Open AccessNew insights into the role of serum amyloid P component, a novel lipopolysaccharide‐binding protein
Author(s) -
Haas Carla J.C
Publication year - 1999
Publication title -
fems immunology & medical microbiology
Language(s) - English
Resource type - Journals
eISSN - 1574-695X
pISSN - 0928-8244
DOI - 10.1111/j.1574-695x.1999.tb01390.x
Subject(s) - serum amyloid p component , lipopolysaccharide , amyloid (mycology) , biology , function (biology) , bacteria , serum amyloid a , plasma protein binding , component (thermodynamics) , biochemistry , binding protein , microbiology and biotechnology , inflammation , immunology , c reactive protein , genetics , botany , gene , physics , thermodynamics
Serum amyloid P component (SAP) is a highly preserved plasma protein named for its ubiquitous presence in amyloid deposits. Although SAP is described to bind many ligands, no clear biological function has been ascribed to it as yet. This review summarizes the current knowledge about the protein SAP, its ligands and functional properties. Finally, the author focuses on the recent finding of the binding of SAP to lipopolysaccharide (LPS) and Gram‐negative bacteria and the possible functional consequences of these interactions.