.
Immunoglobulin lambda-chains (Igλ) are one type of light chain found in the immunoglobulins, also known as antibodies. Antibodies are proteins that play a crucial role in the immune system's response to foreign substances, such as bacteria and viruses.
Immunoglobulins are composed of two heavy chains and two light chains, which are interconnected by disulfide bonds. There are two types of light chains: kappa (κ) and lambda (λ). Igλ chains are one type of light chain that can be found in association with heavy chains to form functional antibodies.
Igλ chains contain a variable region, which is responsible for recognizing and binding to specific antigens, and a constant region, which determines the class of the immunoglobulin (e.g., IgA, IgD, IgE, IgG, or IgM).
In humans, approximately 60% of all antibodies contain Igλ chains, while the remaining 40% contain Igκ chains. The ratio of Igλ to Igκ chains can vary depending on the type of immunoglobulin and its function in the immune response.
Myeloma proteins, also known as monoclonal immunoglobulins or M-proteins, are entire or abnormal immunoglobulin (antibody) molecules produced by a single clone of plasma cells, which are malignant in the case of multiple myeloma and some related disorders. These proteins accumulate in the blood and/or urine and can cause damage to various organs and tissues.
In multiple myeloma, the excessive proliferation of these plasma cells leads to the overproduction of a single type of immunoglobulin or its fragments, which can be detected and quantified in serum and/or urine electrophoresis. The most common types of myeloma proteins are IgG and IgA, followed by light chains (Bence Jones proteins) and, less frequently, IgD and IgM.
The presence and levels of myeloma proteins are important diagnostic markers for multiple myeloma and related disorders, such as monoclonal gammopathy of undetermined significance (MGUS) and Waldenström macroglobulinemia. Regular monitoring of these proteins helps assess the disease's activity, response to treatment, and potential complications like kidney dysfunction or amyloidosis.
Immunoglobulin fragments refer to the smaller protein units that are formed by the digestion or break-down of an intact immunoglobulin, also known as an antibody. Immunoglobulins are large Y-shaped proteins produced by the immune system to identify and neutralize foreign substances such as pathogens or toxins. They consist of two heavy chains and two light chains, held together by disulfide bonds.
The digestion or break-down of an immunoglobulin can occur through enzymatic cleavage, which results in the formation of distinct fragments. The most common immunoglobulin fragments are:
1. Fab (Fragment, antigen binding) fragments: These are formed by the digestion of an intact immunoglobulin using the enzyme papain. Each Fab fragment contains a single antigen-binding site, consisting of a portion of one heavy chain and one light chain. The Fab fragments retain their ability to bind to specific antigens.
2. Fc (Fragment, crystallizable) fragments: These are formed by the digestion of an intact immunoglobulin using the enzyme pepsin or through the natural breakdown process in the body. The Fc fragment contains the constant region of both heavy chains and is responsible for effector functions such as complement activation, binding to Fc receptors on immune cells, and antibody-dependent cellular cytotoxicity (ADCC).
These immunoglobulin fragments play crucial roles in various immune responses and diagnostic applications. For example, Fab fragments can be used in immunoassays for the detection of specific antigens, while Fc fragments can mediate effector functions that help eliminate pathogens or damaged cells from the body.
Deoxyribonucleic acid (DNA) is the genetic material present in the cells of organisms where it is responsible for the storage and transmission of hereditary information. DNA is a long molecule that consists of two strands coiled together to form a double helix. Each strand is made up of a series of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - that are linked together by phosphate and sugar groups. The sequence of these bases along the length of the molecule encodes genetic information, with A always pairing with T and C always pairing with G. This base-pairing allows for the replication and transcription of DNA, which are essential processes in the functioning and reproduction of all living organisms.
BALB/c is an inbred strain of laboratory mouse that is widely used in biomedical research. The strain was developed at the Institute of Cancer Research in London by Henry Baldwin and his colleagues in the 1920s, and it has since become one of the most commonly used inbred strains in the world.
BALB/c mice are characterized by their black coat color, which is determined by a recessive allele at the tyrosinase locus. They are also known for their docile and friendly temperament, making them easy to handle and work with in the laboratory.
One of the key features of BALB/c mice that makes them useful for research is their susceptibility to certain types of tumors and immune responses. For example, they are highly susceptible to developing mammary tumors, which can be induced by chemical carcinogens or viral infection. They also have a strong Th2-biased immune response, which makes them useful models for studying allergic diseases and asthma.
BALB/c mice are also commonly used in studies of genetics, neuroscience, behavior, and infectious diseases. Because they are an inbred strain, they have a uniform genetic background, which makes it easier to control for genetic factors in experiments. Additionally, because they have been bred in the laboratory for many generations, they are highly standardized and reproducible, making them ideal subjects for scientific research.
