@article{2cb18dc074c311dbbee902004c4f4f50,
title = "The co-chaperone p23 is degraded by caspases and the proteasome during apoptosis",
abstract = "The heat shock protein 90 co-chaperone p23 has recently been shown to be up-regulated in cancer cells and down-regulated in atheroschlerotic plaques. We found that p23 is degraded during apoptosis induced by several stimuli, including Fas and TNFa-receptor activation as well as staurosporine treatment. Caspase inhibition protected p23 from degradation in several cell lines. In addition, recombinant caspase-3 and 8 cleaved p23 at Asp 142 generating a degradation product of 18 kDa as seen in apoptotic cells. Truncated p23 is further degraded in a proteasome dependent process during apoptosis. Furthermore, we found that the anti-aggregating activity of truncated p23 was reduced compared to full length p23 indicating that caspase mediated p23 degradation contributes to protein destabilisation in apoptosis.",
author = "Jens Mollerup and Berchtold, {Martin Werner}",
note = "Keywords: Hsp90 co-chaperone; Cytosolic prostaglandin E2 synthase; Caspase-3; Caspase-8",
year = "2005",
doi = "10.1016/j.febslet.2005.06.045",
language = "English",
volume = "579",
pages = "4187--4192",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "19",
}
