Alpha A-crystallin confers cellular thermoresistance.
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.[1]References
- Alpha A-crystallin confers cellular thermoresistance. van den IJssel, P.R., Overkamp, P., Knauf, U., Gaestel, M., de Jong, W.W. FEBS Lett. (1994) [Pubmed]
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