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Volumn 12, Issue 7, 2012, Pages 773-782

Regulation of MMPs during melanoma progression: From genetic to epigenetic

Author keywords

Cancer; Epigenetic; Lymphocyte; Melanoma; MMP

Indexed keywords

BRG1 PROTEIN; CHEMOKINE RECEPTOR CXCR4; ENTINOSTAT; GELATINASE B; HISTONE DEACETYLASE INHIBITOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 2; INTERLEUKIN 8; MACROPHAGE ELASTASE; MATRIX METALLOPROTEINASE; MITOGEN ACTIVATED PROTEIN KINASE; NEUTROPHIL COLLAGENASE; PROTEIN FOS; SMAD PROTEIN; STAT PROTEIN; STROMELYSIN; TISSUE INHIBITOR OF METALLOPROTEINASE 1; VALPROIC ACID;

EID: 84866370600     PISSN: 18715206     EISSN: 18755992     Source Type: Journal    
DOI: 10.2174/187152012802650228     Document Type: Article
Times cited : (14)

References (86)
  • 1
    • 57649111990 scopus 로고    scopus 로고
    • Melanoma prognostic factors found in the dermatopathology report
    • Payette, M. J.; Katz, M., 3rd; Grant-Kels, J. M. Melanoma prognostic factors found in the dermatopathology report, Clin. Dermatol., 2009, 27, 53-74.
    • (2009) Clin. Dermatol , vol.27 , pp. 53-74
    • Payette, M.J.1    Katz, M.2    Grant-Kels, J.M.3
  • 3
    • 38749114263 scopus 로고    scopus 로고
    • Comparison of the prognostic value of matrix metalloproteinases 2 and 9 in cutaneous melanoma
    • Vaisanen, A. H.; Kallioinen, M.; Turpeenniemi-Hujanen, T. Comparison of the prognostic value of matrix metalloproteinases 2 and 9 in cutaneous melanoma, Hum. Pathol., 2008, 39, 377-385.
    • (2008) Hum. Pathol , vol.39 , pp. 377-385
    • Vaisanen, A.H.1    Kallioinen, M.2    Turpeenniemi-Hujanen, T.3
  • 4
    • 79960226262 scopus 로고    scopus 로고
    • Physiology and pathophysiology of matrix metalloproteases
    • Klein, T.; Bischoff, R. Physiology and pathophysiology of matrix metalloproteases, Amino Acids. 2010, 41(2):271-290.
    • (2010) Amino Acids , vol.41 , Issue.2 , pp. 271-290
    • Klein, T.1    Bischoff, R.2
  • 5
    • 79956339528 scopus 로고    scopus 로고
    • Matrix Metalloproteinases and Tissue Inhibitor of Metalloproteinases Are Essential for the Inflammatory Response in Cancer Cells
    • Sun, J. Matrix Metalloproteinases and Tissue Inhibitor of Metalloproteinases Are Essential for the Inflammatory Response in Cancer Cells, J. Signal. Transuct., 2010, 2010, 985132.
    • (2010) J. Signal. Transuct , vol.2010 , pp. 985132
    • Sun, J.1
  • 6
    • 0035988813 scopus 로고    scopus 로고
    • Matrixdirected regulation of pericellular proteolysis and tumor progression
    • Hornebeck, W.; Emonard, H.; Monboisse, J. C.; Bellon, G. Matrixdirected regulation of pericellular proteolysis and tumor progression, Semin. Cancer Biol., 2002, 12, 231-241.
    • (2002) Semin. Cancer Biol , vol.12 , pp. 231-241
    • Hornebeck, W.1    Emonard, H.2    Monboisse, J.C.3    Bellon, G.4
  • 7
    • 27544493290 scopus 로고    scopus 로고
    • Stromal cells as the major source for matrix metalloproteinase-2 in cutaneous melanoma
    • Hofmann, U. B.; Eggert, A. A.; Blass, K.; Brocker, E. B.; Becker, J. C. Stromal cells as the major source for matrix metalloproteinase-2 in cutaneous melanoma, Arch. Dermatol. Res., 2005, 297, 154-160.
