Molecular chaperone properties of serum amyloid P component

The selective binding of serum amyloid P component (SAP) to proteins in the pathological amyloid cross-beta fold suggests a possible chaperone role. H ere we show that human SAP enhances the refolding yield of denatured lactat e dehydrogenase and protects against enzyme inactivation during agitation o f dilute solutions. These effects are independent of calcium ions and are n ot 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, W e discuss the possibility that the chaperone property of SAP, or its failur e, may contribute to the pathogenesis of amyloidosis, (C) 2000 Federation o f European Biochemical Societies.