Heat shock factor 1 prevents the reduction in thrashing due to heat shock in Caenorhabditis elegans

被引：9

作者：

Furuhashi, Tsubasa ^{[1
]}

Sakamoto, Kazuichi ^{[1
]}

机构：

[1] Univ Tsukuba, Grad Sch Life & Environm Sci, Tsukuba, Ibaraki 3052572, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2015年 / 462卷 / 03期

关键词：

Caenorhabditis elegans; Heat shock responses; Heat shock factor; Heat shock protein; DAF-16; Thermotolerance; IN-VIVO; PROTEIN; STRESS; THERMOTOLERANCE; PROTEOTOXICITY; INTERFERENCE; PROTECTION; LONGEVITY; TOXICITY; IMMUNITY;

D O I：

10.1016/j.bbrc.2015.04.086

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：

Heat shock factor 1 (HSF-1) is activated by heat stress and induces the expression of heat shock proteins. However, the role of HSF-1 in thermotolerance remains unclear. We previously reported that heat stress reversibly reduces thrashing movement in Caenorhabditis elegans. In this study, we analyzed the function of HSF-1 on thermotolerance by monitoring thrashing movement. hsf-1 RNAi suppressed the restoration of thrashing reduced by heat stress. In contrast, hsf-1 knockdown cancelled prevention of movement reduction in insulin/IGF-1-like growth factor 1 receptor (daf-2) mutant, but didn't suppress thrashing restoration in daf-2 mutant. In addition, hsf-1 RNAi accelerated the reduction of thrashing in heat-shocked wild-type C. elegans. And, daf-16 KO didn't accelerate the reduction of thrashing by heat stress. Taken together, these results suggest that HSF-1 prevents the reduction of thrashing caused by heat shock. (C) 2015 Elsevier Inc. All rights reserved.

引用

页码：190 / 194

页数：5

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