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Satoyoshi syndrome has exercise-induced painful muscle cramps, muscle hypertrophy, and short stature. Dimethylglycine dehydrogenase deficiency has muscle fatigue, elevated CK, and fishy body odour. Myopathy with myalgia, increased serum creatine kinase, with or without episodic rhabdomyolysis (MMCKR) has train-induced muscle cramps, pain, and fatigue; with some exhibiting proximal muscle weakness. Glycogenosis-like phenotype of congenital hyperinsulinism resulting from HNF4A mutation or MODY1 (maturity-onset diabetes of the younger, kind 1). This phenotype of MODY1 has macrosomia and infantile-onset hyperinsulinemic hypoglycemia, physiological 3-OH butyrate, elevated triglyceride serum levels, elevated stage of glycogen in liver and erythrocytes, increased liver transaminases, transient hepatomegaly, renal Fanconi syndrome, and later develop liver cirrhosis, decreased succinate-dependent respiration (mitochondrial dysfunction), rickets, nephrocalcinosis, chronic kidney disease, and diabetes. Treatment is dependent on the type of glycogen storage illness. Von Gierke illness (GSD-I) is often handled with frequent small meals of carbohydrates and healthy flow capsules cornstarch, referred to as modified cornstarch therapy, to stop low blood sugar, whereas other remedies may embrace allopurinol and human granulocyte colony stimulating issue.

42% of the circumstances are brought on by EPM2A and 58% are brought on by EPM2B (NHLRC1). The most common mutation on the EPM2A gene is the R241X mutation. This genetic mutation is the trigger for 17% of the EPM2A-triggered Lafora disease cases. EPM2A codes for the protein laforin, a dual-specificity phosphatase that acts on carbohydrates by taking phosphates off. NHLRC1 encodes the protein malin, an E3 ubiquitin ligase, that regulates the amount of laforin. Laforin is crucial for making the conventional structure of a glycogen molecule. When the mutation occurs on the EPM2A gene, laforin protein is down-regulated and less of this protein is present or none is made at all. If there can also be a mutation in the NHLRC1 gene that makes the protein malin, then laforin can't be regulated and thus much less of it is made.