ALPHA-CRYSTALLIN - MOLECULAR CHAPERONE AND HEAT-SHOCK PROTEIN

The relationship of alpha-crystallin with the family of small heat sho ck proteins has led to the discovery that the basic subunit alpha B-cr ystallin can, like other heat shock proteins, protect cells against he at stress. Here we show that the acidic subunit alpha A-crystallin, wh ich in contrast to alpha B-crystallin is expressed mainly in the eye l ens, shares this property. Furthermore we have investigated the in vit ro molecular chaperone-like behavior of the natural mutant alpha A(ins )-crystallin that has a large insert peptide and occurs in rodents. We have found the chaperone-like activity of the mutant to be diminished compared to that of the wild type alpha A-crystallin.