A New Negatively Regulated Acute-phase Phosphoprotein Synthesized by Rat Hepatocytes

Overview

Journal Biochem J

Specialty Biochemistry

Date 1985 Sep 15

PMID 4062865

Citations 2

Authors

A Le Cam

G Le Cam

Affiliations

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Abstract

The effect of acute inflammation on the production of the major phosphorylated protein (PP63) excreted by rat hepatocytes was investigated. Both intra- and extracellular forms of the protein labelled with [32P]Pi, [3H]fucose and [35S]methionine were immunoprecipitated with monospecific polyclonal antibodies, and relative rates of PP63 synthesis were measured. The hepatocytes of acutely inflamed rats produced and excreted 85% less 32P- and 3H-labelled PP63 than did control cells. This decreased amount of PP63 did not result from an impairment in the phosphorylation or glycosylation processes or from a blockade in excretion, but rather was found to be due to extensive shut-off in biosynthesis of the protein as measured by [35S]methionine incorporation. Thus PP63 would appear to represent a new negatively regulated acute-phase protein.

Citing Articles

Conditioned media of Kupffer and endothelial liver cells influence protein phosphorylation in parenchymal liver cells. Involvement of prostaglandins.

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PMID: 3166374 PMC: 1149185. DOI: 10.1042/bj2520601.

Functional characterization of the promoter of pp63, a gene encoding a natural inhibitor of the insulin receptor tyrosine kinase.

Falquerho L, Paquereau L, Vilarem M, Galas S, Patey G, Le Cam A Nucleic Acids Res. 1992; 20(8):1983-90.

PMID: 1579501 PMC: 312316. DOI: 10.1093/nar/20.8.1983.

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