The co-chaperone p23 is degraded by caspases and the proteasome during apoptosis

Jens Mollerup; Martin Werner Berchtold

doi:10.1016/j.febslet.2005.06.045

The co-chaperone p23 is degraded by caspases and the proteasome during apoptosis

19 Citations (Scopus)

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.

Original language	English
Journal	FEBS Letters
Volume	579
Issue number	19
Pages (from-to)	4187-4192
ISSN	0014-5793
DOIs	https://doi.org/10.1016/j.febslet.2005.06.045
Publication status	Published - 2005

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10.1016/j.febslet.2005.06.045

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@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 = "FEBS Letters",

issn = "0014-5793",

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number = "19",

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TY - JOUR

T1 - The co-chaperone p23 is degraded by caspases and the proteasome during apoptosis

AU - Mollerup, Jens

AU - Berchtold, Martin Werner

N1 - Keywords: Hsp90 co-chaperone; Cytosolic prostaglandin E2 synthase; Caspase-3; Caspase-8

PY - 2005

Y1 - 2005

N2 - 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.

AB - 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.

U2 - 10.1016/j.febslet.2005.06.045

DO - 10.1016/j.febslet.2005.06.045

M3 - Journal article

C2 - 16038904

SN - 0014-5793

VL - 579

SP - 4187

EP - 4192

JO - FEBS Letters

JF - FEBS Letters

IS - 19

ER -

The co-chaperone p23 is degraded by caspases and the proteasome during apoptosis

Abstract

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