Interleukin 1 Induces Early Protein Phosphorylation and Requires Only a Short Exposure for Late Induced Secretion of Beta-endorphin in a Mouse Pituitary Cell Line

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1990 Apr 1

PMID 2157204

Citations 2

Authors

M O Fagarasan

J F Bishop

M S Rinaudo

J Axelrod

Affiliations

Soon will be listed here.

Abstract

Previous work has shown that prolonged pretreatment of a mouse anterior pituitary cell line, AtT-20 cells, with the cytokine interleukin 1 (IL-1) stimulates beta-endorphin release and potentiates the secretion induced by many secretagogues. Desensitization of protein kinase C (PKC) by pretreatment with phorbol ester [phorbol 12-tetradecanoate 13-acetate (TPA)] for 8 hr abolished the secretion induced by TPA as well as the enhancement of TPA-induced beta-endorphin release produced by IL-1. Desensitization of PKC only partly abolished the potentiating effects of IL-1 on corticotropin-releasing factor-induced beta-endorphin secretion. In contrast, IL-1-induced beta-endorphin release was independent of PKC. We observed that treatment of AtT-20 cells with IL-1 markedly phosphorylated 19-, 20-, and 60-kDa proteins within minutes, presumably by early activation of protein kinases. Prolonged treatment with TPA, which was shown to desensitize an 87-kDa protein (a substrate for PKC), had no effect on IL-1-induced phosphorylation of 20-, 60-, and 87-kDa proteins, indicating that the phosphorylation of these proteins does not involve PKC. IL-1 does not generate cAMP in AtT-20 cells, suggesting that a cAMP-dependent protein kinase is also not involved. Prolonged treatment with IL-1 abolishes the capacity of cytokine to induce the phosphorylation of 20- and 60-kDa proteins. The presence of IL-1 was required initially only for a short time to induce late secretion in AtT-20 cells. These observations indicate that once IL-1 generates an early signal, its presence is no longer necessary for the subsequent secretion of beta-endorphin.

Citing Articles

Interleukin 1 induces beta-endorphin secretion via Fos and Jun in AtT-20 pituitary cells.

Fagarasan M, Aiello F, Muegge K, Durum S, Axelrod J Proc Natl Acad Sci U S A. 1990; 87(20):7871-4.

PMID: 1978316 PMC: 54852. DOI: 10.1073/pnas.87.20.7871.

Investigation of guanine-nucleotide-binding protein involvement and regulation of cyclic AMP metabolism in interleukin 1 signal transduction.

Ray K, Thompson N, Kennard N, Rollins P, Grenfell S, Witham S Biochem J. 1992; 282 ( Pt 1):59-67.

PMID: 1311561 PMC: 1130889. DOI: 10.1042/bj2820059.

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