Immunoglobulin mu-chains (IgM) are a type of heavy chain found in immunoglobulins, also known as antibodies. IgM is the first antibody to be produced in response to an initial exposure to an antigen and plays a crucial role in the early stages of the immune response.
IgM antibodies are composed of four monomeric units, each consisting of two heavy chains and two light chains. The heavy chains in IgM are called mu-chains, which have a molecular weight of approximately 72 kDa. Each mu-chain contains five domains: one variable (V) domain at the N-terminus, four constant (C) domains (Cμ1-4), and a membrane-spanning region followed by a short cytoplasmic tail.
IgM antibodies are primarily found on the surface of B cells as part of the B cell receptor (BCR). When a B cell encounters an antigen, the BCR binds to it, triggering a series of intracellular signaling events that lead to B cell activation and differentiation into plasma cells. In response to activation, the B cell begins to secrete IgM antibodies into the bloodstream.
IgM antibodies have several unique features that make them effective in the early stages of an immune response. They are highly efficient at agglutination, or clumping together, of pathogens and antigens, which helps to neutralize them. IgM antibodies also activate the complement system, a group of proteins that work together to destroy pathogens.
Overall, Immunoglobulin mu-chains are an essential component of the immune system, providing early protection against pathogens and initiating the adaptive immune response.
Immunoglobulin E (IgE) is a type of antibody that plays a key role in the immune response to parasitic infections and allergies. It is produced by B cells in response to stimulation by antigens, such as pollen, pet dander, or certain foods. Once produced, IgE binds to receptors on the surface of mast cells and basophils, which are immune cells found in tissues and blood respectively. When an individual with IgE antibodies encounters the allergen again, the cross-linking of IgE molecules bound to the FcεRI receptor triggers the release of mediators such as histamine, leukotrienes, prostaglandins, and various cytokines from these cells. These mediators cause the symptoms of an allergic reaction, such as itching, swelling, and redness. IgE also plays a role in protecting against certain parasitic infections by activating eosinophils, which can kill the parasites.
In summary, Immunoglobulin E (IgE) is a type of antibody that plays a crucial role in the immune response to allergens and parasitic infections, it binds to receptors on the surface of mast cells and basophils, when an individual with IgE antibodies encounters the allergen again, it triggers the release of mediators from these cells causing the symptoms of an allergic reaction.
Immunoglobulins, also known as antibodies, are proteins produced by the immune system to recognize and neutralize foreign substances like pathogens or antigens. The term "immunoglobulin isotypes" refers to the different classes of immunoglobulins that share a similar structure but have distinct functions and properties.
There are five main isotypes of immunoglobulins in humans, namely IgA, IgD, IgE, IgG, and IgM. Each isotype has a unique heavy chain constant region (CH) that determines its effector functions, such as binding to Fc receptors, complement activation, or protection against pathogens.
IgA is primarily found in external secretions like tears, saliva, and breast milk, providing localized immunity at mucosal surfaces. IgD is expressed on the surface of B cells and plays a role in their activation and differentiation. IgE is associated with allergic responses and binds to mast cells and basophils, triggering the release of histamine and other mediators of inflammation.
IgG is the most abundant isotype in serum and has several subclasses (IgG1, IgG2, IgG3, and IgG4) that differ in their effector functions. IgG can cross the placenta, providing passive immunity to the fetus. IgM is the first antibody produced during an immune response and is primarily found in the bloodstream, where it forms large pentameric complexes that are effective at agglutination and complement activation.
Overall, immunoglobulin isotypes play a crucial role in the adaptive immune response, providing specific and diverse mechanisms for recognizing and neutralizing foreign substances.
Immunoglobulin A (IgA), Secretory is a type of antibody that plays a crucial role in the immune function of mucous membranes. These membranes line various body openings, such as the respiratory and gastrointestinal tracts, and serve to protect the body from potential pathogens by producing mucus.
Secretory IgA (SIgA) is the primary immunoglobulin found in secretions of the mucous membranes, and it is produced by a special type of immune cell called plasma cells located in the lamina propria, a layer of tissue beneath the epithelial cells that line the mucosal surfaces.
SIgA exists as a dimer, consisting of two IgA molecules linked together by a protein called the J chain. This complex is then transported across the epithelial cell layer to the luminal surface, where it becomes associated with another protein called the secretory component (SC). The SC protects the SIgA from degradation by enzymes and helps it maintain its function in the harsh environment of the mucosal surfaces.
SIgA functions by preventing the attachment and entry of pathogens into the body, thereby neutralizing their infectivity. It can also agglutinate (clump together) microorganisms, making them more susceptible to removal by mucociliary clearance or peristalsis. Furthermore, SIgA can modulate immune responses and contribute to the development of oral tolerance, which is important for maintaining immune homeostasis in the gut.
