A monoclonal antibody (MCPR3-7) interfering with the activity of proteinase 3 by an allosteric mechanism

Lisa C. Hinkofer, Susanne A.I. Seidel, Brice Korkmaz, Francisco Silva, Amber M. Hummel, Dieter Braun, Dieter E. Jenne, Ulrich Specks

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

Background: Proteinase 3 is an abundant serine protease with high similarity to neutrophil elastase and a major autoimmune target in systemic vasculitis. Results: We identified a monoclonal antibody that inhibits PR3 activity. Conclusion: PR3-inhibiting antibodies can change its conformation and impair interactions with β1-proteinase inhibitor. Significance: PR3-inhibiting antibodies may play a role in autoimmune vasculitis and could be exploited as highly selective inhibitors.

Original languageEnglish (US)
Pages (from-to)26635-26648
Number of pages14
JournalJournal of Biological Chemistry
Volume288
Issue number37
DOIs
StatePublished - Sep 13 2013

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Hinkofer, L. C., Seidel, S. A. I., Korkmaz, B., Silva, F., Hummel, A. M., Braun, D., Jenne, D. E., & Specks, U. (2013). A monoclonal antibody (MCPR3-7) interfering with the activity of proteinase 3 by an allosteric mechanism. Journal of Biological Chemistry, 288(37), 26635-26648. https://doi.org/10.1074/jbc.M113.495770