Regulation of MT1-MMP/MMP-2/TIMP-2 axis in human placenta

Zoë L Vincent,1,2 Murray D Mitchell,l,3 Anna P Ponnampalam1,2 1Liggins Institute, 2Gravida: National Centre for Growth and Development, University of Auckland, Auckland, New Zealand; 3University of Queensland Centre for Clinical Research, Brisbane, QLD, Australia Abstract: Matrix metallopr...

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Autores principales:	Vincent ZL, Mitchell MD, Ponnampalam AP
Formato:	article
Lenguaje:	EN
Publicado:	Dove Medical Press 2015
Materias:	Pathology RB1-214 Therapeutics. Pharmacology RM1-950
Acceso en línea:	https://doaj.org/article/3dbeea94de0f4c34b2753cd0bc937e1b
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spelling	oai:doaj.org-article:3dbeea94de0f4c34b2753cd0bc937e1b2021-12-02T00:37:14ZRegulation of MT1-MMP/MMP-2/TIMP-2 axis in human placenta1178-7031https://doaj.org/article/3dbeea94de0f4c34b2753cd0bc937e1b2015-10-01T00:00:00Zhttps://www.dovepress.com/regulation-of-mt1-mmpmmp-2timp-2-axis-in-human-placenta-peer-reviewed-article-JIRhttps://doaj.org/toc/1178-7031Zoë L Vincent,1,2 Murray D Mitchell,l,3 Anna P Ponnampalam1,2 1Liggins Institute, 2Gravida: National Centre for Growth and Development, University of Auckland, Auckland, New Zealand; 3University of Queensland Centre for Clinical Research, Brisbane, QLD, Australia Abstract: Matrix metalloproteinases (MMPs) and specific endogenous tissue inhibitors of metalloproteinases (TIMPs) mediate rupture of the fetal membranes in both physiological and pathological conditions. MMPs and TIMPs are subject to regulation by DNA methylation in human malignancies and pre-eclampsia. To determine if membrane type 1 MMP (MT1-MMP), MMP2, and TIMP2 are regulated by DNA methylation in human placentas, we employed an in vitro model where human placental tissues were collected at term gestation and cultured with methylation inhibiting agent 5-aza-2′deoxycytidine (AZA) and lipopolysaccharide. The results suggest that DNA methylation is not directly involved in the regulation of MT1-MMP in placental tissue; however, remodeling of chromatin by a pharmacologic agent such as AZA potentiates an infection-related increase in MT1-MMP. MT1-MMP is a powerful activator of MMP2 and this action, coupled with either no change or a decrease in TIMP2 concentrations, favors a gelatinolytic state leading to extracellular matrix degradation, which could predispose fetal membranes to rupture prematurely during inflammation. Keywords: placenta, epigenetic regulation, DNA methylation, MMPs, laborVincent ZLMitchell MDPonnampalam APDove Medical PressarticlePathologyRB1-214Therapeutics. PharmacologyRM1-950ENJournal of Inflammation Research, Vol 2015, Iss default, Pp 193-200 (2015)
institution	DOAJ
collection	DOAJ
language	EN
topic	Pathology RB1-214 Therapeutics. Pharmacology RM1-950
spellingShingle	Pathology RB1-214 Therapeutics. Pharmacology RM1-950 Vincent ZL Mitchell MD Ponnampalam AP Regulation of MT1-MMP/MMP-2/TIMP-2 axis in human placenta
description	Zoë L Vincent,1,2 Murray D Mitchell,l,3 Anna P Ponnampalam1,2 1Liggins Institute, 2Gravida: National Centre for Growth and Development, University of Auckland, Auckland, New Zealand; 3University of Queensland Centre for Clinical Research, Brisbane, QLD, Australia Abstract: Matrix metalloproteinases (MMPs) and specific endogenous tissue inhibitors of metalloproteinases (TIMPs) mediate rupture of the fetal membranes in both physiological and pathological conditions. MMPs and TIMPs are subject to regulation by DNA methylation in human malignancies and pre-eclampsia. To determine if membrane type 1 MMP (MT1-MMP), MMP2, and TIMP2 are regulated by DNA methylation in human placentas, we employed an in vitro model where human placental tissues were collected at term gestation and cultured with methylation inhibiting agent 5-aza-2′deoxycytidine (AZA) and lipopolysaccharide. The results suggest that DNA methylation is not directly involved in the regulation of MT1-MMP in placental tissue; however, remodeling of chromatin by a pharmacologic agent such as AZA potentiates an infection-related increase in MT1-MMP. MT1-MMP is a powerful activator of MMP2 and this action, coupled with either no change or a decrease in TIMP2 concentrations, favors a gelatinolytic state leading to extracellular matrix degradation, which could predispose fetal membranes to rupture prematurely during inflammation. Keywords: placenta, epigenetic regulation, DNA methylation, MMPs, labor
format	article
author	Vincent ZL Mitchell MD Ponnampalam AP
author_facet	Vincent ZL Mitchell MD Ponnampalam AP
author_sort	Vincent ZL
title	Regulation of MT1-MMP/MMP-2/TIMP-2 axis in human placenta
title_short	Regulation of MT1-MMP/MMP-2/TIMP-2 axis in human placenta
title_full	Regulation of MT1-MMP/MMP-2/TIMP-2 axis in human placenta
title_fullStr	Regulation of MT1-MMP/MMP-2/TIMP-2 axis in human placenta
title_full_unstemmed	Regulation of MT1-MMP/MMP-2/TIMP-2 axis in human placenta
title_sort	regulation of mt1-mmp/mmp-2/timp-2 axis in human placenta
publisher	Dove Medical Press
publishDate	2015
url	https://doaj.org/article/3dbeea94de0f4c34b2753cd0bc937e1b
work_keys_str_mv	AT vincentzl regulationofmt1mmpmmp2timp2axisinhumanplacenta AT mitchellmd regulationofmt1mmpmmp2timp2axisinhumanplacenta AT ponnampalamap regulationofmt1mmpmmp2timp2axisinhumanplacenta
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Regulation of MT1-MMP/MMP-2/TIMP-2 axis in human placenta

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