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Volumn 25, Issue 10, 2004, Pages 810-819

Expression and localization of matrix metalloproteinases (MT1-MMP, MMP-2) and tissue inhibitor of metalloproteinase-2 (TIMP-2) during synepitheliochorial placentation of goats (Capra hircus)

Author keywords

[No Author keywords available]

Indexed keywords

GELATINASE A; INTERSTITIAL COLLAGENASE; MESSENGER RNA; TISSUE INHIBITOR OF METALLOPROTEINASE 2;

EID: 4644294433     PISSN: 01434004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.placenta.2004.03.007     Document Type: Article
Times cited : (16)

References (73)
  • 1
    • 0036203641 scopus 로고    scopus 로고
    • Human placental trophoblast as an in vitro model for tumor progression
    • Lala P.K. Lee B.P. Xu G. Charkraborty C. Human placental trophoblast as an in vitro model for tumor progression Can J Pharmacol 80 2002 142-149
    • (2002) Can. J. Pharmacol. , vol.80 , pp. 142-149
    • Lala, P.K.1    Lee, B.P.2    Xu, G.3    Charkraborty, C.4
  • 2
    • 0026935907 scopus 로고
    • Mechanisms of placental invasion of the uterus and their control
    • Graham C.H. Lala P.K. Mechanisms of placental invasion of the uterus and their control Biochem Cell Biol 70 1992 867-874
    • (1992) Biochem. Cell Biol. , vol.70 , pp. 867-874
    • Graham, C.H.1    Lala, P.K.2
  • 3
    • 0026590570 scopus 로고
    • Current topic: The synepitheliochorial placenta of ruminants: Binucleate cell fusions and hormone production
    • Wooding F.B.P. Current topic: the synepitheliochorial placenta of ruminants: binucleate cell fusions and hormone production Placenta 13 1992 101-113
    • (1992) Placenta , vol.13 , pp. 101-113
    • Wooding, F.B.P.1
  • 4
    • 0020210085 scopus 로고
    • The role of the binucleate cell in ruminant placental structure
    • Wooding F.B.P. The role of the binucleate cell in ruminant placental structure J Reprod Fertil 31 Suppl 1982 31-39
    • (1982) J. Reprod. Fertil. , vol.31 , Issue.SUPPL. , pp. 31-39
    • Wooding, F.B.P.1
  • 5
    • 0000584422 scopus 로고
    • Interspecies differences in the structure and function of trophoblast
    • Y. W. Loke, & A. Whyte (Eds.), Amsterdam: Elsevier
    • Steven D.H. Interspecies differences in the structure and function of trophoblast in: Loke Y.W. Whyte A. eds. Biology of trophoblast 1983 111-136 Elsevier Amsterdam
    • (1983) Biology of Trophoblast , pp. 111-136
    • Steven, D.H.1
  • 6
    • 0036729038 scopus 로고    scopus 로고
    • Establishment of feeder-independent cloned caprine trophoblast cell line which expresses placental lactogen and interferon tau
    • Miyazaki H. Imai M. Hirayama T. Saburi S. Tanaka M. Maruyama M. et al. Establishment of feeder-independent cloned caprine trophoblast cell line which expresses placental lactogen and interferon tau Placenta 23 2002 613-630
    • (2002) Placenta , vol.23 , pp. 613-630
    • Miyazaki, H.1    Imai, M.2    Hirayama, T.3    Saburi, S.4    Tanaka, M.5    Maruyama, M.6
  • 7
    • 0029896682 scopus 로고    scopus 로고
    • Expression and function of matrix metalloproteinases and their inhibitors at the maternal-embryonic boundary during mouse implantation
    • Alexander C.M. Hansell E.J. Beherendsten O. Flannery M.L. Kishnani N.S. Hawkes S.P. et al. Expression and function of matrix metalloproteinases and their inhibitors at the maternal-embryonic boundary during mouse implantation Development 122 1996 1723-1736
    • (1996) Development , vol.122 , pp. 1723-1736
    • Alexander, C.M.1    Hansell, E.J.2    Beherendsten, O.3    Flannery, M.L.4    Kishnani, N.S.5    Hawkes, S.P.6
  • 8
    • 0031913575 scopus 로고    scopus 로고
    • Expression and localization of membrane type matrix metalloproteinase-1 (MT1-MMP) in trophoblast cells of cultured mouse blastocysts and ectoplacental cones
    • Tanaka S.S. Toyooka Y. Sato H. Seiki M. Tojo H. Tachi C. Expression and localization of membrane type matrix metalloproteinase-1 (MT1-MMP) in trophoblast cells of cultured mouse blastocysts and ectoplacental cones Placenta 19 1998 41-48
