Glycogen Storage Disease Type V
Glycogen Storage Disease Type I
Glycogen Storage Disease Type III
Glycogen Storage Disease
Glycogen Storage Disease Type IV
Glycogen Storage Disease Type II
Glycogen Storage Disease Type VII
Glucose-6-Phosphatase
Glycogen Storage Disease Type VI
Glycogen
alpha-Glucosidases
Glycogen Debranching Enzyme System
Glycogen Storage Disease Type VIII
Glucan 1,4-alpha-Glucosidase
Antiporters
Glucose-6-Phosphate
1,4-alpha-Glucan Branching Enzyme
Glycogen Storage Disease Type IIb
Fructose-1,6-Diphosphatase Deficiency
Enzyme Replacement Therapy
Monosaccharide Transport Proteins
Lysosomal Storage Diseases
Glycogen Synthase
Hypoglycemia
Starch
Liver
Collagen Type V
Dependovirus
Genetic Therapy
Polymorphism, Single-Stranded Conformational
Uric Acid
Enterocolitis
Cholesterol Ester Storage Disease
Exons
Glycogen Phosphorylase
Genetic Vectors
Mutation
Charcot-Marie-Tooth Disease
Molecular Sequence Data
McArdle's disease. The unsolved mystery of the reappearing enzyme. (1/44)
We assessed the frequency of muscle fibers showing histochemical phosphorylase activity in 27 muscle biopsies from 25 unrelated patients with McArdle's disease and studied by immunohistochemistry and in situ hybridization whether the muscle-specific isoform was expressed. Positive phosphorylase fibers were observed in 19% of our series of biopsies. We show that the enzyme isoform expressed in regenerating fibers differs according to the genotype of patients: the muscle-specific isoform is transcribed and translated in patients with none of the described mutations in at least one allele of the myophosphorylase gene, whereas it is neither transcribed nor translated in patients with identified mutations in both alleles. (+info)Rhabdomyolysis triggered by an asthmatic attack in a patient with McArdle disease. (2/44)
We describe a patient with McArdle disease who developed rhabdomyolysis triggered by a bronchial asthmatic attack. A 64-year-old man had chronic pulmonary emphysema with asthma, and an asthmatic attack led to severe rhabdomyolysis that required continuous hemodiafiltration. After 2 years, a physical examination revealed atrophy of the extremities compared with previous examinations, especially of the intercostal muscles. During that time, he suffered two severe bronchial asthmatic attacks. His serum level of creatinine kinase remained between 4,000 and 7,000 IU/l when he did not suffer from asthmatic attacks and rhabdomyolysis had abated. Therefore, we suspected that his recent muscle atrophy was caused by asthmatic attacks, and discussed the possibility of his respiratory muscle weakness due to McArdle disease in relation to his severe bronchial asthmatic attacks as well as chronic obstructive pulmonary disease. (+info)The exercise metaboreflex is maintained in the absence of muscle acidosis: insights from muscle microdialysis in humans with McArdle's disease. (3/44)
1. In McArdle's disease, muscle glycogenolysis is blocked, which results in absent lactate and enhanced ammonia production in working muscle. Using McArdle patients as an experimental model, we studied whether lactate and ammonia could be mediators of the exercise pressor reflex. 2. Changes in muscle interstitial ammonia and lactate were compared with changes in blood pressure and muscle sympathetic nerve activity (MSNA) during static arm flexor exercise at 30% of maximal contraction force. Muscle interstitial changes in lactate and ammonia were assessed by microdialysis of the biceps muscle, and MSNA by peroneal nerve microneurography, in six McArdle patients and 11 healthy, matched controls. One McArdle patient also had myoadenylate deaminase deficiency, a condition associated with abolished ammonia production in exercise. 3. Exercise-induced increases were higher in McArdle patients vs. controls for MSNA (change of 164 +/- 71 vs. 59 +/- 19%) and blood pressure (change of 47 +/- 7 vs. 38 +/- 4 mmHg). Interstitial lactate increased in controls (peak change 1.3 +/- 0.2 mmol x l(-1)) and decreased in McArdle patients (peak change -0.5 +/- 0.1 mmol x l(-1)) during and after exercise. Interstitial ammonia did not change during exercise in either group, but was higher post-exercise in McArdle patients, except in the patient with myoadenylate deaminase deficiency who had a flat ammonia response. This patient had an increase in MSNA and blood pressure comparable to other patients. MSNA and blood pressure responses were maintained during post-exercise ischaemia in both groups, indicating that sympathetic activation was caused, at least partly, by a metaboreflex. 4. In conclusion, changes in muscle interstitial lactate and ammonia concentrations during and after exercise are temporally dissociated from changes in MSNA and blood pressure in both patients with McArdle's disease and healthy control subjects. This suggests that muscle acidification and changes in interstitial ammonia concentration are not mediators of sympathetic activation during exercise. (+info)Decreased insulin action in skeletal muscle from patients with McArdle's disease. (4/44)
Insulin action is decreased by high muscle glycogen concentrations in skeletal muscle. Patients with McArdle's disease have chronic high muscle glycogen levels and might therefore be at risk of developing insulin resistance. In this study, six patients with McArdle's disease and six matched control subjects were subjected to an oral glucose tolerance test and a euglycemic-hyperinsulinemic clamp. The muscle glycogen concentration was 103 +/- 45% higher in McArdle patients than in controls. Four of six McArdle patients, but none of the controls, had impaired glucose tolerance. The insulin-stimulated glucose utilization and the insulin-stimulated increase in glycogen synthase activity during the clamp were significantly lower in the patients than in controls (51.3 +/- 6.0 vs. 72.6 +/- 13.1 micromol x min(-1) x kg lean body mass(-1), P < 0.05, and 53 +/- 15 vs. 79 +/- 9%, P < 0.05, n = 6, respectively). The difference in insulin-stimulated glycogen synthase activity between the pairs was significantly correlated (r = 0.96, P < 0.002) with the difference in muscle glycogen level. The insulin-stimulated increase in Akt phosphorylation was smaller in the McArdle patients than in controls (45 +/- 13 vs. 76 +/- 13%, P < 0.05, respectively), whereas basal and insulin-stimulated glycogen synthase kinase 3alpha and protein phosphatase-1 activities were similar in the two groups. Furthermore, the ability of insulin to decrease and increase fat and carbohydrate oxidation, respectively, was blunted in the patients. In conclusion, these data show that patients with McArdle's glycogen storage disease are insulin resistant in terms of glucose uptake, glycogen synthase activation, and alterations in fuel oxidation. The data further suggest that skeletal muscle glycogen levels play an important role in the regulation of insulin-stimulated glycogen synthase activity. (+info)New parameters reducing the interindividual variability of metabolic changes during muscle contraction in humans. A (31)P MRS study with physiological and clinical implications. (5/44)
