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Mol. Hum. Reprod. Advance Access originally published online on August 25, 2006
Molecular Human Reproduction 2006 12(10):633-641; doi:10.1093/molehr/gal072
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© The Author 2006. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Identification of a calcium-dependent matrix metalloproteinase complex in rat chorioallantoid membranes during labour

N. Meraz-Cruz1, A. Ortega2,3, G. Estrada-Gutierrez1, A. Flores1, A. Espejel1, C. Hernandez-Guerrero4 and F. Vadillo-Ortega1,5

1Direccion de Investigacion, 2Departamento de Bioquimica, Instituto Nacional de Perinatologia Isidro Espinosa de los Reyes, 3Departamento de Bioquimica, Facultad de Medicina, Universidad Nacional Autonoma de Mexico, and 4Departamento de Microscopia Electronica, Instituto Nacional de Perinatologia Isidro Espinosa de los Reyes, Mexico City, Mexico

5 To whom correspondence should be addressed at: Instituto Nacional de Perinatologia Isidro Espinosa de los Reyes, Montes Urales 800, Lomas de Virreyes, Mexico, D.F. 11000, Mexico. E-mail: fvadillo{at}servidor.inper.edu.mx

The induction of the expression of matrix metalloproteinases (MMPs) and their extracellular activation are key processes in connective tissue degradation in the chorioallantoid membrane during rat labour. However, the regulatory mechanisms remain largely unknown. Here, we report the identification of a calcium-dependent high molecular weight complex composed of MMP-9, MMP-3, MMP-2, tissue inhibitor of metalloproteinase 1 (TIMP-1) and TIMP-2, identified by zymography and western blotting. Molecular sieve chromatography confirmed the presence of a complex of MMPs and TIMPs with an exclusion volume >670 kDa. Differential scanning calorimetry of the complex confirmed the existence of a macromolecular complex that unfolds with a broad transition; it is denatured over a wide range of temperatures and has a Tm of 72°C in the presence of Ca2+. When denatured in the absence of Ca2+, there were at least eight transitions with Tms that corresponded to pro-MMP-9, MMP-9, pro-MMP-3, MMP-3, pro-MMP-2, MMP-2, TIMP-1 and TIMP-2. Co-localization of the same molecular components was demonstrated by confocal microscopy using cell-depleted chorioallantoid membranes. The assembly and disassembly of the complex can be reproduced at physiological concentrations of Ca2+. This complex provides a potential mechanism for the enzymatic regulation of MMPs, which may participate in connective tissue degradation leading to the rupture of the fetal membranes during labour.

Key words: chorioallantoid/extracellular matrix/matrix metalloproteinases/TIMP


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