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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 capaci...
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Published in: | FEMS microbiology letters 2003-04, Vol.221 (2), p.181-185 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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. |
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ISSN: | 0378-1097 1574-6968 |
DOI: | 10.1016/S0378-1097(03)00178-2 |