Membrane-type matrix metalloproteinase-1 expression at the site of human placentation.
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.
INSERM U. 314, CHU Maison Blance, Reims, France.
B
B
Nawrocki
M
M
Polette
V
V
Marchand
E
E
Maquoi
A
A
Beorchia
J M
JM
Tournier
J M
JM
Foidart
P
P
Birembaut
D015152:Blotting, Northern; D002462:Cell Membrane / Q000201:enzymology*; D002824:Chorionic Villi / Q000201:enzymology; D017364:Collagenases / Q000032:analysis / Q000235:genetics*; D005260:Female; D015870:Gene Expression; D006801:Humans; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D020781:Matrix Metalloproteinase 1; D010920:Placenta / Q000201:enzymology; D010929:Placentation; D011247:Pregnancy; D012333:RNA, Messenger / Q000032:analysis; D014327:Trophoblasts / Q000201:enzymology
D012333:RNA, Messenger; D017364:Collagenases; D020781:Matrix Metalloproteinase 1