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Expression analysis revealed that porcine GYS1 was highly expressed in the skeletal muscle and heart
The GYS1 mutation was detected in 11 breeds; with prevalence of genetic susceptibility to Type 1 Polysaccharide Storage Myopathy varied from 0.5% to 62.4%.
observed that the two miRNAs, namely, eca-miR-33a and miR-17, inhibited LDHA and GYS1 expression via binding to the 3' UTR sequences of each gene
The tissue expression profiles of eGYS1, equine type II hexokinase (eHKII) and muscle-type phosphofructokinase (ePFKM) were determined by real-time PCR and western blot analysis.
Study identified GYS1, encoding skeletal muscle glycogen synthase (GS), as a candidate gene for Polysaccharide storage myopathy; DNA sequence analysis revealed a mutation resulting in an Arg-to-his substitution in a highly conserved region of GS.
The prevalence of a missense mutation of GYS1 in horses with polysaccharide storage myopathy and the prevalence of the mutation based on disease classification are reported.
This GYS1 point mutation appears to cause a gain-of-function of the enzyme and to result in the accumulation of a glycogen-like, less-branched polysaccharide in skeletal muscle.
The GYS1 mutation is an important cause of exertional rhabdomyolysis in UNited Kingdom horse breeds but does not account for all forms of polysaccharide storage myopathy.
Overexpression of GYS1, MIF (show AMH Proteins), and MYC (show MYC Proteins) is associated with adverse outcome and poor response to azacitidine in myelodysplastic syndromes and acute myeloid leukemia (show BCL11A Proteins)
over-expression of muscle glycogen synthase (MGS)was detected in diabetic human kidney
High glycogen synthase 1 expression is associated with myeloid leukemia (show BCL11A Proteins).
Data suggest that although COOH-terminal dephosphorylation is likely necessary for GS activation, protein kinase Akt-2- (Akt2 (show AKT2 Proteins))-dependent NH2-terminal dephosphorylation is site for "fine-tuning" insulin (show INS Proteins)-mediated GS activation in skeletal muscle.
Allosteric regulation and the relationship between phosphorylation and the kinetics of glycogen synthase. [Review]
The present findings demonstrate that physical inactivity-induced insulin (show INS Proteins) resistance in muscle is associated with lower content/activity of key proteins in glucose transport/phosphorylation and storage.
GYS1 regulation by HIF plays a central role in the hypoxic accumulation of glycogen, and hypoxia also upregulates the expression of UTP:glucose-1-phosphate urydylyltransferase (UGP2 (show UGP2 Proteins)) and 1,4-alpha glucan branching enzyme (GBE1 (show GBE1 Proteins))
Exercise unmaskd the effect associated with the GYS1 polymorphism, rendering carriers of this allele less susceptible to the protective effect of exercise on the risk of cardiovascular mortality.
the M416V polymorphism of glycogen synthase 1 gene is not associated with insulin (show INS Proteins) resistance in type 2 diabetes
Data show that myotubes defective in glycogen synthase (GS) activity express insulin (show INS Proteins)-responsive glycogen synthase kinase-3alpha, suggesting that failure of insulin (show INS Proteins) to decrease GS phosphorylation involves abnormal activity of another kinase or phosphatase.
We show that the absence of Epm2aip1 (show EPM2AIP1 Proteins) in mice impairs allosteric activation of GS by glucose 6-phosphate, decreases hepatic glycogen synthesis, increases liver fat, causes hepatic insulin (show INS Proteins) resistance, and protects against age-related obesity
Muscle glycogen synthase isoform is responsible for testicular glycogen synthesis: glycogen overproduction induces apoptosis in male germ cells.
Long-term potentiation (LTP (show SCP2 Proteins)) evoked in the hippocampal CA3 (show CA3 Proteins)-CA1 (show CA1 Proteins) synapse was also decreased in behaving GYS1(Nestin (show NES Proteins)-KO) mice.
Neurodegeneration and functional impairments are associated with glycogen synthase accumulation in the mouse model of Lafora disease.
Overexpression of glycogen synthase in skeletal muscle results in less branched glycogen.
The endogenous glycogen synthase in extracts from mouse brain bound specifically to SAPK2b/p38b (show MAPK11 Proteins) & was phosphorylated at residues Ser644, Ser652, Thr718 and Ser724.
JNK signaling regulates the phosphorylation state of several kinases in skeletal muscle. JNK activation is unlikely to be the major mechanism by which contractile activity increases glycogen synthase activity in skeletal muscle.
the GYS1 gene is not essential for strenuous exercise and has relatively little effect on endurance in mice
In hearts from mPDK1-/- or double GSK3alpha/GSK3beta knockin mice, insulin failed to stimulate the activity of glycogen synthase or induce its dephosphorylation at residues that are phosphorylated by GSK3.
The protein encoded by this gene catalyzes the addition of glucose monomers to the growing glycogen molecule through the formation of alpha-1,4-glycoside linkages. Mutations in this gene are associated with muscle glycogen storage disease. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
glycogen [starch] synthase, muscle
, glycogen synthase 1 (muscle)
, glycogen synthase 3, brain