Expression of matrix metalloproteinase-3 in mouse endometrial stromal cells during early pregnancy: Regulation by interleukin-1α and tenascin-C

References

• Birkedal-Hansen H, Moore WGI, Bodden MK, Windsor LJ, Birkedal-Hansen B, DeCarlo A, Engler JA. Matrix metallo-proteinases: a review. Crit Rev Oral Biol Med 1993;4:197–250.
   PubMedGoogle Scholar
• Birkedal-Hansen H. Proteolytic remodeling of extracellular matrix. Curr Opin Cell Biol 1995;7:728–735.
   PubMed Web of Science ®Google Scholar
• Nagase H, Woessner JF Jr. Matrix metalloproteinases. J Biol Chem 1999;274:21491–21494.
   PubMed Web of Science ®Google Scholar
• Murphy G, Gavrilovic J. Proteolysis and cell migration: creating a path? Curr Opin Cell Biol 1999;11:614–621.
   PubMed Web of Science ®Google Scholar
• Shapiro SD. Matrix metalloproteinase degradation of extra-cellular matrix: biological consequences. Curr Opin Cell Biol 1998;10:602–608.
   PubMed Web of Science ®Google Scholar
• Bischof P, Friedli E, Martelli M, Campana A. Expression of extracellular matrix-degrading metalloproteinases by cultured human cytotrophoblast cells: effect of cell adhesion and immunopurification. Am J Obstet Gynecol 1991;165:1791–1801.
   Google Scholar
• Strickland S, Richards WG. Invasion of the trophoblasts. Cell 1992;71:355–357.
   PubMed Web of Science ®Google Scholar
• Alexander CM, Hansell EJ, Behrendtsen 0, Flannery ML, Kishnani NS, Hawkes SP, Werb Z. Expression and function of matrix metalloproteinases and their inhibitors at the maternal-embryonic boundary during mouse embryo implantation. Development 1996;122:1723–1736.
   Google Scholar
• Das SK, Yano S, Wang J, Edwards DR, Nagase H, Dey SK. Expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in the mouse uterus during the pen-implantation period. Dev Genet 1997;21:44–54.
   PubMedGoogle Scholar
• Bass KE, Hongxia LI, Hawkes SP, Howard E, Bullen E, Thien-Khai HVU, McMaster M, Janatpour M, Fisher SJ. Tissue inhibitor of metalloproteinase-3 expression is upregu-lated during human cytotrophoblast invasion in vitro. Dev Genet 1997;21: 61–67.
   Google Scholar
• Salamonsen LA. Role of proteinases in implantation. Rev Reprod 1999;4:11–22.
   PubMedGoogle Scholar
• Noda N, Minoura H, Nishiura R, Toyoda N, Imanaka-Yoshida K, Sakakura T, Yoshida T. Expression of tenascin-C in stromal cells of the murine uterus during early pregnancy: induction by interleukin- la, prostaglandin E2, and prosta-glandin F2„. Biol Reprod 2000;63: 1713–1720.
   Google Scholar
• Rawdanowicz TJ, Hampton AL, Nagase H, Woolley DE, Salamonsen LA. Matrix metalloproteinase production by cultured human endometrial stromal cells: identification of interstitial collagenase, gelatinase-A, gelatinase-B, and stro-melysin-1 and their differential regulation by interleukin-1 and tumor necrosis factor-a. J Chin Endocrinol Metab 1994;79: 530–536.
   Google Scholar
• Imai K, Hiramatsu A, Fukushima D, Pierschbacher MD, Okada Y. Degradation of decorin by matrix metalloprotei-nases: identification of the cleavage sites, kinetic analyses and transforming growth factor-M. release. Biochem J 1997;322: 809–814.
   Google Scholar
• Osteen KG, Sierra-Rivera E, Keller NR, Fox DB. Interleukin-Lx opposes progesterone-mediated suppression of MMP-7. Ann NY Acad Sci 1997;828:137–145.
   Google Scholar
• Keller NR, Sierra-Rivera E, Eisenberg E, Osteen KG. Progesterone exposure prevents matrix metalloproteinase-3 (MMP-3) stimulation by interleukin-Lx in human endometrial stromal cells. J Clin Endocrinol Metab 200085:1611-1619.
   PubMed Web of Science ®Google Scholar
• Kalembeyi I, Inada H, Nishiura R, Imanaka-Yoshida K, Sakakura T, Yoshida T. Tenascin-C upregulates matrix metalloproteinase-9 in breast cancer cells: direct and syner-gistic effects with transforming growth factor #1. hit J Cancer 2003;105: 53–60.
   Google Scholar
• Sternlicht MD, Lochter A, Sympson CJ, Huey B, Rougier JP, Gray JW, Pinkel D, Bissell MJ, Werb Z. The stromal proteinase MMP3/stromelysin-1 promotes mammary carcino-genesis. Cell 1999;98: 137–146.
   Google Scholar
• Johansson N, Ahonen M, Kahari VM. Matrix metalloprotei-nases in tumor invasion. Cell Mol Life Sci 2000;57:5–15.