Immunoglobulin D (IgD) is a type of antibody that is present in the blood and other bodily fluids. It is one of the five classes of immunoglobulins (IgA, IgD, IgE, IgG, and IgM) found in humans and plays a role in the immune response.
IgD is produced by B cells, a type of white blood cell that is responsible for producing antibodies. It is primarily found on the surface of mature B cells, where it functions as a receptor for antigens (foreign substances that trigger an immune response). When an antigen binds to IgD on the surface of a B cell, it activates the B cell and stimulates it to produce and secrete antibodies specific to that antigen.
IgD is found in relatively low concentrations in the blood compared to other immunoglobulins, and its precise functions are not fully understood. However, it is thought to play a role in the regulation of B cell activation and the immune response. Additionally, some research suggests that IgD may have a direct role in protecting against certain types of infections.
It's worth noting that genetic deficiencies in IgD are not typically associated with any significant immunological abnormalities or increased susceptibility to infection.
Immunoglobulin allotypes refer to the genetic variations in the constant region of immunoglobulins (antibodies) that are caused by differences in the amino acid sequences. These variations are determined by specific alleles at polymorphic loci on chromosome 14 and 22, which are inherited in a Mendelian fashion.
Immunoglobulin allotypes can be used as markers for ancestry, immune response, and the identification of tissue types in transplantation. They also play a role in the regulation of the immune response and can affect the affinity and specificity of antibodies.
It's important to note that while immunoglobulin allotypes are inherited and do not change over an individual's lifetime, they should not be confused with immunoglobulin isotypes (IgA, IgD, IgE, IgG, and IgM) which refer to the different classes of antibodies that have distinct structures and functions.
Immunoglobulin J-chains are small protein structures that play a role in the assembly and structure of certain types of antibodies, specifically IgM and IgA. The J-chain is a polypeptide chain that contains multiple cysteine residues, which allow it to form disulfide bonds with the heavy chains of IgM and IgA molecules.
In IgM antibodies, the J-chain helps to link the five identical heavy chain units together to form a pentameric structure. In IgA antibodies, the J-chain links two dimeric structures together to form a tetrameric structure. This polymerization of IgM and IgA molecules is important for their function in the immune system, as it allows them to form large complexes that can effectively agglutinate and neutralize pathogens.
The J-chain is synthesized by a specialized group of B cells called plasma cells, which are responsible for producing and secreting antibodies. Once synthesized, the J-chain is covalently linked to the heavy chains of IgM or IgA molecules during their assembly in the endoplasmic reticulum of the plasma cell.
Overall, the Immunoglobulin J-chain plays a crucial role in the structure and function of certain classes of antibodies, contributing to their ability to effectively combat pathogens and protect the body from infection.
Immunoglobulin (Ig) Fab fragments are the antigen-binding portions of an antibody that result from the digestion of the whole antibody molecule by enzymes such as papain. An antibody, also known as an immunoglobulin, is a Y-shaped protein produced by the immune system to identify and neutralize foreign substances like bacteria, viruses, or toxins. The antibody has two identical antigen-binding sites, located at the tips of the two shorter arms, which can bind specifically to a target antigen.
Fab fragments are formed when an antibody is cleaved by papain, resulting in two Fab fragments and one Fc fragment. Each Fab fragment contains one antigen-binding site, composed of a variable region (Fv) and a constant region (C). The Fv region is responsible for the specificity and affinity of the antigen binding, while the C region contributes to the effector functions of the antibody.
Fab fragments are often used in various medical applications, such as immunodiagnostics and targeted therapies, due to their ability to bind specifically to target antigens without triggering an immune response or other effector functions associated with the Fc region.
A plasmacytoma is a discrete tumor mass that is composed of neoplastic plasma cells, which are a type of white blood cell found in the bone marrow. Plasmacytomas can be solitary (a single tumor) or multiple (many tumors), and they can develop in various locations throughout the body.
Solitary plasmacytoma is a rare cancer that typically affects older adults, and it usually involves a single bone lesion, most commonly found in the vertebrae, ribs, or pelvis. In some cases, solitary plasmacytomas can also occur outside of the bone (extramedullary plasmacytoma), which can affect soft tissues such as the upper respiratory tract, gastrointestinal tract, or skin.
Multiple myeloma is a more common and aggressive cancer that involves multiple plasmacytomas in the bone marrow, leading to the replacement of normal bone marrow cells with malignant plasma cells. This can result in various symptoms such as bone pain, anemia, infections, and kidney damage.