Interindividual variations in skeletal muscle metabolism make comparative analyses difficult. In this study, we have addressed the issue of capturing the variability of metabolic performance observed during muscle exercise in humans by using an original method of normalization.Metabolic changes induced by various kinds of exercise were investigated using 31P magnetic resonance spectroscopy (MRS) at 4.7 T in 65 normal subjects (23 women and 42 men) and 12 patients with biopsy-proven muscular disorders. Large variations in the extent of PCr breakdown and intracellular acidosis were recorded among subjects and exercise protocols. For all the data pooled, the amplitude of mechanical performance accounts for 50% of these variations. When scaled to the work output, variations of PCr consumption account for 65% of pH changes through a linear relationship. This linear relationship was substantially improved (90%) when both variables were scaled to the square of work output performed (P1 and P2). By capturing most of the initial interindividual variability (90%), P1 vs. P2 relationship represents an ideal standardization procedure, independent of any anthropometric measurements. This relationship also discloses a significant link between the extent of PCr breakdown and intracellular acidosis regardless of exercise protocol. Moreover, changes in the slope of the P1 vs. P2 regression curve, as measured in old subjects and in selected patients, directly reflect alterations of energy production in muscle. (+info)Role of 5'AMP-activated protein kinase in glycogen synthase activity and glucose utilization: insights from patients with McArdle's disease. (6/44)
It has been suggested that 5'AMP-activated protein kinase (AMPK) is involved in the regulation of glucose and glycogen metabolism in skeletal muscle. We used patients with chronic high muscle glycogen stores and deficient glycogenolysis (McArdle's disease) as a model to address this issue. Six McArdle patients were compared with control subjects during exercise. Muscle alpha2AMPK activity increased in McArdle patients (from 1.3 +/- 0.2 to 1.9 +/- 0.2 pmol min(-1) mg(-1), P = 0.05) but not in control subjects (from 1.0 +/- 0.1 to 1.3 +/- 0.3 pmol min(-1) mg(-1)). Exercise-induced phosphorylation of the in vivo AMPK substrate acetyl CoA carboxylase (ACCbeta; Ser(221)) was higher (P < 0.01) in McArdle patients than in control subjects (18 +/- 3 vs. 10 +/- 1 arbitrary units). Exercise-induced whole-body glucose utilization was also higher in McArdle patients than in control subjects (P < 0.05). No correlation between individual AMPK or ACCbeta values and glucose utilization was observed. Glycogen synthase (GS) activity was decreased in McArdle patients from 11 +/- 1.3 to 5 +/- 1.2 % (P < 0.05) and increased in control subjects from 19 +/- 1.6 to 23 +/- 2.3 % (P < 0.05) in response to exercise. This was not associated with activity changes of GS kinase 3 or protein phosphatase 1, but the changes in GS activity could be due to changes in activity of AMPK or protein kinase A (PKA) as a negative correlation between either ACCbeta phosphorylation (Ser(221)) or plasma adrenaline and GS activity was observed. These findings suggest that GS activity is increased by glycogen breakdown and decreased by AMPK and possibly PKA activation and that the resultant GS activity depends on the relative strengths of the various stimuli. Furthermore, AMPK may be involved in the regulation of glucose utilization during exercise in humans, although the lack of correlation between individual AMPK activity or ACCbeta phosphorylation (Ser(221)) values and individual glucose utilization during exercise implies that AMPK may not be an essential regulator. (+info)Reflex sympathetic activation during static exercise is severely impaired in patients with myophosphorylase deficiency. (7/44)
During static exercise, metabolites accumulate in the muscle interstitium where they stimulate chemosensitive afferent nerves that reflexly increase efferent muscle sympathetic nerve activity (MSNA) and blood pressure. In experimental animals, lactic acid potently stimulates the muscle metaboreflex, but its role in humans is more controversial. To determine if lactic acid is a critical mediator of metaboreflex activation in humans, we performed microelectrode recordings of MSNA in eight patients with myophosphorylase deficiency (McArdle's disease) who cannot metabolize intramuscular glycogen and do not generate lactic acid in exercising muscles. Each patient was matched with three healthy control subjects to maximize statistical power. In controls, 2 min of static handgrip performed at 33 % or 45 % of maximal voluntary contraction (MVC) produced intensity-dependent increases in MSNA (171 +/- 22 % and 379 +/- 95 %, respectively). In the patients, MSNA responses to static handgrip were markedly attenuated (33 +/- 14 % at 33 % MVC; 32 +/- 19 % at 45 % MVC; P < 0.05 vs. controls). Likewise, when static handgrip (30 % MVC) was performed to fatigue, MSNA increased by 366 +/- 73 % in controls but only by 51 +/- 14 % in patients (P < 0.05). Pressor responses to static handgrip were also attenuated in patients compared to controls, whereas heart rate responses were identical. In contrast to exercise, the MSNA responses to other reflex stimuli (the cold pressor test or Valsalva's manoeuvre) were similar in patients and controls. Together these data indicate that appropriate activation of glycogenolytic pathways is obligatory for normal metaboreflex-mediated sympathoexcitation during static exercise in humans. (+info)The effect of oral sucrose on exercise tolerance in patients with McArdle's disease. (8/44)
BACKGROUND: Energy metabolism in muscles relies predominantly on the breakdown of glycogen early in exercise. In patients with McArdle's disease, blocked glycogenolysis in muscles results in low exercise tolerance and can lead to muscle injury, particularly in the first minutes of exercise. We hypothesized that ingesting sucrose before exercise would increase the availability of glucose and would therefore improve exercise tolerance in patients with McArdle's disease. METHODS: In a single-blind, randomized, placebo-controlled crossover study, 12 patients with McArdle's disease drank 660 ml of a beverage that had been sweetened with artificial sweeteners (placebo) or with 75 g of sucrose after an overnight fast. Thirty to 40 minutes later, the patients rode a stationary bicycle at a constant workload for 15 minutes while the heart rate, level of perceived exertion, and venous blood glucose levels were monitored. RESULTS: Supplemental sucrose increased the mean plasma glucose level by more than 36 mg per deciliter (2.0 mmol per liter) and resulted in a marked improvement in exercise tolerance in all patients. The mean (+/-SE) heart rate dropped by a maximum of 34+/-3 beats per minute (P<0.001), and the level of perceived exertion fell dramatically when the patients ingested glucose as compared with when they received the placebo. CONCLUSIONS: This study suggests that the ingestion of sucrose before exercise can markedly improve exercise tolerance in patients with McArdle's disease. The treatment takes effect during the time when muscle injury commonly develops in these patients. In addition to increasing the patients' exercise capacity and sense of well-being, the treatment may protect against exercise-induced rhabdomyolysis. (+info)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 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.
