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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adhesins, Bacterial
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Calcium / metabolism
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Cysteine Endopeptidases / pharmacology*
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Enzyme Activation / drug effects
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Gingipain Cysteine Endopeptidases
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Hemagglutinins / pharmacology*
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Humans
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Hydrolysis
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Intracellular Fluid / drug effects
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Intracellular Fluid / metabolism
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Neutrophils / drug effects
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Neutrophils / metabolism*
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Oligopeptides / chemical synthesis
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Oligopeptides / metabolism
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Peptide Fragments / pharmacology
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Porphyromonas gingivalis
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Receptor, PAR-2
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Receptors, Thrombin / blood
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Receptors, Thrombin / drug effects
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Receptors, Thrombin / metabolism*
Substances
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Adhesins, Bacterial
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Gingipain Cysteine Endopeptidases
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Hemagglutinins
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Oligopeptides
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Peptide Fragments
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Receptor, PAR-2
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Receptors, Thrombin
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thrombin receptor peptide (42-55)
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Cysteine Endopeptidases
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Calcium