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

• Published in: FEBS letters 1992-09, Vol.309 (2), p.111-114
• Main Authors: Voorter, Christina E.M., Wintjes, Liesbeth, Bloemendal, Hans, de Jong, Wilfried W.
• Format: Article
• Language: English
• Subjects: Adaptation, Physiological; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Colchicine - pharmacology; Crystallins - metabolism; Eye lens; Female; Fluorescent Antibody Technique; Fundamental and applied biological sciences. Psychology; Heat-Shock Proteins - metabolism; Hot Temperature; Humans; Immunoblotting; Intermediate filament; Miscellaneous; Non-Lenticular tissue; Ovarian Neoplasms - metabolism; PBS; phosphate buffered saline; Proteins; sHSP; Small heat-shock protein; Stress; Tumor Cells, Cultured; Vimentin - drug effects
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(92)81075-W

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.