    • (1998) Placenta , vol.19 , pp. 41-48
    • Tanaka, S.S.1    Toyooka, Y.2    Sato, H.3    Seiki, M.4    Tojo, H.5    Tachi, C.6
  • 9
    • 0034973512 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase-2, -9, -14, and tissue inhibitors of metalloproteinase-1, -2, -3 in the endometrium and placenta of rhesus monkey (Macaca mulatta) during early pregnancy
    • Wang H. Li Q. Shao L. Zhu C. Expression of matrix metalloproteinase-2, -9, -14, and tissue inhibitors of metalloproteinase-1, -2, -3 in the endometrium and placenta of rhesus monkey (Macaca mulatta) during early pregnancy Biol Reprod 65 2001 31-40
    • (2001) Biol. Reprod. , vol.65 , pp. 31-40
    • Wang, H.1    Li, Q.2    Shao, L.3    Zhu, C.4
  • 10
    • 0026714495 scopus 로고
    • Simultaneous expression of 70 kilodalton type IV collagenase and type IV collagen al (IV) chain genes by cells of early human placenta and gestational endometrium
    • Autio-Harmainen H. Hurskainen T. Niskasaari K. Hoyhtya M. Tryggavason K. Simultaneous expression of 70 kilodalton type IV collagenase and type IV collagen al (IV) chain genes by cells of early human placenta and gestational endometrium Lab Invest 67 1992 191-200
    • (1992) Lab. Invest. , vol.67 , pp. 191-200
    • Autio-Harmainen, H.1    Hurskainen, T.2    Niskasaari, K.3    Hoyhtya, M.4    Tryggavason, K.5
  • 11
    • 0028180451 scopus 로고
    • Interleukin-1 beta regulates human cytotrophoblast metalloproteinase activity and invasion in vitro
    • Librach C.L. Feigenbaum S.L. Bass K.E. Cui T.Y. Verastas N. Sadovsky Y. et al. Interleukin-1 beta regulates human cytotrophoblast metalloproteinase activity and invasion in vitro J Biol Chem 269 1994 17125-17131
    • (1994) J. Biol. Chem. , vol.269 , pp. 17125-17131
    • Librach, C.L.1    Feigenbaum, S.L.2    Bass, K.E.3    Cui, T.Y.4    Verastas, N.5    Sadovsky, Y.6
  • 12
    • 0031196116 scopus 로고    scopus 로고
    • Co-coordinated expression of MMP-2 and its putative activator, MT1-MMP, in human placentation
    • Bjorn S.F. Hastrup N. Lund L.R. Co-coordinated expression of MMP-2 and its putative activator, MT1-MMP, in human placentation Mol Hum Reprod 3 1997 713-723
    • (1997) Mol. Hum. Reprod. , vol.3 , pp. 713-723
    • Bjorn, S.F.1    Hastrup, N.2    Lund, L.R.3
  • 13
    • 0031868361 scopus 로고    scopus 로고
    • Expression of metalloproteinases and their inhibitors in human trophoblast continuous cell lines
    • Morgan M. Kniss D. McDonell S. Expression of metalloproteinases and their inhibitors in human trophoblast continuous cell lines Exp Cell Res 242 1998 18-26
    • (1998) Exp. Cell Res. , vol.242 , pp. 18-26
    • Morgan, M.1    Kniss, D.2    McDonell, S.3
  • 14
    • 0034968617 scopus 로고    scopus 로고
    • Effects of matrix proteins on the expression of matrix metaloproteinase-2, -9, and -14 and tissue inhibitors of metalloproteinases in human cytotrophoblast cells during the first trimester
    • Xu P. Wang Y. Piao Y. Bai S. Xiao Z. Jia Y. et al. Effects of matrix proteins on the expression of matrix metaloproteinase-2, -9, and -14 and tissue inhibitors of metalloproteinases in human cytotrophoblast cells during the first trimester Biol Reprod 65 2001 240-246
    • (2001) Biol. Reprod. , vol.65 , pp. 240-246
    • Xu, P.1    Wang, Y.2    Piao, Y.3    Bai, S.4    Xiao, Z.5    Jia, Y.6
  • 15
    • 0029188488 scopus 로고
    • Matrix metalloproteinases and their tissue inhibitors at the ovine trophoblast-uterine interface
    • Salamonsen L.A. Nagase H. Woolley D.E. Matrix metalloproteinases and their tissue inhibitors at the ovine trophoblast-uterine interface J Reprod Fertil (Suppl) 49 1995 29-37
    • (1995) J. Reprod. Fertil. , vol.49 , Issue.SUPPL. , pp. 29-37
    • Salamonsen, L.A.1    Nagase, H.2    Woolley, D.E.3
  • 16
    • 0004889285 scopus 로고
    • Expression of matrix metalloproteinase-11 genes in placentae and uteri of Shiba goats (Capra hircus)
