Literature summary for 2.4.1.11 extracted from

Glintborg, D.; Hojlund, K.; Andersen, N.R.; Hansen, B.F.; Beck-Nielsen, H.; Wojtaszewski, J.F.
Impaired insulin activation and dephosphorylation of glycogen synthase in skeletal muscle of women with polycystic ovary syndrome is reversed by pioglitazone treatment (2008), J. Clin. Endocrinol. Metab., 93, 3618-3626.

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Application

Application	Comment	Organism
medicine	in patients with polycystic ovary syndrome, reduced insulin-mediated glucose disposal is associated with a lower insulin-stimulated glycogen synthase activity, explained by absent insulin-mediated dephosphorylation of glycogen synthase at the NH2-terminal sites 2 + 2a, whereas dephosphorylation at the COOH-terminal sites 3a + 3b is intact in polycystic ovary syndrome subjects. Insulin activation of glycogen synthase is dependent on dephosphorylation of sites 3a + 3b in women with polycystic ovary syndrome. No significant abnormalities in glycogen synthaseK-3 or -3 are found. Pioglitazone treatment improves insulin-stimulated glucose metabolism and glycogen synthase activity in polycystic ovary syndrome and restores the ability of insulin to dephosphorylate glycogen synthase at sites 2 and 2a	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	patients with polycystic ovary syndrome	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
skeletal muscle	-	Homo sapiens	-

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Release 2023.1 (January 2023)