Glycogen Storage Disease Type II
Glycogen Storage Disease Type I
alpha-Glucosidases
Glycogen Storage Disease
Glucan 1,4-alpha-Glucosidase
Glycogen Storage Disease Type III
Glycogen Storage Disease Type IV
Enzyme Replacement Therapy
Glycogen
Glycogen Storage Disease Type VII
Glucose-6-Phosphatase
Glycogen Storage Disease Type VI
Glycogen Debranching Enzyme System
Glycogen Storage Disease Type V
Glycogen Storage Disease Type VIII
Antiporters
Glucose-6-Phosphate
1,4-alpha-Glucan Branching Enzyme
Glycogen Storage Disease Type IIb
Fructose-1,6-Diphosphatase Deficiency
Monosaccharide Transport Proteins
Lysosomal Storage Diseases
Glycogen Synthase
Hypoglycemia
Starch
Liver
Dependovirus
Genetic Therapy
Complete genomic structure and mutational spectrum of PHKA2 in patients with x-linked liver glycogenosis type I and II. (1/211)
X-linked liver glycogenosis (XLG) is probably the most frequent glycogen-storage disease. XLG can be divided into two subtypes: XLG I, with a deficiency in phosphorylase kinase (PHK) activity in peripheral blood cells and liver; and XLG II, with normal in vitro PHK activity in peripheral blood cells and with variable activity in liver. Both types of XLG are caused by mutations in the same gene, PHKA2, that encodes the regulatory alpha subunit of PHK. To facilitate mutation analysis in PHKA2, we determined its genomic structure. The gene consists of 33 exons, spanning >/=65 kb. By SSCP analysis of the different PHKA2 exons, we identified five new XLG I mutations, one new XLG II mutation, and one mutation present in both a patient with XLG I and a patient with XLG II, bringing the total to 19 XLG I and 12 XLG II mutations. Most XLG I mutations probably lead to truncation or disruption of the PHKA2 protein. In contrast, all XLG II mutations are missense mutations or small in-frame deletions and insertions. These results suggest that the biochemical differences between XLG I and XLG II might be due to the different nature of the disease-causing mutations in PHKA2. XLG I mutations may lead to absence of the alpha subunit, which causes an unstable PHK holoenzyme and deficient enzyme activity, whereas XLG II mutations may lead to in vivo deregulation of PHK, which might be difficult to demonstrate in vitro. (+info)Systemic correction of the muscle disorder glycogen storage disease type II after hepatic targeting of a modified adenovirus vector encoding human acid-alpha-glucosidase. (2/211)
This report demonstrates that a single intravenous administration of a gene therapy vector can potentially result in the correction of all affected muscles in a mouse model of a human genetic muscle disease. These results were achieved by capitalizing both on the positive attributes of modified adenovirus-based vectoring systems and receptor-mediated lysosomal targeting of enzymes. The muscle disease treated, glycogen storage disease type II, is a lysosomal storage disorder that manifests as a progressive myopathy, secondary to massive glycogen accumulations in the skeletal and/or cardiac muscles of affected individuals. We demonstrated that a single intravenous administration of a modified Ad vector encoding human acid alpha-glucosidase (GAA) resulted in efficient hepatic transduction and secretion of high levels of the precursor GAA proenzyme into the plasma of treated animals. Subsequently, systemic distribution and uptake of the proenzyme into the skeletal and cardiac muscles of the GAA-knockout mouse was confirmed. As a result, systemic decreases (and correction) of the glycogen accumulations in a variety of muscle tissues was demonstrated. This model can potentially be expanded to include the treatment of other lysosomal enzyme disorders. Lessons learned from systemic genetic therapy of muscle disorders also should have implications for other muscle diseases, such as the muscular dystrophies. (+info)Frequency of glycogen storage disease type II in The Netherlands: implications for diagnosis and genetic counselling. (3/211)
Glycogen storage disease type II (GSD H) is an autosomal recessive myopathy. Early and late-onset phenotypes are distinguished - infantile, juvenile and adult. Three mutations in the acid alpha-glucosidase gene are common in the Dutch patient population: IVS1(-13T-->G), 525delT and delexon18. 63% of Dutch GSD II patients carry one or two of these mutations, and the genotype-phenotype correlation is known. To determine the frequency of GSD II, we have screened an unselected sample of neonates for the occurrence of these three mutations. Based on the calculated carrier frequencies, the predicted frequency of the disease is 1 in 40000 divided by 1 in 138 000 for infantile GSD II and 1 in 57 000 for adult GSD II. This is about two to four times higher than previously suggested, which is a reason to become more familiar with the presentation of GSD II in its different clinical forms and to adjust the risk assessment for genetic counselling. (+info)Human acid alpha-glucosidase from rabbit milk has therapeutic effect in mice with glycogen storage disease type II. (4/211)
Pompe's disease or glycogen storage disease type II (GSDII) belongs to the family of inherited lysosomal storage diseases. The underlying deficiency of acid alpha-glucosidase leads in different degrees of severity to glycogen storage in heart, skeletal and smooth muscle. There is currently no treatment for this fatal disease, but the applicability of enzyme replacement therapy is under investigation. For this purpose, recombinant human acid alpha-glucosidase has been produced on an industrial scale in the milk of transgenic rabbits. In this paper we demonstrate the therapeutic effect of this enzyme in our knockout mouse model of GSDII. Full correction of acid alpha-glucosidase deficiency was obtained in all tissues except brain after a single dose of i.v. enzyme administration. Weekly enzyme infusions over a period of 6 months resulted in degradation of lysosomal glycogen in heart, skeletal and smooth muscle. The tissue morphology improved substantially despite the advanced state of disease at the start of treatment. The results have led to the start of a Phase II clinical trial of enzyme replacement therapy in patients. (+info)Amniotic cell 4-methylumbelliferyl-alpha-glucosidase activity for prenatal diagnosis of Pompe's disease. (5/211)
Using a simple fluorometric assay for alpha-glucosidase activity of cultured amniotic cells, we have monitored two pregnancies from families at risk for Pompe's disease. The fetus was judged to be affected in one, the pregnancy being terminated and unaffected in the other. The accuracy of these predictions was confirmed. These results suggest that this assay allows accurate prenatal diagnosis of Pompe's disease, three weeks after diagnostic amniocentesis. (+info)Pompe's disease or type IIa glycogenosis. (6/211)
This is the report of a five-month-old child presenting clinical evidence of Pompe's disease: severe hypotonicity, hyporeflexia and congestive heart failure. The ECG showed a short PR interval, the chest radiography disclosed marked cardiomegaly, and the echocardiogram revealed marked left ventricular hypertrophy - the most typical finding of this disease. A skeletal muscle biopsy led to final diagnosis, because in the histopathologic study marked increased glycogen accumulation was evident. Death occurred two months after symptom onset. (+info)Evidence for a founder effect in Sicilian patients with glycogen storage disease type II. (7/211)
Glycogen storage disease type II (GSD II) is an autosomal recessive inherited disorder due to the deficiency of the enzyme acid alpha-glucosidase, which causes an accumulation of glycogen in lysosomes. The deletion of exon 18 (delta 18) is a frequent mutation associated with a severe phenotype. We analyzed 25 Italian patients, 5 of whom were found to be delta 18 carriers. All these 5 patients came from Catania, a town in Sicily. We report on the analysis of 5 intragenic single-point polymorphic markers in the delta 18 patients and on the subsequent characterization of a delta 18-associated haplotype. The frequency of this haplotype in GSD II patients and normal individuals was 1 and 0.196, respectively (chi(2) = 20.9; p < 0.001). The high frequency of the delta 18 allele in this Italian subpopulation is likely to be due to a founder effect. (+info)Determination of acid alpha-glucosidase protein: evaluation as a screening marker for Pompe disease and other lysosomal storage disorders. (8/211)
BACKGROUND: In recent years, there have been significant advances in the development of enzyme replacement and other therapies for lysosomal storage disorders (LSDs). Early diagnosis, before the onset of irreversible pathology, has been demonstrated to be critical for maximum efficacy of current and proposed therapies. In the absence of a family history, the presymptomatic detection of these disorders ideally can be achieved through a newborn screening program. One approach to the development of such a program is the identification of suitable screening markers. In this study, the acid alpha-glucosidase protein was evaluated as a marker protein for Pompe disease and potentially for other LSDs. METHODS: Two sensitive immunoquantification assays for the measurement of total (precursor and mature) and mature forms of acid alpha-glucosidase protein were used to determine the concentrations in plasma and dried blood spots from control and LSD-affected individuals. RESULTS: In the majority of LSDs, no significant increases above control values were observed. However, individuals with Pompe disease showed a marked decrease in acid alpha-glucosidase protein in both plasma and whole blood compared with unaffected controls. For plasma samples, this assay gave a sensitivity of 95% with a specificity of 100%. For blood spot samples, the sensitivity was 82% with a specificity of 100%. CONCLUSIONS: This study demonstrates that it is possible to screen for Pompe disease by screening the concentration of total acid alpha-glucosidase in plasma or dried blood spots. (+info)Glycogen Storage Disease Type II, also known as Pompe Disease, is a genetic disorder caused by a deficiency of the enzyme acid alpha-glucosidase (GAA). This enzyme is responsible for breaking down glycogen, a complex sugar that serves as energy storage, within lysosomes. When GAA is deficient, glycogen accumulates in various tissues, particularly in muscle cells, leading to their dysfunction and damage.