The diagnosis of plasmacytoma typically involves a combination of imaging studies, biopsy, and laboratory tests to assess the extent of the disease and determine the appropriate treatment plan. Treatment options for solitary plasmacytoma may include surgery or radiation therapy, while multiple myeloma is usually treated with chemotherapy, targeted therapy, immunotherapy, and/or stem cell transplantation.
Immunoglobulin Fc fragments are the crystallizable fragment of an antibody that is responsible for effector functions such as engagement with Fc receptors on immune cells, activation of the complement system, and neutralization of toxins. The Fc region is located at the tail end of the Y-shaped immunoglobulin molecule, and it is made up of constant regions of the heavy chains of the antibody.
When an antibody binds to its target antigen, the Fc region can interact with other proteins in the immune system, leading to a variety of responses such as phagocytosis, antibody-dependent cellular cytotoxicity (ADCC), and complement activation. These effector functions help to eliminate pathogens and infected cells from the body.
Immunoglobulin Fc fragments can be produced artificially through enzymatic digestion of intact antibodies, resulting in a fragment that retains the ability to interact with Fc receptors and other proteins involved in immune responses. These fragments have potential therapeutic applications in a variety of diseases, including autoimmune disorders, inflammatory conditions, and cancer.
Immunoglobulin G (IgG) gamma chains are the heavy, constant region proteins found in IgG immunoglobulins, which are a type of antibody. These gamma chains are composed of four subunits - two heavy chains and two light chains - and play a crucial role in the immune response by recognizing and binding to specific antigens, such as pathogens or foreign substances.
IgG is the most abundant type of antibody in human serum and provides long-term immunity against bacterial and viral infections. The gamma chains contain a region that binds to Fc receptors found on various immune cells, which facilitates the destruction of pathogens or foreign substances. Additionally, IgG can cross the placenta, providing passive immunity to the fetus.
Abnormalities in the production or function of IgG gamma chains can lead to various immunodeficiency disorders, such as X-linked agammaglobulinemia, which is characterized by a lack of functional B cells and low levels of IgG antibodies.
The Immunoglobulin Joining Region (IgJ or J chain) is a polypeptide chain that is a component of certain immunoglobulins, specifically IgM and IgA. The J chain plays a crucial role in the polymerization of these immunoglobulins, allowing them to form higher-order structures such as pentamers (in the case of IgM) or dimers (in the case of IgA). This polymerization is important for the functioning of these immunoglobulins in the immune response. The J chain contains multiple cysteine residues that form disulfide bonds with each other and with the heavy chains of the immunoglobulin molecules, helping to stabilize the polymeric structure.
Immunoglobulin class switching, also known as isotype switching or class switch recombination (CSR), is a biological process that occurs in B lymphocytes as part of the adaptive immune response. This mechanism allows a mature B cell to change the type of antibody it produces from one class to another (e.g., from IgM to IgG, IgA, or IgE) while keeping the same antigen-binding specificity.
During immunoglobulin class switching, the constant region genes of the heavy chain undergo a DNA recombination event, which results in the deletion of the original constant region exons and the addition of new constant region exons downstream. This switch allows the B cell to express different effector functions through the production of antibodies with distinct constant regions, tailoring the immune response to eliminate pathogens more effectively. The process is regulated by various cytokines and signals from T cells and is critical for mounting an effective humoral immune response.
Antibody diversity refers to the variety of different antibodies that an organism can produce in response to exposure to various antigens. This diversity is generated through a process called V(D)J recombination, which occurs during the development of B cells in the bone marrow.
The variable regions of heavy and light chains of antibody molecules are generated by the random selection and rearrangement of gene segments (V, D, and J) from different combinations. This results in a unique antigen-binding site for each antibody molecule, allowing the immune system to recognize and respond to a vast array of potential pathogens.
Further diversity is generated through the processes of somatic hypermutation and class switch recombination, which introduce additional changes in the variable regions of antibodies during an immune response. These processes allow for the affinity maturation of antibodies, where the binding strength between the antibody and antigen is increased over time, leading to a more effective immune response.
Overall, antibody diversity is critical for the adaptive immune system's ability to recognize and respond to a wide range of pathogens and protect against infection and disease.
Anti-idiotypic antibodies are a type of immune protein that recognizes and binds to the unique identifying region (idiotype) of another antibody. These antibodies are produced by the immune system as part of a regulatory feedback mechanism, where they can modulate or inhibit the activity of the original antibody. They have been studied for their potential use in immunotherapy and vaccine development.