    • (2005) Arch. Dermatol. Res , vol.297 , pp. 154-160
    • Hofmann, U.B.1    Eggert, A.A.2    Blass, K.3    Brocker, E.B.4    Becker, J.C.5
  • 8
    • 0033923006 scopus 로고    scopus 로고
    • Expression and activation of matrix metalloproteinase-2 (MMP-2) and its co-localization with membrane-type 1 matrix metalloproteinase (MT1-MMP) correlate with melanoma progression
    • Hofmann, U. B.; Westphal, J. R.; Zendman, A. J.; Becker, J. C.; Ruiter, D. J.; van Muijen, G. N. Expression and activation of matrix metalloproteinase-2 (MMP-2) and its co-localization with membrane-type 1 matrix metalloproteinase (MT1-MMP) correlate with melanoma progression, J. Pathol., 2000, 191, 245-256.
    • (2000) J. Pathol , vol.191 , pp. 245-256
    • Hofmann, U.B.1    Westphal, J.R.2    Zendman, A.J.3    Becker, J.C.4    Ruiter, D.J.5    van Muijen, G.N.6
  • 9
    • 0033520459 scopus 로고    scopus 로고
    • A novel host/tumor cell interaction activates matrix metalloproteinase 1 and mediates invasion through type I collagen
    • Benbow, U.; Schoenermark, M. P.; Mitchell, T. I.; Rutter, J. L.; Shimokawa, K.; Nagase, H.; Brinckerhoff, C. E. A novel host/tumor cell interaction activates matrix metalloproteinase 1 and mediates invasion through type I collagen, J. Biol. Chem., 1999, 274, 25371-25378.
    • (1999) J. Biol. Chem , vol.274 , pp. 25371-25378
    • Benbow, U.1    Schoenermark, M.P.2    Mitchell, T.I.3    Rutter, J.L.4    Shimokawa, K.5    Nagase, H.6    Brinckerhoff, C.E.7
  • 10
    • 22344448889 scopus 로고    scopus 로고
    • High serum levels of matrix metalloproteinase-9 and matrix metalloproteinase-1 are associated with rapid progression in patients with metastatic melanoma
    • Nikkola, J.; Vihinen, P.; Vuoristo, M. S.; Kellokumpu-Lehtinen, P.; Kahari, V. M.; Pyrhonen, S. High serum levels of matrix metalloproteinase-9 and matrix metalloproteinase-1 are associated with rapid progression in patients with metastatic melanoma, Clin. Cancer. Res., 2005, 11, 5158-5166.
    • (2005) Clin. Cancer. Res , vol.11 , pp. 5158-5166
    • Nikkola, J.1    Vihinen, P.2    Vuoristo, M.S.3    Kellokumpu-Lehtinen, P.4    Kahari, V.M.5    Pyrhonen, S.6
  • 11
    • 79960404098 scopus 로고    scopus 로고
    • A prognostic index in skin melanoma through the combination of matrix metalloproteinase-2, Ki67, and p53
    • Vaisanen, A.; Kuvaja, P.; Kallioinen, M.; Turpeenniemi-Hujanen, T. A prognostic index in skin melanoma through the combination of matrix metalloproteinase-2, Ki67, and p53, Hum. Pathol., 2011, 42(8), 1103-1111
    • (2011) Hum. Pathol , vol.42 , Issue.8 , pp. 1103-1111
    • Vaisanen, A.1    Kuvaja, P.2    Kallioinen, M.3    Turpeenniemi-Hujanen, T.4
  • 12
    • 1442274622 scopus 로고    scopus 로고
    • Elastin-derived peptides upregulate matrix metalloproteinase-2-mediated melanoma cell invasion through elastin-binding protein
    • Ntayi, C.; Labrousse, A. L.; Debret, R.; Birembaut, P.; Bellon, G.; Antonicelli, F.; Hornebeck, W.; Bernard, P. Elastin-derived peptides upregulate matrix metalloproteinase-2-mediated melanoma cell invasion through elastin-binding protein, J. Invest. Dermatol., 2004, 122, 256-265.
