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Statements

Subject Item
n2:RIV%2F00209805%3A_____%2F12%3A%230000328%21RIV13-MZ0-00209805
rdf:type
n14:Vysledek skos:Concept
rdfs:seeAlso
http://www.springerlink.com/content/j27772813123n887/
dcterms:description
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 that the 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. Nonproliferating cells 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 over-expression of HOP in proliferating cells may contribute to excessive Hsp90 activity and stabilization of client proteins in tumors. In a panel of colorectal cancer samples, increased expression of Hsp70 and an increased ratio of HOP to CHIP were found, and were associated with decreased median survival. These data indicate that multiple changes occur in the chaperone/cochaperone system in cancer that impact patient survival. It is likely that the ability to identify individual alterations to this system will be beneficial for treatment strategy decisions, particularly those that employ chaperone inhibitors. 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 that the 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. Nonproliferating cells 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 over-expression of HOP in proliferating cells may contribute to excessive Hsp90 activity and stabilization of client proteins in tumors. In a panel of colorectal cancer samples, increased expression of Hsp70 and an increased ratio of HOP to CHIP were found, and were associated with decreased median survival. These data indicate that multiple changes occur in the chaperone/cochaperone system in cancer that impact patient survival. It is likely that the ability to identify individual alterations to this system will be beneficial for treatment strategy decisions, particularly those that employ chaperone inhibitors.
dcterms:title
Alteration of the HSP70/HSP90 chaperone and the HOP/CHIP co-chaperone system in cancer Alteration of the HSP70/HSP90 chaperone and the HOP/CHIP co-chaperone system in cancer
skos:prefLabel
Alteration of the HSP70/HSP90 chaperone and the HOP/CHIP co-chaperone system in cancer Alteration of the HSP70/HSP90 chaperone and the HOP/CHIP co-chaperone system in cancer
skos:notation
RIV/00209805:_____/12:#0000328!RIV13-MZ0-00209805
n14:predkladatel
n17:ico%3A00209805
n3:aktivita
n10:P
n3:aktivity
P(NS9812)
n3:cisloPeriodika
3
n3:dodaniDat
n16:2013
n3:domaciTvurceVysledku
n9:5713021 n9:5395488 n9:7623933 n9:9637419
n3:druhVysledku
n12:J
n3:duvernostUdaju
n15:S
n3:entitaPredkladatele
n19:predkladatel
n3:idSjednocenehoVysledku
121744
n3:idVysledku
RIV/00209805:_____/12:#0000328
n3:jazykVysledku
n18:eng
n3:klicovaSlova
Chaperone; Co-chaperone; Cancer; Hsp90; Hsp70; HOP; CHIP; HSF1; 17AAG
n3:klicoveSlovo
n4:HOP n4:Co-chaperone n4:Hsp90 n4:HSF1 n4:Chaperone n4:Hsp70 n4:17AAG n4:Cancer n4:CHIP
n3:kodStatuVydavatele
PL - Polská republika
n3:kontrolniKodProRIV
[C4C394FCCC3A]
n3:nazevZdroje
Cellular and molecular biology letters
n3:obor
n11:FD
n3:pocetDomacichTvurcuVysledku
4
n3:pocetTvurcuVysledku
4
n3:projekt
n20:NS9812
n3:rokUplatneniVysledku
n16:2012
n3:svazekPeriodika
17
n3:tvurceVysledku
Vojtěšek, Bořivoj Nenutil, Rudolf Müller, Petr Růčková, Eva
n3:wos
000305349300009
s:issn
1425-8153
s:numberOfPages
13
n6:doi
10.2478/s11658-012-0021-8