𝔖 Bobbio Scriptorium
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Chaperone-like activity revealed in the matricellular protein SPARC

✍ Scribed by Ryan O. Emerson; E. Helene Sage; Joy G. Ghosh; John I. Clark

Book ID
102303613
Publisher
John Wiley and Sons
Year
2006
Tongue
English
Weight
119 KB
Volume
98
Category
Article
ISSN
0730-2312

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✦ Synopsis

Abstract

SPARC (Secreted Protein, Acidic and Rich in Cysteine) is a matricellular glycoprotein that modulates cell proliferation, adhesion, migration, and extracellular matrix (ECM) production. In this report chaperone‐like activity of SPARC was identified in a thermal aggregation assay in vitro. Ultraviolet circular dichroism (UVCD) spectroscopy determined that SPARC was stable at temperatures up to 50°C. Unfolding and aggregation of the chaperone target protein, alcohol dehydrogenase (ADH), were initiated at 50°C. SPARC inhibited the thermal aggregation of ADH in a concentration‐dependent manner, with maximal inhibition at a 1:4 molar ratio of SPARC:ADH. Synergy between the chaperone‐like activities of SPARC and αB‐crystallin, a small heat shock protein and molecular chaperone in the lens, was observed in SPARC‐αB‐crystallin double −/− mice. J. Cell. Biochem. 98: 701–705, 2006. © 2006 Wiley‐Liss, Inc.

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