Insulin action inhibits insulin-like growth factor-II (IGF-II) receptor phosphorylation in H-35 hepatoma cells. IGF-II receptors isolated from insulin-treated cells exhibit enhanced in vitro phosphorylation by casein kinase II.-Reference-Cited by-同舟云学术

Insulin action inhibits insulin-like growth factor-II (IGF-II) receptor phosphorylation in H-35 hepatoma cells. IGF-II receptors isolated from insulin-treated cells exhibit enhanced in vitro phosphorylation by casein kinase II.

Published:1988-03 Issue:7 Volume:263 Page:3116-3122
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Corvera S,Roach P J,DePaoli-Roach A A,Czech M P

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference30 articles.

1. Insulin action rapidly modulates the apparent affinity of the insulin-like growth factor II receptor.

2. Potential mechanism of the stimulatory action of insulin on insulin-like growth factor II binding to the isolated rat adipose cell. Apparent redistribution of receptors cycling between a large intracellular pool and the plasma membrane.

3. Insulin activates the appearance of insulin-like growth factor II receptors on the adipocyte cell surface.

4. The type II insulin-like growth factor receptor is internalized and recycles in the absence of ligand.

5. Mechanism of insulin action on membrane protein recycling: a selective decrease in the phosphorylation state of insulin-like growth factor II receptors in the cell surface membrane.

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