    • (2004) J. Invest. Dermatol , vol.122 , pp. 256-265
    • Ntayi, C.1    Labrousse, A.L.2    Debret, R.3    Birembaut, P.4    Bellon, G.5    Antonicelli, F.6    Hornebeck, W.7    Bernard, P.8
  • 13
    • 38749137345 scopus 로고    scopus 로고
    • Expression and prognostic role of MMP2, MMP9, MMP13, and MMP14 matrix metalloproteinases in sinonasal and oral malignant melanomas
    • Kondratiev, S.; Gnepp, D. R.; Yakirevich, E.; Sabo, E.; Annino, D. J.; Rebeiz, E.; Laver, N. V. Expression and prognostic role of MMP2, MMP9, MMP13, and MMP14 matrix metalloproteinases in sinonasal and oral malignant melanomas, Hum. Pathol., 2008, 39, 337-343.
    • (2008) Hum. Pathol , vol.39 , pp. 337-343
    • Kondratiev, S.1    Gnepp, D.R.2    Yakirevich, E.3    Sabo, E.4    Annino, D.J.5    Rebeiz, E.6    Laver, N.V.7
  • 14
    • 79958247987 scopus 로고    scopus 로고
    • MMP-2 and TIMP-2 in Cutaneous Melanoma: Association With Prognostic Factors and Description in Cutaneous Metastases
    • Rey, M. C.; Bonamigo, R. R.; Cartell, A.; Furian, R.; Bonfa, R. MMP-2 and TIMP-2 in Cutaneous Melanoma: Association With Prognostic Factors and Description in Cutaneous Metastases, Am. J. Dermatopathol., 2011, 33, 413-414.
    • (2011) Am. J. Dermatopathol , vol.33 , pp. 413-414
    • Rey, M.C.1    Bonamigo, R.R.2    Cartell, A.3    Furian, R.4    Bonfa, R.5
  • 15
    • 78650143782 scopus 로고    scopus 로고
    • Variability in melanoma metalloproteinase expression profiling
    • Giricz, O.; Lauer, J. L.; Fields, G. B. Variability in melanoma metalloproteinase expression profiling, J. Biomol. Tech., 2010, 21, 194-204.
    • (2010) J. Biomol. Tech , vol.21 , pp. 194-204
    • Giricz, O.1    Lauer, J.L.2    Fields, G.B.3
  • 16
    • 78650298121 scopus 로고    scopus 로고
    • Comparison of metalloproteinase protein and activity profiling
    • Giricz, O.; Lauer, J. L.; Fields, G. B. Comparison of metalloproteinase protein and activity profiling, Anal. Biochem., 2011, 409, 37-45.
    • (2011) Anal. Biochem , vol.409 , pp. 37-45
    • Giricz, O.1    Lauer, J.L.2    Fields, G.B.3
  • 18
    • 0034650403 scopus 로고    scopus 로고
    • A specific sequence of the noncollagenous domain of the alpha3(IV) chain of type IV collagen inhibits expression and activation of matrix metalloproteinases by tumor cells
    • Pasco, S.; Han, J.; Gillery, P.; Bellon, G.; Maquart, F. X.; Borel, J. P.; Kefalides, N. A.; Monboisse, J. C. A specific sequence of the noncollagenous domain of the alpha3(IV) chain of type IV collagen inhibits expression and activation of matrix metalloproteinases by tumor cells, Cancer Res., 2000, 60, 467-473.