    • Hara T. Tanaka S. Sato H. Seiki M. Koi H. Suenaga A. et al. Expression of matrix metalloproteinase-11 genes in placentae and uteri of Shiba goats (Capra hircus) J Reprod Dev 41 1995 29-39
    • (1995) J. Reprod. Dev. , vol.41 , pp. 29-39
    • Hara, T.1    Tanaka, S.2    Sato, H.3    Seiki, M.4    Koi, H.5    Suenaga, A.6
  • 17
    • 0031656910 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 and -9 and tissue inhibitor of metalloproteinase-1 of the sheep placenta during the last third of gestation
    • Vagnoni K.E. Zheng J. Magness R.R. Matrix metalloproteinase-2 and -9 and tissue inhibitor of metalloproteinase-1 of the sheep placenta during the last third of gestation Placenta 19 1998 447-455
    • (1998) Placenta , vol.19 , pp. 447-455
    • Vagnoni, K.E.1    Zheng, J.2    Magness, R.R.3
  • 18
    • 0033975217 scopus 로고    scopus 로고
    • Involvement of matrix metalloproteinases 2 and 9, tissue inhibitor of metalloproteinases and apoptosis in tissue remodeling in the sheep placenta
    • Riley S.C. Webb C.J. Leask R. McCaig F.M. Howe D.C. Involvement of matrix metalloproteinases 2 and 9, tissue inhibitor of metalloproteinases and apoptosis in tissue remodeling in the sheep placenta J Reprod Fertil 118 2000 19-27
    • (2000) J. Reprod. Fertil. , vol.118 , pp. 19-27
    • Riley, S.C.1    Webb, C.J.2    Leask, R.3    McCaig, F.M.4    Howe, D.C.5
  • 19
    • 0035193123 scopus 로고    scopus 로고
    • Expression of membrane-type 1 matrix metalloproteinase (MT1-MMP) mRNA in trophoblast and endometrial epithelial cell populations of the synepitheliochorial placenta of goats (Capra hircus)
    • Uekita T. Tanaka S.S. Sato H. Seiki M. Tojo H. Tachi C. Expression of membrane-type 1 matrix metalloproteinase (MT1-MMP) mRNA in trophoblast and endometrial epithelial cell populations of the synepitheliochorial placenta of goats (Capra hircus) Arch Histol Cytol 64 2001 411-424
    • (2001) Arch. Histol. Cytol. , vol.64 , pp. 411-424
    • Uekita, T.1    Tanaka, S.S.2    Sato, H.3    Seiki, M.4    Tojo, H.5    Tachi, C.6
  • 20
    • 0037378662 scopus 로고    scopus 로고
    • Differential regulation of the expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases by cytokines and growth factors in bovine endometrial stromal cells and trophoblast cell line BT-1 in vitro
    • Hirata M. Sato T. Tsumagari M. Shimada A. Nakano H. Hashizume K. et al. Differential regulation of the expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases by cytokines and growth factors in bovine endometrial stromal cells and trophoblast cell line BT-1 in vitro Biol Reprod 68 2003 1276-1281
    • (2003) Biol. Reprod. , vol.68 , pp. 1276-1281
    • Hirata, M.1    Sato, T.2    Tsumagari, M.3    Shimada, A.4    Nakano, H.5    Hashizume, K.6
  • 21
    • 0025230509 scopus 로고
    • Metalloproteinases and their inhibitors in tissue remodeling
    • Matrisian L.M. Metalloproteinases and their inhibitors in tissue remodeling Trends Genet 6 1990 121-125
    • (1990) Trends Genet. , vol.6 , pp. 121-125
    • Matrisian, L.M.1
  • 22
    • 0026027556 scopus 로고
    • Cancer metastasis and angiogenesis: An imbalance of positive and negative regulation
    • Liotta L.A. Steeg P.A. Stetler-Stevenson E.G. Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation Cell 64 1991 327-336
    • (1991) Cell , vol.64 , pp. 327-336
    • Liotta, L.A.1    Steeg, P.A.2    Stetler-Stevenson, E.G.3
  • 23
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner J.F. Jr. Matrix metalloproteinases and their inhibitors in connective tissue remodeling FASEB 5 1991 2145-2153
    • (1991) FASEB , vol.5 , pp. 2145-2153
    • Woessner Jr., J.F.1
  • 26
    • 0032830646 scopus 로고    scopus 로고
    • Secretion of tissue inhibitors of matrix metalloproteinases by human fetal membranes, decidua, and placenta at parturition
    • Riley S.C. Leask R. Denison F.C. Wisely K. Calder A.A. Howe D.C. Secretion of tissue inhibitors of matrix metalloproteinases by human fetal membranes, decidua, and placenta at parturition J Endocrinol 162 1999 351-359
