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Alpha A-crystallin confers cellular thermoresistance

Item Type:Article
Title:Alpha A-crystallin confers cellular thermoresistance
Creators Name:van den Ijssel, P.R. and Overkamp, P. and Knauf, U. and Gaestel, M. and de Jong, W.W.
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.
Keywords:alpha-Crystallin, beta-Crystallin, Small Heat Shock Protein, Thermoresistance, Animals, Mice
Source:FEBS Letters
ISSN:0014-5793
Publisher:Elsevier (The Netherlands)
Volume:355
Number:1
Page Range:54-56
Date:21 November 1994
Official Publication:https://doi.org/10.1016/0014-5793(94)01175-3
PubMed:View item in PubMed

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