title: alpha-Crystallin: molecular chaperone and heat shock protein.
abstract: 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.
authors.affiliation: Department of Biochemistry, University of Nijmegen, The Netherlands.
authors.forename: P R
authors.initials: PR
authors.lastname: van den IJssel
authors.forename: R H
authors.initials: RH
authors.lastname: Smulders
authors.forename: W W
authors.initials: WW
authors.lastname: de Jong
authors.forename: H
authors.initials: H
authors.lastname: Bloemendal
mesh_terms: 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
chemical_list: D003459:Crystallins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D011994:Recombinant Proteins