Cited by 375Metabolism, Diabetes, and CancerDiabetes, Cardiovascular Risks, and LipoproteinsAdipokines, Inflammation, and Metabolic Diseases

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Characterization of signal transduction and glucose transport in skeletal muscle from type 2 diabetic patients

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Krook, A, Björnholm, M, Galuska, D, Jiang, X J, Fahlman, R, Myers, M G, Wallberg-Henriksson, H, Zierath, J R·2000·Diabetes

DOI 10.2337/diabetes.49.2.284

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Abstract

We characterized metabolic and mitogenic signaling pathways in isolated skeletal muscle from well-matched type 2 diabetic and control subjects. Time course studies of the insulin receptor, insulin receptor substrate (IRS)-1/2, and phosphatidylinositol (PI) 3-kinase revealed that signal transduction through this pathway was engaged between 4 and 40 min. Insulin-stimulated (0.6-60 nmol/l) tyrosine phosphorylation of the insulin receptor beta-subunit, mitogen-activated protein (MAP) kinase phosphorylation, and glycogen synthase activity were not altered in type 2 diabetic subjects. In contrast, insulin-stimulated tyrosine phosphorylation of IRS-1 and anti-phosphotyrosine-associated PI 3-kinase activity were reduced 40-55% in type 2 diabetic subjects at high insulin concentrations (2.4 and 60 nmol/l, respectively). Impaired glucose transport activity was noted at all insulin concentrations (0.6-60 nmol/l). Aberrant protein expression cannot account for these insulin-signaling defects because expression of insulin receptor, IRS-1, IRS-2, MAP kinase, or glycogen synthase was similar between type 2 diabetic and control subjects. In skeletal muscle from type 2 diabetic subjects, IRS-1 phosphorylation, PI 3-kinase activity, and glucose transport activity were impaired, whereas insulin receptor tyrosine phosphorylation, MAP kinase phosphorylation, and glycogen synthase activity were normal. Impaired insulin signal transduction in skeletal muscle from type 2 diabetic patients may partly account for reduced insulin-stimulated glucose transport; however, additional defects are likely to play a role.

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Authors: Krook, A., Björnholm, M., Galuska, D., Jiang, X. J., Fahlman, R., Myers, M. G., Wallberg-Henriksson, H., & Zierath, J. R.
Affiliations: Karolinska University Hospital (SE)
Department of Clinical Physiology, Karolinska Hospital, Stockholm, Sweden.
ORCID: Krook, A
Björnholm, M
Jiang, X J
Myers, M G
Zierath, J R
Venue: Diabetes
Publisher: American Diabetes Association
Published: 2000-02-01
Volume: 49
Issue: 2
Pages: 284-292
ISSN: 0012-1797 (ISSN-L)
1939-327X
DOI: 10.2337/diabetes.49.2.284
OpenAlex: W2124948826
Cited by: 375
References: 19
Citations by year: 2026: 4 · 2025: 7 · 2024: 10 · 2023: 5 · 2022: 5 · 2021: 13 · 2020: 7 · 2019: 6 · 2018: 20 · 2017: 11 · 2016: 11 · 2015: 13 · 2014: 15 · 2013: 12 · 2012: 13
FWCI: 8.55
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Diabetes (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 › Adipokines, Inflammation, and Metabolic Diseases
Keywords: type 2 diabetes, skeletal muscle, insulin signaling, insulin receptor, IRS-1, insulin receptor substrate 2, phosphatidylinositol 3-kinase, glucose transport, mitogen-activated protein kinase, glycogen synthase, tyrosine phosphorylation, insulin resistance
MeSH terms: Biological Transport, Diabetes Mellitus, Type 2, Glucose, Glycogen Synthase, Humans, Insulin, Male, Middle Aged, Phosphoproteins, Phosphorylation, Receptor, Insulin, Time Factors, Tyrosine, Signal Transduction, Muscle, Skeletal, Phosphotyrosine, Phosphatidylinositol 3-Kinases, Mitogen-Activated Protein Kinases, Insulin Receptor Substrate Proteins

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Characterization of signal transduction and glucose transport in skeletal muscle from type 2 diabetic patients

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