Seasonal influence on heat shock protein 90α and heat shock factor 1 expression during oxidative stress in fish hepatocytes from polluted estuary

2009 ◽  
Vol 372 (1-2) ◽  
pp. 1-8 ◽  
Author(s):  
Ekambaram Padmini ◽  
Munuswamy Usha Rani
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
Seasonal Influence

scholarly journals Increased expression of heat shock protein 70 and heat shock factor 1 in chronic dermal ulcer tissues treated with laser-aided therapy

2008 ◽  
Vol 121 (14) ◽  
pp. 1269-1273 ◽  
Author(s):  
Jian-da ZHOU ◽  
Cheng-qun LUO ◽  
Hui-qing XIE ◽  
Xin-min NIE ◽  
Yan-zhong ZHAO ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1

Transcription regulation of alpha B-crystallin in astrocytes: analysis of HSF and AP1 activation by different types of physiological stress

1996 ◽  
Vol 109 (5) ◽  
pp. 1029-1039
Author(s):  
M.W. Head ◽  
L. Hurwitz ◽  
J.E. Goldman
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Physiological Stress ◽  
Heat Shock Protein 27 ◽  
Heat Shock Factor ◽  
Transcriptional Level ◽  
Heat Shock Factor 1 ◽  
Hypertonic Stress ◽  
Transcriptional Activator Protein ◽  
Different Types

The coordinated cellular responses to physiological stress are known to be effected in part by the activation of heat-shock factor 1, a transcriptional activator protein capable of binding to, and inducing transcription from genes containing heat shock elements. Other stress responsive signal transduction pathways also exist including the stress activated protein kinase cascade that regulates the activity of the transcription factor AP1. We have examined the expression of the low molecular stress proteins, heat shock protein 27 and alpha B-crystallin in astrocytes in response to physiological stress of different types and asked what component of this induction is effected at the transcriptional level and whether activation of heat shock factor 1 and AP1 might account for these events. We have found that stress regulated induction of alpha B-crystallin has a strong transcriptional component and that it may be effected by at least two different transcriptional mechanisms. In one set of phenomena, represented here by cadmium exposure, alpha B-crystallin and heat shock protein 27 are coordinately regulated and this occurs in the presence of activated heat shock factor 1. In the second series of phenomena, represented here by hypertonic stress, alpha B-crystallin is induced in the absence of heat shock factor activation and in the absence of any corresponding change in heat shock protein 27 expression. Although hypertonic stress does activate an AP1-like binding activity, the AP1 consensus binding site in the alpha B-crystallin promoter does not appear to be a target for this hypertonic stress inducible activity. These data suggest that the hypertonic stress response is effected through a heat shock factor independent mechanism and that hypertonic stress regulated induction of alpha B-crystallin does not directly depend on the SAPK pathway and AP1 activity.

scholarly journals Heat Shock Protein-70 Mediates the Cytoprotective Effect of Carbon Monoxide: Involvement of p38β MAPK and Heat Shock Factor-1

2005 ◽  
Vol 175 (4) ◽  
pp. 2622-2629 ◽  
Author(s):  
Hong Pyo Kim ◽  
Xue Wang ◽  
Jinglan Zhang ◽  
Gee Young Suh ◽  
Ivor J. Benjamin ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
Cytoprotective Effect

scholarly journals Role of heat shock factor-1 activation in the doxorubicin-induced heart failure in mice

2010 ◽  
Vol 298 (6) ◽  
pp. H1832-H1841 ◽  
Author(s):  
Kaushik Vedam ◽  
Yoshinori Nishijima ◽  
Lawrence J. Druhan ◽  
Mahmood Khan ◽  
Nicanor I. Moldovan ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Heart Failure ◽  
Heat Shock ◽  
Mrna Level ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
Knock Out ◽  
Apoptotic Protein ◽  
Shock Proteins

Treating cancer patients with chemotherapeutics, such as doxorubicin (Dox), cause dilated cardiomyopathy and congestive heart failure because of oxidative stress. On the other hand, heat shock factor-1 (HSF-1), a transcription factor for heat shock proteins (Hsps), is also known to be activated in response to oxidative stress. However, the possible role of HSF-1 activation and the resultant Hsp25 in chemotherapeutic-induced heart failure has not been investigated. Using HSF-1 wild-type (HSF-1+/+) and knock-out (HSF-1−/−) mice, we tested the hypothesis that activation of HSF-1 plays a role in the development of Dox-induced heart failure. Higher levels of Hsp25 and its phosphorylated forms were found in the failing hearts of Dox-treated HSF-1+/+ mice. More than twofold increase in Hsp25 mRNA level was found in Dox-treated hearts. Proteomic analysis showed that there is accumulation and aggregation of Hsp25 in Dox-treated failing hearts. Additionally, Hsp25 was found to coimmunoprecipitate with p53 and vice versa. Further studies indicated that the Dox-induced higher levels of Hsp25 transactivated p53 leading to higher levels of the pro-apoptotic protein Bax, but other p53-related proteins remained unaltered. Moreover, HSF-1−/− mice showed significantly reduced Dox-induced heart failure and higher survival rate, and there was no change in Bax upon treating with Dox in HSF-1−/− mice. From these results we propose a novel mechanism for Dox-induced heart failure: increased expression of Hsp25 because of oxidant-induced activation of HSF-1 transactivates p53 to increase Bax levels, which leads to heart failure.

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