αA‐crystallin confers cellular thermoresistance

FEBS Letters

Gaestel, Matthias²  Overkamp, Perry¹  de Jong, Wilfried W.¹  van den Ijssel, Paul R.L.A.¹  Knauf, Ursula² 

[1] Department of Biochemistry, University of Nijmegen, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands;Max-Delbrück-Centrum für Molekulare Medizin, R.-Rössle-Strasse 10, D-13122 Berlin, Germany

关键词: α-Crystallin;    β-Crystallin;    Small heat shock protein;    Thermoresistance;    sHSP;    small heat shock protein;    HSP25/27;    mouse/ human small heat shock protein;   

DOI  :  10.1016/0014-5793(94)01175-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown