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Volumn 4, Issue , 2006, Pages

Coordinated elevation of membrane type 1-matrix metalloproteinase and matrix metalloproteinase-2 expression in rat uterus during postpartum involution

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; COLLAGEN TYPE 1; GELATINASE A; GELATINASE B; INTERSTITIAL COLLAGENASE; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 2;

EID: 33747165047     PISSN: 14777827     EISSN: 14777827     Source Type: Journal    
DOI: 10.1186/1477-7827-4-32     Document Type: Article
Times cited : (26)

References (39)
  • 1
    • 0025847582 scopus 로고
    • Matrix metalloproteinase and their inhibitors in connective tissue remodeling
    • Woessner JF Jr: Matrix metalloproteinase and their inhibitors in connective tissue remodeling. FASEB J 1991, 5(8):2145-2154.
    • (1991) FASEB J , vol.5 , Issue.8 , pp. 2145-2154
    • Woessner Jr., J.F.1
  • 2
    • 0026896029 scopus 로고
    • The matrix-degrading metalloproteinases
    • Matrisian LM: The matrix-degrading metalloproteinases. Bioessays 1992, 14(7):455-463.
    • (1992) Bioessays , vol.14 , Issue.7 , pp. 455-463
    • Matrisian, L.M.1
  • 3
    • 0027197860 scopus 로고
    • Demonstration of 72-kDa and 92-kDa forms of type IV collagenase in human skin: Variable expression in various blistering diseases, induction during re-epithelialization, and decrease by topical glucocorticoids
    • Oikarinen A, Kylmefniemi M, Autio-Harmainen H, Autio P, Salo T: Demonstration of 72-kDa and 92-kDa forms of type IV collagenase in human skin: variable expression in various blistering diseases, induction during re-epithelialization, and decrease by topical glucocorticoids. J Invest Dermatol 1992, 101(2):205-210.
    • (1992) J Invest Dermatol , vol.101 , Issue.2 , pp. 205-210
    • Oikarinen, A.1    Kylmefniemi, M.2    Autio-Harmainen, H.3    Autio, P.4    Salo, T.5
  • 4
    • 0027133427 scopus 로고
    • Cell-matrix interactions modulate interstitial collagenase expression by human keratinocytes actively involved in wound healing
    • Saarialho-Kere UK, Kovacs SO, Pentland AP, Olerud JE, Welgus HG, Parks WC: Cell-matrix interactions modulate interstitial collagenase expression by human keratinocytes actively involved in wound healing. J Clin Invest 1993, 92(3):2858-2866.
    • (1993) J Clin Invest , vol.92 , Issue.3 , pp. 2858-2866
    • Saarialho-Kere, U.K.1    Kovacs, S.O.2    Pentland, A.P.3    Olerud, J.E.4    Welgus, H.G.5    Parks, W.C.6
  • 5
    • 0028138470 scopus 로고
    • Developmental regulation of the expression of 72 and 92 kd type IV collagenase in human trophoblast: A possible mechanism for control of trophoblast invasion
    • Shimonnvitz S, Hurwitz A, Dushnik M, Anteby E, Geva-Eldar T, Yagel S: Developmental regulation of the expression of 72 and 92 kd type IV collagenase in human trophoblast: a possible mechanism for control of trophoblast invasion. Am J Obstet Gynecol 1994, 171(3):832-838.
    • (1994) Am J Obstet Gynecol , vol.171 , Issue.3 , pp. 832-838
    • Shimonnvitz, S.1    Hurwitz, A.2    Dushnik, M.3    Anteby, E.4    Geva-Eldar, T.5    Yagel, S.6
  • 6
    • 0025610377 scopus 로고
    • Mechanisms of trophoblast invasiveness and their control: The role of protease inhibitors
    • Lala PK, Graham CH: Mechanisms of trophoblast invasiveness and their control: the role of protease inhibitors. Cancer Metastasis Rev 1991, 9(4):369-379.
    • (1991) Cancer Metastasis Rev , vol.9 , Issue.4 , pp. 369-379
    • Lala, P.K.1    Graham, C.H.2
  • 7
    • 0028302990 scopus 로고
    • Targeted expression of stromelysin-1 in mammary gland provides evidence for a role of proteinase in branching morphogenesis and the requirement for an intact basement membrane for tissue-specific gene expression
    • Sympson CJ, Talhouk RS, Alexander CM, Chin JR, Clift SM, Bissell MJ, Werb Z: Targeted expression of stromelysin-1 in mammary gland provides evidence for a role of proteinase in branching morphogenesis and the requirement for an intact basement membrane for tissue-specific gene expression. J Cell Biol 1994, 125(3):681-693.
