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Volumn 206, Issue 1-2, 1997, Pages 1-9

RNAse protection assays for the simultaneous and semiquantitative analysis of multiple murine matrix metalloproteinase (MMP) and MMP inhibitor mRNAs

Author keywords

Endotoxemia; Lipopolysaccharide; Matrix metalloproteinases; RNase protection assay; Tissue inhibitors of metalloproteinases

Indexed keywords

MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE INHIBITOR; RIBONUCLEASE;

EID: 0030869607     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-1759(97)00077-X     Document Type: Article
Times cited : (36)

References (35)
  • 2
    • 0029705357 scopus 로고    scopus 로고
    • The RNase protection assay
    • Belin, D., 1996. The RNase protection assay. Meth. Mol. Biol. 58, 131.
    • (1996) Meth. Mol. Biol. , vol.58 , pp. 131
    • Belin, D.1
  • 3
    • 0028345963 scopus 로고
    • Cerebral expression of multiple cytokine genes in mice with lymphocytic choriomeningitis
    • Campbell, I.L., Hobbs, M.V., Kemper, P., Oldstone, M.B., 1994. Cerebral expression of multiple cytokine genes in mice with lymphocytic choriomeningitis. J. Immunol. 152, 716.
    • (1994) J. Immunol. , vol.152 , pp. 716
    • Campbell, I.L.1    Hobbs, M.V.2    Kemper, P.3    Oldstone, M.B.4
  • 4
    • 0030581634 scopus 로고    scopus 로고
    • Macrophage metalloelastase degrades matrix and myelin proteins and processes a tumour necrosis factor-alpha fusion protein
    • Chandler, S., Cossins, J., Lury, J., Wells, G., 1996. Macrophage metalloelastase degrades matrix and myelin proteins and processes a tumour necrosis factor-alpha fusion protein. Biochem. Biophys. Res. Commun. 228, 421.
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 421
    • Chandler, S.1    Cossins, J.2    Lury, J.3    Wells, G.4
  • 5
    • 0021186181 scopus 로고
    • The gene family encoding the mouse ribosomal protein L32 contains a uniquely expressed intron-containing gene and an unmutated processed gene
    • Dudov, K.P., Perry, R.P., 1984. The gene family encoding the mouse ribosomal protein L32 contains a uniquely expressed intron-containing gene and an unmutated processed gene. Cell 37, 457.
    • (1984) Cell , vol.37 , pp. 457
    • Dudov, K.P.1    Perry, R.P.2
  • 6
    • 0023057157 scopus 로고
    • A growth-responsive gene (16C8) in normal mouse fibroblasts homologous to a human collagenase inhibitor with erythroid-potentiating activity: Evidence for inducible and constitutive transcripts
    • Edwards, D.R., Waterhouse, P., Holman, M.L., Denhardt, D.T., 1986. A growth-responsive gene (16C8) in normal mouse fibroblasts homologous to a human collagenase inhibitor with erythroid-potentiating activity: Evidence for inducible and constitutive transcripts. Nucleic Acids Res. 14, 8863.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 8863
    • Edwards, D.R.1    Waterhouse, P.2    Holman, M.L.3    Denhardt, D.T.4
  • 7
    • 0029034457 scopus 로고
    • Activation of progelatinase B (MMP-9) by gelatinase A (MMP-2)
    • Fridman, R., Toth, M., Pena, D., Mobashery, S., 1995. Activation of progelatinase B (MMP-9) by gelatinase A (MMP-2). Cancer Res. 55, 2548.
    • (1995) Cancer Res. , vol.55 , pp. 2548
    • Fridman, R.1    Toth, M.2    Pena, D.3    Mobashery, S.4
  • 8
    • 0028292138 scopus 로고
    • Phenotypic alterations in fos-transgenic mice correlate with changes in Fos/Jun-dependent collagenase type I expression. Regulation of mouse metalloproteinases by carcinogens, tumor promoters, cAMP, and Fos oncoprotein
