Open AccessThe collagenase activity of Porphyromonas gingivalis is due to Arg‐gingipain
Author(s) -
Houle MarieAndrée,
Grenier Daniel,
Plamondon Pascale,
Nakayama Koji
Publication year - 2003
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/s0378-1097(03)00178-2
Subject(s) - porphyromonas gingivalis , leupeptin , collagenase , pepstatin , chemistry , gel electrophoresis , cathepsin , protease , polyacrylamide gel electrophoresis , biochemistry , microbiology and biotechnology , autolysis (biology) , sodium dodecyl sulfate , type i collagen , proteases , enzyme , biology , bacteria , genetics , endocrinology
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.