    • (1994) J Cell Biol , vol.125 , Issue.3 , pp. 681-693
    • Sympson, C.J.1    Talhouk, R.S.2    Alexander, C.M.3    Chin, J.R.4    Clift, S.M.5    Bissell, M.J.6    Werb, Z.7
  • 8
    • 0028877124 scopus 로고
    • Matrix metalloproteinases are expressed during ductal and alveolar mammary morphogenesis, and misregulation of stromelysin-1 in transgenic mice induces unscheduled alveolar development
    • Witty JP, Wright J, Matrisian LM: Matrix metalloproteinases are expressed during ductal and alveolar mammary morphogenesis, and misregulation of stromelysin-1 in transgenic mice induces unscheduled alveolar development. Mol Biol Cell 1995, 6(10):1287-1303.
    • (1995) Mol Biol Cell , vol.6 , Issue.10 , pp. 1287-1303
    • Witty, J.P.1    Wright, J.2    Matrisian, L.M.3
  • 9
    • 0023716802 scopus 로고
    • Purification and properties of a small latent matrix metalloproteinase of the rat uterus
    • Woessner JF Jr, Taplin C: Purification and properties of a small latent matrix metalloproteinase of the rat uterus. J Biol Chem 1988, 263(3):16918-16925.
    • (1988) J Biol Chem , vol.263 , Issue.3 , pp. 16918-16925
    • Woessner Jr., J.F.1    Taplin, C.2
  • 10
    • 0019061828 scopus 로고
    • The extraction of a neutral metalloproteinase from the involuting rat uterus, and its action on cartilage proteoglycan
    • Sellers A, Woessner JF Jr: The extraction of a neutral metalloproteinase from the involuting rat uterus, and its action on cartilage proteoglycan. Biochem J 1980, 189(3):521-531.
    • (1980) Biochem J , vol.189 , Issue.3 , pp. 521-531
    • Sellers, A.1    Woessner Jr., J.F.2
  • 11
    • 0014955598 scopus 로고
    • Collagenase from rat uterus.: Isolation and partial characterization
    • Jeffrey JJ, Gross J: Collagenase from rat uterus.: Isolation and partial characterization. Biochemistry 1970, 9(2):268-273.
    • (1970) Biochemistry , vol.9 , Issue.2 , pp. 268-273
    • Jeffrey, J.J.1    Gross, J.2
  • 12
    • 9844236853 scopus 로고
    • Expression of extracellular matrix degrading proteinases and their inhibitors during involution of the mammary gland in CD-1 mice
    • Talhouk RS, Bissell MJ, Werb Z: Expression of extracellular matrix degrading proteinases and their inhibitors during involution of the mammary gland in CD-1 mice. J Cell Biol 1990, 111(1):14a.
    • (1990) J Cell Biol , vol.111 , Issue.1
    • Talhouk, R.S.1    Bissell, M.J.2    Werb, Z.3
  • 13
    • 0026768210 scopus 로고
    • Coordinated expression of extracellular matrix-degrading proteinases and their inhibitors regulates mammary epithelial function during involution
    • Talhouk RS, Bissell MJ, Werb Z: Coordinated expression of extracellular matrix-degrading proteinases and their inhibitors regulates mammary epithelial function during involution. J Cell Biol 1992, 118(5):1271-1282.
    • (1992) J Cell Biol , vol.118 , Issue.5 , pp. 1271-1282
    • Talhouk, R.S.1    Bissell, M.J.2    Werb, Z.3
  • 14
    • 84907131212 scopus 로고
    • Effect of castration on melloproteinase activities in the lateral, dorsal, and anterior lobes of the prostate
    • Wilson MJ, Norris H, Woodson M, Sinha AA: Effect of castration on melloproteinase activities in the lateral, dorsal, and anterior lobes of the prostate. Arch Androl 1995, 35(2):119-125.
