DISORDERS OF GLYCOGEN METABOLISM

PEDIATRICS ◽  
1952 ◽  
Vol 9 (3) ◽  
pp. 263-279
Author(s):  
WILLIAM H. LANGEWISCH ◽  
JOHN A. BIGLER
Keyword(s):  
Glycogen Storage Disease ◽  
Adrenocorticotropic Hormone ◽  
Storage Disease ◽  
Glycogen Metabolism ◽  
Glycogen Storage ◽  
Laboratory Evidence ◽  
Physical Findings ◽  
Treatment Prognosis

Five cases have been presented with evidence of disordered glycogen metabolism. Two cases of glycogen storage disease of the liver are included which were confirmed by biopsy, together with clinical and laboratory evidence. Treatment of one of the cases with adrenocorticotropic hormone resulted in a disappearance of hypoglycemia and acetonuria during the period of therapy. Two cases of glycogen storage disease of the heart are reported together with clinical histories and necropsy reports. An ECG which was recorded on one of the patients is included. A case of galactosemia is reported together with extensive laboratory evidence of marked galactose intolerance. The criteria for the diagnosis of these entities are reviewed and the symptomatology, physical findings, treatment, prognosis and pathologic manifestations are discussed.

Enzymes of Glycogen Metabolism in Human Skin with Particular Reference to Differential Diagnosis of the Glycogen Storage Diseases

1971 ◽  
Vol 40 (3) ◽  
pp. 261-269 ◽  
Author(s):  
P. D. Leathwood ◽  
Brenda E. Ryman
Keyword(s):  
Glycogen Storage Disease ◽  
Glycogen Phosphorylase ◽  
Storage Disease ◽  
Glycogen Metabolism ◽  
Glycogen Storage ◽  
Debranching Enzyme ◽  
Epidermal Tissue ◽  
Glycogen Storage Diseases ◽  
Muscle Phosphorylase ◽  
Type V

1. A vacuum skin-blistering technique has been successfully applied and the human epidermal tissue so obtained has been examined for glycogen content and some of the enzymes involved in glycogen metabolism. 2. Normal values for glycogen phosphorylase, acid α-glucosidase and amylo-1,6-glucosidase (debranching enzyme) in epidermis are reported. Glucose 6-phosphatase activity was not detected. 3. Examination of two patients with Type II glycogen storage disease (Pompe's Disease—lack of lysosomal acid α-glucosidase) revealed an absence of the acid α-glucosidase in their skin. 4. The enzymic lesion in Type V glycogen storage disease (McArdle's Disease—lack of muscle phosphorylase) was not reflected in the epidermal tissue of a patient and a normal level of the enzyme was observed.

scholarly journals Glucose and glycogen metabolism in erythrocytes from normal and glycogen storage disease type III subjects

1968 ◽  
Vol 47 (6) ◽  
pp. 1343-1348 ◽  
Author(s):  
Shimon W. Moses ◽  
Reuben Chayoth ◽  
Stanley Levin ◽  
Ela Lazarovitz ◽  
David Rubinstein
Keyword(s):  
Glycogen Storage Disease ◽  
Storage Disease ◽  
Glycogen Metabolism ◽  
Glycogen Storage Disease Type ◽  
Glycogen Storage ◽  
Disease Type ◽  
Type Iii

scholarly journals Neurological Characteristics of Pediatric Glycogen Storage Disease

2021 ◽  
Vol 12 ◽  
Author(s):  
Julio Henrique Muzetti ◽  
Daniel Almeida do Valle ◽  
Mara L. S. Ferreira Santos ◽  
Bruno Augusto Telles ◽  
Mara L. Cordeiro
Keyword(s):  
Metabolic Control ◽  
Glycogen Storage Disease ◽  
Storage Disease ◽  
Glycogen Metabolism ◽  
Glycogen Storage Disease Type ◽  
Glycogen Storage ◽  
Type I ◽  
Cross Sectional ◽  
Glycogen Storage Diseases ◽  
Multigene Panel

