UMMS Affiliation

University of Massachusetts Medical Center; Program in Molecular Medicine

Date

2-15-1988

Document Type

Article

Subjects

Adipose Tissue; Animals; Cell Membrane; Electrophoresis, Polyacrylamide Gel; Insulin; Insulin-Like Growth Factor II; Octoxynol; Phosphorylation; Polyethylene Glycols; Protein-Tyrosine Kinases; Rats; Rats, Inbred Strains; Receptor, Insulin; Receptors, Somatomedin; Somatomedins; Tyrosine

Disciplines

Medical Molecular Biology

Abstract

Insulin action in intact adipocytes leads to a rapid increase in the concentration of receptors for insulin-like growth factor (IGF) II on the adipocyte cell surface, and to a decrease in the [32P]phosphate content of these receptors on the plasma membrane [Corvera and Czech (1985) Proc. Natl. Acad. Sci. U.S.A. 82. 7314-7318]. It has been previously shown that the receptor for IGF-II can be phosphorylated on tyrosine residues by a kinase activity which is expressed in isolated adipocyte plasma membranes. It is now shown that IGF-II-receptor phosphorylation in vitro, in plasma membranes derived from insulin-treated cells, is markedly decreased compared with the phosphorylation of the receptor in membranes from control cells. This effect of insulin cannot be attributed to an increase in the activity of phosphotyrosyl phosphatase in the membranes. The tyrosine kinase that catalyses the phosphorylation of IGF-II receptors is associated with a fraction of the plasma membrane which is insoluble in Triton X-100. Removal of the Triton X-100-soluble components of the membrane markedly enhances receptor phosphorylation. Moreover, the expression of the inhibitory effect of insulin requires the presence of one or several Triton X-100-soluble components of the plasma membrane.

Rights and Permissions

Citation: Biochem J. 1988 Feb 15;250(1):47-52.

Related Resources

Link to article in PubMed

Journal Title

The Biochemical journal

PubMed ID

2965577

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