    • (1999) J. Endocrinol. , vol.162 , pp. 351-359
    • Riley, S.C.1    Leask, R.2    Denison, F.C.3    Wisely, K.4    Calder, A.A.5    Howe, D.C.6
  • 27
    • 0028900295 scopus 로고
    • 92-kDa type IV collagenase and TIMP-3, but not 72-kDa type IV collagenase or TIMP-1 or TIMP-2, are highly expressed during mouse embryo implantation
    • Reponen P. Leive I. Sahlberg C. Apte S.S. Olsen B.R. Thesleff I. et al. 92-kDa type IV collagenase and TIMP-3, but not 72-kDa type IV collagenase or TIMP-1 or TIMP-2, are highly expressed during mouse embryo implantation Dev Dyn 202 1995 388-396
    • (1995) Dev. Dyn. , vol.202 , pp. 388-396
    • Reponen, P.1    Leive, I.2    Sahlberg, C.3    Apte, S.S.4    Olsen, B.R.5    Thesleff, I.6
  • 28
    • 0030800833 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in the mouse uterus during peri-implantation period
    • Das S.K. Yano S. Wang J. Edwards D.R. Nagase H. Dey S.K. Expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in the mouse uterus during peri-implantation period Dev Genet 21 1997 44-54
    • (1997) Dev. Genet. , vol.21 , pp. 44-54
    • Das, S.K.1    Yano, S.2    Wang, J.3    Edwards, D.R.4    Nagase, H.5    Dey, S.K.6
  • 29
    • 0035031663 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 and tissue inhibitor of metaloproteinase-3 are key regulators of extracellular matrix degradation by mouse embryos
    • Whiteside E.J. Jackson M.M. Herington A.C. Edwards D.R. Harvey M.B. Matrix metalloproteinase-9 and tissue inhibitor of metaloproteinase-3 are key regulators of extracellular matrix degradation by mouse embryos Biol Reprod 64 2001 1331-1337
    • (2001) Biol. Reprod. , vol.64 , pp. 1331-1337
    • Whiteside, E.J.1    Jackson, M.M.2    Herington, A.C.3    Edwards, D.R.4    Harvey, M.B.5
  • 31
    • 0024601013 scopus 로고
    • Cleavage of type VII collagen by interstitial collagenase and type IV collagenase (gelatinase) derived from human skin
    • Seltzer J.L. Eisen A.Z. Bauer E.A. Morris N.P. Glaville R.W. Cleavage of type VII collagen by interstitial collagenase and type IV collagenase (gelatinase) derived from human skin J Biol Chem 264 1989 3822-3826
    • (1989) J. Biol. Chem. , vol.264 , pp. 3822-3826
    • Seltzer, J.L.1    Eisen, A.Z.2    Bauer, E.A.3    Morris, N.P.4    Glaville, R.W.5
  • 32
    • 0027049396 scopus 로고
    • Progesterone regulates the activity of collagenase and related gelatinase A and B in human endometrial explants
    • Marbaix E. Donnez J. Courtoy P.J. Eeckhout Y. Progesterone regulates the activity of collagenase and related gelatinase A and B in human endometrial explants Proc Natl Acad Sci U S A 89 1992 11789-11793
    • (1992) Proc. Natl. Acad. Sci. U S A , vol.89 , pp. 11789-11793
    • Marbaix, E.1    Donnez, J.2    Courtoy, P.J.3    Eeckhout, Y.4
  • 33
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasion tumor cells
    • Sato H. Takino T. Okada Y. Cao J. Shinagawa A. Yamamoto E. et al. A matrix metalloproteinase expressed on the surface of invasion tumor cells Nature 370 1994 61-65
    • (1994) Nature , vol.370 , pp. 61-65
    • Sato, H.1    Takino, T.2    Okada, Y.3    Cao, J.4    Shinagawa, A.5    Yamamoto, E.6
  • 34
    • 0033003771 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases
    • Seiki M. Membrane-type matrix metalloproteinases APMIS 107 1999 137-143
    • (1999) APMIS , vol.107 , pp. 137-143
    • Seiki, M.1
  • 38
    • 0032544524 scopus 로고    scopus 로고
    • Plasma membrane-bound tissue inhibitor of metalloproteinases (TIMP)-2 specifically inhibits matrix metalloproteinase 2 (gelatinase A) activated on the cell surface
    • Itoh Y. Ito A. Iwata K. Tanzawa K. Mori Y. Nagase H. Plasma membrane-bound tissue inhibitor of metalloproteinases (TIMP)-2 specifically inhibits matrix metalloproteinase 2 (gelatinase A) activated on the cell surface J Biol Chem 273 1998 24360-24367
