Photoaffinity Labelling of Hepatic Plasma Membranes Suggests Two Classes of Hepatic Insulin Receptor

Overview

Journal Diabetologia

Specialty Endocrinology

Date 1985 Oct 1

PMID 2998914

Citations 2

Authors

F J Haynes

C C Yip

Affiliations

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Abstract

Photoaffinity labelling of hepatic insulin receptors revealed specifically-labelled bands of 130, 90 and 40 kDa. Endogenous protease activity in hepatic plasma membranes, as well as contaminating proteases present in preparations of clostridial collagenase, degraded some of the 130-kDa insulin-binding subunit to a 115-kDa form. However, a large proportion of the 130-kDa subunits were resistant to degradation, suggesting the presence of two classes of insulin receptor in hepatic plasma membranes. In one class the 130-kDa subunit was sensitive to proteolysis, while in the other it was not. In contrast, the 130-kDa receptor subunits of adipose tissue were all resistant to such degradation. Scatchard analysis of control and collagenase-treated plasma membranes demonstrated that conversion of the 130-kDa subunit to a 115-kDa form did not affect the insulin-binding characteristics of the receptor. It was also apparent that insulin binds to a single class of high-affinity sites in hepatic plasma membranes.

Citing Articles

Cell-surface insulin receptor cycling and its implication in the glycogenic response in cultured foetal hepatocytes.

Soubigou P, Pringault E, Plas C Biochem J. 1986; 239(3):609-15.

PMID: 3548701 PMC: 1147330. DOI: 10.1042/bj2390609.

The structure of the hepatic insulin receptor and insulin binding.

Haynes F, Helmerhorst E, Yip C Biochem J. 1986; 239(1):127-33.

PMID: 3026365 PMC: 1147249. DOI: 10.1042/bj2390127.

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