Cleavage and activation of proteinase-activated receptor-2 on human neutrophils by gingipain-R from Porphyromonas gingivalis.
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.
Department of Biochemistry and Molecular Biology, Monash University, Clayton, Vic., Australia.
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Lourbakos
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Chinni
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Thompson
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Potempa
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Travis
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Mackie
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Pike
D018829:Adhesins, Bacterial; D002118:Calcium / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D000080867:Gingipain Cysteine Endopeptidases; D006388:Hemagglutinins / Q000494:pharmacology*; D006801:Humans; D006868:Hydrolysis; D007424:Intracellular Fluid / Q000187:drug effects / Q000378:metabolism; D009504:Neutrophils / Q000187:drug effects / Q000378:metabolism*; D009842:Oligopeptides / Q000138:chemical synthesis / Q000378:metabolism; D010446:Peptide Fragments / Q000494:pharmacology; D016966:Porphyromonas gingivalis; D044464:Receptor, PAR-2; D018179:Receptors, Thrombin / Q000097:blood / Q000187:drug effects / Q000378:metabolism*
D018829:Adhesins, Bacterial; D000080867:Gingipain Cysteine Endopeptidases; D006388:Hemagglutinins; D009842:Oligopeptides; D010446:Peptide Fragments; D044464:Receptor, PAR-2; D018179:Receptors, Thrombin; C072032:thrombin receptor peptide (42-55); D003546:Cysteine Endopeptidases; D002118:Calcium