    • (1995) Arch Androl , vol.35 , Issue.2 , pp. 119-125
    • Wilson, M.J.1    Norris, H.2    Woodson, M.3    Sinha, A.A.4
  • 16
    • 0027213803 scopus 로고
    • Coordinate induction and activation of metalloproteinase and ascorbate depletion in structural luteolysis
    • Endo T, Aten RF, Wang F, Behrman HR: Coordinate induction and activation of metalloproteinase and ascorbate depletion in structural luteolysis. Endocrinology 1993, 133(2):690-698.
    • (1993) Endocrinology , vol.133 , Issue.2 , pp. 690-698
    • Endo, T.1    Aten, R.F.2    Wang, F.3    Behrman, H.R.4
  • 17
    • 0032998203 scopus 로고    scopus 로고
    • Gonadotripin-releasing hormone agonist has the ability to induce increased matrix metalloproteinase (MMP)-2 and membrane type-1 MMP expression in corpora lutea, and structural luteolysis in rats
    • Goto T, Endo T, Henmi H, Kitajima Y, Kiya T, Nishikawa A, Manase K, Sato H, Kudo R: Gonadotripin-releasing hormone agonist has the ability to induce increased matrix metalloproteinase (MMP)-2 and membrane type-1 MMP expression in corpora lutea, and structural luteolysis in rats. J Endocrinol 1999:393-402.
    • (1999) J Endocrinol , pp. 393-402
    • Goto, T.1    Endo, T.2    Henmi, H.3    Kitajima, Y.4    Kiya, T.5    Nishikawa, A.6    Manase, K.7    Sato, H.8    Kudo, R.9
  • 19
    • 0001487419 scopus 로고
    • The time course and route of loss of collagen from the rat's uterus during post-partum involution
    • Harkness RD, Moralee BE: The time course and route of loss of collagen from the rat's uterus during post-partum involution. J Physiol 1956, 132(3):502-508.
    • (1956) J Physiol , vol.132 , Issue.3 , pp. 502-508
    • Harkness, R.D.1    Moralee, B.E.2
  • 20
    • 0029002420 scopus 로고
    • A targeted mutation at the known collagenase cleavage site in mouse type 11 collagen impairs tissue remodeling
    • Liu X, Wu H, Byrne M, Jeffrey J, Krane S, Jaenisch R: A targeted mutation at the known collagenase cleavage site in mouse type 11 collagen impairs tissue remodeling. J Cell Biol 1995, 130(1):227-237.
    • (1995) J Cell Biol , vol.130 , Issue.1 , pp. 227-237
    • Liu, X.1    Wu, H.2    Byrne, M.3    Jeffrey, J.4    Krane, S.5    Jaenisch, R.6
  • 21
    • 0033757033 scopus 로고    scopus 로고
    • Expression of various matrix proteases and Ets family transcriptional factors in ovarian cancer cell lines: Correlation to invasive potential
    • Nishikawa A, Iwasaki M, Akutagawa N, Manase K, Yamashita S, Endo T, Kudo R: Expression of various matrix proteases and Ets family transcriptional factors in ovarian cancer cell lines: Correlation to invasive potential. Gynecol Oncol 2000, 79(2):256-263.
    • (2000) Gynecol Oncol , vol.79 , Issue.2 , pp. 256-263
    • Nishikawa, A.1    Iwasaki, M.2    Akutagawa, N.3    Manase, K.4    Yamashita, S.5    Endo, T.6    Kudo, R.7
  • 22
    • 0025788863 scopus 로고
    • The primary structure of rat ribosomal protein L38
    • Kuwano Y, Olvera J, Wool IG: The primary structure of rat ribosomal protein L38. Biochem Biophys Res 1991, 175(2):551-555.
    • (1991) Biochem Biophys Res , vol.175 , Issue.2 , pp. 551-555
    • Kuwano, Y.1    Olvera, J.2    Wool, I.G.3
  • 23
    • 0021645876 scopus 로고
    • Prostaglandin F2αinhibits luteinizing hormone (LH)-induced increase in LH receptor binding to isolated rat luteal cells
    • Luborsky JL, Dorflinger LJ, Wright K, Berman HR: Prostaglandin F2αinhibits luteinizing hormone (LH)-induced increase in LH receptor binding to isolated rat luteal cells. Endocrinology 1984, 115:2210-2216.
