| The chaperone action of bovine milk α(S1)- and α(S2)-caseins and their associated form α(S)-casein. | |
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MedLine Citation:
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PMID: 21457703 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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α(S)-Casein, the major milk protein, comprises α(S1)- and α(S2)-casein and acts as a molecular chaperone, stabilizing an array of stressed target proteins against precipitation. Here, we report that α(S)-casein acts in a similar manner to the unrelated small heat-shock proteins (sHsps) and clusterin in that it does not preserve the activity of stressed target enzymes. However, in contrast to sHsps and clusterin, α(S)-casein does not bind target proteins in a state that facilitates refolding by Hsp70. α(S)-Casein was also separated into α(S1)- and α(S2)-casein, and the chaperone abilities of each of these proteins were assessed with amorphously aggregating and fibril-forming target proteins. Under reduction stress, all α(S)-casein species exhibited similar chaperone ability, whereas under heat stress, α(S1)-casein was a poorer chaperone. Conversely, α(S2)-casein was less effective at preventing fibril formation by modified κ-casein, whereas α(S)- and α(S1)-casein were comparably potent inhibitors. In the presence of added salt and heat stress, α(S1)-, α(S2)- and α(S)-casein were all significantly less effective. We conclude that α(S1)- and α(S2)-casein stabilise each other to facilitate optimal chaperone activity of α(S)-casein. This work highlights the interdependency of casein proteins for their structural stability. |
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Authors:
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Teresa M Treweek; David C Thorn; William E Price; John A Carver |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-3-29 |
Journal Detail:
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Title: Archives of biochemistry and biophysics Volume: - ISSN: 1096-0384 ISO Abbreviation: - Publication Date: 2011 Mar |
Date Detail:
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Created Date: 2011-4-4 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0372430 Medline TA: Arch Biochem Biophys Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2011. Published by Elsevier Inc. |
Affiliation:
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Graduate School of Medicine, University of Wollongong, Northfields Ave, Wollongong, New South Wales, 2522, Australia. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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