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.