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PMID: 2068102 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Phosphatidate-dependent protein phosphorylation.

Bocckino SB, Wilson PB, Exton JH

Abstract

Phosphatidate-dependent protein phosphorylation was observed in soluble extracts from rat liver, brain, lung, and testis. The phosphorylation was stimulated by free Ca2+ in the range of 360-800 nM. Incubation mixtures containing phosphatidate provided markedly different profiles of protein phosphorylation from those with phosphatidylserine plus 1,2-diolein. Phosphatidate-dependent phosphorylation of a 30-kDa protein in the soluble fraction from heart was also observed. This phosphorylation did not require Ca2+. Soluble fractions from liver, testis, brain, and lung phosphorylated the 30-kDa heart protein in a phosphatidate-dependent Ca(2+)-independent manner. We propose that part of the action of phosphatidate in cells may be mediated by a protein kinase(s).

MeSH Terms
Adenosine Triphosphate/metabolism Animals Brain/metabolism Cytosol/metabolism Electrophoresis, Polyacrylamide Gel Kinetics Liver/metabolism Lung/metabolism Male Molecular Weight Myocardium/metabolism Organ Specificity Phosphatidic Acids/pharmacology Phosphoproteins/isolation & purification Phosphorylation Proteins/metabolism Rats Rats, Inbred Strains Testis/metabolism
Chemicals
Phosphatidic Acids Phosphoproteins Proteins Adenosine Triphosphate
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Bocckino S B
Howard Hughes Medical Institute Laboratory, Vanderbilt University School of Medicine, Nashville, TN 37232-0295.
Wilson P B
Exton J H
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34 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1991-07-15
Pages
6210-3
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC52052
Subset
IM
Grants
NIGMS NIH HHS · GM40919 · United States
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