The DOI matches its Crossref record; 65 of the 65 references it cites were found in a registry or an index.
Insulin receptor kinase in human skeletal muscle from obese subjects with and without noninsulin dependent diabetes.
Open accessAbstract
We have studied the structure and function of the insulin receptors in obese patients with and without noninsulin dependent diabetes mellitus (NIDDM) and in nonobese controls using partially purified receptors from muscle biopsies. Insulin binding was decreased in obesity due to reduced number of binding sites but no differences were observed in insulin binding between obese subjects with or without NIDDM. The structural characteristics of the receptors, as determined by affinity labeling methods and electrophoretic mobility of the beta-subunit, were not altered in obese or NIDDM compared to normal weight subjects. Furthermore, the ability of insulin to stimulate the autophosphorylation of the beta-subunit and the phosphoamino acid composition of the phosphorylated receptor were the same in all groups. However, insulin receptor kinase activity was decreased in obesity using Glu4:Tyr1 as exogenous phosphoacceptor without any appreciable additional defect when obesity was associated with NIDDM. Thus, our data are supportive of the hypothesis that in muscle of obese humans, insulin resistance is partially due to decreased insulin receptors and insulin receptor kinase activity. In NIDDM the defect(s) in muscle is probably distal to the insulin receptor kinase.
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“insulin binding to solubilized receptors obtained from skeletal muscle and liver has been shown to be normal in obese and lean diabetic individuals [152, 153, 155].”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [152]
In the citing paper
“Early studies have demonstrated a modest 20–30% reduction in insulin binding to monocytes and adipocytes from type 2 diabetic patients, but this has not been a consistent finding [1, 151–154].”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [152]
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 [152]
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Metadata
- Authors
- Caro, J. F., Sinha, M. K., Raju, S. M., Ittoop, O., Pories, W. J., Flickinger, E. G., Meelheim, D., & Dohm, G. L.
- Affiliations
- East Carolina University (US)
- ORCID
- Pories, W J
- Venue
- Journal of Clinical Investigation
- Published
- 1987-05-01
- Volume
- 79
- Issue
- 5
- Pages
- 1330-1337
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC424378
- OpenAlex
- W2104713078
- Cited by
- 341
- References
- 60
- Citations by year
- 2026: 1 · 2024: 6 · 2023: 2 · 2022: 5 · 2021: 6 · 2020: 2 · 2019: 3 · 2018: 3 · 2017: 2 · 2016: 8 · 2015: 5 · 2014: 4 · 2013: 3 · 2012: 6
- FWCI
- 7.58
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (2r01am032585-03)
- 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 receptor kinase, insulin receptor, skeletal muscle, obesity, type 2 diabetes, insulin resistance, insulin binding, receptor autophosphorylation, receptor beta-subunit, affinity labeling
- MeSH terms
- Adult, Diabetes Mellitus, Diabetes Mellitus, Type 2, Female, Humans, Insulin, Insulin Resistance, Male, Muscles, Obesity, Phosphorylation, Protein-Tyrosine Kinases, Receptor, Insulin
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