    • Gack, S., Vallon, R., Schaper, J., Ruther, U., Angel, P., 1994. Phenotypic alterations in fos-transgenic mice correlate with changes in Fos/Jun-dependent collagenase type I expression. Regulation of mouse metalloproteinases by carcinogens, tumor promoters, cAMP, and Fos oncoprotein. J. Biol. Chem. 269, 10363.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10363
    • Gack, S.1    Vallon, R.2    Schaper, J.3    Ruther, U.4    Angel, P.5
  • 9
  • 10
    • 0026670053 scopus 로고
    • Cloning and sequencing of a cDNA encoding mouse stromelysin 1
    • Hammani, K., Henriet, P., Eeckhout, Y., 1992. Cloning and sequencing of a cDNA encoding mouse stromelysin 1. Gene 120, 321.
    • (1992) Gene , vol.120 , pp. 321
    • Hammani, K.1    Henriet, P.2    Eeckhout, Y.3
  • 11
    • 0026722877 scopus 로고
    • Cloning and sequencing of mouse collagenase cDNA. Divergence of mouse and rat collagenases from the other mammalian collagenases
    • Henriet, P., Rousseau, G.G., Eeckhout, Y., 1992. Cloning and sequencing of mouse collagenase cDNA. Divergence of mouse and rat collagenases from the other mammalian collagenases. FEBS Lett. 310, 175.
    • (1992) FEBS Lett. , vol.310 , pp. 175
    • Henriet, P.1    Rousseau, G.G.2    Eeckhout, Y.3
  • 12
    • 0030037395 scopus 로고    scopus 로고
    • Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme
    • Knauper, V., Will, H., Lopez-Otin, C., Smith, B., Atkinson, S.J., Stanton, H., Hembry, R.M., Murphy, G., 1996. Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme. J. Biol. Chem. 271, 17124.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17124
    • Knauper, V.1    Will, H.2    Lopez-Otin, C.3    Smith, B.4    Atkinson, S.J.5    Stanton, H.6    Hembry, R.M.7    Murphy, G.8
  • 13
    • 0026721849 scopus 로고
    • Differential regulation of TIMP-1 and TIMP-2 mRNA expression in normal and Haras-transformed murine fibroblasts
    • Leco, K.J., Hayden, L.J., Sharma, R.R., Rocheleau, H., Greenberg, A.H., Edwards, D.R., 1992. Differential regulation of TIMP-1 and TIMP-2 mRNA expression in normal and Haras-transformed murine fibroblasts. Gene 117, 209.
    • (1992) Gene , vol.117 , pp. 209
    • Leco, K.J.1    Hayden, L.J.2    Sharma, R.R.3    Rocheleau, H.4    Greenberg, A.H.5    Edwards, D.R.6
  • 14
    • 0026458152 scopus 로고
    • Synthesis of tissue inhibitor of metalloproteinase-1 (TIMP-1) in human hepatoma cells (HepG2). Upregulation by interleukin-6 and transforming growth factor beta 1
    • Kordula, T., Guttgemann, I., Rose-John, S., Roeb, E., Osthues, A., Tschesche, H., Koj, A., Heinrich, P.C., Graeve, L., 1992. Synthesis of tissue inhibitor of metalloproteinase-1 (TIMP-1) in human hepatoma cells (HepG2). Upregulation by interleukin-6 and transforming growth factor beta 1. FEBS Lett. 313, 143.
    • (1992) FEBS Lett. , vol.313 , pp. 143
    • Kordula, T.1    Guttgemann, I.2    Rose-John, S.3    Roeb, E.4    Osthues, A.5    Tschesche, H.6    Koj, A.7    Heinrich, P.C.8    Graeve, L.9
  • 15
    • 0028244447 scopus 로고
    • Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues
    • Leco, K.J., Khokha, R., Pavloff, N., Hawkes, S.P., Edwards, D.R., 1994. Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues. J. Biol. Chem. 269, 9352.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9352
    • Leco, K.J.1    Khokha, R.2    Pavloff, N.3    Hawkes, S.P.4    Edwards, D.R.5
  • 17
    • 0029959437 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor 1
    • Levi, E., Fridman, R., Miao, H.Q., Ma, Y.S., Yayon, A., Vlodavsky, I., 1996. Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor 1. Proc. Natl. Acad. Sci. USA 93, 7069.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7069
    • Levi, E.1    Fridman, R.2    Miao, H.Q.3    Ma, Y.S.4    Yayon, A.5    Vlodavsky, I.6
  • 18
