These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: MMP-2 activation by Actinobacillus actinomycetemcomitans supernatant in human PDL cells was corresponded with reduction of TIMP-2.
    Author: Tiranathanagul S, Pattamapun K, Yongchaitrakul T, Pavasant P.
    Journal: Oral Dis; 2004 Nov; 10(6):383-8. PubMed ID: 15533216.
    Abstract:
    OBJECTIVE: Matrix metalloproteinase 2 (MMP-2) has been implicated to play a role in pathogenesis of periodontal disease. We recently reported that Porphyromonas gingivalis supernatant could activate MMP-2 in human periodontal ligament (HPDL) cells. In this study, activation of MMP-2 by Actinobacillus actinomycetemcomitans supernatant and the mechanism was investigated. METHODS: HPDL cells were treated with either A. actinomycetemcomitans or P. gingivalis supernatant for 48 h. To verify the mechanism, pretreated inhibitors were used. Gelatin zymography, RT-PCR and Western blot analysis were used to detect the activation of MMP-2, expression of MT1-MMP and TIMP-2 mRNA and the proteins, respectively. RESULTS: The supernatant from A. actinomycetemcomitans could activate MMP-2 in HPDL cells similar to that from P. gingivalis but by a different mechanism. Activation by A. actinomycetemcomitans supernatant was correlated with a reduction of TIMP-2 secretion without any alteration of MT1-MMP, while activation by P. gingivalis increased MT1-MMP but no change of TIMP-2 was found. CONCLUSION: The supernatant from A. actinomycetemcomitans and P. gingivalis could induce the activation of MMP-2 possibly through the imbalance of MT1-MMP and TIMP-2 in HPDL cells but by different mechanisms. The imbalance of MT1-MMP and TIMP-2 may be another factor that is involved in the severity of periodontal disease.
    [Abstract] [Full Text] [Related] [New Search]