Literature DB >> 6320711

Cell membrane signals in the mechanism of insulin action. Claude P. Brown memorial lecture.

K Cheng, M Thompson, J Craig, C Schwartz, E Locher, J Larner.   

Abstract

Present evidence points to the rapid formation of one or several mediators by proteolysis initiated by insulin and, possibly, other hormones. Mediators act intracellularly at a number of subcellular sites, including cytoplasm, mitochondria, endoplasmic reticulum, cell membrane, and nucleus (figure 9). These mediators control enzymes that are controlled by covalent phosphorylation. As a result, the mediators impart an overall integrated control of metabolism. Evidence strongly suggests that the mediators are peptides. They appear to be formed by limited proteolysis from cell membrane proteins or glycoproteins and act as transmembrane signals following the binding of insulin to its receptor and the activation of the insulin-receptor complex.

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Year:  1984        PMID: 6320711

Source DB:  PubMed          Journal:  Ann Clin Lab Sci        ISSN: 0091-7370            Impact factor:   1.256


  2 in total

1.  Defective insulin response of cyclic adenosine monophosphate-dependent protein kinase in insulin-resistant humans.

Authors:  Y Kida; B L Nyomba; C Bogardus; D M Mott
Journal:  J Clin Invest       Date:  1991-02       Impact factor: 14.808

2.  Further evidence for the involvement of a membrane proteolytic step in insulin action.

Authors:  G Cherqui; M Caron; J Capeau; J Picard
Journal:  Biochem J       Date:  1985-04-01       Impact factor: 3.857

  2 in total

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