Reference : Membrane-type matrix metalloproteinase-1 expression at the site of human placentation
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/91483
Membrane-type matrix metalloproteinase-1 expression at the site of human placentation
English
Nawrocki, B. [ > > ]
Polette, M. E. [ > > ]
Marchand, V. [ > > ]
Maquoi, Erik mailto [Université de Liège - ULg > Département des sciences cliniques > Labo de biologie des tumeurs et du développement >]
Beorchia, A. [ > > ]
Tournier, J. M. [ > > ]
Foidart, Jean-Michel mailto [Université de Liège - ULg > Département des sciences cliniques > Gynécologie - Obstétrique >]
Birembaut, P. [ > > ]
1996
Placenta
W.B. Saunders
17
8
565-72
Yes (verified by ORBi)
International
0143-4004
London
United Kingdom
[en] Human trophoblast implantation is a highly regulated process of invasion that requires action of proteolytic enzymes to degrade extracellular matrix components of the endometrium. Among these enzymes, matrix metalloproteinases (MMPs) seem to be particularly important in this degradative process. We previously showed that gelatinase A is extensively expressed in vivo in the human placenta. A new MMP, MT-MMP-1 (membrane-type matrix metalloproteinase-1), which is thought to activate progelatinase A, has recently been described. In this study, we examined the expression of MT-MMP-1, by immunohistochemistry and in situ hybridization, in human placental bed biopsies taken during the first trimester of gestation. Human first trimester intermediate trophoblasts synthesized MT-MMP-1 mRNAs and the protein. The MT-MMP-1 pattern of distribution in placental beds was similar to that of gelatinase A, suggesting a pivotal role for MT-MMP-1 in placentation, perhaps by activating progelatinase A.
http://hdl.handle.net/2268/91483

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