A postulated mechanism for heparin's potentiation of C1 inhibitor function

Gretchen B. Caughman, Robert J. Boackle, Jana Vesely

Research output: Contribution to journalArticle

63 Scopus citations

Abstract

Conflicting reports exist in the literature concerning the primary mechanism for heparin's inhibition of Ca hemolytic function. We provide evidence here that heparin's most effective inhibition is mediated through interaction with and potentiation of C1-INH. The molecular nature of the interaction between heparin and the C1-INH molecule is evidenced by an anodal shift in the electrophoretic mobility of C1-INH upon the addition of heparin. We also demonstrate that C3 and C4 conversions in normal human serum by classical pathway activators such as heat-aggregated IgG are inhibited by the addition of heparin, yet heparin does not prevent similar C3 conversion in serum depleted of C1-INH. Heparin's inhibitory action is restored to Cl-INH-depleted serum by the addition of purified C1-INH.

Original languageEnglish (US)
Pages (from-to)287-295
Number of pages9
JournalMolecular Immunology
Volume19
Issue number2
DOIs
StatePublished - Feb 1982
Externally publishedYes

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology

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