Alpha-1-antitrypsin-induced inhibition of complement-dependent phagocytosis

Anna Mód, Gyorgy Füst, János Gergely, Susan R. Hollán, M. P. Dierich

Research output: Contribution to journalArticle

5 Citations (Scopus)


In a previous investigation, inhibition of complement-dependent rosette formation by alpha1-antitrypsin (α1-AT) was observed, and it was demonstrated that α1-AT interacts through its carbohydrate portion with C3 and its fragments. In the present study, the effect of α1-AT on the complement-receptor-mediated phagocytosis by human peripheral blood monocytes was examined. Purified α1-AT inhibited in a dose-dependent manner phagocytosis of C3-carrying yeast particles. Inhibition was selective, concerned only C3-receptor-mediated phagocytosis, neither Fc-receptor-mediated phagocytosis nor uptake of untreated yeast particles was blocked by α1-AT. It was demonstrated that α1-AT exerted its inhibitory effect through binding to C3-carrying particles. The activity of α1-AT towards C3 and fragments of C3 was not mediated by its antiprotease effect, but by its carbohydrate moiety. This finding suggests that α1-AT may have an impact on various immune functions involving complement receptors.

Original languageEnglish
Pages (from-to)338-346
Number of pages9
Issue number4
Publication statusPublished - Jan 1 1981



  • EA
  • PBS
  • SRBC
  • alpha-antitrypsin
  • phosphate-buffered saline
  • sensitized erythrocytes
  • sheep red blood cells
  • α -AT

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Hematology

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