Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Biochem Biophys Res Commun. 2003 Mar 28;303(1):350-6.

The eta isoform of protein kinase C inhibits UV-induced activation of caspase-3 in normal human keratinocytes.

Author information

  • 1Institute of Molecular Oncology, Showa University, Shinagawa-ku, Tokyo 142-8555, Japan.

Abstract

Protein kinase C (PKC) fulfills a central role in the decision of cell fate in keratinocytes. Both PKC delta and PKC eta induce growth inhibition and differentiation of normal human keratinocytes (NHK). Here we show that PKC delta and PKC eta play opposite roles in UVB-induced apoptosis in NHK. PKC delta enhanced UVB-induced caspase-3 activity, while overexpression of PKC eta reduced it. In keeping with these observations, the dominant negative mutant of PKC delta significantly inhibited the activation of caspase-3, whereas dominant negative PKC eta increased it in a dose (MOI)-dependent manner. Unlike PKC delta, cleavage and translocation to mitochondria of PKC eta were not observed, resulting in no detection of cytochorome c release. Furthermore, UV-induced activation of p38 MAP kinase, which suppressed the caspase-3 activity in NHK, was blocked by dominant negative PKC eta. These findings suggest that PKC eta negatively regulates UV-induced apoptosis through its localization, resistance to cleavage, and the p38 MAPK pathway.

PMID:
12646210
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk