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Cited by 17Metabolism, Diabetes, and CancerDiabetes, Cardiovascular Risks, and LipoproteinsDiabetes Treatment and Management

Skeletal muscle glycogen synthase activity in subjects with non-insulin-dependent diabetes mellitus after glyburide therapy

Nyomba, Bulangu L., Freymond, Daniel, Raz, Itamar, Stone, Karen, Mott, David M., Bogardus, Clifton·1990·Metabolism
DOI 10.1016/0026-0495(90)90096-u
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Abstract

Sulfonylureas are used in the treatment of non-insulin-dependent diabetes mellitus (NIDDM) largely because of their ability to enhance insulin secretion and possibly to potentiate insulin action. In this study, we investigated the effects of chronic glyburide treatment on glycogen synthase activity determined in skeletal muscle biopsies taken during euglycemic hyperinsulinemic clamps in nine Pima Indians with NIDDM. Insulin was infused at the rate of 40 mU/m2/min (low dose) followed by 400 mU/m2/min (high dose). Compared with the fasting value, the mean glycogen synthase activity assayed at low glucose-6-phosphate (G6P) concentration (active glycogen synthase) showed no significant changes during insulin infusion before glyburide treatment. After glyburide treatment, the mean active glycogen synthase increased by 39% (P less than .05) above the fasting value during the high-dose insulin infusion. Total glycogen synthase activity assayed at high G6P concentration did not change after glyburide treatment. Changes of insulin-stimulated active glycogen synthase associated with glyburide treatment correlated with changes in total body glucose disposal rates (r = .70, P less than .05) during euglycemic clamps. We conclude that glyburide treatment of subjects with NIDDM is associated with an increase in insulin action in vivo and concomitantly with improved insulin action on skeletal muscle glycogen synthase.

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Crossref · 10.1016/0026-0495(90)90096-u

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  • In insulin-resistant nondiabetic and diabetic Pima Indians, insulin activation of muscle PP1 is severely reduced.

    “In insulin-resistant nondiabetic and diabetic Pima Indians, activation of muscle PP1 (glycogen synthase phosphatase) by insulin is severely reduced [219].”

    From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [219]

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Authors
Nyomba, B. L., Freymond, D., Raz, I., Stone, K., Mott, D. M., & Bogardus, C.
Affiliations
National Institutes of Health (US)
Corresponding author
Nyomba, Bulangu L.
ORCID
Venue
Metabolism
Publisher
Elsevier BV
Published
1990-11
Volume
39
Issue
11
Pages
1204-1210
ISSN
0026-0495 (ISSN-L)
DOI
10.1016/0026-0495(90)90096-u
OpenAlex
W2067438306
Cited by
17
References
52
Citations by year
2018: 3 · 2015: 1
FWCI
0.57
Type
journal article
Language
en
Open access
closed
Licence
Locations
  • Metabolism (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
  • Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes, Cardiovascular Risks, and Lipoproteins
  • Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Treatment and Management
Keywords
glycogen synthase, skeletal muscle, type 2 diabetes, glibenclamide, sulfonylureas, insulin action, insulin-stimulated glucose disposal, Pima Indians, glucose-6-phosphate, hyperinsulinemic-euglycemic clamp
MeSH terms
Insulin Secretion, Adult, Blood Glucose, Diabetes Mellitus, Type 2, Dose-Response Relationship, Drug, Epinephrine, Fasting, Female, Glyburide, Glucosephosphates, Glycogen Synthase, Humans, Insulin, Male, Muscles, Glucose-6-Phosphate

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