    • (2000) Cancer Res , vol.60 , pp. 467-473
    • Pasco, S.1    Han, J.2    Gillery, P.3    Bellon, G.4    Maquart, F.X.5    Borel, J.P.6    Kefalides, N.A.7    Monboisse, J.C.8
  • 19
    • 0034693240 scopus 로고    scopus 로고
    • The alpha 3(IV)185-206 peptide from noncollagenous domain 1 of type IV collagen interacts with a novel binding site on the beta 3 subunit of integrin alpha Vbeta 3 and stimulates focal adhesion kinase and phosphatidylinositol 3-kinase phosphorylation
    • Pasco, S.; Monboisse, J. C.; Kieffer, N. The alpha 3(IV)185-206 peptide from noncollagenous domain 1 of type IV collagen interacts with a novel binding site on the beta 3 subunit of integrin alpha Vbeta 3 and stimulates focal adhesion kinase and phosphatidylinositol 3-kinase phosphorylation, J. Biol. Chem., 2000, 275, 32999-33007.
    • (2000) J. Biol. Chem , vol.275 , pp. 32999-33007
    • Pasco, S.1    Monboisse, J.C.2    Kieffer, N.3
  • 24
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad, M.; Werb, Z. New functions for the matrix metalloproteinases in cancer progression, Nat. Rev. Cancer, 2002, 2, 161-174.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 26
    • 0034667542 scopus 로고    scopus 로고
    • Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAPIII, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact
    • van den Steen, P. E.; Proost, P.; Wuyts, A.; van Damme, J.; Opdenakker, G. Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAPIII, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact, Blood, 2000, 96, 2673-2681.
    • (2000) Blood , vol.96 , pp. 2673-2681
    • van den Steen, P.E.1    Proost, P.2    Wuyts, A.3    van Damme, J.4    Opdenakker, G.5
  • 28
    • 0032960519 scopus 로고    scopus 로고
    • Role of interleukin-8 in tumor growth and metastasis of human melanoma
    • Bar-Eli, M. Role of interleukin-8 in tumor growth and metastasis of human melanoma, Pathobiology, 1999, 67, 12-18.
    • (1999) Pathobiology , vol.67 , pp. 12-18
    • Bar-Eli, M.1
  • 30
    • 0025604195 scopus 로고
    • Retroviral vector-mediated gamma-interferon gene transfer into tumor cells generates potent and long lasting antitumor immunity
    • Gansbacher, B.; Bannerji, R.; Daniels, B.; Zier, K.; Cronin, K.; Gilboa, E. Retroviral vector-mediated gamma-interferon gene transfer into tumor cells generates potent and long lasting antitumor immunity, Cancer Res., 1990, 50, 7820-7825.
    • (1990) Cancer Res , vol.50 , pp. 7820-7825
    • Gansbacher, B.1    Bannerji, R.2    Daniels, B.3    Zier, K.4    Cronin, K.5    Gilboa, E.6
  • 31
    • 0025000864 scopus 로고
    • Interleukin 2 gene transfer into tumor cells abrogates tumorigenicity and induces protective immunity
    • Gansbacher, B.; Zier, K.; Daniels, B.; Cronin, K.; Bannerji, R.; Gilboa, E. Interleukin 2 gene transfer into tumor cells abrogates tumorigenicity and induces protective immunity, J. Exp. Med., 1990, 172, 1217-1224.
    • (1990) J. Exp. Med , vol.172 , pp. 1217-1224
    • Gansbacher, B.1    Zier, K.2    Daniels, B.3    Cronin, K.4    Bannerji, R.5    Gilboa, E.6
  • 32
    • 38449107874 scopus 로고    scopus 로고
    • Elastin receptor (spliced galactosidase) occupancy by elastin peptides counteracts proinflammatory cytokine expression in lipopolysaccharide-stimulated human monocytes through NFkappaB down-regulation
    • Baranek, T.; Debret, R.; Antonicelli, F.; Lamkhioued, B.; Belaaouaj, A.; Hornebeck, W.; Bernard, P.; Guenounou, M.; Le Naour, R. Elastin receptor (spliced galactosidase) occupancy by elastin peptides counteracts proinflammatory cytokine expression in lipopolysaccharide-stimulated human monocytes through NFkappaB down-regulation, J. Immunol., 2007, 179, 6184-6192.