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 (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.
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.
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 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.
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.
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.
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 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.
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.
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.
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.
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.
Collagen Type V is a specific type of collagen, which is a protein that provides structure and strength to connective tissues in the body. Collagen Type V is found in various tissues, including the cornea, blood vessels, and hair. It plays a crucial role in the formation of collagen fibers and helps regulate the diameter of collagen fibrils. Mutations in the genes that encode for Collagen Type V can lead to various connective tissue disorders, such as Ehlers-Danlos syndrome and osteogenesis imperfecta.
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.
Single-Stranded Conformational Polymorphism (SSCP) is not a medical condition but rather a laboratory technique used in molecular biology and genetics. It refers to the phenomenon where a single-stranded DNA or RNA molecule can adopt different conformations or shapes based on its nucleotide sequence, even if the difference in the sequence is as small as a single base pair change. This property is used in SSCP analysis to detect mutations or variations in DNA or RNA sequences.
In SSCP analysis, the denatured single-stranded DNA or RNA sample is subjected to electrophoresis on a non-denaturing polyacrylamide gel. The different conformations of the single-stranded molecules migrate at different rates in the gel, creating multiple bands that can be visualized by staining or other detection methods. The presence of additional bands or shifts in band patterns can indicate the presence of a sequence variant or mutation.
SSCP analysis is often used as a screening tool for genetic diseases, cancer, and infectious diseases to identify genetic variations associated with these conditions. However, it has largely been replaced by more sensitive and accurate methods such as next-generation sequencing.
Hepatomegaly is a medical term that refers to an enlargement of the liver beyond its normal size. The liver is usually located in the upper right quadrant of the abdomen and can be felt during a physical examination. A healthcare provider may detect hepatomegaly by palpating (examining through touch) the abdomen, noticing that the edge of the liver extends past the lower ribcage.
There are several possible causes for hepatomegaly, including:
- Fatty liver disease (both alcoholic and nonalcoholic)
- Hepatitis (viral or autoimmune)
- Liver cirrhosis
- Cancer (such as primary liver cancer, metastatic cancer, or lymphoma)
- Infections (e.g., bacterial, fungal, or parasitic)
- Heart failure and other cardiovascular conditions
- Genetic disorders (e.g., Gaucher's disease, Niemann-Pick disease, or Hunter syndrome)
- Metabolic disorders (e.g., glycogen storage diseases, hemochromatosis, or Wilson's disease)
Diagnosing the underlying cause of hepatomegaly typically involves a combination of medical history, physical examination, laboratory tests, and imaging studies like ultrasound, CT scan, or MRI. Treatment depends on the specific cause identified and may include medications, lifestyle changes, or, in some cases, surgical intervention.
Uric acid is a chemical compound that is formed when the body breaks down purines, which are substances that are found naturally in certain foods such as steak, organ meats and seafood, as well as in our own cells. After purines are broken down, they turn into uric acid and then get excreted from the body in the urine.
However, if there is too much uric acid in the body, it can lead to a condition called hyperuricemia. High levels of uric acid can cause gout, which is a type of arthritis that causes painful swelling and inflammation in the joints, especially in the big toe. Uric acid can also form crystals that can collect in the kidneys and lead to kidney stones.
It's important for individuals with gout or recurrent kidney stones to monitor their uric acid levels and follow a treatment plan prescribed by their healthcare provider, which may include medications to lower uric acid levels and dietary modifications.
Enterocolitis is a medical condition that involves inflammation of the small intestine (enteritis) and large intestine (colitis). This condition can affect people of all ages, but it is most commonly seen in infants and young children. The symptoms of enterocolitis may include diarrhea, abdominal cramps, bloating, nausea, vomiting, fever, and dehydration.
There are several types of enterocolitis, including:
1. Infectious Enterocolitis: This type is caused by a bacterial, viral, or parasitic infection in the intestines. Common causes include Salmonella, Shigella, Escherichia coli (E. coli), and norovirus.
2. Antibiotic-Associated Enterocolitis: This type is caused by an overgrowth of harmful bacteria in the intestines following the use of antibiotics that kill off beneficial gut bacteria.
3. Pseudomembranous Enterocolitis: This is a severe form of antibiotic-associated enterocolitis caused by the bacterium Clostridioides difficile (C. diff).