Glycogen storage diseases (GSD) encompass a group of rare inherited diseases due dysfunction of glycogen metabolism. Hypoglycemia is the most common primary manifestation of GSD, and disturbances in glucose metabolism can cause neurological damage. The aims of this study were to first investigate the metabolic, genetic, and neurological profiles of children with GSD, and to test the hypothesis whether GSD type I would have greater neurological impact than GSD type IX. A cross-sectional study was conducted with 12 children diagnosed with GSD [Types: Ia (n=5); 1, Ib (n=1); 4, IXa (n=5); and 1, IXb (n=1)]. Genetic testing was conducted for the following genes using multigene panel analysis. The biochemical data and magnetic resonance imaging of the brain presented by the patients were evaluated. The criteria of adequate metabolic control were adopted based on the European Study on Glycogen Storage Disease type I consensus. Pathogenic mutations were identified using multigene panel analyses. The mutations and clinical chronology were related to the disease course and neuroimaging findings. Adequate metabolic control was achieved in 67% of patients (GSD I, 43%; GSD IX, 100%). Fourteen different mutations were detected, and only two co-occurring mutations were observed across families (G6PC c.247C>T and c.1039C>T). Six previously unreported variants were identified (5 PHKA2; 1 PHKB). The proportion of GSD IX was higher in our cohort compared to other studies. Brain imaging abnormalities were more frequent among patients with GSD I, early-symptom onset, longer hospitalization, and inadequate metabolic control. The frequency of mutations was similar to that observed among the North American and European populations. None of the mutations observed in PHKA2 have been described previously. Therefore, current study reports six GSD variants previously unknown, and neurological consequences of GSD I. The principal neurological impact of GSD appeared to be related to inadequate metabolic control, especially hypoglycemia.

GLUCOSE-6-PHOSPHATASE DEFICIENCY GLYCOGEN STORAGE DISEASE

PEDIATRICS ◽  
1962 ◽  
Vol 29 (4) ◽  
pp. 553-565
Author(s):  
R. Rodney Howell ◽  
Doris M. Ashton ◽  
James B. Wyngaarden
Keyword(s):  
Glycogen Storage Disease ◽  
Storage Disease ◽  
Glycogen Storage ◽  
Serum Triglycerides ◽  
Normal Limits ◽  
Hepatic Glucose ◽  
Low Glucose ◽  
The One ◽  
Physical Findings ◽  
Glucose 6 Phosphate Dehydrogenase

Three siblings with glycogen storage disease have been studied. These children demonstrated the classic physical findings of von Gierke's disease. Liver enzyme assays on one sibling revealed very low glucose 6-phosphatase activity. Hepatic phosphoglucomutase, phosphorylase, glucose 6-phosphate dehydrogenase, and fructose 1,6-diphosphatase activities were within normal limits. Erythrocyte glucose 6-phosphate dehydrogenase activity was also normal. Incubation of liver slices with glucose 1-C14 and glucose 6-C14 revealed an initial rate of C14O2 production at which CO2 from C-1 was three times that from C-6. This is strong evidence for the active operation of the phosphogluconate oxidation pathway in this patient, and taken with the normal assay value of hepatic glucose-6-phosphate dehydrogenase, constitutes a negation of the concept of a dual enzyme defect recently proposed for von Gierke's disease. Striking elevations of free fatty acids in serum, triglycerides, phospholipids, cholesterol, and blood ketones were noted. Potential mechanisms for these elevations have been discussed. Marked hyperuricemia was a persistent finding and was associated with a somewhat low renal clearance of urate in the one patient studied. All three had striking elevations of lactic acid in blood, which is known to interfere with renal urate excretion. Thus renal factors may have contributed to the hyperuricemia, previously considered solely a consequence of enhanced nucleoprotein catabolism secondary to persistent hypoglycemia. Long-term intramuscular administration of glucagon did not produce significant clinical or laboratory improvement in the one patient in whom it was employed.

