期刊
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
卷 1726, 期 2, 页码 168-176出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbagen.2005.08.003
关键词
complement; polysaccharide; interaction; SPR; heparin
资金
- NHLBI NIH HHS [R01 HL052622, HL52622, R01 HL052622-07, R01 HL052622-08] Funding Source: Medline
- NIGMS NIH HHS [R01 GM038060, R01 GM038060-16A2, GM38060, R01 GM038060-17] Funding Source: Medline
Heparin is a naturally occurring polysaccharide known to interact with complement proteins and regulate multiple steps in the complement cascade. Quantitative information, in the form of affinity constants for heparin-complement interactions, is not generally available and there are no reports of a comprehensive analysis using the same interaction method. Such information should improve our understanding of how exogenously administered pharmaceutical heparin and the related endogenous polysaccharide, heparan sulfate, regulate complement activation. The current study provides the first comprehensively analysis of the binding of various complement proteins to heparin using surface plasmon resonance (SPR). Complement proteins Cl, C2, C3, C4, C5, C6, C7, C8, C9, C1INH, factor 1, factor H, factor B and factor P all bind heparin but exhibit different binding kinetics and dissociation constants (K-d) ranging from 2 to 320 nM. By taking into account these K-d values and the serum concentrations of these complement proteins, the percentage of each binding to exogenously administered heparin was calculated and found to range from 2% to 41%. This study provides essential information required for the rational design of new therapeutic agents capable of regulating the complement activation. (c) 2005 Elsevier B.V. All rights reserved.
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