    • 0029836160 scopus 로고    scopus 로고
    • Inhibition of SV 40 T antigen-induced hepatocellular carcinoma in TIMP-1 transgenic mice
    • Martin, D.C., Rüther, U., Sanchez-Sweatman, O.H., Orr, F.W., Khoka, R., 1996. Inhibition of SV 40 T antigen-induced hepatocellular carcinoma in TIMP-1 transgenic mice. Oncogene 13, 569.
    • (1996) Oncogene , vol.13 , pp. 569
    • Martin, D.C.1    Rüther, U.2    Sanchez-Sweatman, O.H.3    Orr, F.W.4    Khoka, R.5
  • 19
    • 0027426024 scopus 로고
    • Mouse gelatinase B. cDNA cloning, regulation of expression and glycosylation in WEHI-3 macrophages and gene organisation
    • Masure, S., Nys, G., Fiten, P., Van Damme, J., Opdenakker, G., 1993. Mouse gelatinase B. cDNA cloning, regulation of expression and glycosylation in WEHI-3 macrophages and gene organisation. Eur. J. Biochem. 218, 129.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 129
    • Masure, S.1    Nys, G.2    Fiten, P.3    Van Damme, J.4    Opdenakker, G.5
  • 20
    • 0028894485 scopus 로고
    • Minimum duplex requirements for restriction enzyme cleavage near the termini of linear DNA fragments
    • Moreira, R.F., Noren, C.J., 1995. Minimum duplex requirements for restriction enzyme cleavage near the termini of linear DNA fragments. Biotechniques 19, 56.
    • (1995) Biotechniques , vol.19 , pp. 56
    • Moreira, R.F.1    Noren, C.J.2
  • 21
    • 0028935326 scopus 로고
    • Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas
    • Okada, A., Bellocq, J.P., Rouyer, N., Chenard, M.P., Rio, M.C., Chambon, P., Basset, P., 1995. Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas. Proc. Natl. Acad. Sci. USA 92, 2730.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2730
    • Okada, A.1    Bellocq, J.P.2    Rouyer, N.3    Chenard, M.P.4    Rio, M.C.5    Chambon, P.6    Basset, P.7
  • 22
    • 0026668874 scopus 로고
    • Molecular cloning of murine 72-kDa type IV collagenase and its expression during mouse development
    • Reponen, P., Sahlberg, C., Huhtala, P., Hurskainen, T., Thesleff, I., Tryggvason, K., 1992. Molecular cloning of murine 72-kDa type IV collagenase and its expression during mouse development. J. Biol. Chem. 267, 7856.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7856
    • Reponen, P.1    Sahlberg, C.2    Huhtala, P.3    Hurskainen, T.4    Thesleff, I.5    Tryggvason, K.6
  • 23
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumour cells
    • 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.
    • (1994) Nature , vol.370 , pp. 61
    • Sato, H.1    Takino, T.2    Okada, Y.3    Cao, J.4    Shinagawa, A.5    Yamamoto, E.6    Seiki, M.7
  • 25
    • 0028932675 scopus 로고
    • Activation of the 92-kDa gelatinase by stromelysin and 4-aminophenylmercuric acetate. Differential processing and stabilization of the carboxyl-terminal domain by tissue inhibitor of metalloproteinases (TIMP)
    • Shapiro, S.D., Fliszar, C.J., Broekelmann, T.J., Mecham, R.P., Senior, R.M., Welgus, H.G., 1995. Activation of the 92-kDa gelatinase by stromelysin and 4-aminophenylmercuric acetate. Differential processing and stabilization of the carboxyl-terminal domain by tissue inhibitor of metalloproteinases (TIMP). J. Biol. Chem. 270, 6351.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6351
    • Shapiro, S.D.1    Fliszar, C.J.2    Broekelmann, T.J.3    Mecham, R.P.4    Senior, R.M.5    Welgus, H.G.6
  • 27
    • 0028210835 scopus 로고
    • Simultaneous analysis of multiple cytokine receptor mRNAs by RNase protection assay in LPS-induced endotoxemia
    • Stalder, A., Campbell, I.L., 1994. Simultaneous analysis of multiple cytokine receptor mRNAs by RNase protection assay in LPS-induced endotoxemia. Lymphok. Cytok. Res. 13, 107.
