Inactivation of various proteinase inhibitors and the complement system in human plasma by the 56-kilodalton proteinase from Serratia marcescens

A. Molla, T. Akaike, H. Maeda

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

The interaction of the 56-kilodalton (kDa) proteinase from Serratia marcescens with human plasma activated C1 (C1̄) inhibitor, α2-antiplasmin, and antithrombin III was investigated. The 56-kDa proteinase was not affected by these inhibitors; on the contrary, all the inhibitors were inactivated by the 56-kDa proteinase within 2 to 6 h. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that all three inhibitors showed decreased in molecular weight of approximately 8,000 to 10,000 as a result of proteolytic cleavage by the 56-kDa proteinase. The 56-kDa proteinase also inactivated serum complement within 2 to 6 h. The loss of inhibitory activity caused by the 56-kDa proteinase, together with the effects of endogenous serine proteinases, may facilitate tissue destruction and inflammation.

Original languageEnglish
Pages (from-to)1868-1871
Number of pages4
JournalInfection and immunity
Volume57
Issue number6
Publication statusPublished - 1989 Jan 1
Externally publishedYes

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases

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