4. Necrotizing Enterocolitis: This is a serious condition that primarily affects premature infants, causing inflammation and damage to the intestinal tissue, which can lead to perforations and sepsis.
5. Ischemic Enterocolitis: This type is caused by reduced blood flow to the intestines, often due to conditions such as mesenteric ischemia or vasculitis.
6. Radiation Enterocolitis: This type occurs as a complication of radiation therapy for cancer treatment, which can damage the intestinal lining and lead to inflammation.
7. Eosinophilic Enterocolitis: This is a rare condition characterized by an excessive buildup of eosinophils (a type of white blood cell) in the intestinal tissue, leading to inflammation and symptoms similar to those seen in inflammatory bowel disease.
Treatment for enterocolitis depends on the underlying cause and severity of the condition. It may include antibiotics, antiparasitic medications, probiotics, or surgery in severe cases.
Cholesteryl Ester Storage Disease (CESD) is a rare genetic disorder characterized by the accumulation of cholesteryl esters in various tissues and organs, particularly in the liver and spleen. It is caused by mutations in the gene responsible for producing lipoprotein lipase (LPL), an enzyme that helps break down fats called triglycerides in the body.
In CESD, the lack of functional LPL leads to an accumulation of cholesteryl esters in the lysosomes of cells, which can cause damage and inflammation in affected organs. Symptoms of CESD can vary widely, but often include enlargement of the liver and spleen, abdominal pain, jaundice, and fatty deposits under the skin (xanthomas).
CESD is typically diagnosed through a combination of clinical evaluation, imaging studies, and genetic testing. Treatment may involve dietary modifications to reduce the intake of fats, medications to help control lipid levels in the blood, and in some cases, liver transplantation.
Exons are the coding regions of DNA that remain in the mature, processed mRNA after the removal of non-coding intronic sequences during RNA splicing. These exons contain the information necessary to encode proteins, as they specify the sequence of amino acids within a polypeptide chain. The arrangement and order of exons can vary between different genes and even between different versions of the same gene (alternative splicing), allowing for the generation of multiple protein isoforms from a single gene. This complexity in exon structure and usage significantly contributes to the diversity and functionality of the proteome.
Glycogen phosphorylase is an enzyme that plays a crucial role in the breakdown of glycogen, a stored form of glucose, to provide energy for the body's needs. This enzyme is primarily located in the liver and muscles.
In the process of glycogenolysis, glycogen phosphorylase catalyzes the phosphorolytic cleavage of the α-1,4-glycosidic bonds between glucose units in glycogen, releasing glucose-1-phosphate. This reaction does not involve water, unlike hydrolysis, making it more energy efficient. The glucose-1-phosphate produced can then be further metabolized to yield ATP and other energy-rich compounds through the glycolytic pathway.
Glycogen phosphorylase exists in two interconvertible forms: the active a form and the less active b form. The conversion between these forms is regulated by various factors, including hormones (such as insulin, glucagon, and epinephrine), enzymes, and second messengers (like cyclic AMP). Phosphorylation and dephosphorylation of the enzyme are critical in this regulation process. When glycogen phosphorylase is phosphorylated, it becomes activated, leading to increased glycogen breakdown; when it's dephosphorylated, it becomes less active or inactive, slowing down glycogenolysis.
Understanding the function and regulation of glycogen phosphorylase is essential for comprehending energy metabolism, particularly during periods of fasting, exercise, and stress when glucose availability from glycogen stores becomes crucial.
A genetic vector is a vehicle, often a plasmid or a virus, that is used to introduce foreign DNA into a host cell as part of genetic engineering or gene therapy techniques. The vector contains the desired gene or genes, along with regulatory elements such as promoters and enhancers, which are needed for the expression of the gene in the target cells.
The choice of vector depends on several factors, including the size of the DNA to be inserted, the type of cell to be targeted, and the efficiency of uptake and expression required. Commonly used vectors include plasmids, adenoviruses, retroviruses, and lentiviruses.
Plasmids are small circular DNA molecules that can replicate independently in bacteria. They are often used as cloning vectors to amplify and manipulate DNA fragments. Adenoviruses are double-stranded DNA viruses that infect a wide range of host cells, including human cells. They are commonly used as gene therapy vectors because they can efficiently transfer genes into both dividing and non-dividing cells.
Retroviruses and lentiviruses are RNA viruses that integrate their genetic material into the host cell's genome. This allows for stable expression of the transgene over time. Lentiviruses, a subclass of retroviruses, have the advantage of being able to infect non-dividing cells, making them useful for gene therapy applications in post-mitotic tissues such as neurons and muscle cells.
Overall, genetic vectors play a crucial role in modern molecular biology and medicine, enabling researchers to study gene function, develop new therapies, and modify organisms for various purposes.
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.
Charcot-Marie-Tooth disease (CMT) is a group of inherited disorders that cause nerve damage, primarily affecting the peripheral nerves. These are the nerves that transmit signals between the brain and spinal cord to the rest of the body. CMT affects both motor and sensory nerves, leading to muscle weakness and atrophy, as well as numbness or tingling in the hands and feet.
The disease is named after the three physicians who first described it: Jean-Martin Charcot, Pierre Marie, and Howard Henry Tooth. CMT is characterized by its progressive nature, meaning symptoms typically worsen over time, although the rate of progression can vary significantly among individuals.
There are several types of CMT, classified based on their genetic causes and patterns of inheritance. The two most common forms are CMT1 and CMT2:
1. CMT1: This form is caused by mutations in the genes responsible for the myelin sheath, which insulates peripheral nerves and allows for efficient signal transmission. As a result, demyelination occurs, slowing down nerve impulses and causing muscle weakness, particularly in the lower limbs. Symptoms usually begin in childhood or adolescence and include foot drop, high arches, and hammertoes.