    • (1994) Lymphok. Cytok. Res. , vol.13 , pp. 107
    • Stalder, A.1    Campbell, I.L.2
  • 28
    • 0030136756 scopus 로고    scopus 로고
    • Dynamics of matrix turnover during pathologic remodeling of the extracellular matrix
    • Stetler-Stevenson, W.G., 1996. Dynamics of matrix turnover during pathologic remodeling of the extracellular matrix. Am. J. Pathol. 148, 1345.
    • (1996) Am. J. Pathol. , vol.148 , pp. 1345
    • Stetler-Stevenson, W.G.1
  • 29
    • 0024394212 scopus 로고
    • Tissue inhibitor of metalloproteinase (TIMP-2). A new member of the metalloproteinase inhibitor family
    • Stetler-Stevenson, W.G., Krutzsch, H.C., Liotta, L.A., 1989. Tissue inhibitor of metalloproteinase (TIMP-2). A new member of the metalloproteinase inhibitor family. J. Biol. Chem. 264, 17374.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17374
    • Stetler-Stevenson, W.G.1    Krutzsch, H.C.2    Liotta, L.A.3
  • 30
    • 0029118269 scopus 로고
    • Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family
    • Takino, T., Sato, H., Shinagawa, A., Seiki, M., 1995. Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family. J. Biol. Chem. 270, 23013.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23013
    • Takino, T.1    Sato, H.2    Shinagawa, A.3    Seiki, M.4
  • 31
    • 0031041575 scopus 로고    scopus 로고
    • Isolation of a mouse MT2-MMP gene from a lung cDNA library and identification of its product
    • Tanaka, M., Sato, H., Takino, T., Iwata, K., Inoue, M., Seiki, M., 1997. Isolation of a mouse MT2-MMP gene from a lung cDNA library and identification of its product. FEBS Lett. 402, 219.
    • (1997) FEBS Lett. , vol.402 , pp. 219
    • Tanaka, M.1    Sato, H.2    Takino, T.3    Iwata, K.4    Inoue, M.5    Seiki, M.6
  • 32
    • 0029206164 scopus 로고
    • Quantitative measurement of mRNA using the RNase protection assay
    • Tymms, M.J., 1995. Quantitative measurement of mRNA using the RNase protection assay. Meth. Mol. Biol. 37, 31.
    • (1995) Meth. Mol. Biol. , vol.37 , pp. 31
    • Tymms, M.J.1
  • 33
    • 0026490153 scopus 로고
    • The primary sequence and the subunit structure of mouse alpha-2-macroglobulin, deduced from protein sequencing of the isolated subunits and from molecular cloning of the cDNA
    • van Leuven, F., Torrekens, S., Overbergh, L., Lorent, K., de Strooper, B., van den Berghe, H., 1992. The primary sequence and the subunit structure of mouse alpha-2-macroglobulin, deduced from protein sequencing of the isolated subunits and from molecular cloning of the cDNA. Eur. J. Biochem. 210, 319.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 319
    • Van Leuven, F.1    Torrekens, S.2    Overbergh, L.3    Lorent, K.4    De Strooper, B.5    Van Den Berghe, H.6
  • 34
    • 0029133344 scopus 로고
    • cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment
    • Will, H., Hinzmann, B., 1995. cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment. Eur. J. Biochem. 231, 602.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 602
    • Will, H.1    Hinzmann, B.2
  • 35
    • 0029025680 scopus 로고
    • The metalloproteinase matrilysin is preferentially expressed by epithelial cells in a tissue-restricted pattern in the mouse
    • Wilson, C.L., Heppner, K.J., Rudolph, L.A., Matrisian, L.M., 1995. The metalloproteinase matrilysin is preferentially expressed by epithelial cells in a tissue-restricted pattern in the mouse. Mol. Biol. Cell. 6, 851.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 851
    • Wilson, C.L.1    Heppner, K.J.2    Rudolph, L.A.3    Matrisian, L.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.