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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Corticotropin-releasing hormone activates protein kinase C in an isoenzyme-specific manner. Dermitzaki, E., Tsatsanis, C., Charalampopoulos, I., Androulidaki, A., Alexaki, V.I., Castanas, E., Gravanis, A., Margioris, A.N. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
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