IGHV@
Allelic exclusion
J. Donald Capra
Large B-cell lymphoma arising in HHV8-associated multicentric Castleman's disease
Antibody
Somatic hypermutation
CD300C
Monoallelic gene expression
History of science and technology in Japan
SIRPB1
Anti-immunoglobulin
Recombinant antibodies
IGKC
Organization and expression of immunoglobulin genes
Split gene theory
Alpha-1-B glycoprotein
RNA splicing
Intron
Mir-650 microRNA precursor family
CD8A
PCBP2
IGH@
Immunoglobulin class switching
Freda Stevenson
Gerald Edelman
Paul David Gottlieb
PDCD1LG2
T. J. Hamblin
Framework region
Laurens Smith
immunoglobulin G heavy chain variable region, partial [Homo sapiens] - Protein - NCBI
Complete sequence assembly and characterization of the C57BL/6 mouse Ig heavy chain V region
SRSF1-3 contributes to diversification of the immunoglobulin variable region gene by promoting accumulation of AID in the...
IGHV@ - Wikipedia
Calculating three‐dimensional changes in protein structure due to amino‐acid substitutions: The variable region of...
Antibody - Wikipedia
PDB 2ddq
Chronic Lymphocytic Leukemia CLL Diagnostic and Prognostic Testing | Quest Diagnostics
Childhood Cancer Genetics: Genomic Landscape and Mechanisms of Pediatric Cancers, Landscape of Cancer Genetics in Pediatrics...
Selling an alternative medicine cancer cure testimonial as an 'N-of-1' trial: Integrative medicine's new propaganda technique? ...
Structural Biology @ UniPV - publications
Epstein-Barr virus and Burkitt lymphoma | Journal of Clinical Pathology
The BLAST Sequence Analysis Tool - The NCBI Handbook - NCBI Bookshelf
B Cells in Autoimmune Diseases
Mécanismes d'action des immunoglobulines - Académie nationale de médecine | Une institution dans son temps
Ighv14-1 MGI Mouse Gene Detail - MGI:4439920 - immunoglobulin heavy variable 14-1
Pharmaceutical biology glossary & taxonomy
Frontiers | Differences in Vitreous Protein Profiles in Patients With Proliferative Diabetic Retinopathy Before and After...
Correlation of 9G4 idiotope with disease activity in patients with systemic lupus erythematosus | Annals of the Rheumatic...
Circulating Th17 T cells at treatment onset predict autoimmune toxicity of PI3Kδ inhibitors | Blood Cancer Journal
CD8A - wikidoc
Chronic Lymphocytic Leukemia: Slow-Appearing Symptoms - Medicine.net
Sperm-Mediated Inheritance of Acquired Characters
Jeff PALATINI | PhD | University of Warsaw, Warsaw | UW | Centre of New Technologies | Research profile
MeSH Browser
Prognosis and survival for chronic lymphocytic leukemia | Canadian Cancer Society
High prognostic value of measurable residual disease detection by flow cytometry in chronic lymphocytic leukemia patients...
The Immune Supporting Properties of Milk - ADPI
FITC Rat Anti-Mouse CD47
Antibodies15
- Antibodies are glycoproteins belonging to the immunoglobulin superfamily . (wikipedia.org)
- Antibodies are heavy (~150 k Da ) proteins of about 10 nm in size, [7] arranged in three globular regions that roughly form a Y shape. (wikipedia.org)
- Intravenous immunoglobulin (IVIG) is a therapeutic preparation of polyspecific antibodies isolated from pools of plasma obtained from several thousand healthy blood donors [1]. (academie-medecine.fr)
- The Id is detectable on anti-dsDNA antibodies, though it must also be present on other immunoglobulins whose specificities remain unknown. (bmj.com)
- Another way of distinguishing antibodies serologically involves an analysis of their idiotypes that may be thought of as phenotypic markers of the variable region genes used to encode the antigen binding (Fab) region of immunoglobulin molecules. (bmj.com)
- The adaptive system is comprised of the 'smartest weapons' in the immune arsenal and the antibodies that make up immunoglobulin fraction in milk are the tip of the spear. (adpi.org)
- Unless specified as isotype-specific, anti-IgG secondary antibodies are raised against whole immunoglobulin, so they are expected to cross-react widely with isotypes other than IgG. (biotium.com)
- Our BSA also is immunoglobulin-free and should not interfere with secondary antibodies. (biotium.com)
- The Immunoglobulin variable region transcripts were sequenced and selected for expression as monoclonal antibodies (n=141). (qxmd.com)
- The approach was applied to five different hybridomas producing human monoclonal antibodies and variable regions for both bold gamma and mu heavy chain and kappa and lambda light chain genes were successfully cloned. (lu.se)
- It will also facilitate structural and functional studies of immunoglobulins as well as the rapid construction of chimeric antibodies. (lu.se)
- Immunoglobulins (Igs), the term is sometimes used interchangeably with "antibodies," are glycoprotein molecules produced by B lymphocytes and plasma cells in response to an immunogen or after recognition of specific epitopes on the antigen. (medscape.com)