2. CMT2: This form is caused by mutations in the genes responsible for the axons, the nerve fibers that transmit signals within peripheral nerves. As a result, axonal degeneration occurs, leading to muscle weakness and atrophy. Symptoms usually begin in early adulthood and progress more slowly than CMT1. They primarily affect the lower limbs but can also involve the hands and arms.
Diagnosis of CMT typically involves a combination of clinical evaluation, family history, nerve conduction studies, and genetic testing. While there is no cure for CMT, treatment focuses on managing symptoms and maintaining mobility and function through physical therapy, bracing, orthopedic surgery, and pain management.
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.
Glycogen storage disease type I
Glycogen storage disease type III
Glycogen storage disease type VI
Glycogen storage disease type V
Glycogen storage disease type 0
Glycogen storage disease type IV
Glycogen storage disease type II
Glycogen storage disease type IX
Glycogen storage disease
Glycogen branching enzyme
Glycogen debranching enzyme
Glycogen synthase
Phosphofructokinase deficiency
Glycogen-branching enzyme deficiency
Lafora disease
Liver disease
Glucose 6-phosphatase
Shin Joong Oh
Glucose-6-phosphate exchanger SLC37A4
Barbara Illingworth Brown
Pseudoathletic appearance
Medical genetics of Jews
G6PC
Acid alpha-glucosidase
Corn starch
Peter J. Taub
PHKG2
Glucose cycle
Glycogen phosphorylase
Danon disease
Glycogen storage disease type I - Wikipedia
Glycogen storage disease type IV: MedlinePlus Genetics
Glycogen Storage Disease Type IV
Type IV Glycogen Storage Disease: Practice Essentials, Pathophysiology, Prognosis
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
Association of the congenital neuromuscular form of glycogen storage disease type IV with a large deletion and recurrent...
Type V Glycogen Storage Disease: Practice Essentials, Pathophysiology, Epidemiology
Glycogen storage disease type II (Pompe disease)
Glycogen storage disease type VI
Glycogen storage disease type III diagnosis and management guidelines. | Read by QxMD
Glycogen Storage Disease Type 1b - CureGSD1b
Glycogen-Storage Disease Type 0 Differential Diagnoses
Glycogen Storage Disease Type V | Profiles RNS
Glycogen Storage Disease Type IIIa, (GSD IIIa)
Type V Glycogen Storage Disease: Background, Pathophysiology, Epidemiology
Glycogen storage disease type I: Video & Anatomy | Osmosis
Molecular Genetics of Type 1 Glycogen Storage Diseases. | Read by QxMD
Understanding glycogen storage disease type 1b and its impacts. - Sci Ani
Glycogen Storage Disease, Type 1A (G6PC), 9 Variants | ARUP Laboratories Test Directory
Glycogen debranching enzyme - wikidoc
Pulmonary arterial hypertension and type-I glycogen-storage disease: the serotonin hypothesis - The Lincoln Repository
Pharmacological and nutritional treatment for McArdle disease (Glycogen Storage Disease type V) | Evidence-Based Medicine...
A glycogen storage disease type 1a patient with type 2 diabetes | BMC Medical Genomics | Peer Review
PAA849Hu02 | Polyclonal Antibody to Glycogen Phosphorylase, Liver (PYGL) | Homo sapiens (Human) USCN(Wuhan USCN Business Co.,...
Glycogen Storage Disease Type VII (GSD VII) | Syndromes: Rapid Recognition and Perioperative Implications |...
Genes to Cells: Vol 18, No 12
Cirrhosis: Practice Essentials, Overview, Etiology
Cirrhosis: Practice Essentials, Overview, Etiology
Metabolic Crises | SpringerLink
Mutations9
- GBE1 gene mutations that cause GSD IV lead to a shortage (deficiency) of the glycogen branching enzyme. (medlineplus.gov)
- Glycogen storage disease type IV (GSD IV), or Andersen disease, is an autosomal recessive disorder caused by mutations in the gene-encoding glycogen-branching enzyme necessary for normal glycogen metabolism. (medscape.com)
- This case report also highlights the need for a more comprehensive search for large deletion mutations associated with glycogen storage disease type IV, especially if routine GBE1 gene sequencing results are equivocal. (nih.gov)
- GSD type V is an autosomal recessive disease resulting from mutations in the PYGM gene that encodes for the muscle isoform of glycogen phosphorylase (myophosphorylase). (medscape.com)
- Mutations in the liver glycogen synthase gene in children with hypoglycemia due to glycogen storage disease type 0. (medscape.com)
- Glycogen synthase deficiency (glycogen storage disease type 0) presenting with hyperglycemia and glucosuria: report of three new mutations. (medscape.com)
- [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)
- Constitutively active AMP kinase mutations cause glycogen storage disease mimicking hypertrophic cardiomyopathy. (springer.com)
- Mutations in this gene cause glycogen storage disease type 9D, also known as X-linked muscle glycogenosis. (nih.gov)
Phosphorylase8
- Glycogen storage disease type VI is a type of glycogen storage disease caused by a deficiency in liver glycogen phosphorylase . (chemeurope.com)
- Together with phosphorylase , glycogen debranching enzymes function in glycogen breakdown and glucose mobilization. (wikidoc.org)
- When phosphorylase has digested a glycogen branch down to four glucose residues, it will not remove further residues. (wikidoc.org)
- Glycogen debranching enzymes assist phosphorylase, the primary enzyme involved in glycogen breakdown , mobilize glycogen stores. (wikidoc.org)
- 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)
- because 1 in 10 residues is branched, cleavage by phosphorylase alone would not be sufficient in mobilizing 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)
- Magnetic Luminex Assay Kit for Glycogen Phosphorylase, Liver (PYGL) ,etc. (uscnk.com)
Caused by a deficiency4
- 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)
- Anderson disease, also known as glycogen storage disease type IV (MIM 232500), is a rare autosomal recessive disorder caused by a deficiency of glycogen branching enzyme. (nih.gov)
- Glycogen storage disease type 1 (GSD-1), also known as von Gierke disease, is caused by a deficiency in the activity of the enzyme glucose-6-phosphatase (G6Pase). (qxmd.com)
- A case of pulmonary arterial hypertension in a patient with type-Ia glycogen-storage disease, a rare autosomal recessive disorder caused by a deficiency of glucose-6-phosphatase is reported in this study. (lincoln.ac.uk)
