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Insulin resistance differentially affects the PI 3-kinase- and MAP kinase-mediated signaling in human muscle
Open accessAbstract
The broad nature of insulin resistant glucose metabolism in skeletal muscle of patients with type 2 diabetes suggests a defect in the proximal part of the insulin signaling network. We sought to identify the pathways compromised in insulin resistance and to test the effect of moderate exercise on whole-body and cellular insulin action. We conducted euglycemic clamps and muscle biopsies on type 2 diabetic patients, obese nondiabetics and lean controls, with and without a single bout of exercise. Insulin stimulation of the phosphatidylinositol 3-kinase (PI 3-kinase) pathway, as measured by phosphorylation of the insulin receptor and IRS-1 and by IRS protein association with p85 and with PI 3-kinase, was dramatically reduced in obese nondiabetics and virtually absent in type 2 diabetic patients. Insulin stimulation of the MAP kinase pathway was normal in obese and diabetic subjects. Insulin stimulation of glucose-disposal correlated with association of p85 with IRS-1. Exercise 24 hours before the euglycemic clamp increased phosphorylation of insulin receptor and IRS-1 in obese and diabetic subjects but did not increase glucose uptake or PI 3-kinase association with IRS-1 upon insulin stimulation. Thus, insulin resistance differentially affects the PI 3-kinase and MAP kinase signaling pathways, and insulin-stimulated IRS-1-association with PI 3-kinase defines a key step in insulin resistance.
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“Using the euglycemic insulin clamp with skeletal muscle biopsy, a number of investigators have examined the insulin signal transduction system in human skeletal muscle of type 2 diabetic subjects and consistently demonstrated defects in IRS-1 tyrosine phosphorylation and PI-3 kinase and Akt activation ( 26 , 54 , 55 ).”
From Skeletal Muscle Insulin Resistance Is the Primary Defect in Type 2 Diabetes (2009) · cites this paper as [54]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Insulin resistance in skeletal muscle is manifested by decreased insulin-stimulated glucose uptake and results from impaired insulin signaling and multiple post-receptor intracellular defects including impaired glucose transport, glucose phosphorylation, and reduced glucose oxidation and glycogen synthesis.”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [7]
In the citing paper
“In contrast, as the MAPK pathway has normal sensitivity to insulin, hyperinsulinemia activates the MAPK pathway, promoting vascular smooth muscle cell growth and activating inflammatory pathways, such as IkB/NF-kB and JNK [107,108].”
From Sarcopenic obesity, insulin resistance, and their implications in cardiovascular and metabolic consequences (2020) · cites this paper as [107]
In the citing paper
“Association of the p85 subunit of PI3K with IRS-1 and activation of PI3K also are greatly attenuated in obese nondiabetic and type 2 diabetic subjects compared with lean healthy controls [7, 165, 166].”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [7]
In the citing paper
“The ability of insulin to activate insulin receptor and IRS-1 tyrosine phosphorylation in muscle in obese nondiabetic subjects is modestly reduced; whereas in type 2 diabetics insulin-stimulated insulin receptor and IRS-1 tyrosine phosphorylation are severely impaired [7].”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [7]
In the citing paper
“Most [1, 7, 152, 153, 156, 161] but not all [155] investigators have found a reduction in tyrosine kinase activity that cannot be explained by alterations in insulin receptor number or insulin receptor binding affinity.”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [7]
In the citing paper
“In insulin-resistant obese nondiabetic subjects, in the NGT insulin resistant offspring of two diabetic parents, and in type 2 diabetic subjects, a substantial decrease in insulin receptor tyrosine phosphorylation has been demonstrated.”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [7]
In the citing paper
“The decrease in insulin-stimulated association of the p85 regulatory subunit of PI3K with IRS-1 is closely correlated with the reduction in insulin-stimulated muscle glycogen synthase activity and in vivo insulin-stimulated glucose disposal [7].”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [7]
In the citing paper
“Intact stimulation of the MAPK pathway by insulin in the presence of insulin resistance in the PI3K pathway may play an important role in the development of atherosclerosis [7].”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [7]
In the citing paper
“Insulin resistance in the PI3K signaling pathway contrasts with an intact stimulation of the MAPK pathway by insulin in insulin-resistant type 2 diabetic and obese nondiabetics individuals [7, 165].”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [7]
In the citing paper
“Under basal conditions, total glycogen synthase activity in type 2 diabetic subjects is reduced, and the ability of insulin to activate glycogen synthase is severely impaired [7, 215–217].”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [7]
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Self-citation
Metadata
- Authors
- Cusi, K., Maezono, K., Osman, A., Pendergrass, M., Patti, M. E., Pratipanawatr, T., DeFronzo, R. A., Kahn, C. R., & Mandarino, L. J.
- Affiliations
- The University of Texas at San Antonio Health Science Center (US)
- Harvard University (US)
- Tulane University (US)
- Joslin Diabetes Center (US)
- Corresponding author
- Mandarino, Lawrence J.
- ORCID
- Venue
- Journal of Clinical Investigation
- Published
- 2000-02-01
- Volume
- 105
- Issue
- 3
- Pages
- 311-320
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC377440
- OpenAlex
- W2120852510
- Cited by
- 1,139
- References
- 48
- Citations by year
- 2026: 12 · 2025: 13 · 2024: 19 · 2023: 27 · 2022: 35 · 2021: 45 · 2020: 33 · 2019: 35 · 2018: 24 · 2017: 37 · 2016: 52 · 2015: 54 · 2014: 53 · 2013: 57 · 2012: 65
- FWCI
- 13.25
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Diabetes Association
- National Institutes of Health (5k08dk002526-03)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01-DK-24092, DK02526, R01DK047936, R01DK033201, R01DK024092, R01-DK-47936)
- National Center for Research Resources (M01RR001346)
- 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
- insulin resistance, skeletal muscle, type 2 diabetes, PI3K signaling, MAPK signaling, insulin receptor, IRS-1, p85 regulatory subunit, physical activity, glucose uptake, obesity, euglycemic clamp, insulin signaling
- MeSH terms
- Adult, Diabetes Mellitus, Type 2, Female, Humans, Insulin Resistance, Male, Phosphoproteins, Receptor, Insulin, Signal Transduction, Muscle, Skeletal, Phosphatidylinositol 3-Kinases, Mitogen-Activated Protein Kinases, Insulin Receptor Substrate Proteins
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