    • (2007) J. Immunol , vol.179 , pp. 6184-6192
    • Baranek, T.1    Debret, R.2    Antonicelli, F.3    Lamkhioued, B.4    Belaaouaj, A.5    Hornebeck, W.6    Bernard, P.7    Guenounou, M.8    Le Naour, R.9
  • 34
    • 33847683870 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase gene expression
    • Yan, C.; Boyd, D. D. Regulation of matrix metalloproteinase gene expression, J. Cell Physiol., 2007, 211, 19-26.
    • (2007) J. Cell Physiol , vol.211 , pp. 19-26
    • Yan, C.1    Boyd, D.D.2
  • 35
    • 77149137406 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Evolution, gene regulation and functional analysis in mouse models
    • Fanjul-Fernandez, M.; Folgueras, A. R.; Cabrera, S.; Lopez-Otin, C. Matrix metalloproteinases: evolution, gene regulation and functional analysis in mouse models, Biochim. Biophys. Acta, 2010, 1803, 3-19.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 3-19
    • Fanjul-Fernandez, M.1    Folgueras, A.R.2    Cabrera, S.3    Lopez-Otin, C.4
  • 37
    • 15244357105 scopus 로고    scopus 로고
    • Role of matrix metalloproteinases in melanoma cell invasion
    • Hofmann, U. B.; Houben, R.; Brocker, E. B.; Becker, J. C. Role of matrix metalloproteinases in melanoma cell invasion, Biochimie, 2005, 87, 307-314.
    • (2005) Biochimie , vol.87 , pp. 307-314
    • Hofmann, U.B.1    Houben, R.2    Brocker, E.B.3    Becker, J.C.4
  • 38
    • 0030810640 scopus 로고    scopus 로고
    • Matrix metalloproteinases in skin
    • Kahari, V. M.; Saarialho-Kere, U. Matrix metalloproteinases in skin, Exp. Dermatol., 1997, 6, 199-213.
    • (1997) Exp. Dermatol , vol.6 , pp. 199-213
    • Kahari, V.M.1    Saarialho-Kere, U.2
  • 39
    • 34848868145 scopus 로고    scopus 로고
    • Signal transduction and celltype specific regulation of matrix metalloproteinase gene expression: Can MMPs be good for you?
    • Vincenti, M. P.; Brinckerhoff, C. E. Signal transduction and celltype specific regulation of matrix metalloproteinase gene expression: can MMPs be good for you?, J. Cell Physiol., 2007, 213, 355-364.
    • (2007) J. Cell Physiol , vol.213 , pp. 355-364
    • Vincenti, M.P.1    Brinckerhoff, C.E.2
  • 40
    • 0036716282 scopus 로고    scopus 로고
    • Strategies for MMP inhibition in cancer: Innovations for the post-trial era
    • Overall, C. M.; Lopez-Otin, C. Strategies for MMP inhibition in cancer: innovations for the post-trial era, Nat. Rev. Cancer, 2002, 2, 657-672.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 657-672
    • Overall, C.M.1    Lopez-Otin, C.2
  • 41
    • 33847748493 scopus 로고    scopus 로고
    • Mda-9/Syntenin regulates the metastatic phenotype in human melanoma cells by activating nuclear factor-kappaB
    • Boukerche, H.; Su, Z. Z.; Emdad, L.; Sarkar, D.; Fisher, P. B. Mda-9/Syntenin regulates the metastatic phenotype in human melanoma cells by activating nuclear factor-kappaB, Cancer Res., 2007, 67, 1812-1822.
    • (2007) Cancer Res , vol.67 , pp. 1812-1822
    • Boukerche, H.1    Su, Z.Z.2    Emdad, L.3    Sarkar, D.4    Fisher, P.B.5
  • 42
    • 0035986312 scopus 로고    scopus 로고
    • High levels of MMP-1 expression in the absence of the 2G single nucleotide polymorphism is mediated by p38 and ERK1/2 mitogen-activated protein kinases in VMM5 melanoma cells
    • Benbow, U.; Tower, G. B.; Wyatt, C. A.; Buttice, G.; Brinckerhoff, C. E. High levels of MMP-1 expression in the absence of the 2G single nucleotide polymorphism is mediated by p38 and ERK1/2 mitogen-activated protein kinases in VMM5 melanoma cells, J. Cell Biochem., 2002, 86, 307-319.
