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At least 397 records · Page 22Linked to original sources
PubMed2002

Glycogenosis type I and diabetes mellitus: a common mechanism for renal dysfunction?

Diabetes mellitus and glycogen storage disease type I (GSDI) may initially appear disparate in metabolic profile: one characterized by uncontrolled hyperglycaemia due to disturbed insulin function and the other by fasting hypoglycaemia caused by impaired gluconeogenesis and glycogenolysis. However, they share a remarkably similar pattern and progression of renal dysfunction. This may be, we suggest, due to a convergence of their metabolic sequelae in upregulation of flux through the pentose phosphate pathway. This pathway yields triose phosphate molecules, which are precursors of the lipid, diacylglycerol (DAG). DAG plays an important role in the intrarenal renin-angiotensin system via the protein kinase C pathway. GSDI may be an interesting model which helps to unravel further the contributions of the many, varied nephropathic influences in diabetes. Conversely patients with this rare disorders would have much to gain from the innovative and vastly greater body of research carried out in diabetes.

Angiotensins↗
PubMed2002

[Familial hypertrophic cardiomyopathy associated with Wolff-Parkinson-White syndrome revealing type II glycogenosis].

UNLABELLED: Symptoms of the late infantile form of type II glycogen storage disease are mainly due to functional impairment of skeletal muscle. Cardiac muscle can be involved in the late stage of the disease. CASE REPORT: We report the cases of two siblings seven and 12 years old with type II glycogen storage disease. The initial symptoms were hypertrophic cardiomyopathy with Wolf-Parkinson-White syndrome. CONCLUSION: Hypertrophic cardiomyopathy may be the form of presentation of the late infantile form of type II glycogen storage disease. The risk of sudden death is high.

Age Factors↗
PubMed1999

[Value of pulmonary gas exchange study during exercise in the diagnosis of a muscular glycogenosis].

BACKGROUND: The diagnosis of muscular glycogen storage disease is usually difficult to demonstrate as symptoms normally consist of muscular cramps and exercise intolerance. Informations obtained from the study of the pulmonary gas exchange during exercise in a young patient with a glycogen storage disease are reported. CASE REPORT: The ventilatory and gas exchange responses to a cyclo-ergometer exercise were studied in a 17-year-old girl during a ramp-like test (5 W/min). The temporal profile of CO2 production (VCO2) response was clearly abnormal: VCO2 was always lower than oxygen consumption throughout the test, reflecting the lack of lactate buffering by the bicarbonates due to the absence of lactate production. The respiratory ratio was still around 0.75 at the peak of the test. In contrast, responses were perfectly normal in the other members of the family, allowing rejection of the diagnosis of glycogen storage disease without any blood sampling. CONCLUSION: This case illustrates the benefit of studying pulmonary gas exchange during exercise for a non-invasive diagnosis of muscular glycogen storage disease and detection of the disease in the other members of family.

Adolescent↗
PubMed1999

Reversible severe myopathy of respiratory muscles due to adult-onset type III glycogenosis.

Subacute severe myopathy of the respiratory muscles developed in a 47-year-old woman after a 3-week period of strict fasting. Histological and biochemical work-up of muscle biopsy specimens permitted the diagnosis of debrancher deficiency. The course of the disease was characterized by subacute respiratory failure and prolonged mechanical ventilation. After initiation of a high-protein diet the patient was successfully weaned from the respirator and recovered well. To our knowledge this is the first reported case of adult-onset debrancher deficiency myopathy presenting with subacute respiratory failure and responding to high-protein diet.

Age of Onset↗
PubMed1996

Mutations in the testis/liver isoform of the phosphorylase kinase gamma subunit (PHKG2) cause autosomal liver glycogenosis in the gsd rat and in humans.

Heritable deficiency of phosphorylase kinase (Phk), a regulatory enzyme of glycogen metabolism, is responsible for 25% of all cases of glycogen storage disease and occurs with a frequency of -1 in 100,000 births. It is genetically and clinically heterogeneous, occurring in X-linked and autosomal-recessive forms and exhibiting various patterns of principally affected tissues (liver only, muscle only, liver and muscle, liver and kidney, heart only). This heterogeneity is thought to reflect the enzyme's structural complexity [subunit composition, (alpha beta gamma delta)4] and isoform diversity. Two isoforms encoded by separate genes are known for the subunits alpha (muscle [alpha M] and liver [alpha L isoforms) and gamma (muscle [gamma M] and testis [gamma T] isoforms), whereas only one gene appears to exist for the subunit beta. The subunit delta is calmodulin; identical calmodulins are expressed from three different human genes. Additional isoform diversity arises by differential mRNA splicing of the alpha M, alpha L and beta subunits. Mutations responsible for the various forms of Phk deficiency are sought in those subunit/isoform genes with a matching chromosomal location and tissue-specificity of expression. We report here that autosomal liver-specific Phk deficiency is associated with mutations in the gene encoding the testis/liver isoform of the catalytic gamma subunit (PHKG2). We found homozygous PHKG2 mutations in three human patients of consanguineous parentage and in the gsd (glycogen storage disease) rat strain, which is thus identified as an animal model for the human disorder. One human mutation is a single base-pair insertion in codon 89 that causes a frameshift and premature chain termination. The three other mutations result in non-conservative replacements of amino acid residues (V106E, G189E, D215N) that are highly conserved within the catalytic core regions of all protein kinases. These are the first mutations to be reported for an autosomal form of Phk deficiency. The findings suggest that the PHKG2 gene product is the predominant isoform of the catalytic gamma subunit of Phk not only in testis but also in liver, erythrocytes and, possibly, other non-muscle tissues.

Adolescent↗