Defective glycogen synthase1
- Interestingly, GSD type 0 also is described and is a disorder causing glycogen deficiency due to defective glycogen synthase. (medscape.com)
Accumulation4
- thus, an enzyme deficiency results in glycogen accumulation in specific tissues. (medscape.com)
- Carbohydrate metabolic pathways are blocked, leading to excess glycogen accumulation in affected tissues and/or disturbances in energy production. (medscape.com)
- Because free glucose is the product of the hepatic glucose-6 phosphatase reaction, either type leads to accumulation of liver glycogen, accompanied by fasting hypoglycemia. (lu.se)
- At the opportunity, the pathologist visualized glycogen accumulation in vesicles inside the cardiac fibers1. (bvsalud.org)
Form of glycogen2
- 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)
- About 1 in 25,000 infants has some form of glycogen storage disease. (msdmanuals.com)
Gene5
- People with one copy of the faulty gene are carriers of the disease and have no symptoms. (wikipedia.org)
- As with other autosomal recessive diseases, each child born to two carriers of the disease has a 25% chance of inheriting both copies of the faulty gene and manifesting the disease. (wikipedia.org)
- The GBE1 gene provides instructions for making the glycogen branching enzyme. (medlineplus.gov)
- A novel mutation in the glycogen synthase 2 gene in a child with glycogen storage disease type 0. (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)
Deficiency of glycogen1
- Infantile hypoglycaemia due to inherited deficiency of glycogen synthetase in liver. (medscape.com)
Metabolism of glycogen2
- Glycogen storage disease (GSD) type IIIa is a disorder that affects the metabolism of glycogen. (wisdompanel.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)
Break down glycogen2
- The inability of muscle cells to break down glycogen for energy leads to muscle weakness and wasting. (medlineplus.gov)
- Glycogen storage diseases are caused by the lack of an enzyme needed to change glucose into glycogen and break down glycogen into glucose. (msdmanuals.com)
Glucose from glycogen2
- With intense exercise, glucose from glycogen stores in muscle becomes the predominant resource. (medscape.com)
- Patients with glycogen storage disease type I are unable to release glucose from glycogen. (lu.se)
Congenital3
- The congenital muscular type of GSD IV is usually not evident before birth but develops in early infancy. (medlineplus.gov)
- Infants with the congenital muscular type of GSD IV typically survive only a few months. (medlineplus.gov)
- 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)
Neuromuscular6
- The fatal perinatal neuromuscular type is the most severe form of GSD IV, with signs developing before birth. (medlineplus.gov)
- Infants with the fatal perinatal neuromuscular type of GSD IV have very low muscle tone (severe hypotonia) and muscle wasting (atrophy). (medlineplus.gov)
- The childhood neuromuscular type of GSD IV develops in late childhood and is characterized by myopathy and dilated cardiomyopathy. (medlineplus.gov)
- Individuals with the fatal perinatal neuromuscular type tend to produce less than 5 percent of usable enzyme, while those with the childhood neuromuscular type may have around 20 percent of enzyme function. (medlineplus.gov)
- The childhood neuromuscular subtype is rare and the course is variable, ranging from onset in the second decade with a mild disease course to a more severe, progressive course resulting in death in the third decade. (nih.gov)
- 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)
Hepatic10
- The progressive hepatic type is the most common form of GSD IV. (medlineplus.gov)
- Children with the progressive hepatic type of GSD IV often die of liver failure in early childhood. (medlineplus.gov)
- The non-progressive hepatic type of GSD IV has many of the same features as the progressive hepatic type, but the liver disease is not as severe. (medlineplus.gov)
- In the non-progressive hepatic type, hepatomegaly and liver disease are usually evident in early childhood, but affected individuals typically do not develop cirrhosis. (medlineplus.gov)
- Patient complaints probably relate to end-organ injuries of Andersen disease, such as hepatic failure, cardiomyopathy, or muscular atrophy. (medscape.com)
- Aynsley-Green A, Williamson DH, Gitzelmann R. Asymptomatic hepatic glycogen-synthetase deficiency. (medscape.com)
- Hepatic glycogen synthetase deficiency. (medscape.com)
- Effect of growth hormone treatment on hypoglycemia in a patient with both hepatic glycogen synthase and isolated growth hormone deficiencies. (medscape.com)
- Glucose homeostasis in adulthood and in pregnancy in a patient with hepatic glycogen synthetase deficiency. (medscape.com)
- Hepatic glycogen synthase deficiency: an infrequently recognized cause of ketotic hypoglycemia. (medscape.com)
Synthase deficiency4
- Spiegel R, Mahamid J, Orho-Melander M, Miron D, Horovitz Y. The variable clinical phenotype of liver glycogen synthase deficiency. (medscape.com)
- Liver glycogen synthase deficiency: a rarely diagnosed entity. (medscape.com)
- Laberge AM, Mitchell GA, van de Werve G. Long-term follow-up of a new case of liver glycogen synthase deficiency. (medscape.com)
- Rutledge SL, Atchison J, Bosshard NU, Steinmann B. Case report: liver glycogen synthase deficiency--a cause of ketotic hypoglycemia. (medscape.com)
Abnormal glycogen3
- Abnormal glycogen molecules called polyglucosan bodies accumulate in cells, leading to damage and cell death. (medlineplus.gov)
- Other GSDs do not have this abnormal glycogen structure. (medscape.com)
- For types I, III, and VI, symptoms are low levels of sugar in the blood ( hypoglycemia ) and protrusion of the abdomen (because excess or abnormal glycogen may enlarge the liver). (msdmanuals.com)
GSDs3
- Although at least 14 unique GSDs are discussed in the literature, the four 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)
- In general, no specific treatment exists to cure glycogen storage diseases (GSDs). (medscape.com)
- 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)
Clinical15
- The clinical manifestations of glycogen storage disease type IV (GSD IV) discussed in this entry span a continuum of different subtypes with variable ages of onset, severity, and clinical features. (nih.gov)