    • (1998) J. Biol. Chem. , vol.273 , pp. 24360-24367
    • Itoh, Y.1    Ito, A.2    Iwata, K.3    Tanzawa, K.4    Mori, Y.5    Nagase, H.6
  • 39
    • 0030756920 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases (MT-MMPs) in cell invasion
    • Sato H. Okada Y. Seiki M. Membrane-type matrix metalloproteinases (MT-MMPs) in cell invasion Thromb Haemost 78 1997 497-500
    • (1997) Thromb. Haemost. , vol.78 , pp. 497-500
    • Sato, H.1    Okada, Y.2    Seiki, M.3
  • 40
    • 0032582686 scopus 로고    scopus 로고
    • Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysis
    • Hiraoka N. Allen E. Apel I.J. Gyetko M.R. Weiss S.J. Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysis Cell 95 1998 365-377
    • (1998) Cell , vol.95 , pp. 365-377
    • Hiraoka, N.1    Allen, E.2    Apel, I.J.3    Gyetko, M.R.4    Weiss, S.J.5
  • 41
    • 0035947766 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration
    • Kajita M. Itoh Y. Chiba T. Mori H. Okada A. Kinoh H. et al. Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration J Cell Biol 153 2001 893-904
    • (2001) J. Cell Biol. , vol.153 , pp. 893-904
    • Kajita, M.1    Itoh, Y.2    Chiba, T.3    Mori, H.4    Okada, A.5    Kinoh, H.6
  • 42
    • 0035945354 scopus 로고    scopus 로고
    • Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity
    • Uekita T. Itoh Y. Yana I. Ohno H. Seiki M. Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity J Cell Biol 155 2001 1345-1356
    • (2001) J. Cell Biol. , vol.155 , pp. 1345-1356
    • Uekita, T.1    Itoh, Y.2    Yana, I.3    Ohno, H.4    Seiki, M.5
  • 44
    • 0032568932 scopus 로고    scopus 로고
    • TIMP-2 promotes activation of progelatinase A by membrane-type 1 matrix metalloproteinase immobilized on agarose beads
    • Kinoshita T. Sato H. Okada A. Ohuchi E. Imai K. Okada Y. et al. TIMP-2 promotes activation of progelatinase A by membrane-type 1 matrix metalloproteinase immobilized on agarose beads J Biol Chem 273 1998 16098-16103
    • (1998) J. Biol. Chem. , vol.273 , pp. 16098-16103
    • Kinoshita, T.1    Sato, H.2    Okada, A.3    Ohuchi, E.4    Imai, K.5    Okada, Y.6
  • 45
    • 0031984868 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP)
    • Zucker S. Drews M. Conner C. Foda H.D. DeClerck Y.A. Langley K.E. et al. Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP) J Biol Chem 273 1998 1216-1222
    • (1998) J. Biol. Chem. , vol.273 , pp. 1216-1222
    • Zucker, S.1    Drews, M.2    Conner, C.3    Foda, H.D.4    DeClerck, Y.A.5    Langley, K.E.6
  • 46
    • 0038266866 scopus 로고    scopus 로고
    • Sequence motifs of tissue inhibitor of metalloproteinases 2 (TIMP-2) determining progelatinase A (proMMP-2) binding and activation by membrane-type metalloproteinase 1 (MT1-MMP)
    • Worley J.R. Thompkins P.B. Lee M.H. Hutton M. Soloway P. Edwards D.R. et al. Sequence motifs of tissue inhibitor of metalloproteinases 2 (TIMP-2) determining progelatinase A (proMMP-2) binding and activation by membrane-type metalloproteinase 1 (MT1-MMP) Biochem J 372 2003 799-809
    • (2003) Biochem. J. , vol.372 , pp. 799-809
    • Worley, J.R.1    Thompkins, P.B.2    Lee, M.H.3    Hutton, M.4    Soloway, P.5    Edwards, D.R.6
  • 47
    • 0141790968 scopus 로고    scopus 로고
    • TIMP-2 (tissue inhibitor of metalloproteinase-2) regulates MMP-2 (matrix metalloproteinase-2) activity in the extracellular environment after pro-MMP-2 activation by MT1 (membrane type 1)-MMP
    • Bernardo M.M. Fridman R. TIMP-2 (tissue inhibitor of metalloproteinase-2) regulates MMP-2 (matrix metalloproteinase-2) activity in the extracellular environment after pro-MMP-2 activation by MT1 (membrane type 1)-MMP Biochem J 374 2003 739-745
    • (2003) Biochem. J. , vol.374 , pp. 739-745
    • Bernardo, M.M.1    Fridman, R.2
  • 48
    • 0037188508 scopus 로고    scopus 로고
    • Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2
    • Morgunova E. Tuuttila A. Bergmann U. Tryggvason K. Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2 Proc Natl Acad Sci U S A 99 2002 7414-7419