scholarly journals Analyzing the Distribution of Mutations for Glycogen Storage Disease Type 1a in Turkey and Suggested Gene Therapy Methods for Its Treatment

2020 ◽  
Author(s):  
Aysun Mantas ◽  
Cemre Ucaryilmaz ◽  
Busra Seniz Demir ◽  
Fatma Nur Guler ◽  
Sezgin Mengi ◽  
...  
Keyword(s):  
Gene Therapy ◽  
Glycogen Storage Disease ◽  
Storage Disease ◽  
Tertiary Structure ◽  
Glycogen Metabolism ◽  
Glycogen Storage Disease Type ◽  
Glycogen Storage ◽  
New Therapeutic Approaches ◽  
Tertiary Protein Structure

One of the rare diseases throughout the world is Glycogen Storage Disease, which appears due to problems in glycogen metabolism. Among various subtypes of GSD, GSD Type 1a is the most abundant one of GSD Type 1, seen in approximately 80% and caused by different kinds of mutations in the Glucose-6-Phosphatase Catalytic Subunit (G6PC) gene in human chromosome 17q21. G6PC gene encodes for glucose-6-phosphatase (G6Pase) protein, which cleaves glucose-6-phosphate into glucose and inorganic phosphate (Pi), and GSD Type 1a patients fail to breakdown glucose-6-phosphate due to several mutations in the G6PC gene. In our study, we aim to create new therapeutic approaches for GSD 1a. We collected mutation data of 57 GSD Type 1a patients from Turkey. According to the data, 16 types of mutations were observed in the G6PC gene. Allele frequencies of these mutations are calculated as 59% for R83C/H, 11% for W160*, 7% for G270V, and 28% for others which have less frequency. Up to now, the tertiary protein structure of G6Pase has not been structured yet. To understand the possible impacts of these mutations, we statistically obtained possible tertiary structure predictions of G6Pase by running 5 different tools. At the end of the study, we suggest two effective and promising gene therapy methods for GSD Type 1a, Prime Editing for R83C/H mutations, and mRNA delivery for other mutations, in addition to a promising, commercially available drug suggestion for patients with W160*, W86*, and S15* mutations, although the drug belongs to another disease.

scholarly journals BIOMARKERS OF APOPTOSIS IN GLYCOGEN STORAGE DISEASE IN CHILDREN

2019 ◽  
Vol 20 (2) ◽  
pp. 74-79
Author(s):  
A. N. Surkov ◽  
L. S. Namazova-Baranova ◽  
I. E. Smirnov ◽  
A. G. Kucherenko
Keyword(s):  
Cytochrome C ◽  
Glycogen Storage Disease ◽  
Structural Changes ◽  
Storage Disease ◽  
Annexin V ◽  
Glycogen Metabolism ◽  
Glycogen Storage ◽  
Fas Receptor ◽  
Tnf Α ◽  
Genetically Determined

Glycogen storage disease (GSD) is a rare form of the pathology in children caused by genetically determined pathological changes of the formation or cleavage of glycogen. Depending on the disorders of functions of enzymes involved in glycogen metabolism, there are known up to 15 GSD types, among them there are isolated liver, muscular and mixed forms. There are presented data of the immunoassay analysis of changes in concentrations of the array of proteins considered as biomarkers of apoptosis: sAPO-1/FAS receptor, sFAS-L, cytochrome C, annexin V, caspase-8, caspase-9 and TNF-α in the serum of GSD with the prevailed liver damage (I, III, VI and IX types). There was established the excess of the concentration of cytochrome C in the serum of GSD children by 2,7 times sAPO-1/FAS receptor - 8,9 times, sFAS-L - 2,5 times, annexin V - 4,8 times and TNF-α - 2,9 times in comparison with reference values. Whereby the excess in the cytochrome C content, sAPO-1/FAS receptor, sFAS-L annexin V and the serum was observed in all patients, that indicating to the higher activity of apoptosis in GSD. In this connection GSD in children can be considered as a form of pathology associated with the pronounced apoptosis that contributes to the progression of structural changes in the liver.

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