Alteration of the HSP70/HSP90 chaperone and the HOP/CHIP co-chaperone system in cancer

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00209805%3A_____%2F12%3A%230000328" target="_blank" >RIV/00209805:_____/12:#0000328 - isvavai.cz</a>

Výsledek na webu

<a href="http://www.springerlink.com/content/j27772813123n887/" target="_blank" >http://www.springerlink.com/content/j27772813123n887/</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.2478/s11658-012-0021-8" target="_blank" >10.2478/s11658-012-0021-8</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Alteration of the HSP70/HSP90 chaperone and the HOP/CHIP co-chaperone system in cancer

Popis výsledku v původním jazyce

Activation of the Hsp90 chaperone system is a characteristic of cancer cells. The regulation of chaperone activities involves their interaction with cochaperones; therefore we investigated the expression of Hsp70 and Hsp90 and their specific co-chaperones HOP and CHIP in cancer cell lines and primary cancers. Inhibition of Hsp90 by 17AAG increased the levels of Hsp70, Hsp90 and HOP but not CHIP mRNA in cancer cells. These changes are linked to activation of the HSF1 transcription factor and we show thatthe HOP promoter contains HSF1 binding sites, and that HSF1 binding to the HOP promoter is increased following 17AAG. The lack of alteration in the co-chaperone CHIP is explained by a lack of HSF response elements in the CHIP promoter. Nonproliferatingcells expressed higher levels of CHIP and lower HOP, Hsp70 and Hsp90 levels compared to proliferating cells. Decreased expression of CHIP in proliferating cancer cells is in keeping with its proposed tumor suppressor properties, while ove

Název v anglickém jazyce

Alteration of the HSP70/HSP90 chaperone and the HOP/CHIP co-chaperone system in cancer

Popis výsledku anglicky

Activation of the Hsp90 chaperone system is a characteristic of cancer cells. The regulation of chaperone activities involves their interaction with cochaperones; therefore we investigated the expression of Hsp70 and Hsp90 and their specific co-chaperones HOP and CHIP in cancer cell lines and primary cancers. Inhibition of Hsp90 by 17AAG increased the levels of Hsp70, Hsp90 and HOP but not CHIP mRNA in cancer cells. These changes are linked to activation of the HSF1 transcription factor and we show thatthe HOP promoter contains HSF1 binding sites, and that HSF1 binding to the HOP promoter is increased following 17AAG. The lack of alteration in the co-chaperone CHIP is explained by a lack of HSF response elements in the CHIP promoter. Nonproliferatingcells expressed higher levels of CHIP and lower HOP, Hsp70 and Hsp90 levels compared to proliferating cells. Decreased expression of CHIP in proliferating cancer cells is in keeping with its proposed tumor suppressor properties, while ove

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

FD - Onkologie a hematologie

OECD FORD obor

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Projekt

<a href="/cs/project/NS9812" target="_blank" >NS9812: Ubiquitin-chaperonový degradační systém a jeho role v procesu nádorové přeměny buňky: možnosti ovlivnění jeho buněčných funkcí cílenými inhibitory.</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2012

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Cellular and molecular biology letters

ISSN

1425-8153

e-ISSN

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Svazek periodika

17

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

PL - Polská republika

Počet stran výsledku

13

Strana od-do

446-458

Kód UT WoS článku

000305349300009

EID výsledku v databázi Scopus

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