Hsp90 inhibitor geldanamycin increases hsp70 mRNA stabilisation but fails to activate HSF1 in cells exposed to hydrostatic pressure

被引：16
作者：
Elo, MA
Kaarniranta, K
Helminen, HJ
Lammi, MJ
机构：
[1] Univ Kuopio, Dept Anat, FIN-70211 Kuopio, Finland
[2] Kuopio Univ Hosp, Dept Ophthalmol, Kuopio 70211, Finland
来源：
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2005年 / 1743卷 / 1-2期
关键词：
hydrostatic pressure; heat shock protein; mRNA stabilisation; geldanamycin;
D O I：
10.1016/j.bbamcr.2004.09.004
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
High hydrostatic pressure (HP) increases Hsp70 protein and mRNA levels by increasing the mRNA half-life without activation of HSF1 transcription factor. We investigated whether this change in gene expression requires Hsp90, previously shown to regulate hsp70 genes via HSF1. In HeLa cells, both HP and Hsp90 inhibitor geldanamycin (GA) up-regulated Hsp70 expression through mRNA stabilisation. GA, unlike HP, increased HSF1 activation. However, when exposures were used together a marked Hsp70 response was observed with mRNA stabilisation without coincidence of HSF1 activation. Our data suggests that Hsp90 is involved in hsp70 mRNA stabilisation and the HSF1 activation can be suppressed by high HP. (c) 2004 Elsevier B.V. All rights reserved.
引用
收藏
页码：115 / 119
页数：5
相关论文
共 38 条
[1]   THE HUMAN HEAT-SHOCK PROTEIN HSP70 INTERACTS WITH HSF, THE TRANSCRIPTION FACTOR THAT REGULATES HEAT-SHOCK GENE-EXPRESSION [J].
ABRAVAYA, K ;
MYERS, MP ;
MURPHY, SP ;
MORIMOTO, RI .
GENES & DEVELOPMENT, 1992, 6 (07) :1153-1164
[2]   Stress (heat shock) proteins - Molecular chaperones in cardiovascular biology and disease [J].
Benjamin, IJ ;
McMillan, DR .
CIRCULATION RESEARCH, 1998, 83 (02) :117-132
[3]   Hydrostatic pressure has different effects on the assembly of tubulin, actin, myosin II, vinculin, talin, vimentin, and cytokeratin in mammalian tissue cells [J].
Crenshaw, HC ;
Allen, JA ;
Skeen, V ;
Harris, A ;
Salmon, ED .
EXPERIMENTAL CELL RESEARCH, 1996, 227 (02) :285-297
[4]   THE HEAT-SHOCK RESPONSE IS SELF-REGULATED AT BOTH THE TRANSCRIPTIONAL AND POSTTRANSCRIPTIONAL LEVELS [J].
DIDOMENICO, BJ ;
BUGAISKY, GE ;
LINDQUIST, S .
CELL, 1982, 31 (03) :593-603
[5]   The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR [J].
Donzé, O ;
Abbas-Terki, T ;
Picard, D .
EMBO JOURNAL, 2001, 20 (14) :3771-3780
[6]  
Elo MA, 2000, J CELL BIOCHEM, V79, P610, DOI 10.1002/1097-4644(20001215)79:4<610::AID-JCB100>3.0.CO
[7]  
2-J
[8]  
Feng LL, 1997, ADV EXP MED BIOL, V407, P281
[9]   VARIOUS RAT ADULT TISSUES EXPRESS ONLY ONE MAJOR MESSENGER-RNA SPECIES FROM THE GLYCERALDEHYDE-3-PHOSPHATE-DEHYDROGENASE MULTIGENIC FAMILY [J].
FORT, P ;
MARTY, L ;
PIECHACZYK, M ;
ELSABROUTY, S ;
DANI, C ;
JEANTEUR, P ;
BLANCHARD, JM .
NUCLEIC ACIDS RESEARCH, 1985, 13 (05) :1431-1442
[10]   Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex [J].
Guo, YL ;
Guettouche, T ;
Fenna, M ;
Boellmann, F ;
Pratt, WB ;
Toft, DO ;
Smith, DF ;
Voellmy, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (49) :45791-45799
1234