The severity of Pompe Disease can vary significantly, depending on the amount of functional enzyme activity remaining. The classic infantile-onset form presents within the first few months of life with severe muscle weakness, hypotonia, feeding difficulties, and respiratory insufficiency. This form is often fatal by 1-2 years of age if left untreated.
A later-onset form, which can present in childhood, adolescence, or adulthood, has a more variable clinical course. Affected individuals may experience progressive muscle weakness, respiratory insufficiency, and cardiomyopathy, although the severity and rate of progression are generally less pronounced than in the infantile-onset form.
Enzyme replacement therapy with recombinant human GAA is available for the treatment of Pompe Disease and has been shown to improve survival and motor function in affected individuals.
Glycogen Storage Disease Type I (GSD I) is a rare inherited metabolic disorder caused by deficiency of the enzyme glucose-6-phosphatase, which is necessary for the liver to release glucose into the bloodstream. This leads to an accumulation of glycogen in the liver and abnormally low levels of glucose in the blood (hypoglycemia).
There are two main subtypes of GSD I: Type Ia and Type Ib. In Type Ia, there is a deficiency of both glucose-6-phosphatase enzyme activity in the liver, kidney, and intestine, leading to hepatomegaly (enlarged liver), hypoglycemia, lactic acidosis, hyperlipidemia, and growth retardation. Type Ib is characterized by a deficiency of glucose-6-phosphatase enzyme activity only in the neutrophils, leading to recurrent bacterial infections.
GSD I requires lifelong management with frequent feedings, high-carbohydrate diet, and avoidance of fasting to prevent hypoglycemia. In some cases, treatment with continuous cornstarch infusions or liver transplantation may be necessary.
Alpha-glucosidases are a group of enzymes that break down complex carbohydrates into simpler sugars, such as glucose, by hydrolyzing the alpha-1,4 and alpha-1,6 glycosidic bonds in oligosaccharides, disaccharides, and polysaccharides. These enzymes are located on the brush border of the small intestine and play a crucial role in carbohydrate digestion and absorption.
Inhibitors of alpha-glucosidases, such as acarbose and miglitol, are used in the treatment of type 2 diabetes to slow down the digestion and absorption of carbohydrates, which helps to reduce postprandial glucose levels and improve glycemic control.
Glycogen storage disease (GSD) is a group of rare inherited metabolic disorders that affect the body's ability to break down and store glycogen, a complex carbohydrate that serves as the primary form of energy storage in the body. These diseases are caused by deficiencies or dysfunction in enzymes involved in the synthesis, degradation, or transport of glycogen within cells.
There are several types of GSDs, each with distinct clinical presentations and affected organs. The most common type is von Gierke disease (GSD I), which primarily affects the liver and kidneys. Other types include Pompe disease (GSD II), McArdle disease (GSD V), Cori disease (GSD III), Andersen disease (GSD IV), and others.
Symptoms of GSDs can vary widely depending on the specific type, but may include:
* Hypoglycemia (low blood sugar)
* Growth retardation
* Hepatomegaly (enlarged liver)
* Muscle weakness and cramping
* Cardiomyopathy (heart muscle disease)
* Respiratory distress
* Developmental delays
Treatment for GSDs typically involves dietary management, such as frequent feedings or a high-protein, low-carbohydrate diet. In some cases, enzyme replacement therapy may be used to manage symptoms. The prognosis for individuals with GSDs depends on the specific type and severity of the disorder.
Glucan 1,4-alpha-glucosidase, also known as amyloglucosidase or glucoamylase, is an enzyme that catalyzes the hydrolysis of 1,4-glycosidic bonds in starch and other oligo- and polysaccharides, breaking them down into individual glucose molecules. This enzyme specifically acts on the alpha (1->4) linkages found in amylose and amylopectin, two major components of starch. It is widely used in various industrial applications, including the production of high fructose corn syrup, alcoholic beverages, and as a digestive aid in some medical supplements.
Glycogen Storage Disease Type III, also known as Cori or Forbes disease, is a rare inherited metabolic disorder caused by deficiency of the debranching enzyme amylo-1,6-glucosidase, which is responsible for breaking down glycogen in the liver and muscles. This results in an abnormal accumulation of glycogen in these organs leading to its associated symptoms.
There are two main types: Type IIIa affects both the liver and muscles, while Type IIIb affects only the liver. Symptoms can include hepatomegaly (enlarged liver), hypoglycemia (low blood sugar), hyperlipidemia (high levels of fats in the blood), and growth retardation. In Type IIIa, muscle weakness and cardiac problems may also occur.
The diagnosis is usually made through biochemical tests and genetic analysis. Treatment often involves dietary management with frequent meals to prevent hypoglycemia, and in some cases, enzyme replacement therapy. However, there is no cure for this condition and life expectancy can be reduced depending on the severity of the symptoms.
Glycogen Storage Disease Type IV (GSD IV), also known as Andersen's disease, is a rare inherited metabolic disorder that affects the body's ability to break down glycogen, a complex carbohydrate that serves as a source of energy for the body.
In GSD IV, there is a deficiency in the enzyme called glycogen branching enzyme (GBE), which is responsible for adding branches to the glycogen molecule during its synthesis. This results in an abnormal form of glycogen that accumulates in various organs and tissues, particularly in the liver, heart, and muscles.
The accumulation of this abnormal glycogen can lead to progressive damage and failure of these organs, resulting in a variety of symptoms such as muscle weakness, hypotonia, hepatomegaly (enlarged liver), cardiomyopathy (heart muscle disease), and developmental delay. The severity of the disease can vary widely, with some individuals experiencing milder symptoms while others may have a more severe and rapidly progressing form of the disorder.
Currently, there is no cure for GSD IV, and treatment is focused on managing the symptoms and slowing down the progression of the disease. This may include providing nutritional support, addressing specific organ dysfunction, and preventing complications.
Enzyme Replacement Therapy (ERT) is a medical treatment approach in which functional copies of a missing or deficient enzyme are introduced into the body to compensate for the lack of enzymatic activity caused by a genetic disorder. This therapy is primarily used to manage lysosomal storage diseases, such as Gaucher disease, Fabry disease, Pompe disease, and Mucopolysaccharidoses (MPS), among others.
In ERT, the required enzyme is produced recombinantly in a laboratory using biotechnological methods. The purified enzyme is then administered to the patient intravenously at regular intervals. Once inside the body, the exogenous enzyme is taken up by cells, particularly those affected by the disorder, and helps restore normal cellular functions by participating in essential metabolic pathways.
ERT aims to alleviate disease symptoms, slow down disease progression, improve quality of life, and increase survival rates for patients with lysosomal storage disorders. However, it does not cure the underlying genetic defect responsible for the enzyme deficiency.
Glycogen is a complex carbohydrate that serves as the primary form of energy storage in animals, fungi, and bacteria. It is a polysaccharide consisting of long, branched chains of glucose molecules linked together by glycosidic bonds. Glycogen is stored primarily in the liver and muscles, where it can be quickly broken down to release glucose into the bloodstream during periods of fasting or increased metabolic demand.
In the liver, glycogen plays a crucial role in maintaining blood glucose levels by releasing glucose when needed, such as between meals or during exercise. In muscles, glycogen serves as an immediate energy source for muscle contractions during intense physical activity. The ability to store and mobilize glycogen is essential for the proper functioning of various physiological processes, including athletic performance, glucose homeostasis, and overall metabolic health.
