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αA‐crystallin confers cellular thermoresistance
Author(s) -
van den Ijssel Paul R.L.A.,
Overkamp Perry,
Knauf Ursula,
Gaestel Matthias,
de Jong Wilfried W.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01175-3
Subject(s) - transfection , crystallin , microbiology and biotechnology , heat shock protein , hela , chaperone (clinical) , lens (geology) , chemistry , biology , cell culture , cell , gene , biochemistry , genetics , medicine , paleontology , pathology
The bovine eye lens protein αA‐crystallin has been overexpressed both by stable transfection of HeLa cells and by transient transfection of NIH 3T3 cells. In both experimental systems αA‐crystallin overexpression results in an increased cellular thermoresistance as judged by different clonal survival assays. In contrast, similar overexpression of another stable lens protein, βB2‐crystallin, does not confer thermoresistance. These results indicate that the structural relationship of αA‐crystallin to the small heat shock proteins HSP25/27 and to αB‐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.