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Insulin-stimulated glycogen synthase (GS) activity was completely ablated during hyperinsulinemic hypoglycemia, and catecholamine signaling via cAMP-dependent protein kinase (PKA) and phosphorylation of inhibiting sites on GS all increased.
Overexpression of GYS1, MIF, and MYC is associated with adverse outcome and poor response to azacitidine in myelodysplastic syndromes and acute myeloid leukemia
over-expression of muscle glycogen synthase (MGS)was detected in diabetic human kidney
High glycogen synthase 1 expression is associated with myeloid leukemia.
Data suggest that although COOH-terminal dephosphorylation is likely necessary for GS activation, protein kinase Akt-2- (Akt2)-dependent NH2-terminal dephosphorylation is site for "fine-tuning" insulin-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 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) and 1,4-alpha glucan branching enzyme (GBE1)
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 resistance in type 2 diabetes
Data show that myotubes defective in glycogen synthase (GS) activity express insulin-responsive glycogen synthase kinase-3alpha, suggesting that failure of insulin to decrease GS phosphorylation involves abnormal activity of another kinase or phosphatase.
Phosphorylation at site 2 in the elderly and at site 3a + 3b in young twins had a genetic component.
no nuclear export signal was identified in the sequence of the protein, the region comprising amino acids 555-633, which has an Arg-rich cluster involved in the allosteric activation is crucial for its nuclear concentration and aggregation.
3 siblings were identified with profound muscle glycogen deficiency and homozygous stop mutations in GYS1
Pioglitazone treatment improved insulin-stimulated glucose metabolism and glycogen synthase activity in PCOS.
After overnight low muscle glycogen level and/or in response to exhausting exercise-induced glycogenolysis, GSY is associated with spherical structures at the I-band of sarcomeres.
Dysregulation of glycogen synthase phosphorylation plays a major role in impaired insulin regulation of GS in obesity and type 2 diabetes mellitus.
The regulation of glucose-6-phosphate dehydrogenase and glycogen synthase activities by insulin superfamily peptides in myometrium of pregnant women and its impairments under different types of diabetes mellitus
Expression analysis revealed that porcine GYS1 was highly expressed in the skeletal muscle and heart
Elevated activity of the mutant glycogen synthase is associated with ineffective regulation via phosphorylation rendering it constitutively active.
the occurrence of the mutated GYS1 allele is influenced by coat colour
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.
These results demonstrate that pharmacological agents that activate GYS1, the main GS subtype found in skeletal muscle, have potential for use as novel treatments for diabetes that improve glucose metabolism in skeletal muscle.
We show that the absence of Epm2aip1 in mice impairs allosteric activation of GS by glucose 6-phosphate, decreases hepatic glycogen synthesis, increases liver fat, causes hepatic insulin 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) evoked in the hippocampal CA3-CA1 synapse was also decreased in behaving GYS1(Nestin-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 & 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