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Alpha A-crystallin Confers Cellular Thermoresistance

P R van den IJssel, P Overkamp, U Knauf, M Gaestel, W W de Jong

FEBS Lett. 1994 Nov 21;355(1):54-6.

PMID: 7957962

Abstract:

The bovine eye lens protein alpha A-crystallin has been overexpressed both by stable transfection of HeLa cells and by transient transfection of NIH 3T3 cells. In both experimental systems alpha A-crystallin overexpression results in an increased cellular thermoresistance as judged by different clonal survival assays. In contrast, similar overexpression of another stable lens protein, beta B2-crystallin, does not confer thermoresistance. These results indicate that the structural relationship of alpha A-crystallin to the small heat shock proteins HSP25/27 and to alpha B-crystallin is sufficient for the shared thermoprotective function of all of these molecules and strongly suggests that the chaperone-like properties that they have in common are responsible for the conferred cellular thermoresistance.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
IAR42414607 α-B-Crystallin from bovine eye lens α-B-Crystallin from bovine eye lens Price
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