Binding of serum amyloid P component to heparin in human serum

X. A. Li, K. Hatanaka, L. Guo, Y. Kitamura, A. Yamamoto

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

It has been proposed that the function of serum amyloid P component (SAP) may closely relate with its binding to polysaccharides, especially glycosaminoglycans. We employed a quantitative immunoelectrophoresis (QIE) method and a native polyacrylamide gel electrophoresis (PAGE) method to characterize the SAP-heparin binding in soluble state. The SAP-heparin binding showed positive cooperativity. The apparent numbers of heparin molecules bound to SAP varied with the calcium concentration with a ratio of 1:1 (SAP/heparin), a Kd of 2.06·10-7 M at 0.1 mM CaCl2 and a ratio of 1:1.6 (SAP/heparin), a Kd of 3.91·10-7 M at 2 mM CaCl2, when estimated by the QIE method. No binding between SAP and heparin was observed in the absence of calcium. Magnesium and barium failed to induce the formation of SAP-heparin complex. Furthermore, they showed inhibitory effects on the calcium-mediated complex formation. We propose that heparin might be a regular to modulate the anticoagulant activity of SAP and a useful drug to prevent SAP deposition on amyloid deposits.

Original languageEnglish
Pages (from-to)143-148
Number of pages6
JournalBiochimica et Biophysica Acta - General Subjects
Volume1201
Issue number2
DOIs
StatePublished - Nov 11 1994

Bibliographical note

Funding Information:
Abbreviations: SAP, serum amyloid P component; QIE, quantitative immunoelectrophoresis; PAGE, polyacrylamide gel electrophoresis; BSA, bovine serum albumin. * Corresponding author. Fax: +81 6 8727485. l Visiting scholar from Taishan Medical College, Taian, Shandong, China, financially supported by the Japan Health Science Foundation. 2 Visiting scholar from Taian Central Hospital, Taian, Shandong, China.

Keywords

  • Amyloid P component
  • Binding
  • Glycosaminoglycan
  • Heparin
  • Serum

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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