    • (2002) Proc. Natl. Acad. Sci. U S A , vol.99 , pp. 7414-7419
    • Morgunova, E.1    Tuuttila, A.2    Bergmann, U.3    Tryggvason, K.4
  • 49
    • 0032161747 scopus 로고    scopus 로고
    • Cell surface activation of progelatinase A (proMMP-2) and cell migration
    • Nagase H. Cell surface activation of progelatinase A (proMMP-2) and cell migration Cell Res 8 1998 179-186
    • (1998) Cell Res. , vol.8 , pp. 179-186
    • Nagase, H.1
  • 50
    • 0031985228 scopus 로고    scopus 로고
    • The TIMP-2 membrane type I metalloproteinase receptor regulates the concentration and efficient activation of progelatinase A: A kinetic study
    • Butler G.S. Butler M.J. Atkinson S.J. Will H. Tamura T. van Weatrum S.S. The TIMP-2 membrane type I metalloproteinase receptor regulates the concentration and efficient activation of progelatinase A: a kinetic study J Biol Chem 273 1998 871-880
    • (1998) J. Biol. Chem. , vol.273 , pp. 871-880
    • Butler, G.S.1    Butler, M.J.2    Atkinson, S.J.3    Will, H.4    Tamura, T.5    van Weatrum, S.S.6
  • 51
    • 0028936798 scopus 로고
    • Proteinase expression in early mouse embryos is regulated by leukemia inhibitory factor and epidermal growth factor
    • Harvey M.B. Leco K.J. Arcellana-Panlilio M.Y. Zhang X. Edwards D.R. Schultz G.A. Proteinase expression in early mouse embryos is regulated by leukemia inhibitory factor and epidermal growth factor Development 121 1995 1005-1014
    • (1995) Development , vol.121 , pp. 1005-1014
    • Harvey, M.B.1    Leco, K.J.2    Arcellana-Panlilio, M.Y.3    Zhang, X.4    Edwards, D.R.5    Schultz, G.A.6
  • 52
    • 0032952938 scopus 로고    scopus 로고
    • Gelatinases A and B and tissue inhibitors of metaloproteinases 1, 2, and 3 during in vivo and in vitro decidualization of rat endometrial stromal cells
    • Nuttall R.K. Kennedy T.G. Gelatinases A and B and tissue inhibitors of metaloproteinases 1, 2, and 3 during in vivo and in vitro decidualization of rat endometrial stromal cells Biol Reprod 60 1999 471-478
    • (1999) Biol. Reprod. , vol.60 , pp. 471-478
    • Nuttall, R.K.1    Kennedy, T.G.2
  • 53
    • 0034464218 scopus 로고    scopus 로고
    • Epidermal growth factor and basic fibroblast growth factor increase the production of matrix metalloproteinases during in vitro decidualization of rat endometrial stromal cells
    • Nuttall R.K. Kennedy T.G. Epidermal growth factor and basic fibroblast growth factor increase the production of matrix metalloproteinases during in vitro decidualization of rat endometrial stromal cells Endocrinology 141 2000 629-636
    • (2000) Endocrinology , vol.141 , pp. 629-636
    • Nuttall, R.K.1    Kennedy, T.G.2
  • 54
    • 0031913920 scopus 로고    scopus 로고
    • Immunohistochemistry of matrix metalloproteinases (MMP), their substrates, and their inhibitors (TIMP) during trophoblast invasion in the human placenta
    • Huppertz B. Kertshanska S. Demir A.Y. Frank H.G. Kaufmann P. Immunohistochemistry of matrix metalloproteinases (MMP), their substrates, and their inhibitors (TIMP) during trophoblast invasion in the human placenta Cell Tissue Res 291 1998 133-148
    • (1998) Cell Tissue Res. , vol.291 , pp. 133-148
    • Huppertz, B.1    Kertshanska, S.2    Demir, A.Y.3    Frank, H.G.4    Kaufmann, P.5
  • 55
    • 0034968617 scopus 로고    scopus 로고
    • Effects of matrix proteins on the expression of matrix metalloproteinase-2, -9 and -14 and tissue inhibitors of metalloproteinases in human cytotrophoblast cells during the first trimester
    • Ping X. Wang Y.I. Piao Y.S. Bai S.X. Xiao Z.J. Jia Y.I. et al. Effects of matrix proteins on the expression of matrix metalloproteinase-2, -9 and -14 and tissue inhibitors of metalloproteinases in human cytotrophoblast cells during the f irst trimester Biol Reprod 65 2001 240-246
    • (2001) Biol. Reprod. , vol.65 , pp. 240-246
    • Ping, X.1    Wang, Y.I.2    Piao, Y.S.3    Bai, S.X.4    Xiao, Z.J.5    Jia, Y.I.6
  • 56