Glycogen Storage Disease Type VII, also known as Tarui's disease, is a rare inherited metabolic disorder caused by a deficiency of the enzyme phosphofructokinase (PFK), which is required for glycogenolysis – the breakdown of glycogen to glucose-1-phosphate and ultimately into glucose. This enzyme deficiency results in the accumulation of glycogen, particularly in muscle and red blood cells, leading to symptoms such as exercise-induced muscle cramps, myoglobinuria (the presence of myoglobin in the urine), and hemolytic anemia. The disease can also cause muscle weakness, fatigue, and dark-colored urine after strenuous exercise. It is inherited in an autosomal recessive manner, meaning that an individual must inherit two copies of the mutated gene (one from each parent) to develop the condition.
Glucose-6-phosphatase is an enzyme that plays a crucial role in the regulation of glucose metabolism. It is primarily located in the endoplasmic reticulum of cells in liver, kidney, and intestinal mucosa. The main function of this enzyme is to remove the phosphate group from glucose-6-phosphate (G6P), converting it into free glucose, which can then be released into the bloodstream and used as a source of energy by cells throughout the body.
The reaction catalyzed by glucose-6-phosphatase is as follows:
Glucose-6-phosphate + H2O → Glucose + Pi (inorganic phosphate)
This enzyme is essential for maintaining normal blood glucose levels, particularly during periods of fasting or starvation. In these situations, the body needs to break down stored glycogen in the liver and convert it into glucose to supply energy to the brain and other vital organs. Glucose-6-phosphatase is a key enzyme in this process, allowing for the release of free glucose into the bloodstream.
Deficiencies or mutations in the gene encoding glucose-6-phosphatase can lead to several metabolic disorders, such as glycogen storage disease type I (von Gierke's disease) and other related conditions. These disorders are characterized by an accumulation of glycogen and/or fat in various organs, leading to impaired glucose metabolism, growth retardation, and increased risk of infection and liver dysfunction.
Glycogen Storage Disease Type VI, also known as Hers disease, is a rare inherited metabolic disorder caused by deficiency of the liver enzyme called glycogen phosphorylase. This enzyme is responsible for breaking down glycogen, which is a stored form of glucose, into glucose-1-phosphate during the process of glycogenolysis.
In GSD Type VI, the lack of this enzyme leads to an abnormal accumulation of glycogen in the liver, causing hepatomegaly (enlarged liver) and elevated liver enzymes. The symptoms of this condition are usually milder compared to other types of GSD, and may include fatigue, weakness, and hypoglycemia (low blood sugar), especially after prolonged fasting or physical exertion.
The diagnosis of GSD Type VI is typically made through biochemical tests that measure the activity of the glycogen phosphorylase enzyme in liver tissue, as well as genetic testing to identify mutations in the gene responsible for the enzyme's production. Treatment may involve dietary management, such as frequent feeding and avoidance of prolonged fasting, to prevent hypoglycemia. In some cases, medication may be necessary to manage symptoms and prevent complications.
The Glycogen Debranching Enzyme System, also known as glycogen debranching enzyme or Amy-1, is a crucial enzyme complex in human biochemistry. It plays an essential role in the metabolism of glycogen, which is a large, branched polymer of glucose that serves as the primary form of energy storage in animals and fungi.
The Glycogen Debranching Enzyme System consists of two enzymatic activities: a transferase and an exo-glucosidase. The transferase activity transfers a segment of a branched glucose chain to another part of the same or another glycogen molecule, while the exo-glucosidase activity cleaves the remaining single glucose units from the outer branches of the glycogen molecule.
This enzyme system is responsible for removing the branched structures of glycogen, allowing the linear chains to be further degraded by other enzymes into glucose molecules that can be used for energy production or stored for later use. Defects in this enzyme complex can lead to several genetic disorders, such as Glycogen Storage Disease Type III (Cori's disease) and Type IV (Andersen's disease), which are characterized by the accumulation of abnormal glycogen molecules in various tissues.
Glycogen Storage Disease Type V, also known as McArdle's disease, is a genetic disorder that affects the body's ability to break down glycogen, a complex carbohydrate stored in muscles, into glucose, which provides energy for muscle contraction.
This condition results from a deficiency of the enzyme myophosphorylase, which is responsible for breaking down glycogen into glucose-1-phosphate within the muscle fibers. Without sufficient myophosphorylase activity, muscles become easily fatigued and may cramp or become rigid during exercise due to a lack of available energy.
Symptoms typically appear in childhood or adolescence and can include muscle weakness, stiffness, cramps, and myoglobinuria (the presence of myoglobin, a protein found in muscle cells, in the urine) following exercise. Diagnosis is usually confirmed through genetic testing and enzyme assays. Treatment typically involves avoiding strenuous exercise and ensuring adequate hydration and rest before and after physical activity. In some cases, dietary modifications such as high-protein or high-carbohydrate intake may be recommended to help manage symptoms.
Glycogen Storage Disease Type VIII, also known as Phosphorylase Kinase Deficiency, is a rare genetic metabolic disorder that affects the production and breakdown of glycogen in the body. Glycogen is a complex carbohydrate that serves as the primary form of energy storage in the body.
In this condition, there is a deficiency or dysfunction of the enzyme phosphorylase kinase (PhK), which plays a crucial role in activating glycogen phosphorylase, an enzyme responsible for breaking down glycogen into glucose-1-phosphate during periods of increased energy demand.
The deficiency or dysfunction of PhK leads to the abnormal accumulation of glycogen in various tissues, particularly in the liver and muscles. This accumulation can result in hepatomegaly (enlarged liver), hypoglycemia (low blood sugar levels), growth retardation, and muscle weakness.
Glycogen Storage Disease Type VIII is inherited in an autosomal recessive manner, meaning that an individual must inherit two defective copies of the gene, one from each parent, to develop the condition. There are four subtypes of GSD Type VIII, classified based on the specific genetic mutation and the severity of symptoms.
Treatment for Glycogen Storage Disease Type VIII typically involves managing the symptoms and complications associated with the disorder, such as providing a high-carbohydrate diet to prevent hypoglycemia and addressing any liver or muscle dysfunction. Regular monitoring by a healthcare team experienced in metabolic disorders is essential for optimizing treatment and ensuring appropriate management of this complex condition.
Antiporters, also known as exchange transporters, are a type of membrane transport protein that facilitate the exchange of two or more ions or molecules across a biological membrane in opposite directions. They allow for the movement of one type of ion or molecule into a cell while simultaneously moving another type out of the cell. This process is driven by the concentration gradient of one or both of the substances being transported. Antiporters play important roles in various physiological processes, including maintaining electrochemical balance and regulating pH levels within cells.
Glucose-6-phosphate (G6P) is a vital intermediate compound in the metabolism of glucose, which is a simple sugar that serves as a primary source of energy for living organisms. G6P plays a critical role in both glycolysis and gluconeogenesis pathways, contributing to the regulation of blood glucose levels and energy production within cells.
In biochemistry, glucose-6-phosphate is defined as:
A hexose sugar phosphate ester formed by the phosphorylation of glucose at the 6th carbon atom by ATP in a reaction catalyzed by the enzyme hexokinase or glucokinase. This reaction is the first step in both glycolysis and glucose storage (glycogen synthesis) processes, ensuring that glucose can be effectively utilized for energy production or stored for later use.
G6P serves as a crucial metabolic branch point, leading to various pathways such as:
1. Glycolysis: In the presence of sufficient ATP and NAD+ levels, G6P is further metabolized through glycolysis to generate pyruvate, which enters the citric acid cycle for additional energy production in the form of ATP, NADH, and FADH2.
2. Gluconeogenesis: During periods of low blood glucose levels, G6P can be synthesized back into glucose through the gluconeogenesis pathway, primarily occurring in the liver and kidneys. This process helps maintain stable blood glucose concentrations and provides energy to cells when dietary intake is insufficient.
3. Pentose phosphate pathway (PPP): A portion of G6P can be shunted into the PPP, an alternative metabolic route that generates NADPH, ribose-5-phosphate for nucleotide synthesis, and erythrose-4-phosphate for aromatic amino acid production. The PPP is essential in maintaining redox balance within cells and supporting biosynthetic processes.
Overall, glucose-6-phosphate plays a critical role as a central metabolic intermediate, connecting various pathways to regulate energy homeostasis, redox balance, and biosynthesis in response to cellular demands and environmental cues.
