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Evaluation of the Expression and Enzyme Activity of Matrix Metalloproteinase—7 in Fetal Membranes During Premature Rupture of Membranes at Term in HumansDepartment of Obstetrics and Gynecology, Juntendo University School of Medicine, Tokyo, Japan, saori68{at}med.juntendo.ac.jp
Department of Host Defense and Biochemical Research, Juntendo University School of Medicine, Tokyo, Japan
Department of Obstetrics and Gynecology, Juntendo University School of Medicine, Tokyo, Japan
Department of Obstetrics and Gynecology, Juntendo University School of Medicine, Tokyo, Japan
Department of Obstetrics and Gynecology, Juntendo University School of Medicine, Tokyo, Japan
Department of Host Defense and Biochemical Research, Juntendo University School of Medicine, Tokyo, Japan
Department of Obstetrics and Gynecology, Juntendo University School of Medicine, Tokyo, Japan Amnion, chorion, and decidua were separated from fetal membranes at term from women with no labor (cesarean delivery [CS], n = 10), labor (normal delivery, n = 10), and labor during premature rupture of membranes (PROM; n = 8) for evaluation of matrix metalloproteinase (MMP)—7. The expression of pro-MMP-7 was immunohistochemically demonstrated in amnion, chorion, and decidua. Interestingly, however, Western blotting revealed that pro-MMP-7 and MMP-7 expression was the lowest in amnion from PROM, whereas it was the highest in chorion and decidua from PROM. Importantly, the enzymatic activity of MMP-7 determined with an MMP-7—specific substrate was higher in amnion from PROM than that from CS. Moreover, the tissue inhibitor of metalloproteinase (TIMP)—1 level was lower in amnion from PROM than that from CS. Thus, MMP-7 is expressed in fetal membranes (amnion, chorion, and decidua), and its activity is increased in amnion of PROM at term, accompanied with the reduced level of TIMP-1, which may suggest the possible involvement of MMP-7 in PROM.
Key Words: Matrix metalloproteinase MMP-7 premature rupture of membranes.
Reproductive Sciences, Vol. 15, No. 2,
156-165 (2008) |
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