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Volumn 267, Issue 11, 2000, Pages 3323-3329

Cloning of MMP-26. A novel matrilysin-like proteinase

Author keywords

Cancer; CDNA; Matrix metalloproteinase; Matrixin; Metastasis

Indexed keywords

BETA CASEIN; COMPLEMENTARY DNA; GELATIN; MATRILYSIN; MATRIX METALLOPROTEINASE; MESSENGER RNA; RECOMBINANT PROTEIN;

EID: 0034043835     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01363.x     Document Type: Article
Times cited : (109)

References (33)
  • 1
    • 0030715322 scopus 로고    scopus 로고
    • ECM and cell surface proteolysis: Regulating cellular ecology
    • 1. Werb, Z. (1997) ECM and cell surface proteolysis: regulating cellular ecology. Cell 91, 439-442.
    • (1997) Cell , vol.91 , pp. 439-442
    • Werb, Z.1
  • 2
    • 0025230509 scopus 로고
    • Metalloproteinases and their inhibitors in matrix remodeling
    • 2 Matrisian, L.M. (1990) Metalloproteinases and their inhibitors in matrix remodeling. Trends. Genet. 6, 121-125.
    • (1990) Trends. Genet. , vol.6 , pp. 121-125
    • Matrisian, L.M.1
  • 3
    • 0028006518 scopus 로고
    • Expression of type-IV collagenases in human tumor cell lines that can form liver colonies in chick embryos
    • 3 Tsuchiya, Y., Endo, Y., Sato, H., Okada, Y., Mai, M., Sasaki, T. & Seiki, M. (1994) Expression of type-IV collagenases in human tumor cell lines that can form liver colonies in chick embryos. Int. J. Cancer 56, 46-51.
    • (1994) Int. J. Cancer , vol.56 , pp. 46-51
    • Tsuchiya, Y.1    Endo, Y.2    Sato, H.3    Okada, Y.4    Mai, M.5    Sasaki, T.6    Seiki, M.7
  • 5
    • 0029005284 scopus 로고
    • Human macrophage metalloelastase. Genomic organisation, chromosomal location, gene linkage, and tissue-specific expression
    • 5 Belaaouaj, A., Shipley, J.M., Kobayashi, D.K., Zimonjic, D.B., Popescu, N., Silverman, G.A. & Shapiro, S.D. (1995) Human macrophage metalloelastase. Genomic organisation, chromosomal location, gene linkage, and tissue-specific expression. J. Biol. Chem. 270, 14568-14575.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14568-14575
    • Belaaouaj, A.1    Shipley, J.M.2    Kobayashi, D.K.3    Zimonjic, D.B.4    Popescu, N.5    Silverman, G.A.6    Shapiro, S.D.7
  • 6
    • 0023716802 scopus 로고
    • Purification and properties of a small latent matrix metalloproteinase of the rat uterus
    • 6 Woessner, J.F.J. & Taplin, C.J. (1988) Purification and properties of a small latent matrix metalloproteinase of the rat uterus. J. Biol. Chem. 263, 16918-16925.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16918-16925
    • Woessner, J.F.J.1    Taplin, C.J.2
  • 8
    • 0026664782 scopus 로고
    • Molecular characterization of a low-molecular-mass matrix metalloproteinase secreted by glomerular mesangial cells as PUMP-1
    • 8 Marti, H.P., McNeil, L., Thomas, G., Davies, M. & Lovett, D.H. (1992) Molecular characterization of a low-molecular-mass matrix metalloproteinase secreted by glomerular mesangial cells as PUMP-1. Biochem. J. 285, 899-905.
    • (1992) Biochem. J. , vol.285 , pp. 899-905
    • Marti, H.P.1    McNeil, L.2    Thomas, G.3    Davies, M.4    Lovett, D.H.5
  • 9
    • 0031041647 scopus 로고    scopus 로고
    • Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution
    • 9 Pendas, A.M., Knauper, V., Puente, X.S., Llano, E., Mattei, M.G., Apte, S., Murphy, G. & Lopez-Otin, C. (1997) Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution. J. Biol. Chem. 272, 4281-4286.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4281-4286
    • Pendas, A.M.1    Knauper, V.2    Puente, X.S.3    Llano, E.4    Mattei, M.G.5    Apte, S.6    Murphy, G.7    Lopez-Otin, C.8
  • 11
    • 0025096722 scopus 로고
    • Multiple modes of activation of latent human fibroblast collagenase: Evidence for the role of a Cys73 active-site zinc complex in latency and a 'cysteine switch' mechanism for activation
    • 11 Springman, E.B., Angleton, E.L., Birkedal-Hansen, H. & Van Wart, H.E. (1990) Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a 'cysteine switch' mechanism for activation. Proc. Natl Acad. Sci. USA 87, 364-368.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 364-368
    • Springman, E.B.1    Angleton, E.L.2    Birkedal-Hansen, H.3    Van Wart, H.E.4
  • 12
    • 0025916877 scopus 로고
    • Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway
