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PMID: 6751318 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Preliminary characterization of a heat-stable protein from rat adipose tissue whose phosphorylation is stimulated by insulin.

The Biochemical journal ·Vol. 204 ·No. 3 ·1982-06-15 ·Pages 817-24

Blackshear PJ, Nemenoff RA, Avruch J

Abstract

Exposure of 32P-labelled isolated rat adipocytes or epididymal fat-pads to insulin resulted in an increase in the phosphorylation of a heat-stable acid-soluble protein of Mr 22 000. The phosphorylation of this protein was unaffected by isoprenaline (isoproterenol) in intact cells, nor was its phosphorylation catalysed by exposure in vitro to the cyclic AMP-dependent protein kinase or smooth-muscle myosin light-chain kinase. The properties of the Mr-22 000 protein include: heat-stability; solubility in 1% trichloroacetic acid; pI 4.9; elution at apparent Mr 37 500 on gel filtration; and it contains both phosphoserine and phosphothreonine. It can be distinguished from the heat-stable phosphatase inhibitor 1 of adipose tissue (inhibitor 1A) and the phosphorylated form of adipose-tissue myosin light chain by several criteria. Its identity, and the possible functional significance of the insulin-stimulated phosphorylation, remain problems for future study.

MeSH Terms
Adipose Tissue/cytology,drug effects,metabolism Animals Cell-Free System Electrophoresis, Polyacrylamide Gel Hot Temperature In Vitro Techniques Insulin/pharmacology Male Myosins/metabolism Phosphoproteins/metabolism Phosphorylation Rats Rats, Inbred Strains
Chemicals
Insulin Phosphoproteins Myosins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Blackshear P J
Nemenoff R A
Avruch J
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19 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2040817
Published
1982-06-15
Pages
817-24
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1158425
Subset
IM
Grants
NIADDK NIH HHS · AM 17776 · United States
External Links
PubMed source DOI: 10.1042/bj2040817 PMC Full Text View journal details
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