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Molecular chaperone properties of serum amyloid P component
Author(s) -
Coker Alun R.,
Purvis Alan,
Baker Douglas,
Pepys Mark B.,
Wood Steve P.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01530-1
Subject(s) - pentamer , serum amyloid p component , chaperone (clinical) , chemistry , amyloidosis , biochemistry , amyloid (mycology) , lactate dehydrogenase , peptide , amyloid disease , enzyme , biophysics , amyloid fibril , amyloid β , biology , inflammation , medicine , immunology , inorganic chemistry , c reactive protein , pathology , disease
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.