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.
Department of Biochemistry, University of Nijmegen, The Netherlands.
P R
PR
van den IJssel
P
P
Overkamp
U
U
Knauf
M
M
Gaestel
W W
WW
de Jong
D016475:3T3 Cells; D000818:Animals; D002470:Cell Survival; D003459:Crystallins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006367:HeLa Cells; D006358:Hot Temperature; D006801:Humans; D051379:Mice; D014162:Transfection
D003459:Crystallins