    • 0017378294 scopus 로고
    • Biological characteristics of miniature "Shiba" goats
    • Kano Y. Sawasaki T. Oyama T. Biological characteristics of miniature "Shiba" goats Exp Anim 26 1977 239-246
    • (1977) Exp. Anim. , vol.26 , pp. 239-246
    • Kano, Y.1    Sawasaki, T.2    Oyama, T.3
  • 57
    • 0000692805 scopus 로고
    • Extraction and purification of RNA
    • 2nd ed. New York: Cold Spring Harbor
    • Sambrook J. Fritsch E.E. Maniatis T. Extraction and purification of RNA in: Molecular cloning 2nd ed. 1989 7.3-7.32 Cold Spring Harbor New York
    • (1989) Molecular Cloning , pp. 73-732
    • Sambrook, J.1    Fritsch, E.E.2    Maniatis, T.3
  • 58
    • 0032168205 scopus 로고    scopus 로고
    • Proteolytic processing of membrane-type-1 matrix metalloproteinase is associated with gelatinase A activation at the cell surface
    • Lehti K. Lohi J. Valtanen H. Keski-Oja J. Proteolytic processing of membrane-type-1 matrix metalloproteinase is associated with gelatinase A activation at the cell surface Biochem J 334 1998 345-353
    • (1998) Biochem. J. , vol.334 , pp. 345-353
    • Lehti, K.1    Lohi, J.2    Valtanen, H.3    Keski-Oja, J.4
  • 59
    • 4644250286 scopus 로고    scopus 로고
    • Dynamics of ßig-h3 mRNA expression during pregnancy in the uterus and the placenta of the mouse: A possible regulatory factor for trophoblastic invasion
    • Uekita T. Kim Y.J. Yamanouchi K. Tojo H. Tachi C. Dynamics of ßig-h3 mRNA expression during pregnancy in the uterus and the placenta of the mouse: a possible regulatory factor for trophoblastic invasion J Reprod Dev 49 2003 243-252
    • (2003) J. Reprod. Dev. , vol.49 , pp. 243-252
    • Uekita, T.1    Kim, Y.J.2    Yamanouchi, K.3    Tojo, H.4    Tachi, C.5
  • 60
    • 0021058806 scopus 로고
    • Collagen degradation in the mouse uterus during postpartum involution: Extracellular pathway
    • Shimizu K. Maekawa K. Collagen degradation in the mouse uterus during postpartum involution: extracellular pathway Acta Anat 117 1983 257-260
    • (1983) Acta Anat. , vol.117 , pp. 257-260
    • Shimizu, K.1    Maekawa, K.2
  • 61
    • 0025889774 scopus 로고
    • Cyclic adenosine 3′, 5′-monophosphate suppresses interleukin 1-induced synthesis of matrix metalloproteinases but not of tissue inhibitor of metalloproteinases in human uterine cervical fibroblasts
    • Takahashi S. Ito A. Nagino M. Mori Y. Xie B. Nagase H. Cyclic adenosine 3′, 5′-monophosphate suppresses interleukin 1-induced synthesis of matrix metalloproteinases but not of tissue inhibitor of metalloproteinases in human uterine cervical fibroblasts J Biol Chem 266 1991 19894-19899
    • (1991) J. Biol. Chem. , vol.266 , pp. 19894-19899
    • Takahashi, S.1    Ito, A.2    Nagino, M.3    Mori, Y.4    Xie, B.5    Nagase, H.6
  • 62
    • 0027934326 scopus 로고
    • Matrix metalloproteinase production by cultured human endometrial stromal cells: Identification of interstitial collagenase, gelatinase-A, gelatinase-B, and stromelysin-1 and their differential regulation by interleukin-1 alpha and tumor necrosis factor-alpha
    • Rawdanowicz T.J. Hampton A.L. Nagase H. Woolley D.E. Salamonsen L.A. Matrix metalloproteinase production by cultured human endometrial stromal cells: identification of interstitial collagenase, gelatinase-A, gelatinase-B, and stromelysin-1 and their differential regulation by interleukin-1 alpha and tumor necrosis factor-alpha J Clin Endocrinol Metab 79 1994 530-536
    • (1994) J. Clin. Endocrinol. Metab. , vol.79 , pp. 530-536
    • Rawdanowicz, T.J.1    Hampton, A.L.2    Nagase, H.3    Woolley, D.E.4    Salamonsen, L.A.5
  • 63
    • 0037259079 scopus 로고    scopus 로고
    • Matrix metalloproteinases-2 and -9 are secreted from human fibroblasts
    • Kobayashi T. Hattori S. Shinkai H. Matrix metalloproteinases-2 and -9 are secreted from human fibroblasts Acta Derm Venereol 83 2003 105-107
    • (2003) Acta Derm. Venereol. , vol.83 , pp. 105-107
    • Kobayashi, T.1    Hattori, S.2    Shinkai, H.3
