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 language | English |
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Pages (from-to) | 45-48 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 435 |
Issue number | 1 |
DOIs | |
Publication status | Published - 11 Sept 1998 |
Keywords
- Gingipain-R
- Neutrophil
- Porphyromonas gingivalis
- Proteinase-activated receptor