- Antibodies belong to immunoglobulin family of protein and have 5 isotypes (G, A, M, E, D) with further subclasses of G and A. The classes are differentiated with the characteristics of the Ig heavy chain of the antibody. (medscape.com)
- Abbott ARCHITECT anti-HCV assay is a chemiluminescent microparticle immunoassay (CMIA) for the qualitative detection of immunoglobulin G (IgG) and immunoglobulin M (IgM) antibodies to hepatitis C virus (anti HCV) in human serum and plasma (potassium EDTA, lithium heparin, and sodium heparin). (cdc.gov)
- The infections are likely related to lower-than-normal levels of special proteins called antibodies or immunoglobulins, particularly immunoglobulin M (IgM) or immunoglobulin G (IgG). (medlineplus.gov)
Unmutated immunoglobulin heavy-chain variable region2
- Median progression-free survival was 26 months for those with 17p deletion, 55 months for those with deletion 11q, 43 months for those with unmutated immunoglobulin heavy-chain variable region ( IGVH ), and not reached for those with deletion 13q. (ascopost.com)
- In terms of the study population there were a number of patients with poor risk features, this included 56% of the study population with an unmutated immunoglobulin heavy chain variable region, 17% of the study population with either deletion 17p or TP53 mutation and 19% of the study population with a complex karyotype. (ecancer.org)
Genes5
- To better understand these processes, we have assembled the entire 2.5-Mb mouse IgH (Igh) V region sequence of the C57BL/6 strain from public sequences and present the first complete annotated map of the region, including V genes, pseudogenes, repeats, and nonrepetitive intergenic sequences. (nih.gov)
- IMGT/GENE-DB: a comprehensive database for human and mouse immunoglobulin and T cell receptor genes. (jax.org)
- The sharing of idiotypes by immunoglobulins from different people implies that the genes that encode the idiotypes are also shared. (bmj.com)
- The latter process involves segments of the antibody (immunoglobulin) genes undergoing recombination, generating an enormous repertoire of antigen-binding sites segments (the variable region) of the immunoglobulin molecule. (adpi.org)
- Following antigen encounter, two distinct processes modify immunoglobulin genes. (lu.se)
Chains5
- Both alpha and beta chains share significant homology to immunoglobulin variable light chains. (wikidoc.org)
- The paired immunoglobulin fragments composed of the variable domains of the heavy and light chains. (nih.gov)
- Mouse immunoglobulin chains. (wikidata.org)
- It means that the antibody will bind to epitopes on both the heavy chains (constant regions) and light chains (variable regions) of the target species immunoglobulin. (biotium.com)
- Novel methods for designing humanized immunoglobulins having one or more complementary determining regions (CDR's) from a donor immunoglobulin and a framework region from a human immunoglobulin comprising first comparing the framework or variable region amino acid sequence of the donor immunoglobulin to corresponding sequences in a collection of human immunoglobulin chains, and selecting as the human immunoglobulin one of the more homologous sequences from the collection. (pof.com.au)
Somatic4
- 26 27 In contrast, the chromosomal breakpoint in sBL and HIV-associated BL occurs most commonly in the class switch region, 28 but since both somatic hypermutation and class switching are events that are normally confined to GC B cells and GC centroblast markers are expressed on BL cells, the BL progenitor cells most likely arise from B cells subjected to chromosomal rearrangements in the GC. (bmj.com)
- We also found that GNA13-deficient mice have increased numbers of GC B cells that display impaired caspase-mediated cell death and increased frequency of somatic hypermutation in the immunoglobulin VH locus. (duke.edu)
- The variable region is diversified by somatic hypermutation while the constant region may be changed by class-switch recombination. (lu.se)
- Here we compare the contributions of classs-witch recombination and somatic hypermutation to the diversification of the serum immunoglobulin repertoire and review evidence that suggests that, despite clear differences, the two processes may share some aspects of their mechanism in common. (lu.se)
Antigen3
- That region of the immunoglobulin molecule that varies in its amino acid sequence and composition, and comprises the binding site for a specific antigen. (nih.gov)
- The stem of the 'Y' is conserved and the outer tips of the 'Y' contain the variable parts, which house the antigen binding sites of the molecule. (adpi.org)
- When combined into an intact antibody, the humanized immunoglobulins of the present invention will be substantially non-immunogenic in humans and retain substantially the same affinity as the donor immunoglobulin to the antigen, such as a protein or other compound containing an epitope. (pof.com.au)
Protein9
- Ig heavy chain V-III region VH26 is a protein that in humans is encoded by the IGHV@ gene. (wikipedia.org)
