Expression of matrix metalloproteinase (MMP)-2 and MMP-9 in human placenta and fetal membranes in relation to preterm and term labor.

Expression of matrix metalloproteinase (MMP)-2 and MMP-9 in human placenta and fetal membranes in relation to preterm and term labor.
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DOI:
10.1210/jcem.87.3.8320
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发表时间:
2002-03
期刊:
The Journal of clinical endocrinology and metabolism
影响因子:
--
通讯作者:
P. Xu;N. Alfaidy;J. Challis
P. Xu;N. Alfaidy;J. Challis
中科院分区:
其他
文献类型:
--
作者:
P. Xu;N. Alfaidy;J. Challis

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广泛的细胞外基质(ECM)重塑被发现在许多过程中,人类分娩在足月和早产。这些包括宫颈成熟、胎膜破裂和胎盘从母体子宫脱落。基质金属蛋白酶(MMPs)是ECM降解的主要介质。本研究旨在探讨MMP-2和MMP-9在早产和足月分娩的人胎膜(FM)和胎盘(PL)组织中的表达。MMP-9在早产和足月产FM中的表达均显著高于非临产FM(P < 0.01)。足月产PL组MMP-9水平也明显高于足月非临产组(P < 0.05)。MMP-2在分娩组织和非分娩组织中的表达无显著性差异。免疫定位研究揭示了MMP-2和MMP-9的特定分布模式。MMP-2定位于羊膜间充质、绒毛膜滋养层、壁蜕膜和PL绒毛血管。MMP-9主要定位于羊膜上皮细胞、绒毛膜滋养细胞、壁蜕膜和PL合胞体滋养细胞。分离的细胞培养从不同层的FM和纯化的PL滋养层细胞的培养表明,PL合胞体滋养层和羊膜上皮细胞专门产生MMP-9,绒毛膜滋养层细胞分泌MMP-2和MMP-9,但羊膜间充质细胞只产生MMP-2。我们的结论是,MMP-2和MMP-9表现出细胞特异性表达的人PL。MMP-9表达的增加可能有助于FM和PL中ECM的降解,从而促进早产和足月分娩时FM破裂和PL从母体子宫脱离。
Extensive extracellular matrix (ECM) remodeling is found in many processes during human parturition at term and preterm. These include cervical ripening, fetal membrane rupture, and placental detachment from the maternal uterus. Matrix metalloproteinases (MMPs) are the main mediators of ECM degradation. The present study was designed to investigate the expression of MMP-2 and MMP-9 in human fetal membranes (FMs) and placental (PL) tissues with or without labor at preterm and term parturition. Both zymography and Western blot analysis showed that MMP-9 was significantly (P < 0.01) increased in preterm and term labor FM, compared with nonlabor. Term labor PL also had a much higher (P < 0.05) level of MMP-9 than that of term nonlabor. No significant difference in MMP-2 expression was found between labor and nonlabor tissues. Immunolocalization studies revealed a specific distribution pattern for MMP-2 and MMP-9. MMP-2 was localized to the amnion mesenchyme, chorion laeve trophoblast, decidua parietalis, and blood vessels in PL villi. MMP-9 was localized mainly to amnion epithelia, chorion laeve trophoblast, decidua parietalis, and PL syncytiotrophoblasts. Separate cell culture from different layers of FM and culture of purified PL trophoblast cells showed that PL syncytiotrophoblast and amnion epithelial cells exclusively produced MMP-9; chorion trophoblast cells secreted both MMP-2 and MMP-9, but amnion mesenchymal cells produced only MMP-2. We concluded that MMP-2 and MMP-9 exhibited cell-specific expression in the human PL. An increase in MMP-9 expression may contribute to degradation of the ECM in the FM and PL, thereby facilitating FM rupture and PL detachment from the maternal uterus at labor, both preterm and term.