Molecular Human Reproduction, Vol. 9, No. 6, 367-373,
June 2003
© 2003 European Society of Human Reproduction and Embryology
Article |
Differential activity of the gelatinases (matrix metalloproteinases 2 and 9) in the fetal membranes and decidua, associated with labour
Submitted on January 20, 2003; accepted on February 17, 2003
1 Laboratory for Research in Reproductive Sciences, Department of Obstetrics and Gynecology, HaEmek Medical Center, 18101, Afula and 2 Rappaport Faculty of Medicine, Technion-Israel Institute of Technology, Haifa, Israel
3 To whom correspondence should be addressed at: Department of Obstetrics and Gynecology, HaEmek Medical Center, Afula 18101, Israel. e-mail: shaleve{at}tx.technion.ac.il
Degradation of the extracellular matrix in fetal membranes has been implicated in the rupture of fetal membranes, the process of parturition and placental detachment from the decidua after parturition. In this study we assessed labour-associated changes in gelatinase activity in cultured human amnion, chorion and decidua, as well as in amniotic fluid. We found that in media conditioned by decidua, following the establishment of uterine contractions, matrix metalloproteinase-2 (MMP-2) activity is increased while the protein tissue inhibitors of matrix metalloproteinase-1 (TIMP-1) level is decreased. The formation of a 130 kDa gelatinase band was also significantly increased after contractions began. In media conditioned by chorion, the initiation of uterine contractions did not change MMP activity or TIMP-1 levels. However, an increase in MMP-9 activity and a decrease in TIMP-1 protein levels were observed following the establishment of uterine contractions in media conditioned by amnion. We suggest that this differential spatial regulation provides a form for modulatory hierarchal activity of the MMPs in the onset of labour allowing rupture of the membranes while avoiding premature placental separation.
Key words: contractions/decidua/fetal membrane/matrix metalloproteinase-2, -9/TIMP
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