A liver cell adenoma is a benign tumor that develops in the liver and is composed of cells similar to those normally found in the liver (hepatocytes). These tumors are usually solitary, but multiple adenomas can occur, especially in women who have taken oral contraceptives for many years. Liver cell adenomas are typically asymptomatic and are often discovered incidentally during imaging studies performed for other reasons. In rare cases, they may cause symptoms such as abdominal pain or discomfort, or complications such as bleeding or rupture. Treatment options include monitoring with periodic imaging studies or surgical removal of the tumor.
1,4-Alpha-Glucan Branching Enzyme (GBE) is an enzyme that plays a crucial role in the synthesis of glycogen, a complex carbohydrate that serves as the primary form of energy storage in animals and fungi. GBE catalyzes the transfer of a segment of a linear glucose chain (alpha-1,4 linkage) to an alpha-1,6 position on another chain, creating branches in the glucan molecule. This branching process enhances the solubility and compactness of glycogen, allowing it to be stored more efficiently within cells.
Defects in GBE are associated with a group of genetic disorders known as glycogen storage diseases type IV (GSD IV), also called Andersen's disease. This autosomal recessive disorder is characterized by the accumulation of abnormally structured glycogen in various tissues, particularly in the liver and muscles, leading to progressive liver failure, muscle weakness, cardiac complications, and sometimes neurological symptoms.
Glycogen Storage Disease Type IIb, also known as Pompe Disease, is a genetic disorder caused by a deficiency of the enzyme acid alpha-glucosidase (GAA). This enzyme is responsible for breaking down glycogen, a complex carbohydrate, into glucose within lysosomes. When GAA activity is lacking, glycogen accumulates in various tissues, including muscle and nerve cells, leading to cellular dysfunction and damage.
Type IIb Pompe Disease is characterized by progressive muscle weakness and hypertrophy (enlargement) of the heart muscle (cardiomyopathy). This form of the disease typically presents in infancy or early childhood and can progress rapidly, often resulting in severe cardiac complications and respiratory failure if left untreated.
Early diagnosis and treatment with enzyme replacement therapy (ERT) can significantly improve outcomes for individuals with Type IIb Pompe Disease. ERT involves administering recombinant human GAA to replace the deficient enzyme, helping to reduce glycogen accumulation in tissues and alleviate symptoms.
Fructose-1,6-diphosphatase deficiency is a rare inherited metabolic disorder that affects the body's ability to metabolize carbohydrates, particularly fructose and glucose. This enzyme deficiency results in an accumulation of certain metabolic intermediates, which can cause a variety of symptoms, including hypoglycemia (low blood sugar), lactic acidosis, hyperventilation, and seizures. The condition is typically diagnosed in infancy or early childhood and is treated with a diet low in fructose and other sugars that can't be metabolized properly due to the enzyme deficiency. If left untreated, the disorder can lead to serious complications, such as brain damage and death.
Monosaccharide transport proteins are a type of membrane transport protein that facilitate the passive or active transport of monosaccharides, such as glucose, fructose, and galactose, across cell membranes. These proteins play a crucial role in the absorption, distribution, and metabolism of carbohydrates in the body.
There are two main types of monosaccharide transport proteins: facilitated diffusion transporters and active transporters. Facilitated diffusion transporters, also known as glucose transporters (GLUTs), passively transport monosaccharides down their concentration gradient without the need for energy. In contrast, active transporters, such as the sodium-glucose cotransporter (SGLT), use energy in the form of ATP to actively transport monosaccharides against their concentration gradient.
Monosaccharide transport proteins are found in various tissues throughout the body, including the intestines, kidneys, liver, and brain. They play a critical role in maintaining glucose homeostasis by regulating the uptake and release of glucose into and out of cells. Dysfunction of these transporters has been implicated in several diseases, such as diabetes, cancer, and neurological disorders.
Lysosomal storage diseases (LSDs) are a group of rare inherited metabolic disorders caused by defects in lysosomal function. Lysosomes are membrane-bound organelles within cells that contain enzymes responsible for breaking down and recycling various biomolecules, such as proteins, lipids, and carbohydrates. In LSDs, the absence or deficiency of specific lysosomal enzymes leads to the accumulation of undigested substrates within the lysosomes, resulting in cellular dysfunction and organ damage.
These disorders can affect various organs and systems in the body, including the brain, nervous system, bones, skin, and visceral organs. Symptoms may include developmental delays, neurological impairment, motor dysfunction, bone abnormalities, coarse facial features, hepatosplenomegaly (enlarged liver and spleen), and recurrent infections.
Examples of LSDs include Gaucher disease, Tay-Sachs disease, Niemann-Pick disease, Fabry disease, Pompe disease, and mucopolysaccharidoses (MPS). Treatment options for LSDs may include enzyme replacement therapy, substrate reduction therapy, or bone marrow transplantation. Early diagnosis and intervention can help improve the prognosis and quality of life for affected individuals.
Liver glycogen is the reserve form of glucose stored in hepatocytes (liver cells) for the maintenance of normal blood sugar levels. It is a polysaccharide, a complex carbohydrate, that is broken down into glucose molecules when blood glucose levels are low. This process helps to maintain the body's energy needs between meals and during periods of fasting or exercise. The amount of glycogen stored in the liver can vary depending on factors such as meal consumption, activity level, and insulin regulation.
Glycogen synthase is an enzyme (EC 2.4.1.11) that plays a crucial role in the synthesis of glycogen, a polysaccharide that serves as the primary storage form of glucose in animals, fungi, and bacteria. This enzyme catalyzes the transfer of glucosyl residues from uridine diphosphate glucose (UDP-glucose) to the non-reducing end of an growing glycogen chain, thereby elongating it.
Glycogen synthase is regulated by several mechanisms, including allosteric regulation and covalent modification. The activity of this enzyme is inhibited by high levels of intracellular glucose-6-phosphate (G6P) and activated by the binding of glycogen or proteins that bind to glycogen, such as glycogenin. Phosphorylation of glycogen synthase by protein kinases, like glycogen synthase kinase-3 (GSK3), also reduces its activity, while dephosphorylation by protein phosphatases enhances it.
The regulation of glycogen synthase is critical for maintaining glucose homeostasis and energy balance in the body. Dysregulation of this enzyme has been implicated in several metabolic disorders, including type 2 diabetes and non-alcoholic fatty liver disease (NAFLD).
Hypoglycemia is a medical condition characterized by an abnormally low level of glucose (sugar) in the blood. Generally, hypoglycemia is defined as a blood glucose level below 70 mg/dL (3.9 mmol/L), although symptoms may not occur until the blood sugar level falls below 55 mg/dL (3.0 mmol/L).
Hypoglycemia can occur in people with diabetes who are taking insulin or medications that increase insulin production, as well as those with certain medical conditions such as hormone deficiencies, severe liver illnesses, or disorders of the adrenal glands. Symptoms of hypoglycemia include sweating, shaking, confusion, rapid heartbeat, and in severe cases, loss of consciousness or seizures.
Hypoglycemia is typically treated by consuming fast-acting carbohydrates such as fruit juice, candy, or glucose tablets to rapidly raise blood sugar levels. If left untreated, hypoglycemia can lead to serious complications, including brain damage and even death.
I'm happy to help! However, it seems there might be a bit of confusion here. Starch is not typically considered a medical term, but rather a nutritional and biochemical concept. Here's a brief explanation:
Starch is a complex carbohydrate that serves as the primary form of energy storage in plants. It is made up of long chains of glucose molecules and can be found in various foods such as grains, legumes, fruits, and vegetables. Amylase, an enzyme present in our saliva and digestive system, helps break down starch into simpler sugars during the digestion process so that our bodies can absorb them for energy.
I hope this clarifies any confusion! If you have any other questions or need further information on a medical topic, please don't hesitate to ask.
The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:
1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.
Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.
A dependovirus, also known as a dependent adenovirus or satellite adenovirus, is a type of virus that requires the presence of another virus, specifically an adenovirus, to replicate. Dependoviruses are small, non-enveloped viruses with a double-stranded DNA genome. They cannot complete their replication cycle without the help of an adenovirus, which provides necessary functions for the dependovirus to replicate.
Dependoviruses are clinically significant because they can cause disease in humans, particularly in individuals with weakened immune systems. In some cases, dependoviruses may also affect the severity and outcome of adenovirus infections. However, it is important to note that not all adenovirus infections are associated with dependovirus co-infections.
