Expression of the small heat shock protein gene, hsp30, in Rana catesbeiana fibroblasts

被引:9
作者
Mulligan-Tuttle, Anne [1 ]
Heikkila, John J. [1 ]
机构
[1] Univ Waterloo, Dept Biol, Waterloo, ON N2L 3G1, Canada
来源
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-MOLECULAR & INTEGRATIVE PHYSIOLOGY | 2007年 / 148卷 / 02期
基金
加拿大自然科学与工程研究理事会;
关键词
heat shock protein; mRNA; molecular chaperone; immunohistochemistry; confocal microscopy; stress;
D O I
10.1016/j.cbpa.2007.04.022
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
In the present study, we examined the expression of the Rana catesbeiana small heat shock protein gene, hsp30, in an FT fibroblast cell line. Northern and western blot analyses revealed that hsp30 mRNA or HSP30 protein was not present constitutively but was strongly induced at a heat shock temperature of 35 degrees C. However, treatment of FT cells with sodium arsenite at concentrations that induced hsp gene expression in other amphibian systems caused cell death. Non-lethal concentrations of sodium arsenite (10 mu M) induced only minimal accumulation of hsp30 mRNA or protein after 12 h. Immunocytochemical analyses employing laser scanning confocal microscopy detected the presence of heat-inducible HSP30, in a granular or punctate pattern. HSP30 was enriched in the nucleus with more diffuse localization in the cytoplasm. The nuclear localization of HSP30 was more prominent with continuous heat shock. These heat treatments did not alter FT cell shape or disrupt actin cytoskeletal organization. Also, HSP30 did not co-localize with the actin cytoskeleton. (c) 2007 Elsevier Inc. All rights reserved.
引用
收藏
页码:308 / 316
页数:9
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