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See detailInduction of membrane-type matrix metalloproteinase 1 (MT1-MMP) expression in human fibroblasts by breast adenocarcinoma cells.
Polette, M.; Gilles, Christine ULg; Marchand, V. et al

in Clinical & Experimental Metastasis (1997), 15(2), 157-63

Membrane-type matrix metalloproteinase 1 (MT1-MMP) has been recently described as an activator of proMMP-2 (MMP-2) which is involved in tumor invasion. We have shown by in situ hybridization that MT1-MMP ... [more ▼]

Membrane-type matrix metalloproteinase 1 (MT1-MMP) has been recently described as an activator of proMMP-2 (MMP-2) which is involved in tumor invasion. We have shown by in situ hybridization that MT1-MMP is produced by stromal cells in close contact to preinvasive and invasive tumor cells of breast carcinomas. Of particular interest was the observation that some fibroblasts express this enzyme in focal areas in preinvasive lesions, suggesting that particular tumor cells may stimulate fibroblasts to produce MT1-MMP. We have therefore compared the ability of two different breast cancer cell lines, one non-invasive (MCF7) and one invasive (MDA-MB-231) to stimulate MT1-MMP production in human fibroblasts with consequent proMMP-2-activation. The MDA-MB-231 conditioned medium induced MT1-MMP mRNAs in human fibroblasts and a parallel activation of proMMP-2 whereas MCF7 conditioned medium did not have any effect. These results suggest the existence of soluble factor(s) secreted by invasive or some preinvasive breast tumor cells which stimulate fibroblasts to produce and activate MMPs, and emphasize the cooperation between cancer and stromal cells in tumor invasion. [less ▲]

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See detailTumor collagenase stimulatory factor (TCSF) expression and localization in human lung and breast cancers.
Polette, M.; Gilles, Christine ULg; Marchand, V. et al

in Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society (1997), 45(5), 703-9

Tumor cell-derived collagenase stimulatory factor (TCSF) stimulates in vitro the biosynthesis of various matrix metalloproteinases involved in tumor invasion, such as interstitial collagenase, gelatinase ... [more ▼]

Tumor cell-derived collagenase stimulatory factor (TCSF) stimulates in vitro the biosynthesis of various matrix metalloproteinases involved in tumor invasion, such as interstitial collagenase, gelatinase A, and stromelysin 1. The expression of TCSF mRNAs was studied in vivo, using in situ hybridization and Northern blotting analysis, in seven normal tissues and in 22 squamous cell carcinomas of the lung, and in seven benign proliferations and in 22 ductal carcinomas of the mammary gland. By in situ hybridization, TCSF mRNAs were detected in 40 of 44 carcinomas, in pre-invasive and invasive cancer cells of both lung and breast cancers. TCSF mRNAs and gelatinase A mRNAs were both visualized in the same areas in serial sections in breast cancers, and were expressed by different cells, tumor cells, and fibroblasts. The histological results were confirmed by Northern blot analysis, which showed a higher expression of TCSF mRNAs in cancers than in benign and normal tissues. These observations support the hypothesis that TCSF is an important factor in lung and breast tumor progression. [less ▲]

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See detailMembrane-type matrix metalloproteinase-1 expression at the site of human placentation
Nawrocki, B.; Polette, M. E.; Marchand, V. et al

in Placenta (1996), 17(8), 565-72

Human trophoblast implantation is a highly regulated process of invasion that requires action of proteolytic enzymes to degrade extracellular matrix components of the endometrium. Among these enzymes ... [more ▼]

Human trophoblast implantation is a highly regulated process of invasion that requires action of proteolytic enzymes to degrade extracellular matrix components of the endometrium. Among these enzymes, matrix metalloproteinases (MMPs) seem to be particularly important in this degradative process. We previously showed that gelatinase A is extensively expressed in vivo in the human placenta. A new MMP, MT-MMP-1 (membrane-type matrix metalloproteinase-1), which is thought to activate progelatinase A, has recently been described. In this study, we examined the expression of MT-MMP-1, by immunohistochemistry and in situ hybridization, in human placental bed biopsies taken during the first trimester of gestation. Human first trimester intermediate trophoblasts synthesized MT-MMP-1 mRNAs and the protein. The MT-MMP-1 pattern of distribution in placental beds was similar to that of gelatinase A, suggesting a pivotal role for MT-MMP-1 in placentation, perhaps by activating progelatinase A. [less ▲]

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