Role of Cyclooxygense-2 in Lipopolysacharide induced Matrix Metalloproteinase-2 and -9 expressions in human trophoblast (TL) cell line / 대한산부인과학회잡지
Korean Journal of Obstetrics and Gynecology
;
: 1752-1757, 2002.
Article
in Korean
| WPRIM
| ID: wpr-37865
ABSTRACT
OBJECTIVE:
To evaluate whether lipopolysaccharide (LPS) modulates the expression of cyclooxy- genase-2 (COX-2) and also whether COX-2 is involved in the LPS induced matrix metalloproteinase-2 (MMP-2) and MMP-9 activation in human trophoblastic (TL) cell line.METHODS:
We used the TL (trophoblast-like) cells and evaluated the effect of LPS on expression of COX-2 mRNA and protein and on activities of MMP-2 and MMP-9. Also, we pretreated cell line with LPS and NS398, a COX-2 inhibitor, and compared MMPs activities with LPS only group. In the present study, COX-2 was analyzed by RT-PCR and western blot analysis and gelatin zymography was done for the evaluation of gelatinase activities of MMP-2 and MMP-9.RESULTS:
The mRNA and protein expressions of COX-2 were increased by LPS in time- and dose-dependant fashions. COX-2 mRNA expression began to rise from 1 hour of LPS treatment and was increased steadily thereafter. COX-2 protein expression was detected from 1 hour of LPS treatment, but maximally increased by the 3 hours of treatment. LPS also increased MMP-2 and MMP-9 activities in time and dose dependant fashions. Especially, active form of MMP-9 was observed in the high concentration of LPS (>50 microgram/ml). When adding COX-2 inhibitor (NS398) to LPS pretreated cell line, the MMPs activities increased in two or three fold compared to LPS only group.CONCLUSION:
Our results suggested that LPS induces expression COX-2 and up-regulates activities of MMP-2 and MMP-9 in trophoblastic cell, but COX-2 although involved in LPS mediated MMP-2 and MMP-9 activation, may act through a different pathway than the commonly known prostaglandin metabolites mediated one.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Trophoblasts
/
RNA, Messenger
/
Cell Line
/
Blotting, Western
/
Gelatinases
/
Matrix Metalloproteinase 2
/
Matrix Metalloproteinases
/
Gelatin
Limits:
Humans
Language:
Korean
Journal:
Korean Journal of Obstetrics and Gynecology
Year:
2002
Type:
Article
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