title: Activation of MMP-2 by Porphyromonas gingivalis in human periodontal ligament cells.
abstract: It has been reported that matrix metalloproteinase (MMP) produced by host cells plays a major role in periodontal tissue destruction. In addition, secreted virulence factors from Porphyromonas gingivalis can alter MMP secretion and cause activation in host cells that lead to the tissue degradation. In this study, we examine the effects of P. gingivalis supernatant on matrix metalloproteinase-2 (MMP-2) activation in human periodontal ligament (HPDL) cells. Cultures of HPDL cells were treated with P. gingivalis supernatant for 48 h and the level of MMP-2 activation was monitored by gelatin zymography. The profound activation of MMP-2 was seen only in the treated group. The activation of MMP-2 was inhibited by MMP inhibitors phenanthroline and EDTA, but not serine protease or cysteine protease inhibitors. To study the correlation between the expression of membrane-type-1 matrix metalloproteinase (MT1-MMP) and the activation of MMP-2, the level of MT1-MMP was analyzed. The results from reverse-transcription polymerase chain reaction (RT-PCR) and Western analysis indicated that P. gingivalis supernatant up-regulated the expression of MT1-MMP in both transcription and translation levels within 48 h. These results suggest that P. gingivalis supernatant can activate MMP-2 in HPDL cells and the mechanism of activation may involve the increased amount of MT1-MMP. It is possible that the activation of MMP-2 by P. gingivalis plays a role in the process of chronic periodontitis.
authors.affiliation: Department of Anatomy, Faculty of Dentistry, Chulalongkorn University, Bangkok, Thailand.
authors.forename: Kassara
authors.initials: K
authors.lastname: Pattamapun
authors.forename: Siriluck
authors.initials: S
authors.lastname: Tiranathanagul
authors.forename: Tussanee
authors.initials: T
authors.lastname: Yongchaitrakul
authors.forename: Jintakorn
authors.initials: J
authors.lastname: Kuwatanasuchat
authors.forename: Prasit
authors.initials: P
authors.lastname: Pavasant
mesh_terms: D018929:Cell Culture Techniques; D002614:Chelating Agents / Q000494:pharmacology; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D004789:Enzyme Activation; D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D020778:Matrix Metalloproteinase 2 / Q000032:analysis / Q000378:metabolism*; D061965:Matrix Metalloproteinase Inhibitors; D053504:Matrix Metalloproteinases, Membrane-Associated; D008666:Metalloendopeptidases / Q000032:analysis / Q000235:genetics; D010513:Periodontal Ligament / Q000166:cytology / Q000201:enzymology*; D010618:Phenanthrolines / Q000494:pharmacology; D016966:Porphyromonas gingivalis / Q000201:enzymology* / Q000378:metabolism; D014176:Protein Biosynthesis / Q000235:genetics; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology; D013997:Time Factors; D019714:Tissue Inhibitor of Metalloproteinases / Q000494:pharmacology; D014158:Transcription, Genetic / Q000235:genetics; D015854:Up-Regulation; D037521:Virulence Factors / Q000378:metabolism
chemical_list: D002614:Chelating Agents; D015853:Cysteine Proteinase Inhibitors; D061965:Matrix Metalloproteinase Inhibitors; D010618:Phenanthrolines; D015842:Serine Proteinase Inhibitors; D019714:Tissue Inhibitor of Metalloproteinases; D037521:Virulence Factors; D004492:Edetic Acid; D053504:Matrix Metalloproteinases, Membrane-Associated; D008666:Metalloendopeptidases; D020778:Matrix Metalloproteinase 2