[Identification of extracellular matrix metalloprotease 3 in the fetal membrane of the rat and its possible implication in the rupture of chorioamniotic membranes].
OBJECTIVE
Human corioamniotic membranes, or their equivalent in the rat, function as selective barrier during gestation and their rupture is part of the mechanisms implied in the labor. Molecular mechanisms carried out in this process are unknown.


METHODS
Experimental animal model.


METHODS
Corioamniotic membranes (obtained at the beginning of the labor) of rats with programmed and synchronous pregnancies were analized. The coexistence and distribution of metalloproteinase of extracellular-3 matrix (estromelisine) in these tissues were determined.


RESULTS
Secretion and tissue location of metalloproteinase of extracellular-3 matrix in fetal membranes were identified for the first time. Metalloproteinase of extracellular-3 matrix was immunolocated in the compact layer of the amnion and its secretion (by the membranes) was confirmed through electrophoresis, zimography and Western blot. By confocal microscopy it was verified that metalloproteinase of extracellular-3 matrix is located in the same places of that of extracellular-9 matrix.


CONCLUSIONS
Rupture of corioamniotic membranes relates to the expression and local activity of the metalloproteinases of extracellular matrix. The coexistence of metalloproteinase of extracellular-3 matrix in the amnion of the rat has been identified; this element is added to the biochemical process of rupture, since metalloproteinase of extracelular-3 matrix is an activator of that of extracellular-9 matrix. It is possible that the physiological function of this enzyme is implied, of a main way, in the process of rupture of corioamniotic membranes during the childbirth.
Meraz Cruz
Noemí
N
Instituto Nacional de Perinatología Isidro Espinosa de los Reyes, Lomas de Virreyes, México, DF.
Beltrán Montoya
Jorge
J
Estrada Gutiérrez
Guadalupe
G
Vadillo Ortega
Felipe
F
D000650:Amnion / Q000201:enzymology* / Q000378:metabolism / Q000648:ultrastructure; D000818:Animals; D001485:Basement Membrane / Q000201:enzymology; D004792:Enzyme Precursors / Q000032:analysis; D004847:Epithelial Cells / Q000201:enzymology / Q000378:metabolism; D005109:Extracellular Matrix / Q000201:enzymology; D016326:Extracellular Matrix Proteins / Q000032:analysis; D005260:Female; D018093:Gelatinases / Q000032:analysis; D020778:Matrix Metalloproteinase 2 / Q000032:analysis; D019278:Matrix Metalloproteinase 3 / Q000032:analysis / Q000378:metabolism / Q000502:physiology*; D020780:Matrix Metalloproteinase 9 / Q000032:analysis; D008666:Metalloendopeptidases / Q000032:analysis; D018613:Microscopy, Confocal; D011247:Pregnancy; D051381:Rats / Q000378:metabolism*; D017208:Rats, Wistar; D012422:Rupture, Spontaneous
D004792:Enzyme Precursors; D016326:Extracellular Matrix Proteins; D018093:Gelatinases; D008666:Metalloendopeptidases; C120487:pro-matrix metalloproteinase 9; C069860:progelatinase; D019278:Matrix Metalloproteinase 3; D020778:Matrix Metalloproteinase 2; D020780:Matrix Metalloproteinase 9