- Snow, ME & Amzel, LM 1986, ' Calculating three‐dimensional changes in protein structure due to amino‐acid substitutions: The variable region of immunoglobulins ', Proteins: Structure, Function, and Bioinformatics , vol. 1, no. 3, pp. 267-279. (johnshopkins.edu)
- An antibody ( Ab ), also known as an immunoglobulin ( Ig ), [1] is a large, Y-shaped protein used by the immune system to identify and neutralize foreign objects such as pathogenic bacteria and viruses . (wikipedia.org)
- CD47 is a 50-kDa plasma membrane protein with an extracellular immunoglobulin variable region-like domain, a multiple membrane-spanning segment, and a short C-terminal cytoplasmic tail. (bdbiosciences.com)
- Molecular cloning of integrin-associated protein: an immunoglobulin family member with multiple membrane-spanning domains implicated in alpha v beta 3-dependent ligand binding. (bdbiosciences.com)
- Heimdall, an alternative protein issued from a ncRNA related to kappa light chain variable region of immunoglobulins from astrocytes: a new player in neural proteome. (sav.sk)
- BACKGROUND: A significant challenge in bioinformatics is to develop methods for detecting and modeling patterns in variable DNA sequence sites, such as protein-binding sites in regulatory DNA. (duke.edu)
- Each receptor has an amino-terminal immunoglobulin variable-region-like (IgV-like) domain that, owing to its presence at the N terminus of the protein, is often known as the N domain. (shu.edu)
- This epitope overlaps substantially with the spike protein N-terminal domain (NTD) -interacting region and is exposed only when the spike is in the open conformation, with one or more RBDs accessible. (bvsalud.org)
IGHV1
- CLL cells with a changed, or mutated, gene for IGHV (immunoglobulin heavy chain variable region) have a more favourable prognosis. (cancer.ca)
Rearrangement1
- and (3) the Gene Rearrangement Theory, which holds that antibody diversity is generated by the rearrangement of IMMUNOGLOBULIN VARIABLE REGION gene segments during the differentiation of the ANTIBODY-PRODUCING CELLS. (bvsalud.org)
Fragment6
- The accuracy of the procedure is tested by calculating the conformation of a region of the human immunoglobulin fragment Fab Kol based on the analogous region of the human immunoglobulin fragment Fab New. (johnshopkins.edu)
- It is located at the N-terminus of the Fab fragment of the immunoglobulin. (nih.gov)
- The Arthromyces ramosus peroxidase gene (arp) was genetically fused to either the 5′- or 3′-terminal ends of the gene encoding llama variable heavy chain antibody fragment VHH R9, resulting in the fusion expression cassettes ARP-R9 or R9-ARP. (tno.nl)
- Structurally-modified Antibody, Immunoglobulin, Or Fragment Thereof (e.g. (justia.com)
- Justia Patents Drug, Bio-affecting And Body Treating Compositions Patents Immunoglobulin, Antiserum, Antibody, Or Antibody Fragment, Except Conjugate Or Complex Of The Same With Nonimmunoglobulin Material Patents Structurally-modified Antibody, Immunoglobulin, Or Fragment Thereof (e.g. (justia.com)
- they have receptors for the crystallizable fragment (Fc) region of immunoglobulin (Ig) G and for complement, which enable them to bind with immune complexes and present the complex to B cells in germinal centers of secondary lymphoid organs. (msdmanuals.com)
Interchangeably2
- The terms antibody and immunoglobulin are often used interchangeably, [1] though the term 'antibody' is sometimes reserved for the secreted, soluble form, i.e. excluding B-cell receptors. (wikipedia.org)
- In many cases the term antibody and immunoglobulin are used interchangeably. (adpi.org)
Molecule2
- Immunoglobulin is a more precise term as it usually allows identification of the sub-class of immunoglobulin molecule. (adpi.org)
- Variable region constitutes the antibody binding region of the molecule to the different antigens as it consists of about 110 amino acids that vary widely among the different antibody molecules. (medscape.com)
Recombination2
- This complete and definitive assembly of the mouse Igh V region will facilitate detailed study of promoter function and large-scale mechanisms associated with V(D)J recombination including locus contraction and antisense intergenic transcription. (nih.gov)
- Moreover, the breakpoint in the Ig gene to which MYC is transferred in eBL occurs at the V(D)J region, suggesting that translocation occurs during V(D)J recombination. (bmj.com)
Fragments2
- Ces mécanismes dépendent des fragments constants (Fc) et/ou variables (Fab')2. (academie-medecine.fr)
- We report the expression and production of llama variable heavy-chain antibody fragments (VHHs) by Aspergillus awamori. (tno.nl)
Chimeric1
- It is the overall sequence of the variable region that is considered and then judged to more closely resemble human sequences (i.e., fully human and humanized mAbs) or non-human sequences (i.e., chimeric mAbs). (jcadonline.com)
Extracellular1