   PubMed Web of Science ®Google Scholar
• Tremble P, Chiquet-Ehrismann R, Werb Z. The extracellular matrix ligands fibronectin and tenascin collaborate in regulat-ing collagenase gene expression in fibroblasts. Mol Biol Cell 1994;5:439–453.
   PubMed Web of Science ®Google Scholar
• Jacobs AL, Carson DD. Uterine epithelial cell section of interleukin-1 a induces prostaglandin E2 (PGE2) and P0F2. secretion by uterine stromal cells in vitro. Endocrinology 1993;132:300–308.
   Google Scholar
• Yoshida T, Yoshimura E, Numata H, Sakakura Y, Sakakura, T. Involvement of tenascin-C in proliferation and migration of laryngeal carcinoma cells. Virchows Arch 1999;435:496–500.
   Google Scholar
• Chomczynski P. A reagent for the single-step simultaneous isolation of RNA, DNA and proteins from cell and tissue samples. Biotechniques 1993;15:532–535.
   PubMed Web of Science ®Google Scholar
• Sillem M, Prifti S, Koch A, Neher M, Jauckus J, Runnebaum B. Regulation of matrix metalloproteinases and their inhibitors in uterine endometrial cells of patients with and without endometriosis. Eur J Obstet Gynecol Reprod Biol 2001;95:167–174.
   PubMed Web of Science ®Google Scholar
• Freitas S, Meduri G, Nestour EL, Bausero P, Perrot-Applant M. Expression of metalloproteinases and their inhibitors in blood vessels in human endometrium. Biol Reprod 1999;61:1070–1082.
   Google Scholar
• Suzuki M, Raab G, Moses MA, Fernandez CA, Klagsbrun M. Matrix metalloproteinase-3 releases active heparin-binding EGF-like growth factor by cleavage at a specific juxtamem-brane site. J Biol Chem 1997;272: 31730–31737.
   Google Scholar
• Schonbeck U, Mach F, Libby P. Generation of biologically active IL-lx by matrix metalloproteinases: a novel caspase-1-independent pathway of IL-1a processing. J Immunol 1998;161: 3340–3346.
   Google Scholar
• Fowlkes JL, Suzuki K, Nagase H, Thraikill KM. Proteolysis of insulin-like growth factor binding protein-3 during rat pregnancy: a role for matrix metalloproteinases. Endocrinol-ogy 1994;135:2810–2813.
   Google Scholar
• Coppock HA, White A, Aplin JD, Westwood M. Matrix metalloprotease-3 and -9 proteolyze insulin-like growth factor-binding protein-1. Biol Reprod 2004;71:438–443.
   PubMedGoogle Scholar
• Simon C, Moreno C, Remohi J, Pellicer A. Molecular interactions between embryo and uterus in the adhesion phase of human implantation. Hum Reprod 1998;13(Suppl 3):219–232.
   Google Scholar
• Kauma SW. Cytokines in implantation. J Reprod Fertil Suppl 2000;55:31–42.
   PubMedGoogle Scholar
• Kimber SJ. Molecular interactions at the maternal-embryonic interface during the early phase of implantation. Semin Reprod Med 2000;18:237–253.
   PubMedGoogle Scholar
• Osteen KG, Keller NR, Feltus FA, Melner MH. Paracrine regulation of matrix metalloproteinase expression in the normal human endometrium. Gynecol Obstet Invest 1999;48(Suppl 1):2–13.
   Google Scholar
• Yang ZM, Chen DB, Le SP, Harper MJK. Interleukin- la in the rabbit uterus during early pregnancy. Early Pregnancy 1995;1:201–205.
   Google Scholar
• Julian J, Chipuet-Ehrismann R, Erickson HP, Carson DD. Tenascin is induced at implantation sites in the mouse uterus and interferes with epithelial cell adhesion. Development 1994;120:661–671.
   PubMed Web of Science ®Google Scholar
• Kida H, Taga M, Minaguchi H, Hanazono M, Ohashi T, Sakakura T, Kusakabe M. The change in tenascin expression in mouse uterus during early pregnancy. J Assist Reprod Genet 1997;14:44–50.
   Google Scholar
• Slater M, Murphy CR, Barden JA. Tenascin, E-cadherin and P2X calcium channel receptor expression is increased during rat blastocyst implantation. Histochem J 2002;34: 13–19.
   Google Scholar
• Eliceiri BP, Cheresh DA. Adhesion events in angiogenesis. Curr Opin Cell Biol 2001;13:563–568.
   PubMed Web of Science ®Google Scholar
• Schoppet M, Chavakis T, Al-Fakhri N, Kanse SM, Preissner KT. Molecular interactions and functional interference between vitronectin and transforming growth factor-#. Lab Invest 2002;82:37–46.
   Google Scholar
• Whitelock JM, Murdoch AD, Iozzo RV, Underwood PA. The degradation of human endothelial cell-derived perlcan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin and heparanases. J Biol Chem 1996;271:10079–10086.
   PubMed Web of Science ®Google Scholar
• Noe V, Fingleton B, Jacobs K, Crawford HC, Vermeulen S, Steelant W, Bruyneel E, Matrisian LM, Mareel M. Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1. J Cell Sci 2000;114: 111–118.
   Google Scholar