Relocalization of αB‐crystallin by heat shock in ovarian carcinoma cells

FEBS Letters

Voorter, Christina E.M.¹  Bloemendal, Hans¹  de Jong, Wilfried W.¹  Wintjes, Liesbeth¹ 

[1] Department of Biochemistry, Centre of Eye Research, University of Nijmegen, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands

关键词: Small heat-shock protein;    Stress;    Non-Lenticular tissue;    Eye lens;    Intermediate filament;    sHSP;    small heat-shock protein;    PBS;    phosphate buffered saline;   

DOI  :  10.1016/0014-5793(92)81075-W

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

αB-Crystallin, a major lens protein, is present in clearly detectable amounts in cultured ovarian carcinoma cells. After heat-shock treatment of these cells at 45°C αB-crystallin relocalizes from the detergent-soluble, cytosolic fraction to the non-ionic detergent-insoluble nuclear/cytoskeletal fraction. Colchicine treatment of the cells, alhough giving rise to a vimentin collapse on the nucleus, does not result in redistribution of ß-cyrstallin. When this colchicine treatment is followed by heat shock, αB-crystallin relocalizes again to the insoluble fraction, indicating that this relocalization is independent of the collapse of the vimentin network.

【 授权许可】

Unknown