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Epidermal Growth Factor and Basic Fibroblast Growth Factor Increase the Production of Matrix Metalloproteinases during in Vitro Decidualization of Rat Endometrial Stromal Cells

Departments of Physiology and Obstetrics and Gynaecology, University of Western Ontario, London, Ontario, Canada N6A 5C1

Address all correspondence and requests for reprints to: Dr. T. G. Kennedy, Department of Physiology, University of Western Ontario, London, Ontario, Canada N6A 5C1. E-mail: tkennedy{at}physiology.uwo.ca

Numerous growth factors are involved in mediating proliferation and differentiation of endometrial stromal cells during decidualization. During this period, the extracellular matrix of the endometrium undergoes extensive remodeling. We tested the hypothesis that epidermal growth factor (EGF), basic fibroblast growth factor (bFGF), and transforming growth factor-ß regulate expression of matrix metalloproteinases (MMPs) and their inhibitors, tissue inhibitors of metalloproteinases (TIMPs), during decidualization. Stromal cells were isolated from uteri hormonally sensitized to undergo decidualization and were cultured in the absence or presence of a growth factor. Using substrate-gel electrophoresis with gelatin as the substrate, we detected activity for gelatinase A and B, and collagenase-3, and using casein as a substrate, we detected activity for stromelysin-1. Increasing concentrations of EGF and bFGF resulted in increased activity of gelatinase B, collagenase-3, and stromelysin-1. Northern blot analyses revealed that EGF and bFGF also increased messenger RNA levels for these MMPs. There was no effect of these growth factors on gelatinase or TIMP-1, -2, and -3, nor was there an effect of transforming growth factor-ß on any MMP or TIMP examined. These data demonstrate that EGF and bFGF increase levels of proteolytic enzymes produced by endometrial stromal cells undergoing decidualization in vitro while having no effect on their inhibitors.

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