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• W2938973823 abstract "The cumulative thesis presented characterizes the expression and functional significance of matrix metalloproteinases (MMPs) and their tissue inhibitors of metalloproteinases (TIMPs) in bovine placental cells in vitro and in vivo with special reference to trophoblast giant cell (TGC) invasion/migration and placental retention. The bovine synepitheliochorial placenta is characterized by restricted trophoblast invasion/migration, a unique feature of which the regulatory mechanisms are not completely understood. The activity of MMPs in the extracellular space is specifically inhibited by counteracting TIMPs to serve and control cell migration and tissue remodelling. MMP-9 is present in the bovine placenta throughout gestation; its proteolysis is believed to be predominantly regulated by the action of endogenous TIMP-1. Epidermal growth factor (EGF), as regulator of fundamental cell properties, is expressed in the bovine placenta and capable to up-regulate MMP-9 activity in a variety of cells types. Aim of this in vitro study was therefore to examine the influence of EGF on cell motility, proliferation, as well as MMP-9 and TIMP-1 expression in cultured bovine trophoblast cells. The effect of EGF on MMP-9 and TIMP-1 expression was examined in a trophoblast cell line (F3) by semiquantitative RT-PCR. The proteolytic activity of MMP-9 was determined by zymography. Migration assays were performed using a Boyden chamber and cell motility was measured by time-lapse analyses. To identify the involved signalling cascades, phosphorylation of mitogen-activated protein kinase (MAPK) 42/44 and Akt was detected by Western blot. EGF treatment increased both the abundance of MMP-9 and TIMP-1 mRNAs and the proteolytic activity of MMP-9. Furthermore, EGF stimulated proliferation and migration of F3 cells. Addition of specific inhibitors of MAPK (PD98059) and/or phosphatidylinositol 3-kinases (LY294002) activation abolished or reduced EGF-induced effects in all experiments. The results of the in vitro study suggest that EGF could also be responsible for stimulating migration and proliferation of bovine trophoblast cells in vivo, and thus may be involved in bovine placental tissue remodelling and postpartum release of fetal membranes by the upregulation MMP-9 and TIMP-1. The retention of fetal membranes is one of the most common reproductive diseases in cattle causing considerable economic loss (e.g. reduced milk yield, poorer fertility). To allow a physiological release of fetal membranes and avoid placental retention, the tight feto-maternal connection established by fetal cotyledonary villi interdigitating with maternal caruncles must be separated. Membrane-type MMPs have been suggested as potential activators controlling extracellular matrix (ECM) degradation and remodelling. In particular, MMP-14 is able to degrade ECM substrates and activate MMP-2 through binding TIMP-2 at the cell surface. We hypothesize that impaired modulation of the ECM by MMPs/TIMPs participates in the aetiology of bovine retained fetal membranes. This involvement was analysed in vivo comparing placentomes from cows at term parturition and timely release of fetal membranes and cows with retained fetal membranes after various treatments for the induction of parturition, and after elective caesarean sections. The expression of MMP-14, MMP-2 and TIMP-2 was examined by real-time-PCR, immunohistochemistry, Western blot and zymography. The relative mRNA expression levels of MMP-14 was similar in all groups, while the expression levels of MMP-2 and TIMP-2 were higher in most animals with induced parturition and retention of fetal membranes compared to animals without placental retention. In cows with placental retention, MMP-14 protein was expressed in cells of the fetal mesenchyme and maternal stroma, whereas in cows with release of fetal membranes MMP-14 was localized in uninucleated trophoblast cells. MMP-2 could be detected in uninucleated trophoblast cells and the fetal mesenchyme, while TIMP-2 was present exclusively in trophoblast giant cells. The enzyme activity was confirmed by zymography. The co-localization of MMP-14, MMP-2 and TIMP-2 in the fetal compartment, especially in trophoblast cells at term, allows the modulation of ECM composition at the feto-maternal interface and therefore could influence the timely release of fetal membranes in cattle. In conclusion, the specific expression of MMPs and TIMPs in bovine trophoblast cells in vitro and in vivo suggests an involvement of the MMP/TIMP system in TGC migration/invasion and in the aetiology of placental retention. The capability of growth factors, in particular EGF, to induce proteolysis by MMPs and changes in the MMP/TIMP system itself can lead to alterations of the ECM composition and therefore support the release of fetal membranes." @default.
• W2938973823 created "2019-04-25" @default.
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• W2938973823 date "2011-01-01" @default.
• W2938973823 modified "2023-09-23" @default.
• W2938973823 title "Expression of matrix metalloproteinases (MMPs) and their tissue inhibitors (TIMPs) in bovine placental cells in vivo and in vitro" @default.
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