  • 65
    • 0026035032 scopus 로고
    • Cellular changes in the peripartum bovine fetal placenta related to placental separation
    • Gross T.S. Williams W.F. Russek-Cohen Cellular changes in the peripartum bovine fetal placenta related to placental separation Placenta 12 1991 27-35
    • (1991) Placenta , vol.12 , pp. 27-35
    • Gross, T.S.1    Williams, W.F.2    Russek-Cohen, A.3
  • 66
    • 0023696675 scopus 로고
    • Inhibition by human recombinant tissue inhibitor of metalloproteinases of human amnion invasion and lung colonization by murine B16-F10 melanoma cells
    • Schultz R.M. Silberman S. Persky B. Bajkowski A.S. Carmichael D.F. Inhibition by human recombinant tissue inhibitor of metalloproteinases of human amnion invasion and lung colonization by murine B16-F10 melanoma cells Cancer Res 48 1988 5539-5545
    • (1988) Cancer Res. , vol.48 , pp. 5539-5545
    • Schultz, R.M.1    Silberman, S.2    Persky, B.3    Bajkowski, A.S.4    Carmichael, D.F.5
  • 67
    • 0028651852 scopus 로고
    • Clinical trials of a low molecular weight matrix metalloproteinase inhibitor in cancer
    • Brown P.D. Clinical trials of a low molecular weight matrix metalloproteinase inhibitor in cancer Ann N Y Acad Sci 732 1994 217-221
    • (1994) Ann. N Y Acad. Sci. , vol.732 , pp. 217-221
    • Brown, P.D.1
  • 68
    • 0029188425 scopus 로고
    • Matrix metalloproteinase inhibitors: A novel class of anticancer agents
    • Brown P.D. Matrix metalloproteinase inhibitors: a novel class of anticancer agents Adv Enzyme Regul 35 1995 293-301
    • (1995) Adv. Enzyme Regul. , vol.35 , pp. 293-301
    • Brown, P.D.1
  • 69
    • 0033034041 scopus 로고    scopus 로고
    • Clinical studies with matrix metalloproteinase inhibitors
    • Brown P.D. Clinical studies with matrix metalloproteinase inhibitors APMIS 107 1999 174-180
    • (1999) APMIS , vol.107 , pp. 174-180
    • Brown, P.D.1
  • 70
    • 0029103339 scopus 로고
    • Expression of membrane-type matrix metalloproteinase in human gastric carcinomas
    • Nomura H. Sato H. Seiki M. Mai M. Okada Y. Expression of membrane-type matrix metalloproteinase in human gastric carcinomas Cancer Res 55 1995 3263-3266
    • (1995) Cancer Res. , vol.55 , pp. 3263-3266
    • Nomura, H.1    Sato, H.2    Seiki, M.3    Mai, M.4    Okada, Y.5
  • 71
    • 9044246674 scopus 로고    scopus 로고
    • Differential expression of membrane-type matrix metalloproteinase and its correlation with gelatinase A activation in human malignant brain tumors in vivo and in vitro
    • Yamamoto M. Mohanam S. Sawaya R. Fuller G.N. Seiki M. Sato H. Differential expression of membrane-type matrix metalloproteinase and its correlation with gelatinase A activation in human malignant brain tumors in vivo and in vitro Cancer Res 56 1996 384-392
    • (1996) Cancer Res. , vol.56 , pp. 384-392
    • Yamamoto, M.1    Mohanam, S.2    Sawaya, R.3    Fuller, G.N.4    Seiki, M.5    Sato, H.6
  • 72
    • 0032959030 scopus 로고    scopus 로고
    • Expression and tissue localization of membrane-type 1, 2, and 3 matrix metalloproteinase in human astrocytic tumors
    • Nakada M. Nakamura H. Ikeda E. Fujimoto N. Yamashita J. Sato H. Expression and tissue localization of membrane-type 1, 2, and 3 matrix metalloproteinase in human astrocytic tumors Am J Pathol 154 1999 417-428
    • (1999) Am. J. Pathol. , vol.154 , pp. 417-428
    • Nakada, M.1    Nakamura, H.2    Ikeda, E.3    Fujimoto, N.4    Yamashita, J.5    Sato, H.6
  • 73
    • 0036582737 scopus 로고    scopus 로고
    • Recent advances in the regulation of matrix metalloproteinase 2 activation: From basic research to clinical implication
    • Yoshizaki T. Sato H. Furukawa M. Recent advances in the regulation of matrix metalloproteinase 2 activation: from basic research to clinical implication Oncol Rep 9 2002 607-611
    • (2002) Oncol. Rep. , vol.9 , pp. 607-611
    • Yoshizaki, T.1    Sato, H.2    Furukawa, M.3


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