Molecular chaperone properties of serum amyloid P component

FEBS Letters

Pepys, Mark B.²  Purvis, Alan¹  Wood, Steve P.¹  Baker, Douglas¹  Coker, Alun R.¹ 

[1] Division of Biochemistry and Molecular Biology, School of Biological Sciences, University of Southampton, Bassett Crescent East, Southampton SO16 7PX, UK;Centre for Amyloidosis and Acute Phase Proteins, Department of Medicine, Royal Free and University College Medical School, Rowland Hill Street, London NW3 2PF, UK

关键词: Serum amyloid P component;    Amyloidosis;    Protein folding;    Chaperone;    CRP;    C-reactive protein;    LDH;    lactate dehydrogenase;    MOβDG;    4;    6-O-(1-carboxyethylidene)-β-D-galactopyranoside;    SAP;    serum amyloid P component;   

DOI  :  10.1016/S0014-5793(00)01530-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The selective binding of serum amyloid P component (SAP) to proteins in the pathological amyloid cross-β fold suggests a possible chaperone role. Here we show that human SAP enhances the refolding yield of denatured lactate dehydrogenase and protects against enzyme inactivation during agitation of dilute solutions. These effects are independent of calcium ions and are not inhibited by compounds that block the amyloid recognition site on the B face of SAP, implicating the A face and/or the edges of the SAP pentamer. We discuss the possibility that the chaperone property of SAP, or its failure, may contribute to the pathogenesis of amyloidosis.

【 授权许可】

Unknown