Genetic therapy, also known as gene therapy, is a medical intervention that involves the use of genetic material, such as DNA or RNA, to treat or prevent diseases. It works by introducing functional genes into cells to replace missing or faulty ones caused by genetic disorders or mutations. The introduced gene is incorporated into the recipient's genome, allowing for the production of a therapeutic protein that can help manage the disease symptoms or even cure the condition.
There are several approaches to genetic therapy, including:
1. Replacing a faulty gene with a healthy one
2. Inactivating or "silencing" a dysfunctional gene causing a disease
3. Introducing a new gene into the body to help fight off a disease, such as cancer
Genetic therapy holds great promise for treating various genetic disorders, including cystic fibrosis, muscular dystrophy, hemophilia, and certain types of cancer. However, it is still an evolving field with many challenges, such as efficient gene delivery, potential immune responses, and ensuring the safety and long-term effectiveness of the therapy.
Amylopectin is a type of complex carbohydrate molecule known as a polysaccharide. It is a component of starch, which is found in plants and is a major source of energy for both humans and other animals. Amylopectin is made up of long chains of glucose molecules that are branched together in a bush-like structure.
Amylopectin is composed of two types of glucose chain branches: outer chains, which are made up of shorter, highly branched chains of glucose molecules; and inner chains, which are made up of longer, less branched chains. The branching pattern of amylopectin allows it to be digested and absorbed more slowly than other types of carbohydrates, such as simple sugars. This slower digestion and absorption can help to regulate blood sugar levels and provide sustained energy.
Amylopectin is found in a variety of plant-based foods, including grains, legumes, vegetables, and fruits. It is an important source of calories and energy for humans and other animals that consume these types of plants as part of their diet.
Glycogen storage disease type II
Liver disease
Acid alpha-glucosidase
Medical genetics
Joannes Cassianus Pompe
Glucose 6-phosphatase
Α-Glucosidase
Glycogen storage disease type I
Glycogen storage disease type III
Glycogen storage disease type IV
Kocher-Debre-Semelaigne syndrome
Hypotonia
John Crowley (biotech executive)
Henri Termeer
Avalglucosidase alfa
Cipaglucosidase alfa
Macroglossia
Pompe
List of MeSH codes (C10)
Chromosome 17
Lysosomal storage disease
List of MeSH codes (C18)
William Canfield
Alglucosidase alfa
Finnish Lapphund
Miglustat
Restrictive cardiomyopathy
Glucose-6-phosphate exchanger SLC37A4
Hoffmann syndrome
Type 2
Glycogen storage disease type II - Wikipedia
Type II Glycogen Storage Disease (Pompe Disease): Practice Essentials, Background, Pathophysiology
Genetics of Glycogen-Storage Disease Type II (Pompe Disease) Medication: Enzyme replacement, Pharmacologic Chaperones
Biochemical and molecular investigation of two Korean patients with glycogen storage disease type III
Type II Glycogen Storage Disease (Pompe Disease): Practice Essentials, Background, Pathophysiology
Glycogen storage disease type II (Pompe disease)
Type II Glycogen Storage Disease (Pompe Disease) Differential Diagnoses
Glycogen storage disease type II (NORD): Video | Osmosis
Type II Glycogen Storage Disease (Pompe Disease): Practice Essentials, Background, Pathophysiology
A glycogen storage disease type 1a patient with type 2 diabetes | BMC Medical Genomics | Peer Review
Pompe disease: MedlinePlus Genetics
Genotype-phenotype correlation in two frequent mutations and mutation update in type III glycogen storage disease. | Read by...
Correction of glycogen storage disease type II by enzyme replacement with a recombinant human acid maltase produced by over...
Wilson Disease Differential Diagnoses
Gene Therapy for Pompe Disease: The Time is now
BNIP3 Is Involved in Muscle Fiber Atrophy in Late-Onset Pompe Disease Patients
Information of NSP Disorders - Delaware Health and Social Services - State of Delaware
Hepatocellular carcinoma: A comprehensive review
Glycogen Storage Disorders Panel, Sequencing | Test Fact Sheet
Newborn Screening Program Disorders | South Dakota Department of Health
Newborn Screening in Unselected Children Using Genomic Sequencing | Research Square
Mary-Alice Abbott's research topics | Profiles RNS
Italian Dermatological Treatment Analysis & Statistics
These highlights do not include all the information needed to use MYOZYME safely and effectively. See full prescribing...
KoreaMed
Jeffrey E. Pessin - Publications - Albert Einstein College of Medicine
Department of Exercise Science - Research output - Experts@Syracuse
Department of Exercise Science - Research output - Experts@Syracuse
Milap Sandhu - Research Output - Northwestern Scholars
Family Medicine and Community Health (Twin Cities) - Research output - Experts@Minnesota
Called Pompe disease1
- Glycogen storage disease type II, also called Pompe disease, and formerly known as GSD-IIa. (wikipedia.org)
Pompe62
- GSD-II and Danon disease are the only glycogen storage diseases with a defect in lysosomal metabolism, and Pompe disease was the first glycogen storage disease to be identified, in 1932 by the Dutch pathologist J. C. Pompe. (wikipedia.org)
- Pompe disease (type II glycogen storage disease) is an inherited enzyme defect that usually manifests in childhood. (medscape.com)
- Although at least 14 unique GSDs are discussed in the literature, the 4 that cause clinically significant muscle weakness are Pompe disease (GSD type II, acid maltase deficiency ), Cori disease ( GSD type III , debranching enzyme deficiency), McArdle disease ( GSD type V , myophosphorylase deficiency), and Tarui disease ( GSD type VII , phosphofructokinase deficiency). (medscape.com)
- These inherited enzyme defects usually manifest in childhood, although some, such as McArdle disease and Pompe disease, have separate adult-onset forms. (medscape.com)
- Pompe disease). (medscape.com)
- Enzyme replacement therapies are available for all age groups (ie, infantile [early onset] or late onset [juvenile/adult]) affected by Pompe disease. (medscape.com)
- Replaces rhGAA, which is deficient or lacking in persons with Pompe disease. (medscape.com)
- Myozyme has been shown to improve ventilator-free survival in patients with infantile-onset Pompe disease compared with untreated historical controls. (medscape.com)
- It has not been adequately studied for treatment of other forms of Pompe disease. (medscape.com)
- Lumizyme is indicated for infantile-onset Pompe disease and also for late (non-infantile) Pompe disease. (medscape.com)
- Indicated for treatment of patients aged 1 year and older with late-onset Pompe disease. (medscape.com)
- Indicated in combination with miglustat (Opfolda) for adults with late-onset Pompe disease (lysosomal acid alpha-glucosidase [GAA] deficiency) who weigh ≥40 kg and are not improving on their current enzyme replacement therapy (ERT). (medscape.com)
- Pompe disease: early diagnosis and early treatment make a difference. (medscape.com)
- Clinical features and predictors for disease natural progression in adults with Pompe disease: a nationwide prospective observational study. (medscape.com)
- A French multicenter Phase 4 open label extension study of long -term safety and efficacy in patients with Pompe disease who previously participated in avalglucosidase development studies in France. (institut-myologie.org)
- Pompe disease , also called glycogen storage disease type II, is a genetically inherited condition caused by insufficient functioning of an enzyme called lysosomal acid alpha-1,4-glucosidase, or just acid alpha-glucosidase, and it's caused by a mutation of the GAA gene. (osmosis.org)
- In Pompe disease , a mutation of the GAA gene prevents the production of enough functional acid alpha-glucosidase, and as a result, lysosomes can't break down glycogen . (osmosis.org)
- In individuals with Pompe, glycogen mostly accumulates in the lysosomes of those cells. (osmosis.org)
- Pompe disease is an autosomal recessive condition - so in other words, both parents must be carriers. (osmosis.org)
- Jeffrey S. FDA Expands Approval of Pompe Disease Drug. (medscape.com)
- Diagnostic efficacy of the fluorometric determination of enzyme activity for Pompe disease from dried blood specimens compared with lymphocytes-possibility for newborn screening. (medscape.com)
- The new era of Pompe disease: advances in the detection, understanding of the phenotypic spectrum, pathophysiology, and management. (medscape.com)
- A cross-sectional single-centre study on Pompe disease in 42 German patients: Molecular analysis of the GAA gene, manifestation and genotype-phenotype correlations. (medscape.com)
