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

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Standard

The co-chaperone p23 is degraded by caspases and the proteasome during apoptosis. / Mollerup, Jens; Berchtold, Martin Werner.

I: FEBS Letters, Bind 579, Nr. 19, 2005, s. 4187-4192.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Mollerup, J & Berchtold, MW 2005, 'The co-chaperone p23 is degraded by caspases and the proteasome during apoptosis', FEBS Letters, bind 579, nr. 19, s. 4187-4192. https://doi.org/10.1016/j.febslet.2005.06.045

APA

Mollerup, J., & Berchtold, M. W. (2005). The co-chaperone p23 is degraded by caspases and the proteasome during apoptosis. FEBS Letters, 579(19), 4187-4192. https://doi.org/10.1016/j.febslet.2005.06.045

Vancouver

Mollerup J, Berchtold MW. The co-chaperone p23 is degraded by caspases and the proteasome during apoptosis. FEBS Letters. 2005;579(19):4187-4192. https://doi.org/10.1016/j.febslet.2005.06.045

Author

Mollerup, Jens ; Berchtold, Martin Werner. / The co-chaperone p23 is degraded by caspases and the proteasome during apoptosis. I: FEBS Letters. 2005 ; Bind 579, Nr. 19. s. 4187-4192.

Bibtex

@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",

}

RIS

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

VL - 579

SP - 4187

EP - 4192

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 19

ER -

ID: 87730