- Clinical features and predictors for disease natural progression in adults with Pompe disease: a nationwide prospective observational study. (medscape.com)
- 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)
- Glycogen storage disease type IV has a broad clinical spectrum ranging from a perinatal lethal form to a nonprogressive later-onset disease in adults. (nih.gov)
- Heterozygotes usually do not manifest clinical features of the disease. (medscape.com)
- Glycogen storage disease type III is a rare disease of variable clinical severity affecting primarily the liver, heart, and skeletal muscle. (qxmd.com)
- Glycogen storage disease type III manifests a wide clinical spectrum. (qxmd.com)
- Please note: It is possible that disease signs similar to the ones caused by the GSD mutation could develop due to a different genetic or clinical cause. (wisdompanel.com)
- The disease presents with both clinical and biochemical heterogeneity consistent with the existence of two major subgroups, GSD-1a and GSD-1b, which have been confirmed at the molecular genetic level. (qxmd.com)
- Clinical features similar to GSD type V. Temporary weakness and painful muscle cramps occur after exercise. (mhmedical.com)
- Three clinical forms have been described: classic, infantile onset, and late onset type. (mhmedical.com)
- Merle U, Schaefer M, Ferenci P, Stremmel W. Clinical presentation, diagnosis and long-term outcome of Wilson's disease: a cohort study. (medscape.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)
- This classification is fundamental to the type of marketing authorization (MA), and therefore to the controls to be performed, from preclinical stages through clinical trials to pharmacovigilance, to meet the safety requirements for patients. (frontiersin.org)
- Hepatomegaly is the clinical hallmark of disease. (lu.se)
Degradation3
- It is caused by deficient activity of glycogen debranching enzyme, which is a key enzyme in glycogen degradation. (qxmd.com)
- glucose cannot be used as a source of energy and glycogen accumulates because of impaired degradation and/or excess synthesis. (mhmedical.com)
- Protein targeting to glycogen (PTG) is a scaffolding protein that targets protein phosphatase 1α (PP1α) to glycogen, and links it to enzymes involved in glycogen synthesis and degradation. (jci.org)
McArdle4
- These inherited enzyme defects usually present in childhood, although some, such as McArdle disease and Pompe disease, have separate adult-onset forms. (medscape.com)
- Myophosphorylase, the deficient enzyme in McArdle disease, is found in muscle tissue. (medscape.com)
- One hallmark of McArdle disease is weakness with exertion. (medscape.com)
- Pharmacological and Nutritional Treatment for McArdle Disease (Glycogen Storage Disease Type V)." Evidence-Based Medicine Guidelines , Duodecim Medical Publications Limited, 2019. (unboundmedicine.com)
Pompe Disease12
- 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)
- 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)
- to investigate nursing team knowledge and practices regarding care for children with Pompe disease in intensive care. (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)
Glycogenosis1
- Glycogenosis type VII. (mhmedical.com)
Disorder8
- Glycogen storage disease type IV (GSD IV) is an inherited disorder caused by the buildup of a complex sugar called glycogen in the body's cells. (medlineplus.gov)
- People with this type of the disorder can also have hypotonia and muscle weakness (myopathy). (medlineplus.gov)
- Generally, the severity of the disorder is linked to the amount of functional glycogen branching enzyme that is produced. (medlineplus.gov)
- Glycogen Storage Disease Type 1b (GSD1b) is a rare genetic disorder that has a huge impact on patients' lives and the lives of their families. (sciani.com)
- RBCK1-related disease: A rare multisystem disorder with polyglucosan storage, auto-inflammation, recurrent infections, skeletal, and cardiac myopathy-Four additional patients and a review of the current literature. (nih.gov)
- Glycogen Storage Disease Type Ia (GSD Ia) is a severe metabolic disorder causing critically low blood sugar levels and liver enlargement. (wisdompanel.com)
- von Willebrand's Disease (vWD) type 1 is a clotting disorder that usually causes mild bleeding tendencies in affected dogs though some may have more severe signs. (wisdompanel.com)
- NORD is not a medical provider or health care facility and thus can neither diagnose any disease or disorder nor endorse or recommend any specific medical treatments. (rarediseases.org)
Tyrosinemia1
- Reversibility of cirrhotic regenerative liver nodules upon NTBC treatment in a child with tyrosinemia type I. Acta Paediatr. (springer.com)
Autosomal1
- This disease is autosomal recessive meaning that two copies of the mutation are needed for disease signs to occur. (wisdompanel.com)
Genetics2
- Molecular Genetics of Type 1 Glycogen Storage Diseases. (qxmd.com)
- Kieffer DA, Medici V. Wilson disease: at the crossroads between genetics and epigenetics-A review of the evidence. (medscape.com)
Lipid2
- These data suggest that PTG plays a critical role in glycogen synthesis and is necessary to maintain the appropriate metabolic balance for the partitioning of fuel substrates between glycogen and lipid. (jci.org)
- The metabolic myopathies (MM) are a group of muscle disorders resulting from failed energy production related to defects in glycogen, lipid or mitochondrial metabolism. (pediatriconcall.com)
Diagnosis12
- The diagnosis is established in a proband by the demonstration of glycogen branching enzyme (GBE) deficiency in liver, muscle, or skin fibroblasts or the identification of biallelic pathogenic variants in GBE1 on molecular genetic testing. (nih.gov)
- If the GBE1 pathogenic variants have been identified in an affected family member, test at-risk relatives to allow for early diagnosis and management of disease manifestations. (nih.gov)
- Lin CY, Hwang B, Hsiao KJ, Jin YR. Pompe's disease in Chinese and prenatal diagnosis by determination of alpha-glucosidase activity. (medscape.com)
- Frequency of glycogen storage disease type II in The Netherlands: implications for diagnosis and genetic counselling. (medscape.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)
- 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)