    • (1984) Endocrinology , vol.115 , pp. 2210-2216
    • Luborsky, J.L.1    Dorflinger, L.J.2    Wright, K.3    Berman, H.R.4
  • 24
    • 0020539666 scopus 로고
    • Clearance of materials from breakdown of uterine collagen in mice during postpartum involution
    • Shimizu K, Furuya T, Takeo Y, Shirama K, Maekawa K: Clearance of materials from breakdown of uterine collagen in mice during postpartum involution. Acta Anat (Basel) 1983, 116(1):10-13.
    • (1983) Acta Anat (Basel) , vol.116 , Issue.1 , pp. 10-13
    • Shimizu, K.1    Furuya, T.2    Takeo, Y.3    Shirama, K.4    Maekawa, K.5
  • 25
    • 0036720845 scopus 로고    scopus 로고
    • Increased level of matrix metalloproteinases 2 and 9 in the ripening process of the human cervix
    • Stygar D, Wang H, Vladic YS, Ekman G, Eriksson H, Sahlin L: Increased level of matrix metalloproteinases 2 and 9 in the ripening process of the human cervix. Biol Reprod 2002, 67:889-94.
    • (2002) Biol Reprod , vol.67 , pp. 889-894
    • Stygar, D.1    Wang, H.2    Vladic, Y.S.3    Ekman, G.4    Eriksson, H.5    Sahlin, L.6
  • 26
    • 0036076296 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinases (type IV collagenases) and their inhibitors in the virgin, timed pregnant, and postpartum rat uterus and cervix by prostaglandin E(2)-cyclic adenosine monophosphate
    • Regulation of matrix metalloproteinases (type IV collagenases) and their inhibitors in the virgin, timed pregnant, and postpartum rat uterus and cervix by prostaglandin E(2)-cyclic adenosine monophosphate. Am J Obstet Gynecol 2002, 187(1):202-8.
    • (2002) Am J Obstet Gynecol , vol.187 , Issue.1 , pp. 202-208
  • 27
    • 0033967064 scopus 로고    scopus 로고
    • Up-regulation of matrix metalloproteinase-9 in human myometrium during labour: A cytokine-mediated process in uterine smooth muscle cells
    • Roh CR, Oh WJ, Yoon BK, Lee JH: Up-regulation of matrix metalloproteinase-9 in human myometrium during labour: a cytokine-mediated process in uterine smooth muscle cells. Mol Hum Reprod 2000, 6:96-102.
    • (2000) Mol Hum Reprod , vol.6 , pp. 96-102
    • Roh, C.R.1    Oh, W.J.2    Yoon, B.K.3    Lee, J.H.4
  • 28
    • 0021806687 scopus 로고
    • Increase in plasminogen activator in the involuting uterus of the postpartum rat
    • Shimada H, Okamura H, Espey LL, Mori T: Increase in plasminogen activator in the involuting uterus of the postpartum rat. J Endocrinol 1985, 104(2):295-298.
    • (1985) J Endocrinol , vol.104 , Issue.2 , pp. 295-298
    • Shimada, H.1    Okamura, H.2    Espey, L.L.3    Mori, T.4
  • 30
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumor cells
    • Sato H, Takino T, Okada Y, Cao J, Shinagawa A, Yamamoto E, Seiki M: A matrix metalloproteinase expressed on the surface of invasive tumor cells. Nature 1994, 370(6484):61-65.
    • (1994) Nature , vol.370 , Issue.6484 , pp. 61-65
    • Sato, H.1    Takino, T.2    Okada, Y.3    Cao, J.4    Shinagawa, A.5    Yamamoto, E.6    Seiki, M.7
  • 31
    • 0028940033 scopus 로고
    • Cloning of a human gene potentially encoding a novel matrix metalloproteinase having a C-terminal transmembrane domain
    • Takino T, Sato H, Yamamoto E, Seiki M: Cloning of a human gene potentially encoding a novel matrix metalloproteinase having a C-terminal transmembrane domain. Gene 1955, 155(2):293-298.
    • (1955) Gene , vol.155 , Issue.2 , pp. 293-298
    • Takino, T.1    Sato, H.2    Yamamoto, E.3    Seiki, M.4
  • 32
    • 0029891956 scopus 로고    scopus 로고
    • Processing of a precursor of 72-kilodalton type IV collagenase/gelatinase A by a recombinant membrane-type 1 matrix metalloproteinase
    • Kinoshita T, Sato H, Takino T, Itoh M, Akizawa T, Seiki M: Processing of a precursor of 72-kilodalton type IV collagenase/gelatinase A by a recombinant membrane-type 1 matrix metalloproteinase. Cancer Res 1996, 56(11):2535-2538.
