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Corticotropin-releasing hormone activates protein kinase C in an isoenzyme-specific manner.

Abstract：

:Protein kinase C (PKC) has recently emerged as mediator of corticotropin-releasing hormone (CRH) effects. Aim of the present study was to study the effects of CRH on each PKC isoenzyme. As a model we have used the PC12 rat pheochromocytoma cell line, expressing the CRH type 1 receptor (CRHR1). Our data were as follows: (a) CRH-induced rapid phosphorylation of conventional PKCalpha and PKCbeta, accompanied by parallel increase of their concentration within nucleus. (b) CRH suppressed the phosphorylation of novel PKCdelta and PKCtheta;, which remained in the cytosol. (c) CRH-induced transient phosphorylation of atypical PKClambda and had no effect on PKCmu. (d) The effect of CRH on each PKC isoenzyme was blocked by a CRHR1 antagonist. (e) Blockade of conventional PKC phosphorylation inhibited CRH-induced calcium ion mobilization from intracellular stores as well as the CRH-induced apoptosis and Fas ligand production. In conclusion, our findings suggest that CRH via its CRHR1 receptor differentially regulates PKC-isoenzyme phosphorylation, an apparently physiologically relevant effect since blockade of conventional PKC phosphorylation abolished the biological effect of CRH.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Dermitzaki E,Tsatsanis C,Charalampopoulos I,Androulidaki A,Alexaki VI,Castanas E,Gravanis A,Margioris AN

doi

10.1016/j.bbrc.2004.12.078

subject

Has Abstract

pub_date

2005-02-18 00:00:00

pages

828-36

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(04)02852-9

journal_volume

327

pub_type

杂志文章

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