Insulin-like growth factor I binding and receptor kinase in red and white muscle.

Abstract:

:IGF-I receptors were partially purified from red and white skeletal muscle by lectin-affinity chromatography and the resultant fraction was depleted of insulin receptors by insulin affinity chromatography. Equilibrium binding of 125I-IGF-I to receptor preparations from red and white muscle yielded identical Scatchard plots. The integrity of the IGF-I receptor preparation in the two fiber types was identical as determined by affinity cross-linking. The tyrosine kinase activity of the receptor from red muscle was 2-3-fold more active towards exogenous substrates in both the basal and ligand-activated states as compared to white muscle. These data show that there is IGF-I-dependent kinase activity intrinsic to IGF-I receptors from skeletal muscle, and suggest that identical cellular factors may regulate the kinase activity of insulin and IGF-I receptors in a parallel manner in vivo.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Zorzano A,James DE,Ruderman NB,Pilch PF

doi

10.1016/0014-5793(88)80093-0

subject

Has Abstract

pub_date

1988-07-18 00:00:00

pages

257-62

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(88)80093-0

journal_volume

234

pub_type

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