- The diagnosis and management of the acutely ill child with suspected metabolic disease can present a formidable challenge to even the most astute clinician. (springer.com)
- Diagnosis and treatment of Wilson disease: an update. (medscape.com)
- Schilsky ML. Wilson disease: diagnosis, treatment, and follow-up. (medscape.com)
- Most articles standardize to single equal sign top level parent headings: Disease Entity, Diagnosis, Management, Additional Resources, References that are more responsive to mobile friendly style changes. (aao.org)
Buildup1
- Because of the glycogen buildup, GSD I patients typically present with enlarged livers from non-alcoholic fatty liver disease. (wikipedia.org)
Enzymes4
- Together with phosphorylases , debranching enzymes mobilize glucose reserves from glycogen deposits in the muscles and liver. (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)
- Normally your enzymes break carbohydrates down into glucose (a type of sugar). (medlineplus.gov)
Biochemical1
- Metabolic disease may present in a fulminate fashion to the pediatric intensivist with profound biochemical disturbances, encephalopathy and even cardiac failure. (springer.com)
Tissues1
- One of the four glycogen storage diseases characterized by phosphofructokinase deficiency in the muscles and associated with abnormal deposition of glycogen in muscle tissues, exercise intolerance, and anemia. (mhmedical.com)
Hypoglycemia5
- Because glycogenolysis is the principal metabolic mechanism by which the liver supplies glucose to the body during fasting, both deficiencies cause severe hypoglycemia and, over time, excess glycogen storage in the liver and (in some cases) in the kidneys. (wikipedia.org)
- However, after birth, the inability to maintain blood glucose from stored glycogen in the liver causes measurable hypoglycemia in no more than 1-2 hours after feedings. (wikipedia.org)
- Fasting blood glucose testing is indicated because hypoglycemia sometimes can be found in some types of GSD. (medscape.com)
- Meticulous adherence to a dietary regimen to maintain a euglycemic state and prevent the formation of excessive glycogen may reduce the liver size, prevent hypoglycemia, reduce symptoms, and allow growth and development. (medscape.com)
- Individuals with glycogen storage disease type III present with hepatomegaly, hypoglycemia, hyperlipidemia, and growth retardation. (qxmd.com)
Cleave1
- 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)
GSD1B2
- Sophie's Hope Foundation and CureGSD1b, in partnership with Sanguine Biosciences, is reaching out to raise awareness about an at-home research opportunity for adult patients and children diagnosed with Glycogen storage disease type 1B (GSD1B). (curegsd1b.org)
- Over the past 18 months we have worked closely with doctors, researchers, drug developers, policy makers and other rare disease organizations to get a better understanding of how we move the needle forward for GSD1b care and new treatments. (curegsd1b.org)
Gierke2
- The disease was named after German doctor Edgar von Gierke, who first described it in 1929. (wikipedia.org)
- The von Gierke disease (GSD type Ia, glucose-6-phosphatase deficiency) causes clinically significant end-organ disease with substantial morbidity. (medscape.com)
Liver disease6
- Children with this type develop a form of liver disease called cirrhosis that often is irreversible. (medlineplus.gov)
- however, they are likely to survive without progression of the liver disease and may not show cardiac, skeletal muscle, or neurologic involvement. (nih.gov)
- 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)
- 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)
- Copper: its role in the pathogenesis of liver disease. (medscape.com)
MeSH1
- Glycogen Storage Disease Type V" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (sdsu.edu)
Blood-glucose levels1
- Glycogen breakdown is highly regulated in the body, especially in the liver , by various hormones including insulin and glucagon , to maintain a homeostatic balance of blood-glucose levels. (wikidoc.org)
Rare diseases2
- Rare-X is a collaborative platform for global data sharing and analysis to accelerate treatments for rare diseases. (curegsd1b.org)
- Rare Disease PHGKB is an online, continuously updated, searchable database of published scientific literature, CDC and NIH resources, and other information that address the public health impact and translation of genomic and other precision health discoveries into improved health outcomes related to rare diseases. (cdc.gov)
Maple Syrup U1
- Maple syrup urine disease: it has come a long way. (springer.com)
Acid maltase de1
- Glycogen storage disease type II: acid alpha-glucosidase (acid maltase) deficiency. (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)
Protein2
- Ricin is a potent (type 2) ribosome-inactivating protein toxin produced in the seeds of the castor bean plant Ricinus communis . (mdpi.com)
- 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)
Deficient1
- Gordon N. Classic diseases revisited: carbohydrate-deficient glycoprotein syndromes. (springer.com)
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)
Fatigue1
- Fatigue develops when the glycogen supply is exhausted. (medscape.com)
Centers for Diseas2
Skeletal1
- These mice have reduced glycogen stores in adipose tissue, liver, heart, and skeletal muscle, corresponding with decreased glycogen synthase activity and glycogen synthesis rate. (jci.org)
IIIa1
- Glycogen storage disease type IIIa in curly-coated retrievers. (wisdompanel.com)
Severe2
- To test this hypothesis, plasma serotonin concentrations were prospectively measured in 13 patients with type-Ia glycogen-storage disease, one patient with severe pulmonary hypertension and type-Ia glycogen-storage disease, 16 patients displaying severe pulmonary arterial hypertension, and 26 normal healthy controls. (lincoln.ac.uk)
- It is concluded that type-Ia glycogen-storage disease may be another condition in which abnormal handling of serotonin is one event in a multistep process leading to severe pulmonary arterial hypertension. (lincoln.ac.uk)
Abnormalities1
- Chitkara DK, Nurko S, Shoffner JM, Buie T, Flores A. Abnormalities in gastrointestinal motility are associated with diseases of oxidative phosphorylation in children. (springer.com)