alpha-Crystallin: molecular chaperone and heat shock protein.
The relationship of alpha-crystallin with the family of small heat shock proteins has led to the discovery that the basic subunit alpha B-crystallin can, like other heat shock proteins, protect cells against heat stress. Here we show that the acidic subunit alpha A-crystallin, which in contrast to alpha B-crystallin is expressed mainly in the eye lens, shares this property. Furthermore we have investigated the in vitro 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.
van den IJssel
P R
PR
Department of Biochemistry, University of Nijmegen, The Netherlands.
Smulders
R H
RH
de Jong
W W
WW
Bloemendal
H
H
D016475:3T3 Cells; D000818:Animals; D003459:Crystallins / Q000737:chemistry*; D006360:Heat-Shock Proteins / Q000737:chemistry*; D051379:Mice; D018832:Molecular Chaperones / Q000737:chemistry*; D011485:Protein Binding; D011994:Recombinant Proteins / Q000737:chemistry; D013329:Structure-Activity Relationship; D014162:Transfection
D003459:Crystallins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D011994:Recombinant Proteins