Abstract
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.
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