    • (1996) Cancer Res , vol.56 , Issue.11 , pp. 2535-2538
    • Kinoshita, T.1    Sato, H.2    Takino, T.3    Itoh, M.4    Akizawa, T.5    Seiki, M.6
  • 33
    • 0025883916 scopus 로고
    • Efficient purification of TIMP-2 from culture medium conditioned by human hepatoma cell line, and its inhibitory effects on mettaloproteinase and in vitro tumor invasion
    • Umenishi F, Umeda M, Miyazaki K: Efficient purification of TIMP-2 from culture medium conditioned by human hepatoma cell line, and its inhibitory effects on mettaloproteinase and in vitro tumor invasion. J Cell Biol 1991, 110(2):189-195.
    • (1991) J Cell Biol , vol.110 , Issue.2 , pp. 189-195
    • Umenishi, F.1    Umeda, M.2    Miyazaki, K.3
  • 34
    • 0028947020 scopus 로고
    • Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type 1 collagen generating the specific 3/4- and 1/4-length fragments
    • Aimes RT, Quigley JP: Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type 1 collagen generating the specific 3/4- and 1/4-length fragments. J Biol Chem 1995, 270(11):5872-5876.
    • (1995) J Biol Chem , vol.270 , Issue.11 , pp. 5872-5876
    • Aimes, R.T.1    Quigley, J.P.2
  • 35
    • 0028126675 scopus 로고
    • Structure-function relationships in the tissue inhibitory effects of metalloproteinase
    • Willenbrock F, Murphy G: Structure-function relationships in the tissue inhibitory effects of metalloproteinase. Am J Respir Crit Care Med 1994, 150(6Pt2):S165-S170.
    • (1994) Am J Respir Crit Care Med , vol.150 , Issue.6 PART 2
    • Willenbrock, F.1    Murphy, G.2
  • 36
    • 0024394212 scopus 로고
    • Tissue inhibitor of metalloproteinase 2 (TIMP-2). A new member of the metalloproteinase inhibitor family
    • Stetler-Stevenson WG, Krutzsch HC, Liotta LA: Tissue inhibitor of metalloproteinase 2 (TIMP-2). A new member of the metalloproteinase inhibitor family. J Biol Chem 1989, 264(29):5331-239.
    • (1989) J Biol Chem , vol.264 , Issue.29 , pp. 239-5331
    • Stetler-Stevenson, W.G.1    Krutzsch, H.C.2    Liotta, L.A.3
  • 37
    • 0030010940 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinase 1 is a gelatinolytic enzyme and is secreted in a complex with tissue inhibitor of metalloproteinase 2
    • Imai K, Ohuchi E, Aoki T, Nomura H, Fujii Y, Sato H, Seiki M, Okada Y: Membrane-type matrix metalloproteinase 1 is a gelatinolytic enzyme and is secreted in a complex with tissue inhibitor of metalloproteinase 2. Cancer Res 1996, 56(2):2707-2710.
    • (1996) Cancer Res , vol.56 , Issue.2 , pp. 2707-2710
    • Imai, K.1    Ohuchi, E.2    Aoki, T.3    Nomura, H.4    Fujii, Y.5    Sato, H.6    Seiki, M.7    Okada, Y.8
  • 38
    • 0030756920 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases (MT-MMPs) in cell invation
    • Sato H, Okada Y, Seiki M: Membrane-type matrix metalloproteinases (MT-MMPs) in cell invation. Thromb Haemost 1997, 78(1):497-500.
    • (1997) Thromb Haemost , vol.78 , Issue.1 , pp. 497-500
    • Sato, H.1    Okada, Y.2    Seiki, M.3
  • 39
    • 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, Seiki M: TIMP-2 promotes activation of progelatinase A by membrane-type 1 matrix metalloproteinase immobilized on agarose beads. J Biol Chem 1998, 273(26):16098-16103.
    • (1998) J Biol Chem , vol.273 , Issue.26 , pp. 16098-16103
    • Kinoshita, T.1    Sato, H.2    Okada, A.3    Ohuchi, E.4    Imai, K.5    Okada, Y.6    Seiki, M.7


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