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Rabbit uterine cervical fibroblasts in culture produces tissue inhibitor of metalloproteinases (TIMP)-1 and TIMP-2. When cells were treated with physiological concentrations of progesterone, the production of two TIMPs increased, and essentially all TIMP-2 was found to be complexed with promatrix metalloproteinase 2 (proMMP-2)/progelatinase A. Progesterone did not modulate the production of proMMP-2 and resulted in the increased total amount of proMMP-2-TIMP-2 complex. These observations provide the first evidence that progesterone participates in maintaining the homeostasis of connective tissue matrix in uterine cervix by augmenting both TIMP-1 and TIMP-2 production along with the known suppressive effects on the proMMP-1 and proMMP-3 production.

Original publication




Journal article


Febs lett

Publication Date





109 - 112


Animals, Cells, Cultured, Cervix Uteri, Culture Media, Extracellular Matrix Proteins, Female, Fibroblasts, Glycoproteins, Humans, Metalloendopeptidases, Progesterone, Protein Biosynthesis, Protein Precursors, Rabbits, Tissue Inhibitor of Metalloproteinase-2, Tissue Inhibitor of Metalloproteinases