title: Casein proteins as molecular chaperones.
abstract: Under conditions of stress, such as elevated temperature, molecular chaperones stabilize proteins from unfolding, aggregating, and precipitating. We have investigated the chaperone activity of the major milk proteins alpha(S)-, beta-, and kappa-casein with reduced insulin and the milk whey proteins, alpha-lactalbumin and beta-lactoglobulin, and compared it with that of the mammalian small heat shock protein (sHsp), alpha-crystallin, and clusterin. alpha(S)-Casein exhibited different chaperone behavior under reduction and heat stresses, i.e., chaperone activity increased with increasing temperature (as observed with alpha-crystallin), but under reduction stress, its chaperone activity increased at lower temperatures. beta- and kappa-casein had comparable chaperone ability with each other but were less effective than alpha(S)-casein. Under molecular crowding conditions, precipitation of stressed protein was accelerated, and alpha(S)-casein was a poorer chaperone. Furthermore, at slightly alkaline pH values, alpha(S)-casein was a less effective chaperone than at neutral pH. Detailed fluorescence, size exclusion chromatography, and real-time NMR studies studies indicated that the casein proteins underwent conformational changes and stabilized the partially unfolded whey proteins prior to formation of high molecular weight soluble complexes. These results are consistent with casein proteins acting as molecular chaperones in a manner similar to sHsps and clusterin.
authors.affiliation: Department of Chemistry, University of Wollongong, Northfields Avenue, Wollongong, New South Wales 2522, Australia.
authors.forename: Philip E
authors.initials: PE
authors.lastname: Morgan
authors.forename: Teresa M
authors.initials: TM
authors.lastname: Treweek
authors.forename: Robyn A
authors.initials: RA
authors.lastname: Lindner
authors.forename: William E
authors.initials: WE
authors.lastname: Price
authors.forename: John A
authors.initials: JA
authors.lastname: Carver
mesh_terms: D000817:Anilino Naphthalenesulfonates; D002364:Caseins / Q000378:metabolism* / Q000494:pharmacology; D002851:Chromatography, High Pressure Liquid; D005456:Fluorescent Dyes; D006358:Hot Temperature; D007328:Insulin / Q000378:metabolism; D007768:Lactalbumin / Q000378:metabolism; D007782:Lactoglobulins / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008894:Milk Proteins / Q000378:metabolism; D018832:Molecular Chaperones / Q000494:pharmacology / Q000502:physiology*; D010084:Oxidation-Reduction; D013050:Spectrometry, Fluorescence; D000067816:Whey Proteins; D038201:alpha-Crystallins / Q000378:metabolism / Q000494:pharmacology
chemical_list: D000817:Anilino Naphthalenesulfonates; D002364:Caseins; D005456:Fluorescent Dyes; D007328:Insulin; D007782:Lactoglobulins; D008894:Milk Proteins; D018832:Molecular Chaperones; D000067816:Whey Proteins; D038201:alpha-Crystallins; C027132:1-anilino-8-naphthalenesulfonate; D007768:Lactalbumin