- Oropharyngeal dysphagia in infants and children with infantile Pompe disease. (medscape.com)
- Phupong V, Shotelersuk V. Prenatal exclusion of Pompe disease by electron microscopy. (medscape.com)
- Pompe disease in infants: improving the prognosis by newborn screening and early treatment. (medscape.com)
- Newborn screening for Pompe disease: an update, 2011. (medscape.com)
- Ambrosino N, Confalonieri M, Crescimanno G, Vianello A, Vitacca M. The role of respiratory management of Pompe disease. (medscape.com)
- Angelini C, Nascimbeni AC, Semplicini C. Therapeutic advances in the management of Pompe disease and other metabolic myopathies. (medscape.com)
- Persistence of high sustained antibodies to enzyme replacement therapy despite extensive immunomodulatory therapy in an infant with Pompe disease: need for agents to target antibody-secreting plasma cells. (medscape.com)
- The FDA has approved the lysosomal glycogen-specific enzyme alglucosidase alfa ( Lumizyme ) for the treatment of infantile-onset Pompe disease, including in patients younger than age 8. (medscape.com)
- This approval eliminates previous restrictions on the drug's use to late (non-infantile) onset Pompe disease in patients 8 years of age and older. (medscape.com)
- Approval was based on new data demonstrating similarities between Lumizyme and Myozyme , which is already approved for use in younger patients, and on a study of 18 patients with infantile-onset Pompe disease that showed similar improvements in ventilator-free survival as patients treated with Myozyme . (medscape.com)
- Pompe disease is an inherited disorder caused by the buildup of a complex sugar called glycogen in the body's cells. (medlineplus.gov)
- Researchers have described three types of Pompe disease, which differ in severity and the age at which they appear. (medlineplus.gov)
- The classic form of infantile-onset Pompe disease begins within a few months of birth. (medlineplus.gov)
- If untreated, this form of Pompe disease leads to death from heart failure in the first year of life. (medlineplus.gov)
- The non-classic form of infantile-onset Pompe disease usually appears by age 1. (medlineplus.gov)
- The muscle weakness in this disorder leads to serious breathing problems, and most children with non-classic infantile-onset Pompe disease live only into early childhood. (medlineplus.gov)
- The late-onset type of Pompe disease may not become apparent until later in childhood, adolescence, or adulthood. (medlineplus.gov)
- Late-onset Pompe disease is usually milder than the infantile-onset forms of this disorder and is less likely to involve the heart. (medlineplus.gov)
- Most individuals with late-onset Pompe disease experience progressive muscle weakness, especially in the legs and the trunk, including the muscles that control breathing. (medlineplus.gov)
- Pompe disease affects about 1 in 40,000 people in the United States. (medlineplus.gov)
- Mutations in the GAA gene cause Pompe disease. (medlineplus.gov)
- This buildup damages organs and tissues throughout the body, particularly the muscles, leading to the progressive signs and symptoms of Pompe disease. (medlineplus.gov)
- Fukuda T, Roberts A, Plotz PH, Raben N. Acid alpha-glucosidase deficiency (Pompe disease). (medlineplus.gov)
- Pompe disease (PD) is caused by the deficiency of the lysosomal enzyme acid α-glucosidase (GAA), resulting in systemic pathological glycogen accumulation. (nih.gov)
- Late-onset Pompe disease (LOPD) is a rare genetic disorder produced by mutations in the GAA gene and is characterized by progressive muscle weakness. (nih.gov)
- These results open the door to potential new treatments targeting BNIP3 to reduce its deleterious effects on muscle fiber atrophy in Pompe disease. (nih.gov)
- MYOZYME ® (alglucosidase alfa) is a lysosomal glycogen-specific enzyme indicated for use in patients with Pompe disease (GAA deficiency). (nih.gov)
- MYOZYME has been shown to improve ventilator-free survival in patients with infantile-onset Pompe disease as compared to an untreated historical control, whereas use of MYOZYME in patients with other forms of Pompe disease has not been adequately studied to assure safety and efficacy. (nih.gov)
- Pompe disease (glycogen storage disease type II) is an autosomal recessive disorder caused by deficiency of acid-alpha-glucosidase (GAA) resulting in lysosomal glycogen accumulation in multiple tissue, particularly cardiac and skeletal. (koreamed.org)
- As Postdoc she developed innovative in vivo AAV gene therapy approaches based on liver gene transfer or multi-tissue gene expression to target the multi-organ manifestations of Pompe disease, a LSD that presents with neuromuscular impairment. (stanford.edu)
- to investigate nursing team knowledge and practices regarding care for children with Pompe disease in intensive care. (bvsalud.org)
- Pompe en cuidados intensivos. (bvsalud.org)
- Pompe Disease (PD) was discovered in 1932 by pathologist Joannes Cassianus Pompe, during the autopsy of a seven-month-old child who died from idiopathic myocardial hypertrophy. (bvsalud.org)
- In Pompe disease, the concentration of a tetrasaccharide, consisting of four glucose residues, is reputedly increased in urine and plasma, but faster and more sensitive methods are required for the analysis of this, and other oligosaccharides, from biologic fluids. (uhi.ac.uk)
- 10-year Global therapeutic forecast for BMN701 (reveglucosidase alfa) indicated for Glycogen Storage Disease Type 2 (Pompe Disease). (blueprintorphan.com)
- The treatment of Pompe disease. (blueprintorphan.com)
- Vascular involvement in Late Onset Pompe Disease, glycogen storage disease type II characterized by limb-girdle muscle and diaphragmatic weakness, is well documented. (bvsalud.org)
- N-Butyl-l-deoxynojirimycin (l-NBDNJ): Synthesis of an Allosteric Enhancer of α-Glucosidase Activity for the Treatment of Pompe Disease. (ox.ac.uk)
- l-NBDNJ is able to enhance lysosomal α-glucosidase levels in Pompe disease fibroblasts, either when administered singularly or when coincubated with the recombinant human α-glucosidase. (ox.ac.uk)
Deficiency9
- It is caused by an accumulation of glycogen in the lysosome due to deficiency of the lysosomal acid alpha-glucosidase enzyme. (wikipedia.org)
- The deficiency of this enzyme results in the accumulation of structurally normal glycogen in lysosomes and cytoplasm in affected individuals. (wikipedia.org)
- Enzyme deficiency results in glycogen accumulation in tissues. (medscape.com)
- One form, Von Gierke disease ( GSD type Ia , glucose-6-phosphatase deficiency ), causes clinically significant end-organ disease with significant morbidity. (medscape.com)
- Acid maltase deficiency is a unique glycogenosis in that the glycogen accumulation is lysosomal rather than in the cytoplasm. (medscape.com)
- Glycogen storage disease type II: acid alpha-glucosidase (acid maltase) deficiency. (medscape.com)
- Glycogen storage disease type III (GSD-III) is an inborn error of glycogen metabolism caused by a deficiency of the glycogen debranching enzyme, amylo-1,6-glucosidase,4-α-glucanotransferase (AGL). (degruyter.com)
- Deficiency of glycogen debranching enzyme (AGL) activity causes glycogen storage disease type III (GSD-III). (qxmd.com)
- Gaucher's disease, also known as glucocerebrosidase deficiency, is an autosomal recessive disease that affects about 1 in 20,000 live births. (medscape.com)
Accumulation of glycogen1
- LOPD muscle biopsies show accumulation of glycogen along with the autophagic vacuoles associated with atrophic muscle fibers. (nih.gov)
Lysosomes5
- Excessive glycogen storage within lysosomes may interrupt normal functioning of other organelles and lead to cellular injury. (wikipedia.org)
- It binds to mannose-6-phosphate receptors and then is transported into lysosomes, then undergoes proteolytic cleavage that results in increased enzymatic activity and ability to cleave glycogen. (medscape.com)
- Now for some reason, and it's not really understood why, but small amounts of glycogen end up in the lysosomes, where it's broken down by an enzyme called acid alpha-glucosidase, to release glucose from the glycogen chain. (osmosis.org)
- This leads to a buildup of glycogen within the cytoplasm and lysosomes, and that leads to cellular damage and destruction. (osmosis.org)
- Mutations in the GAA gene prevent acid alpha-glucosidase from breaking down glycogen effectively, which allows this sugar to build up to toxic levels in lysosomes. (medlineplus.gov)
Metabolism2
- Glycogen storage diseases (GSDs) are a group of inborn errors of metabolism, typically caused by enzyme defects, resulting in a buildup of glycogen in the liver, muscles, and other organs. (arupconsult.com)
