Screening of novel matrix metalloproteinases (MMPs) in human fetal membranes

Stephen J. Fortunato, Ramkumar Menon

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)483-486
Number of pages4
JournalJournal of Assisted Reproduction and Genetics
Volume19
Issue number10
DOIs
StatePublished - Oct 1 2002
Externally publishedYes

Fingerprint

Extraembryonic Membranes
Matrix Metalloproteinases
Matrix Metalloproteinase 16
Placenta
Matrix Metalloproteinase 17
Membranes
Matrix Metalloproteinase 20
Matrix Metalloproteinase 15
Rupture
Matrix Metalloproteinase 7
Matrix Metalloproteinase Inhibitors

Keywords

  • Amniochorion
  • MMP
  • MT-MMP
  • PCR
  • Premature rupture of the membranes
  • Preterm labor

ASJC Scopus subject areas

  • Obstetrics and Gynecology
  • Developmental Biology
  • Genetics
  • Reproductive Medicine

Cite this

Screening of novel matrix metalloproteinases (MMPs) in human fetal membranes. / Fortunato, Stephen J.; Menon, Ramkumar.

In: Journal of Assisted Reproduction and Genetics, Vol. 19, No. 10, 01.10.2002, p. 483-486.

Research output: Contribution to journalArticle

@article{0ee6e094328840a7afe81fbb19408801,
title = "Screening of novel matrix metalloproteinases (MMPs) in human fetal membranes",
abstract = "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.",
keywords = "Amniochorion, MMP, MT-MMP, PCR, Premature rupture of the membranes, Preterm labor",
author = "Fortunato, {Stephen J.} and Ramkumar Menon",
year = "2002",
month = "10",
day = "1",
doi = "10.1023/A:1020362519981",
language = "English (US)",
volume = "19",
pages = "483--486",
journal = "Journal of in Vitro Fertilization and Embryo Transfer",
issn = "0740-7769",
publisher = "Springer New York",
number = "10",

}

TY - JOUR

T1 - Screening of novel matrix metalloproteinases (MMPs) in human fetal membranes

AU - Fortunato, Stephen J.

AU - Menon, Ramkumar

PY - 2002/10/1

Y1 - 2002/10/1

N2 - 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.

AB - 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.

KW - Amniochorion

KW - MMP

KW - MT-MMP

KW - PCR

KW - Premature rupture of the membranes

KW - Preterm labor

UR - http://www.scopus.com/inward/record.url?scp=0036773499&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036773499&partnerID=8YFLogxK

U2 - 10.1023/A:1020362519981

DO - 10.1023/A:1020362519981

M3 - Article

VL - 19

SP - 483

EP - 486

JO - Journal of in Vitro Fertilization and Embryo Transfer

JF - Journal of in Vitro Fertilization and Embryo Transfer

SN - 0740-7769

IS - 10

ER -