Regulation of glycogen synthase and phosphorylase activities by glucose and insulin in human skeletal muscle.

Yki-Järvinen, H; Mott, D; Young, A A; Stone, K; Bogardus, C

doi:10.1172/jci113069

Cited by 123Metabolism, Diabetes, and CancerGlycogen Storage Diseases and MyoclonusDiabetes, Cardiovascular Risks, and Lipoproteins

Regulation of glycogen synthase and phosphorylase activities by glucose and insulin in human skeletal muscle.

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Yki-Järvinen, H, Mott, D, Young, A A, Stone, K, Bogardus, C·1987·Journal of Clinical Investigation

DOI 10.1172/jci113069PMC PMC442206

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Abstract

We examined the insulin dose-response characteristics of human muscle glycogen synthase and phosphorylase activation. We also determined whether increasing the rate of glucose disposal by hyperglycemia at a fixed insulin concentration activates glycogen synthase. Physiological increments in plasma insulin but not glucose increased the fractional activity of glycogen synthase. The ED50: s for insulin stimulation of whole body and forearm glucose disposal were similar and unaffected by glycemia. Glycogen synthase activation was exponentially related to the insulin-mediated component of whole body and forearm glucose disposal at each glucose concentration. Neither insulin nor glucose changed glycogen phosphorylase activity. These results suggest that insulin but not the rate of glucose disposal per se regulates glycogen synthesis by a mechanism that involves dephosphorylation of glycogen synthase but not phosphorylase. This implies that the low glycogen synthase activities found in insulin-resistant states are a consequence of impaired insulin action rather than reduced glucose disposal.

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Glycogen synthase is the key insulin-regulated enzyme controlling the rate of muscle glycogen synthesis.
“Glycogen synthase is the key insulin-regulated enzyme that controls the rate of muscle glycogen synthesis [148, 150, 200, 212–214].”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [212]

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Authors: Yki-Järvinen, H., Mott, D., Young, A. A., Stone, K., & Bogardus, C.
Affiliations: National Institutes of Health (US)
ORCID: Bogardus, C
Venue: Journal of Clinical Investigation
Publisher: American Society for Clinical Investigation
Published: 1987-07-01
Volume: 80
Issue: 1
Pages: 95-100
ISSN: 0021-9738 (ISSN-L)
DOI: 10.1172/jci113069
PMC: PMC442206
OpenAlex: W2023027042
Cited by: 123
References: 47
Citations by year: 2024: 1 · 2023: 2 · 2022: 2 · 2021: 1 · 2020: 1 · 2019: 2 · 2018: 4 · 2017: 3 · 2016: 2 · 2015: 3 · 2014: 1 · 2013: 4 · 2012: 5
FWCI: 2.48
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Journal of Clinical Investigation (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Health Sciences › Medicine › Rheumatology › Glycogen Storage Diseases and Myoclonus
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes, Cardiovascular Risks, and Lipoproteins
Keywords: glycogen synthase, glycogen phosphorylase, insulin, glucose disposal, skeletal muscle, glycogen synthesis, insulin resistance, enzyme dephosphorylation, hyperglycemia, dose-response relationship, forearm glucose uptake
MeSH terms: Adult, Blood Glucose, Enzyme Activation, Glucose, Phosphorylases, Glycogen Synthase, Humans, Insulin, Male, Muscles

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Regulation of glycogen synthase and phosphorylase activities by glucose and insulin in human skeletal muscle.

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