- Most of the rest of the extracellular part of each receptor is comprised of a variable number of immunoglobulin constant-region-type-2-like (IgC2-like) domains. (shu.edu)
Serum2
- However, it is important to avoid using blocking serum from the same host species as your primary antibody that is detected by a secondary antibody against the same species (immunoglobulins in the blocking serum will compete for the secondary binding). (biotium.com)
- In European registry data, serious infections were not related to presenting levels of serum immunoglobulin G (IgG). (medscape.com)
Repertoire1
- The mechanisms that regulate variable (V) gene selection during the development of the mouse IgH repertoire are not fully understood, due in part to the absence of the complete locus sequence. (nih.gov)
Tertiary1
- These regions encode tertiary structures termed idiotopes. (bmj.com)
Progenitor1
- Astrocytes express aberrant immunoglobulins as putative gatekeeper of astrocytes to neuronal progenitor conversion. (sav.sk)
Proteins1
- Note that 'antibody' is a descriptive term that reflects the functionality of the group of proteins that comprise the immunoglobulins which are found in the whey fraction of milk [1] . (adpi.org)
20181
- Before November 16, 2018, patients' reasons for travel, exposure country, and exposure region were not linked to an individual diagnosis. (cdc.gov)
Domains1
- Each chain has domains called the V (variable) region and C (constant) region. (medscape.com)
Aberrant1
- A mutant immunoglobulin light chain is formed by aberrant DNA- and RNA-splicing events. (wikidata.org)
Putative1
- and c100-3, representing the putative nonstructural (NS3 and NS4) regions of HCV. (cdc.gov)
Comprise1
- Each humanized immunoglobulin chain may comprise about 3 or more amino acids from the donor immunoglobulin in addition to the CDR's, usually at least one of which is immediately adjacent to a CDR in the donor immunoglobulin. (pof.com.au)
Mutation3
- When various characteristics were looked at and a Forest plot analysis was presented at the ASCO meeting, various variables did not affect the CR rate and these included age, stage of disease, 17p or TP53 mutation status or immunoglobulin heavy chain variable region mutation status. (ecancer.org)
- Patients who have common variable immunodeficiency and autoimmune conditions appear to have very low numbers of isotype-switched memory B cells in peripheral blood and are more likely to have a mutation in the gene that encodes TACI ( TNFRST13B ). (medscape.com)
- A high mutation rate of immunoglobulin heavy chain variable region gene associates with a poor survival and chemotherapy response of mantle cell lymphoma patients. (cdc.gov)
Translocation1
- The hallmark of all BL tumours is the translocation between the MYC gene and one of the immunoglobulin (Ig) heavy or light chain loci. (bmj.com)
Enzyme1
- These changes alter a region of the PLCγ2 enzyme that controls whether it is turned on or off. (medlineplus.gov)
Receptors1
- The constant region at the carboxyl-terminal end of the heavy chain, called the Fc region, binds to the Fc receptors of neutrophils, eosinophils, macrophages, dendritic cells, B cells, and the natural killer (NK) cells. (medscape.com)
Diversification1
- Activation-induced cytidine deaminase (AID) is essential for diversification of the Ig variable region (IgV). (elsevierpure.com)
Sequences3
- Find regions of similarity between this sequence and other sequences using BLAST. (nih.gov)
- Finds sub-sequences or patterns in the sequence and highlights the matching regions. (nih.gov)
- We have identified clusters of conserved region-specific intergenic sequences and have verified our assembly by genic and intergenic Southern blotting. (nih.gov)
Chain1
- We describe a general approach to rapidly obtain the DNA sequence encoding the variable region of any immunoglobulin chain using the polymerase chain reaction and a mixture of upstream primers corresponding to the leader sequence, and one downstream primer designed from the conserved nucleotide sequence of the constant region. (lu.se)
Cytoplasmic1
- The cytoplasmic tail region is expressed as alternatively spliced forms, which are differentially expressed in diverse tissues, suggesting that IAP may have distinct functions in various tissues. (bdbiosciences.com)
Constant region1
- The constant region at the trunk of the antibody includes sites involved in interactions with other components of the immune system. (wikipedia.org)
Sites2
- H3K9me2 was found at several paternally methylated imprinted regions in sperm, suggesting that this histone mark signals special sites of the paternal genome where methylation is maintained. (i-sis.org.uk)
- Complemen- tary independent variables are sampling sites and sampling events within the population cycle. (cdc.gov)
Cluster1
- We have observed that V pseudogenes are not evenly spread throughout the V region, but rather cluster together. (nih.gov)