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IRR: A Novel Member of the Insulin Receptor Family
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IRR: A Novel Member of the Insulin Receptor Family

Abstract

Insulin’s effects, including its pivotal regulation of blood glucose levels, are mediated by a cell-surface receptor (reviewed in Olefsky, 1990; Ullrich and Schlessinger, 1990). The structure of the insulin receptor, defined using recombinant DNA techniques, exhibits a high degree of overall similarity with the receptor for the structurally related insulin-like growth factor (IGF), IGF-I (for review, see Czech, 1989). These heterotetrameric glycoproteins consists of extracellular a-subunits containing the insulin-binding region disulfide-bonded to β-subunits which span the membrane and contain a cytoplasmic tyrosine kinase activated by insulin binding (Ebina et al., 1985; Ullrich et al., 1985; Ullrich et al., 1986). The α-and β-subunits are derived by proteolytic cleavage of the proreceptor.

Authors

Watt VM; Shier P; Chan J; Petrisor BA; Mathi SK

Series

Advances in Experimental Medicine and Biology

Volume

343

Pagination

pp. 125-132

Publisher

Springer Nature

Publication Date

January 1, 1993

DOI

10.1007/978-1-4615-2988-0_13

Conference proceedings

Advances in Experimental Medicine and Biology

ISSN

0065-2598
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