Cleavage and activation of proteinase-activated receptor-2 on human neutrophils by gingipain-R from Porphyromonas gingivalis

Afrodite Lourbakos, Carla Chinni, Philip Thompson, Jan Potempa, James Travis, Eleanor J. MacKie, Robert N. Pike

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Abstract

Gingipain-R, the major arginine-specific proteinase from Porphyromonas gingivalis, a causative agent of adult periodontal disease, was found to cleave a model peptide representing the cleavage site of proteinase-activated receptor-2 (PAR-2), a G-protein-coupled receptor found on the surface of neutrophils. The bacterial proteinase was also shown to induce an increase in the intracellular calcium concentration of enzyme-treated neutrophils, most probably due to PAR-2 activation. This response by neutrophils to gingipain-R may be a mechanism for the development of inflammation associated with periodontal disease. Copyright (C) 1998 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)45-48
Number of pages4
JournalFEBS Letters
Volume435
Issue number1
DOIs
Publication statusPublished - 11 Sep 1998

Keywords

  • Gingipain-R
  • Neutrophil
  • Porphyromonas gingivalis
  • Proteinase-activated receptor

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