Abnormal regulation of protein tyrosine phosphatase activities in skeletal muscle of insulin-resistant humans

McGuire, M. C., Fields, R. M., Nyomba, B. L., Raz, I., Bogardus, C., Tonks, N. K., Sommercorn, J. (July 1991) Abnormal regulation of protein tyrosine phosphatase activities in skeletal muscle of insulin-resistant humans. Diabetes, 40 (7). pp. 939-942. ISSN 0012-1797

URL: http://www.ncbi.nlm.nih.gov/pubmed/1647997
DOI: 10.2337/diabetes.40.7.939

Abstract

Insulin resistance in skeletal muscle may be an expression of the genetic basis of a common form of non-insulin-dependent diabetes mellitus (NIDDM) in humans. Impaired insulin action results from an apparent postreceptor defect in insulin signal transduction that limits the influence of the hormone on various protein serine/threonine kinases and phosphatases that are thought to contribute to the mechanism by which insulin affects intracellular events. The fact that numerous responses to insulin are affected suggests that the cause of insulin resistance involves an early step in insulin action. Therefore, we examined the influence of insulin on protein tyrosine phosphatase (PTPase) activities, which may counteract the protein tyrosine kinase activity of the insulin receptor in skeletal muscle of insulin-sensitive and insulin-resistant humans. Insulin infusion in vivo produced a rapid 25% suppression of soluble-PTPase activity in muscle of insulin-sensitive subjects, but this response was severely impaired in subjects who were insulin resistant. Insulin did not affect PTPase activity in the particulate fraction of muscle from either group, but basal particulate activity was 33% higher in resistant subjects than in sensitive subjects. Either or both of these abnormal characteristics of PTPase activities could be central to the causes of insulin resistance and NIDDM.

Item Type: Paper
Uncontrolled Keywords: XENOPUS OOCYTES KINASE-ACTIVITY HUMAN-PLACENTA RECEPTOR MICROINJECTION SEQUENCE INVIVO CELLS
Subjects: diseases & disorders > nutritional and metabolic diseases > diabetes
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
organism description > animal > mammal > primates > hominids > human
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein tyrosine phosphatase
CSHL Authors:
Communities: CSHL labs > Tonks lab
Depositing User: Matt Covey
Date: July 1991
Date Deposited: 17 Dec 2013 15:40
Last Modified: 17 Dec 2013 15:40
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29092

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