    • 12 Hosaka, M., Nagahama, M., Kim, W.S., Watanabe, T., Hatsuzawa, K., Ikemizu, J., Murakami, K. & Nakayama, K. (1991) Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway. J. Biol. Chem. 266, 12127-12130.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12127-12130
    • Hosaka, M.1    Nagahama, M.2    Kim, W.S.3    Watanabe, T.4    Hatsuzawa, K.5    Ikemizu, J.6    Murakami, K.7    Nakayama, K.8
  • 13
    • 0343812072 scopus 로고    scopus 로고
    • Relating matrix metalloproteinase structure to function: Why the 'hemopexin' domain?
    • 13 Murphy, G. & Knauper, V. (1997) Relating matrix metalloproteinase structure to function: why the 'hemopexin' domain? Matrix Biol. 15, 511-518.
    • (1997) Matrix Biol. , vol.15 , pp. 511-518
    • Murphy, G.1    Knauper, V.2
  • 14
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumour cells
    • 14 Sato, H., Takino, T., Okada, Y., Cao, J., Shinagawa, A., Yamamoto, E. & Seiki, M. (1994) A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 370, 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    Seiki, M.7
  • 15
    • 0028940033 scopus 로고
    • Cloning of a human gene potentially encoding a novel matrix metalloproteinase having a C-terminal transmembrane domain
    • 15 Takino, T., Sato, H., Yamamoto, E. & Seiki, M. (1995) Cloning of a human gene potentially encoding a novel matrix metalloproteinase having a C-terminal transmembrane domain. Gene 155, 293-298.
    • (1995) Gene , vol.155 , pp. 293-298
    • Takino, T.1    Sato, H.2    Yamamoto, E.3    Seiki, M.4
  • 16
    • 0026664782 scopus 로고
    • Molecular characterization of a low-molecular-mass matrix metalloproteinase secreted by glomerular mesangial cells as PUMP-1
    • 16 Marti, H.P., McNeil, L., Thomas, G., Davies, M. & Lovett, D.H. (1992) Molecular characterization of a low-molecular-mass matrix metalloproteinase secreted by glomerular mesangial cells as PUMP-1. Biochem. J. 285, 899-905.
    • (1992) Biochem. J. , vol.285 , pp. 899-905
    • Marti, H.P.1    McNeil, L.2    Thomas, G.3    Davies, M.4    Lovett, D.H.5
  • 17
    • 0033582513 scopus 로고    scopus 로고
    • Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members
    • 17 Velasco, G., Pendas, A.M., Fueyo, A., Knauper, V., Murphy. G. & Lopez-Otin, C. (1999) Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members. J. Biol. Chem. 274, 4570-4576.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4570-4576
    • Velasco, G.1    Pendas, A.M.2    Fueyo, A.3    Knauper, V.4    Murphy, G.5    Lopez-Otin, C.6
  • 18
    • 0026647156 scopus 로고
    • Demonstration of a second ligand for the low affinity receptor for immunoglobulin E (CD23) using recombinant CD23 reconstituted into fluorescent liposomes
    • 18 Pochon, S., Graber, P., Yeager, M., Jansen, K., Bernard, A.R., Aubry, J.P. & Bonnefoy, J.Y. (1992) Demonstration of a second ligand for the low affinity receptor for immunoglobulin E (CD23) using recombinant CD23 reconstituted into fluorescent liposomes. J. Exp. Med. 176, 389-397.
    • (1992) J. Exp. Med. , vol.176 , pp. 389-397
    • Pochon, S.1    Graber, P.2    Yeager, M.3    Jansen, K.4    Bernard, A.R.5    Aubry, J.P.6    Bonnefoy, J.Y.7
  • 19
    • 0027529650 scopus 로고
    • Human CD40-ligand: Molecular cloning, cellular distribution and regulation of expression by factors controlling IgE production
    • 19 Gauchat, J.F., Aubry, J.P., Mazzei, G., Life, P., Jomotte, T., Elson, G. & Bonnefoy, J.Y. (1993) Human CD40-ligand: molecular cloning, cellular distribution and regulation of expression by factors controlling IgE production. FEBS. Lett. 315, 259-266.
    • (1993) FEBS. Lett. , vol.315 , pp. 259-266
    • Gauchat, J.F.1    Aubry, J.P.2    Mazzei, G.3    Life, P.4    Jomotte, T.5    Elson, G.6    Bonnefoy, J.Y.7
  • 20
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonucleasc fragments to high specific activity
    • 20 Feinberg, A.P. (1983) A technique for radiolabeling DNA restriction endonucleasc fragments to high specific activity. Anal Biochem. 132, 6-13.
    • (1983) Anal Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.P.1
  • 21
    • 0023515393 scopus 로고
    • High-efficiency cloning of full-length cDNA; construction and screening of cDNA expression libraries for mammalian cells
    • 21 Okayama, H., Kawaichi, M., Brownstein, M., Lee, F., Yokota, T. & Aral, K. (1987) High-efficiency cloning of full-length cDNA; construction and screening of cDNA expression libraries for mammalian cells. Methods Enzymol. 154, 3-28.
    • (1987) Methods Enzymol. , vol.154 , pp. 3-28
