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FEBS Lett. 1998 Sep 11;435(1):45-8.

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

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1
Department of Biochemistry and Molecular Biology, Monash University, Clayton, Vic., Australia.

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.

PMID:
9755856
DOI:
10.1016/s0014-5793(98)01036-9
[Indexed for MEDLINE]
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