• 9
    Feb
  • Modulation of 72-Kilodalton Type IV Collagenase (Matrix Metalloproteinase-2) by Ascorbic Acid in Cultured Human Amnion-Derived Cells(2)

This background, and the fact that pregnancy implies an extra demand of nutrients, suggest that marginal deficiency of vitamin C should be further studied. buy ortho tri-cyclen online

A novel physiopathogenic mechanism for PROM, involving increased collagen degradation in chorioamnion mediated by matrix metalloproteinases (MMPs), has been recently proposed. MMPs, such as collagenase, stro-melysin, and type IV collagenases/gelatinases, are a group of enzymes that are involved in extracellular matrix catabolism. This family of enzymes plays a key role in connective tissue turnover and has been implicated in many normal and pathological processes.

These enzymes are synthesized by chorioamnion cells, and MMP-2 or 72-kDa type IV collagenase is a constitutive enzyme during pregnancy. It seems that collagen degradation plays an important role in PROM; therefore the main objective of this study was to assess whether ascorbic acid may exert a direct action on collagenolysis using cultured chorioamniotic membrane resident cells as a study model of extracellular matrix catabolism modulation by vitamin C.

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