- that occur when there is a defect in the enzymes that are involved in the metabolism of glycogen, often resulting in growth abnormalities, weakness, a large liver, low blood sugar, and confusion. (msdmanuals.com)
Metabolic diseases2
- [1] When glycogen breakdown is compromised by mutations in the glycogen debranching enzyme, metabolic diseases such as Glycogen storage disease type III can result. (wikidoc.org)
- Dr. Timothy M. Cox of Addenbrooke's Hospital Cambridge, U.K., an expert in metabolic diseases, told Reuters Health by email, "While the ICGG Registry is comprehensive, like nearly all company registries (it has) are 'holes' and 'gaps. (medscape.com)
Muscles4
- The build-up of glycogen causes progressive muscle weakness (myopathy) throughout the body and affects various body tissues, particularly in the heart, skeletal muscles, liver and the nervous system. (wikipedia.org)
- This results in glycogen accumulation in tissues, especially muscles, and impairs their ability to function normally. (medscape.com)
- Any glucose that is not used immediately for energy is held in reserve in the liver, muscles, and kidneys in the form of glycogen and is released when needed by the body. (msdmanuals.com)
- Together with phosphorylases , debranching enzymes mobilize glucose reserves from glycogen deposits in the muscles and liver. (wikidoc.org)
GSDs3
- Glycogen storage diseases (GSDs) are inherited glycogen metabolic disorders which have various subtypes. (biomedcentral.com)
- GSDs of type I, III, IV, VI, and IX show liver involvement and are considered as hepatic types of GSDs. (biomedcentral.com)
- Glycogen storage diseases (GSDs) refer to a group of inherited disorders caused by the absence of essential enzymes in the synthesis or degradation of glycogen [ 1 , 2 ]. (biomedcentral.com)
Genetic8
- Frequency of glycogen storage disease type II in The Netherlands: implications for diagnosis and genetic counselling. (medscape.com)
- Follow-up of the three families confirmed that one child was diagnosed with PKU and two children with GJB2 variants were scheduled to undergo hearing loss testing every six months after genetic counceling due to the nature of incomplete penetrance of hearing loss. (researchsquare.com)
- Currently, testing for other diseases such as Spinal Muscular Atrophy (SMA) is being implemented and additional conditions are being considered for national genetic screening of newborns. (researchsquare.com)
- To analyze a wide variety of polymorphisms in patients with endometriosis is important since this disease has a strong genetic component. (koreamed.org)
- Dr. Colella is committed to researching innovative ways to combat genetic diseases and making a positive impact on the lives of patients. (stanford.edu)
- The two companies have partnered for the purpose of helping each company provide its genetic tests to a larger market. (familytree.com)
- Although Gaucher's disease is pan-ethnic, type 1 is the most common inherited Jewish genetic disease. (medscape.com)
- We're looking at five different products that have been approved by the FDA, which is pretty impressive in the grand scheme of genetic diseases. (medscape.com)
Degradation2
- The protein is an enzyme that normally degrades the alpha -1,4 and alpha -1,6 linkages in glycogen, maltose and isomaltose and is required for the degradation of 1-3% of cellular glycogen. (wikipedia.org)
- It is caused by deficient activity of glycogen debranching enzyme, which is a key enzyme in glycogen degradation. (qxmd.com)
Disorders3
- there are many types and subtypes, and other disorders may have overlapping phenotypes. (arupconsult.com)
- Glycogen and lysosomal storage diseases, fatty acid oxidation disorders, and urea cycle disorders are represented among others. (geneticpassport.org)
- The development of therapies for lysosomal storage disorders has created a need for biochemical markers to monitor the efficacy of therapy and methods to quantify these markers in biologic samples. (uhi.ac.uk)
Autosomal1
- Maple syrup urine disease (MSUD) is rare autosomal recessive metabolic disorder caused by the dysfunction of the mitochondrial branched-chain 2-ketoacid dehydrogenase (BCKD) enzyme complex leading to massive accumulation of branched-chain amino acids and 2-keto acids. (stanford.edu)
Congenital Heart D1
- Congenital Heart Disease Croatia InTech Publishing. (westminster.ac.uk)
20191
- CV004 trade name] may also be used in the treatment of coronavirus disease 2019 (COVID-19) in adult and adolescent patients (aged 12 years and older with body weight of at least 40 kg) who require supplemental oxygen therapy. (who.int)
Genes7
- 61 Mendelian Diseases, 151 Primary Immunodeficiency Diseases(PID) and 5 DPWG recommeded Essential pharmacogenetic(PGx) genes were analyzed. (researchsquare.com)
- The results suggest that using GS may be a suitable method for screening newborns for variants in a large number of disease associated genes. (researchsquare.com)
- Different methods for identification of mutated genes, including Targeted Region Sequencing (TRS), ES and GS, is currently standard procedure in newborn children with a suspected disease. (researchsquare.com)
- 5 kb) genes in the retina for treating Stargardt disease and Usher Syndrome type I B, both of which cause untreatable forms of blindness. (stanford.edu)
- We and others have tested AAV gene therapy in mice for two of the three genes involved in MSUD, BCKDHA and DBT. (stanford.edu)
- Genes Genes are segments of deoxyribonucleic acid (DNA) that contain the code for a specific protein that functions in one or more types of cells in the body or the code for functional ribonucleic. (msdmanuals.com)
- J Mol Diag 2021 23:1501-1506 external icon ) ClinGen Variant Curation Expert Panels nominated 546 pathogenic and difficult to detect variants ( link to table of variants excel icon ) in 84 disease-associated genes ( link to table of genes word icon ). (cdc.gov)
Biochemical1
- Biochemical and molecular investigation of two Korean patients with glycogen storage disease type III" Clinical Chemistry and Laboratory Medicine , vol. 46, no. 9, 2008, pp. 1245-1249. (degruyter.com)
Mutations3
- Genotype-phenotype correlation in two frequent mutations and mutation update in type III glycogen storage disease. (qxmd.com)
- Here we report two frequent mutations, each of which was found in the homozygous state in multiple patients, and each of which was associated with a subset of clinical phenotype in those patients with that mutation. (qxmd.com)
- These two mutations together account for more than 12% of the molecular defects in the GSD-III patients tested. (qxmd.com)
Alpha-glucosidase2
- citation needed] The disease is caused by a mutation in a gene (acid alpha-glucosidase: also known as acid maltase) on long arm of chromosome 17 at 17q25.2-q25.3 (base pair 75,689,876 to 75,708,272). (wikipedia.org)
- Lin CY, Hwang B, Hsiao KJ, Jin YR. Pompe's disease in Chinese and prenatal diagnosis by determination of alpha-glucosidase activity. (medscape.com)
Genetics3
- Kieffer DA, Medici V. Wilson disease: at the crossroads between genetics and epigenetics-A review of the evidence. (medscape.com)
- Dr. Colella received her summa cum laude Bachelor of Science degree in Biology from the University of Naples Federico II (Italy) and her PhD in Human Genetics from The Open University (UK) at the Telethon Institute of Genetics and Medicine (TIGEM, Italy). (stanford.edu)
- 2. Provide specialty medical service professionals in the areas of Endocrinology, Pulmonology, Hematology, Immunology/Infectious Disease, Cardiology and Metabolic/Genetics. (uky.edu)
Enzymes9
- The enzymes affected normally catalyze reactions that ultimately convert glycogen compounds to monosaccharides, of which glucose is the predominant component. (medscape.com)
- Glucosyltransferase and glucosidase are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in E. coli and other bacteria, complicating nomenclature. (wikidoc.org)
- Proteins that catalyze both functions are referred to as glycogen debranching enzymes (GDEs). (wikidoc.org)
- When glucosyltransferase and glucosidase are catalyzed by distinct enzymes, "glycogen debranching enzyme" usually refers to the glucosidase enzyme . (wikidoc.org)
- Together with phosphorylase , glycogen debranching enzymes function in glycogen breakdown and glucose mobilization. (wikidoc.org)
- Glycogen debranching enzymes assist phosphorylase, the primary enzyme involved in glycogen breakdown , mobilize glycogen stores. (wikidoc.org)
- Thus the debranching enzymes, transferase and α-1,6- glucosidase converts the branched glycogen structure into a linear one, paving the way for further cleavage by phosphorylase. (wikidoc.org)
- In E. coli and other bacteria, glucosyltransferase and glucosidase functions are performed by two distinct enzymes. (wikidoc.org)
