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Biochem Biophys Res Commun. 1998 Mar 6;244(1):249-52.

Serum amyloid P component associates with high density lipoprotein as well as very low density lipoprotein but not with low density lipoprotein.

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  • 1Department of Biochemistry, Taishan Medical College, Taian, Shandong, P. R. China. xiangali@res.ncvc.go.jp

Abstract

Serum amyloid P component (SAP) is a glycoprotein in human plasma. We previously showed that SAP is specifically localized in human atherosclerotic lesions, suggesting that SAP may play a role in atherogenesis. In this study, the interactions between human SAP and high density lipoprotein (HDL), low density lipoprotein (LDL) and very low density lipoprotein (VLDL) were investigated by using a solid phase plate assay. Biotinylated SAP bound to immobilized HDL and VLDL in a calcium-dependent, saturable manner. The SAP-HDL and SAP-VLDL bindings reached saturation at 4 nM and 16 nM of SAP, respectively. The bindings were inhibited by native SAP in a dose-dependent manner. No binding between SAP and LDL was found in the presence of calcium or EDTA, which indicates the specificity of SAP-lipoproteins interactions. These results suggest that the function of SAP is related to its capability to interact with lipoproteins and this may have important implications in atherosclerosis and in amyloidosis.

PMID:
9514915
DOI:
10.1006/bbrc.1998.8248
[PubMed - indexed for MEDLINE]
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