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Updated: Aug 14, 2026
Detection of Functional Matrix Metalloproteinases by Zymography
Published on: November 8, 2010
Screening of novel matrix metalloproteinases (MMPs) in human fetal membranes
Stephen J Fortunato1, Ramkumar Menon
1The Perinatal Research Center of The Women's Health Research and Education Foundation, Nashville, Tennessee 37203, USA. fortunat@edge.net
Objective:
Endogenous activation of matrix metalloproteinase (MMP) in human fetal membranes is hypothesized to contribute to membrane weakening leading to early rupture and is also involved in the initiation of labor. Our laboratory and several others have studied the source and action of some of these MMPs. The objective of this study is to document the expression pattern of most of the MMPs cloned and sequenced so far in amniochorion during preterm premature rupture of membranes (pPROM), at term not in labor and during term labor.
Materials And Methods:
Placentas were collected from women with PROM, term not in labor after C-sections and from women after term vaginal delivery. Membranes were separated from the placenta and a section away from the rupture site was selected. Amniochorion were separated from the placenta. RT-PCR was performed to study the expression pattern of MMP15 (MT2-MMP), MMP16 (MT3-MMP), MMP17 (MT4-MMP), MMP18, MMP20, MMP23, MMP24 (MT5-MMP), MMP25 (MT6-MMP), and MMP 26 using specific primers.
Results:
A differential pattern of expression was noted for some of the novel MMPs screened in this study in human fetal membranes. mRNA for most of the MMPs were expressed by amniochorion. MMP16 [membrane type metalloproteinase 3], MMP20 [enamelysin], and MMP26 [matrilysin] were not expressed.
Conclusion:
Amniochorion expresses several of the MMP genes at the time of pPROM, term not in labor and during active labor. We have previously reported the expression pattern of other MMPs and their inhibitors and their potential role in PROM. These findings support our hypothesis that amniochorion has a fully functional MMP system.
Insights
Human fetal membranes express matrix metalloproteinase (MMP) genes in preterm premature rupture of membranes (pPROM) and during labor. This confirms a functional MMP system in the amniochorion.
Area of Science:
- Reproductive biology
- Biochemistry
- Genetics
Background:
- Endogenous matrix metalloproteinases (MMPs) in human fetal membranes are implicated in membrane weakening, leading to preterm premature rupture of membranes (pPROM), and in labor initiation.
- Previous studies have investigated the source and function of specific MMPs.
Purpose of the Study:
- To document the expression patterns of various matrix metalloproteinases (MMPs) in the amniochorion.
- To compare MMP expression during preterm premature rupture of membranes (pPROM), term pregnancy without labor, and term labor.
Main Methods:
- Human placentas were collected from women experiencing PROM, undergoing C-sections without labor, and delivering vaginally.
- Amniochorion tissues were isolated, and reverse transcription-polymerase chain reaction (RT-PCR) was used to analyze the expression of MMP15, MMP16, MMP17, MMP18, MMP20, MMP23, MMP24, MMP25, and MMP26.
Main Results:
- A differential expression pattern was observed for several novel MMPs in the human fetal membranes.
- Messenger RNA (mRNA) for most investigated MMPs was expressed by the amniochorion.
- MMP16 (membrane type metalloproteinase 3), MMP20 (enamelysin), and MMP26 (matrilysin) were notably not expressed.
Conclusions:
- The amniochorion expresses multiple matrix metalloproteinase (MMP) genes during preterm premature rupture of membranes (pPROM), at term without labor, and during active labor.
- These findings support the hypothesis that the amniochorion possesses a fully functional MMP system.
- Previous research on other MMPs and their inhibitors further supports their potential role in PROM.