    • Okayama, H.1    Kawaichi, M.2    Brownstein, M.3    Lee, F.4    Yokota, T.5    Aral, K.6
  • 22
    • 0022484665 scopus 로고
    • UV cross-linking of RNA to nylon membrane enhances hybridization signals
    • 22 Khandjian, E.W. (1986) UV cross-linking of RNA to nylon membrane enhances hybridization signals. Mol. Biol. Report 11, 107-115.
    • (1986) Mol. Biol. Report , vol.11 , pp. 107-115
    • Khandjian, E.W.1
  • 23
    • 0019551730 scopus 로고
    • 'Western blotting': Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • 23 Burnette, W.N. (1981) 'Western blotting': electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112, 195-203.
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 24
    • 0028969678 scopus 로고
    • The metzincins - Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases
    • 24 Stocker, W., Grams, F., Baumann, U., Reinemer, P., Gomis-Ruth, F.X., McKay, D.B. & Bode, W. (1995) The metzincins - topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci. 4, 823-840.
    • (1995) Protein Sci. , vol.4 , pp. 823-840
    • Stocker, W.1    Grams, F.2    Baumann, U.3    Reinemer, P.4    Gomis-Ruth, F.X.5    McKay, D.B.6    Bode, W.7
  • 25
    • 0033256294 scopus 로고    scopus 로고
    • Leukolysin/MMP25/MT6-MMP: A novel matrix metalloproteinase specifically expressed in the leukocyte lineage
    • 25 Pei, D. (1999) Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage. Cell Res. 9, 291-303.
    • (1999) Cell Res. , vol.9 , pp. 291-303
    • Pei, D.1
  • 26
    • 0027409432 scopus 로고
    • Role of zinc-binding-and hemopexin domain-encoded sequences in the substrate specificity of collagenase and stromelysin-2 as revealed by chimeric proteins
    • 26 Sanchez-Lopez, R., Alexander, C.M., Behrendtsen, O., Breathnach, R. & Werb, Z. (1993) Role of zinc-binding-and hemopexin domain-encoded sequences in the substrate specificity of collagenase and stromelysin-2 as revealed by chimeric proteins. J. Biol. Chem. 268, 7238-7247.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7238-7247
    • Sanchez-Lopez, R.1    Alexander, C.M.2    Behrendtsen, O.3    Breathnach, R.4    Werb, Z.5
  • 28
    • 0029030448 scopus 로고
    • Matrilysin-inhibitor complexes: Common themes among metalloproteases
    • 28 Browner, M.F., Smith, W.W. & Castelhano, A.L. (1995) Matrilysin-inhibitor complexes: common themes among metalloproteases. Biochemistry 34, 6602-6610.
    • (1995) Biochemistry , vol.34 , pp. 6602-6610
    • Browner, M.F.1    Smith, W.W.2    Castelhano, A.L.3
  • 30
    • 0030061278 scopus 로고    scopus 로고
    • Matrilysin: An epithelial matrix metalloproteinase with potentially novel functions
    • 30 Wilson, C.L. & Matrisian, L.M. (1996) Matrilysin: an epithelial matrix metalloproteinase with potentially novel functions. Int. J. Biochem. Cell Biol. 28, 123-136.
    • (1996) Int. J. Biochem. Cell Biol. , vol.28 , pp. 123-136
    • Wilson, C.L.1    Matrisian, L.M.2
  • 31
    • 0028291374 scopus 로고
    • Human progelatinase A can be activated by matrilysin
    • 31 Crabbe, T., Smith, B., O'Connell, J. & Docherty, A. (1994) Human progelatinase A can be activated by matrilysin. FEBS Lett. 345, 14-16.
    • (1994) FEBS Lett. , vol.345 , pp. 14-16
    • Crabbe, T.1    Smith, B.2    O'Connell, J.3    Docherty, A.4
  • 32
    • 0028913443 scopus 로고
    • Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precursor, interaction with other matrix metalloproteinases and enzymic properties
    • 32 Imai, K., Yokohama, Y., Nakanishi, I., Ohuchi, E., Fujii, Y., Nakai, N. & Okada, Y. (1995) Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precursor, interaction with other matrix metalloproteinases and enzymic properties. J. Biol. Chem. 270, 6691-6697.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6691-6697
    • Imai, K.1    Yokohama, Y.2    Nakanishi, I.3    Ohuchi, E.4    Fujii, Y.5    Nakai, N.6    Okada, Y.7
  • 33
    • 0026690901 scopus 로고
    • The matrix metalloproteinase pump-1 catalyzes formation of low molecular weight (pro) urokinase in cultures of normal human kidney cells
    • 33 Marcotte, P.A., Kozan, I.M., Dorwin, S.A. & Ryan, J.M. (1992) The matrix metalloproteinase pump-1 catalyzes formation of low molecular weight (pro) urokinase in cultures of normal human kidney cells. J. Biol. Chem. 267, 13803-13806.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13803-13806
    • Marcotte, P.A.1    Kozan, I.M.2    Dorwin, S.A.3    Ryan, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.