title: Expression of gelatinases A and B and their tissue inhibitors by cells of early and term human placenta and gestational endometrium.
abstract: BACKGROUND
  Human placentation is mediated by fetal trophoblastic cells that invade the maternal uterine endometrium. Trophoblast invasion requires a precisely regulated secretion of specific proteolytic enzymes able to degrade the endometrial basement membrane and extracellular matrix.
  
  
  METHODS
  Several studies have documented the key roles of matrix metalloproteinases and their tissue inhibitors in the invasion of various matrices by cultured trophoblasts. In vitro studies suggest that placentation could result from a balance between the secretion of these enzymes by trophoblast cells and their inhibition by the natural tissue inhibitors (TIMPs) produced by maternal decidual cells. The precise localization and levels of expression of these proteins that account for and control invasion during human placentation in vivo however, have not been described. We have evaluated, in vivo, by immunohistochemistry, Northern blot analysis and in situ hybridization, the expression of two metalloproteinases (gelatinases A and B) and their two tissue inhibitors (TIMPs 1 and 2) in placental villi and placental beds of first and third trimesters of normal pregnancy.
  
  
  RESULTS
  Human first trimester intermediate trophoblast produced both gelatinases A and B; these two gelatinases were respectively less and no more detected at term in these cells. We found that both TIMP1 and 2 were also expressed in maternal decidual cells with a dramatic increase of TIMP1 at the term of pregnancy. In floating villi, gelatinase A and TIMP1 were localized in the stromal compartment, whereas gelatinase B and TIMP2 were codistributed in trophoblast cells.
  
  
  CONCLUSIONS
  The gelatinases A and B and their tissue inhibitors are thus expressed by specific cells in early and late placental beds and villi. This pattern of expression varies during pregnancy. Therefore, our morphologic study supports biologic findings suggesting that these proteins may participate in placentation.
authors: Inserm U.314, CHU Maison Blanche, Reims, France.
authors: M
authors: M
authors: Polette
authors: B
authors: B
authors: Nawrocki
authors: A
authors: A
authors: Pintiaux
authors: C
authors: C
authors: Massenat
authors: E
authors: E
authors: Maquoi
authors: L
authors: L
authors: Volders
authors: J P
authors: JP
authors: Schaaps
authors: P
authors: P
authors: Birembaut
authors: J M
authors: JM
authors: Foidart
mesh_terms: D015152:Blotting, Northern; D002824:Chorionic Villi / Q000201:enzymology; D017364:Collagenases / Q000096:biosynthesis* / Q000502:physiology; D004717:Endometrium / Q000201:enzymology*; D005260:Female; D018093:Gelatinases / Q000096:biosynthesis* / Q000502:physiology; D006023:Glycoproteins / Q000096:biosynthesis* / Q000502:physiology; D006801:Humans; D007124:Immunoenzyme Techniques; D017403:In Situ Hybridization; D020778:Matrix Metalloproteinase 2; D020780:Matrix Metalloproteinase 9; D008666:Metalloendopeptidases / Q000096:biosynthesis* / Q000502:physiology; D010920:Placenta / Q000201:enzymology*; D010929:Placentation / Q000502:physiology; D011247:Pregnancy; D014176:Protein Biosynthesis; D011506:Proteins / Q000502:physiology; D019716:Tissue Inhibitor of Metalloproteinase-2; D019714:Tissue Inhibitor of Metalloproteinases; D014327:Trophoblasts / Q000201:enzymology
chemical_list: D006023:Glycoproteins; D011506:Proteins; D019714:Tissue Inhibitor of Metalloproteinases; D019716:Tissue Inhibitor of Metalloproteinase-2; D017364:Collagenases; D018093:Gelatinases; D008666:Metalloendopeptidases; D020778:Matrix Metalloproteinase 2; D020780:Matrix Metalloproteinase 9