- [10] Activity of the two enzymes is not always necessarily coupled. (wikidoc.org)
Diagnosis10
- Merle U, Schaefer M, Ferenci P, Stremmel W. Clinical presentation, diagnosis and long-term outcome of Wilson's disease: a cohort study. (medscape.com)
- Diagnosis and treatment of Wilson disease: an update. (medscape.com)
- Schilsky ML. Wilson disease: diagnosis, treatment, and follow-up. (medscape.com)
- The disease diagnosis and treatment segment embodies an indispensable component of global healthcare systems. (reportlinker.com)
- Glycogen storage disease type III diagnosis and management guidelines. (qxmd.com)
- This guideline for the management of glycogen storage disease type III was developed as an educational resource for health care providers to facilitate prompt and accurate diagnosis and appropriate management of patients. (qxmd.com)
- This management guideline specifically addresses evaluation and diagnosis across multiple organ systems (cardiovascular, gastrointestinal/nutrition, hepatic, musculoskeletal, and neuromuscular) involved in glycogen storage disease type III. (qxmd.com)
- A guideline that will facilitate the accurate diagnosis and appropriate management of individuals with glycogen storage disease type III was developed. (qxmd.com)
- This guideline will help health care providers recognize patients with all forms of glycogen storage disease type III, expedite diagnosis, and minimize stress and negative sequelae from delayed diagnosis and inappropriate management. (qxmd.com)
- However, they add, "the interval between diagnosis and initiation of ERT has decreased, most strikingly in pediatric patients who have the most severe disease. (medscape.com)
Pathological1
- Bijvoet AG, Van Hirtum H, Vermey M. Pathological features of glycogen storage disease type II highlighted in the knockout mouse model. (medscape.com)
Mutation1
- The H1069Q mutation in ATP7B is associated with late and neurologic presentation in Wilson disease: results of a meta-analysis. (medscape.com)
Acid2
- secrets pile acid (a yellowish-green liquid sap) which help digestion, in particular, digest fat, convert glucose to glycogen and store it, produce urea, makes amino acids, filter harmful substances in the blood (such as alcohol, chemicals, poisons) and stores some vitamins & minerals. (gastrodigestivesystem.com)
- It is thought to proceed through a two step acid base assistance type mechanism, with an oxocarbenium ion intermediate, and retention of configuration in glucose. (wikidoc.org)
Cirrhosis1
- Specific medical therapies may be applied to many liver diseases in an effort to diminish symptoms and to prevent or forestall the development of cirrhosis. (medscape.com)
Cleave1
- Phosphorylase can only cleave α-1,4- glycosidic bond between adjacent glucose molecules in glycogen but branches exist as α-1,6 linkages. (wikidoc.org)
Alglucosidase alfa1
- Enzyme replacement therapy with alglucosidase alfa in 44 patients with late-onset glycogen storage disease type 2: 12-month results of an observational clinical trial. (medscape.com)
Cytoplasm1
- Now, normally, glycogen is found in the largest amounts in the cytoplasm of liver cells and all three types of muscle cell . (osmosis.org)
Skeletal5
- PD can present with cardiac, skeletal muscle, and central nervous system manifestations, as a continuum of phenotypes among two main forms: classical infantile-onset PD (IOPD) and late-onset PD (LOPD). (nih.gov)
- Glycogen storage disease type III is a rare disease of variable clinical severity affecting primarily the liver, heart, and skeletal muscle. (qxmd.com)
- Those with type IIIa have symptoms related to liver disease and progressive muscle (cardiac and skeletal) involvement that varies in age of onset, rate of disease progression, and severity. (qxmd.com)
- As Dr. Pramod K. Mistry told Reuters Health by email, "Prior to the introduction of alglucerase/imiglucerase enzyme-replacement therapy for Gaucher disease type 1, patients tended to have had prior splenectomy and destructive skeletal complications, such as bone crises and avascular necrosis. (medscape.com)
- After nearly two decades since the introduction of imiglucerase," he added, "the new generation of patients are rarely splenectomized and the prevalence of disabling skeletal complications is strikingly lower. (medscape.com)
Proteins1
- Carbohydrates Carbohydrates, proteins, and fats are the main types of macronutrients in food (nutrients that are required daily in large quantities). (msdmanuals.com)
Clinical5
- Here, we describe two unrelated Korean patients with GSD-III and review their clinical and laboratory findings. (degruyter.com)
- Soni D, Shukla G, Singh S, Goyal V, Behari M. Cardiovascular and sudomotor autonomic dysfunction in Wilson's disease--limited correlation with clinical severity. (medscape.com)
- Journal of Clinical Neuromuscular Disease. (elsevierpure.com)
- Glycogen storage disease type III manifests a wide clinical spectrum. (qxmd.com)
- The patient should be observed closely for signs that the dose may need to be altered, such as changes in clinical status resulting from disease remissions or exacerbations. (who.int)
Gaucher2
- NEW YORK (Reuters Health) - Alglucerase/imiglucerase enzyme-replacement therapy (ERT) has reduced the need for potentially harmful procedures in patients with Gaucher disease type 1, according to registry data. (medscape.com)
- The Ashkenazi Jewish Panel includes the following diseases: Bloom syndrome, Canavan disease, Fanconi anemia type C, familial dysautonomia, Gaucher disease, glycogen storage disease type 1a, Mucolipidosis IV, Neimann-Pick disease, and Tay-Sachs disease. (cdc.gov)
20211
- The present retrospective study aimed to evaluate the long-term outcomes of eight patients with GSD types I, III, and IV who underwent LT in the affiliated hospitals of Shiraz University of Medical Sciences, from March 2013 to June 2021. (biomedcentral.com)
Gene8
- This means the defective gene is located on an autosome, and two faulty copies of the gene-one from each parent-are required to be born with the disorder. (wikipedia.org)
- Correction of glycogen storage disease type 1a in a mouse model by gene therapy. (medscape.com)
- Stuehler B, Reichert J, Stremmel W, Schaefer M. Analysis of the human homologue of the canine copper toxicosis gene MURR1 in Wilson disease patients. (medscape.com)
- GAA gene transfer with adeno-associated virus (AAV) vectors has been shown to reduce glycogen storage and improve the PD phenotype in preclinical studies following different approaches. (nih.gov)
- Here, we present an overview of the different gene therapy approaches for PD, focusing on in vivo gene transfer with AAV vectors and discussing the potential opportunities and challenges in developing safe and effective gene therapies for the disease. (nih.gov)
- Dr. Pasqualina Colella is a scientist with extensive expertise in cell therapy and gene therapy approaches for the treatment of inherited diseases. (stanford.edu)
- 532 disease terms (MeSH) has been reported with ACE gene. (cdc.gov)
- Because usually two copies of the abnormal gene are necessary for the disorder to occur, usually neither parent has the disorder. (msdmanuals.com)
Cardiac2
- At the opportunity, the pathologist visualized glycogen accumulation in vesicles inside the cardiac fibers1. (bvsalud.org)
- OBJECTIVE: Infantile Pompe's disease is a lethal cardiac and muscular disorder. (omeka.net)
Organs1
- it resulted in accelerated disease in bone and in other organs as well as life-threatening complications such as pulmonary hypertension. (medscape.com)
Liver disease3
- Copper: its role in the pathogenesis of liver disease. (medscape.com)
- Those with type IIIb primarily have symptoms related to liver disease. (qxmd.com)
- Other individuals have a multitude of the most severe symptoms of end-stage liver disease and a limited chance for survival. (medscape.com)
Glucose residues2
- When phosphorylase has digested a glycogen branch down to four glucose residues, it will not remove further residues. (wikidoc.org)
- 4-α-D-glucanotransferase ( EC 2.4.1.25 ), or glucosyltransferase , transfers three glucose residues from the four-residue glycogen branch to a nearby branch. (wikidoc.org)
Homocystinuria1
- 121 Mendelian pathogenic or likely pathogenic variants associated with 31 inherited diseases were detected, among these hearing loss, congenital hypothyroidism, methylmalonic acidemia, methylmalonic acidemia with homocystinuria, phenylketonuria(PKU) and benign hyperphenylalaninemia accounted for half of the carrier variants. (researchsquare.com)
Accumulates1
- The disease occurs when the lipid glucosylceramide accumulates in the bone marrow, lungs, spleen, liver, and sometimes the brain. (medscape.com)