Relocalization of alpha B-crystallin by heat shock in ovarian carcinoma cells.
alpha B-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 degrees C alpha B-crystallin relocalizes from the detergent-soluble, cytosolic fraction to the non-ionic detergent-insoluble nuclear/cytoskeletal fraction. Colchicine treatment of the cells, although giving rise to a vimentin collapse on the nucleus, does not result in redistribution of alpha B-cyrstallin. When this colchicine treatment is followed by heat shock, alpha B-crystallin relocalizes again to the insoluble fraction, indicating that this relocalization is independent of the collapse of the vimentin network.
Voorter
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CE
Department of Biochemistry, University of Nijmegen, The Netherlands.
Wintjes
L
L
Bloemendal
H
H
de Jong
W W
WW
D000222:Adaptation, Physiological; D003078:Colchicine / Q000494:pharmacology; D003459:Crystallins / Q000378:metabolism*; D005260:Female; D005455:Fluorescent Antibody Technique; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006358:Hot Temperature; D006801:Humans; D015151:Immunoblotting; D010051:Ovarian Neoplasms / Q000378:metabolism*; D014407:Tumor Cells, Cultured; D014746:Vimentin / Q000187:drug effects
D003459:Crystallins; D006360:Heat-Shock Proteins; D014746:Vimentin; D003078:Colchicine