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

Xiang An Li, Chikao Yutani, Kentaro Shimokado

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

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.

Original languageEnglish
Pages (from-to)249-252
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume244
Issue number1
DOIs
StatePublished - Mar 6 1998

Bibliographical note

Funding Information:
1This work was supported in part by National Natural Science Foundation of China, China Excellent Young Teacher's Foundation and Japan Cardiovascular Research Foundation.

Keywords

  • Amyloid P component
  • Amyloidosis
  • Atherosclerosis
  • Binding
  • Lipoprotein
  • Pentraxin

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Serum amyloid P component associates with high density lipoprotein as well as very low density lipoprotein but not with low density lipoprotein'. Together they form a unique fingerprint.

Cite this