The collagenase activity of Porphyromonas gingivalis is due to Arg-gingipain.
Degradation of type I collagen by Porphyromonas gingivalis was monitored by fluorogenic, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and growth assays. All three assays showed that inactivation of both the rgpA and rgpB genes was necessary to completely eliminate the capacity of P. gingivalis to cleave type I collagen. Leupeptin, an Arg-gingipain-specific protease inhibitor, almost completely inhibited collagen degradation by P. gingivalis cells whereas cathepsin B inhibitor II, a Lys-gingipain inhibitor, did not. A purified preparation of Arg-gingipains A and B hydrolyzed gelatin but did not cleave type I collagen, suggesting that the enzymes must be attached to the cell surface to exert collagenase activity. A number of substances used as adjuncts in periodontal therapy were also tested for their capacity to inhibit collagenase activity of P. gingivalis. Tetracycline, doxycycline, and chlorhexidine strongly inhibited collagenase activity.
Groupe de Recherche en Ecologie Buccale, Faculté de Médecine Dentaire, Université Laval, Cité universitaire, Québec, QC, Canada.
Marie-Andrée
MA
Houle
Daniel
D
Grenier
Pascale
P
Plamondon
Koji
K
Nakayama
D018829:Adhesins, Bacterial; D003094:Collagen / Q000378:metabolism*; D017364:Collagenases / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D000080867:Gingipain Cysteine Endopeptidases; D006388:Hemagglutinins / Q000378:metabolism*; D010518:Periodontitis / Q000382:microbiology; D016966:Porphyromonas gingivalis / Q000187:drug effects / Q000201:enzymology* / Q000254:growth & development; D011480:Protease Inhibitors / Q000494:pharmacology
D018829:Adhesins, Bacterial; D000080867:Gingipain Cysteine Endopeptidases; D006388:Hemagglutinins; D011480:Protease Inhibitors; D003094:Collagen; D003546:Cysteine Endopeptidases; D017364:Collagenases