Molecular chaperone properties of serum amyloid P component

被引：41

作者：

Coker, AR

Purvis, A

Baker, D

Pepys, MB

Wood, SP

机构：

[1] Univ Southampton, Sch Biol Sci, Div Biochem & Mol Biol, Southampton SO16 7PX, Hants, England

[2] UCL Royal Free & Univ Coll Med Sch, Dept Med, Ctr Amyloidosis & Acute Phase Prot, London NW3 2PF, England

来源：

FEBS LETTERS | 2000年 / 473卷 / 02期

关键词：

serum amyloid P component; amyloidosis; protein folding; chaperone;

D O I：

10.1016/S0014-5793(00)01530-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The selective binding of serum amyloid P component (SAP) to proteins in the pathological amyloid cross-beta 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, (C) 2000 Federation of European Biochemical Societies.

引用

收藏

页码：199 / 202

页数：4

相关论文

共 27 条

[1] CALCIUM-DEPENDENT AGGREGATION OF HUMAN-SERUM AMYLOID-P COMPONENT [J].

BALTZ, ML ;

DEBEER, FC ;

FEINSTEIN, A ;

PEPYS, MB .

BIOCHIMICA ET BIOPHYSICA ACTA, 1982, 701 (02) :229-236

[2]

Booth DR, 1999, AMYLOID AND AMYLOIDOSIS 1998, P23

[3] Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis [J].

Booth, DR ;

Sunde, M ;

Bellotti, V ;

Robinson, CV ;

Hutchinson, WL ;

Fraser, PE ;

Hawkins, PN ;

Dobson, CM ;

Radford, SE ;

Blake, CCF ;

Pepys, MB .

NATURE, 1997, 385 (6619) :787-793

[4] Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene [J].

Botto, M ;

Hawkins, PN ;

Bickerstaff, MCM ;

Herbert, J ;

Bygrave, AE ;

McBride, A ;

Hutchinson, WL ;

Tennent, GA ;

Walport, MJ ;

Pepys, MB .

NATURE MEDICINE, 1997, 3 (08) :855-859

[5] Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants [J].

Canet, D ;

Sunde, M ;

Last, AM ;

Miranker, A ;

Spencer, A ;

Robinson, CV ;

Dobson, CM .

BIOCHEMISTRY, 1999, 38 (20) :6419-6427

[6] Designing conditions for in vitro formation of amyloid protofilaments and fibrils [J].

Chiti, F ;

Webster, P ;

Taddei, N ;

Clark, A ;

Stefani, M ;

Ramponi, G ;

Dobson, CM .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (07) :3590-3594

[7] From Levinthal to pathways to funnels [J].

Dill, KA ;

Chan, HS .

NATURE STRUCTURAL BIOLOGY, 1997, 4 (01) :10-19

[8] ROLES OF MOLECULAR CHAPERONES IN PROTEIN-FOLDING [J].

ELLIS, RJ .

CURRENT OPINION IN STRUCTURAL BIOLOGY, 1994, 4 (01) :117-122

[9] STRUCTURE OF PENTAMERIC HUMAN SERUM AMYLOID-P COMPONENT [J].

EMSLEY, J ;

WHITE, HE ;

OHARA, BP ;

OLIVA, G ;

SRINIVASAN, N ;

TICKLE, IJ ;

BLUNDELL, TL ;

PEPYS, MB ;

WOOD, SP .

NATURE, 1994, 367 (6461) :338-345

[10] Molecular chaperones in cellular protein folding [J].

Hartl, FU .

NATURE, 1996, 381 (6583) :571-580