    • (2002) J. Cell Biochem , vol.86 , pp. 307-319
    • Benbow, U.1    Tower, G.B.2    Wyatt, C.A.3    Buttice, G.4    Brinckerhoff, C.E.5
  • 43
    • 0032404174 scopus 로고    scopus 로고
    • A single nucleotide polymorphism in the matrix metalloproteinase-1 promoter creates an Ets binding site and augments transcription
    • Rutter, J. L.; Mitchell, T. I.; Buttice, G.; Meyers, J.; Gusella, J. F.; Ozelius, L. J.; Brinckerhoff, C. E. A single nucleotide polymorphism in the matrix metalloproteinase-1 promoter creates an Ets binding site and augments transcription, Cancer Res., 1998, 58, 5321-5325.
    • (1998) Cancer Res , vol.58 , pp. 5321-5325
    • Rutter, J.L.1    Mitchell, T.I.2    Buttice, G.3    Meyers, J.4    Gusella, J.F.5    Ozelius, L.J.6    Brinckerhoff, C.E.7
  • 46
    • 45549090884 scopus 로고    scopus 로고
    • Culture of human A375 melanoma cells in the presence of fibronectin causes expression of MMP-9 and activation of MMP-2 in culture supernatants
    • Banerji, A.; Das, S.; Chatterjee, A. Culture of human A375 melanoma cells in the presence of fibronectin causes expression of MMP-9 and activation of MMP-2 in culture supernatants, J. Environ. Pathol. Toxicol. Oncol., 2008, 27, 135-145.
    • (2008) J. Environ. Pathol. Toxicol. Oncol , vol.27 , pp. 135-145
    • Banerji, A.1    Das, S.2    Chatterjee, A.3
  • 47
    • 0038191064 scopus 로고    scopus 로고
    • Osteopontin induces nuclear factor kappa B-mediated promatrix metalloproteinase-2 activation through I kappa B alpha /IKK signaling pathways, and curcumin (diferulolylmethane) down-regulates these pathways
    • Philip, S.; Kundu, G. C. Osteopontin induces nuclear factor kappa B-mediated promatrix metalloproteinase-2 activation through I kappa B alpha /IKK signaling pathways, and curcumin (diferulolylmethane) down-regulates these pathways, J. Biol. Chem., 2003, 278, 14487-14497.
    • (2003) J. Biol. Chem , vol.278 , pp. 14487-14497
    • Philip, S.1    Kundu, G.C.2
  • 49
    • 0035137707 scopus 로고    scopus 로고
    • A novel role of metalloproteinase in cancer-mediated immunosuppression
    • Sheu, B. C.; Hsu, S. M.; Ho, H. N.; Lien, H. C.; Huang, S. C.; Lin, R. H. A novel role of metalloproteinase in cancer-mediated immunosuppression, Cancer Res., 2001, 61, 237-242.
    • (2001) Cancer Res , vol.61 , pp. 237-242
    • Sheu, B.C.1    Hsu, S.M.2    Ho, H.N.3    Lien, H.C.4    Huang, S.C.5    Lin, R.H.6
  • 50
    • 22044450897 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 (MMP-2) and MMP-9 in pulmonary pathology
    • Chakrabarti, S.; Patel, K. D. Matrix metalloproteinase-2 (MMP-2) and MMP-9 in pulmonary pathology, Exp. Lung Res., 2005, 31, 599-621.
    • (2005) Exp. Lung Res , vol.31 , pp. 599-621
    • Chakrabarti, S.1    Patel, K.D.2
  • 51
    • 0029925375 scopus 로고    scopus 로고
    • Prognostic value of tumor infiltrating lymphocytes in the vertical growth phase of primary cutaneous melanoma
    • Clemente, C. G.; Mihm, M. C., Jr.; Bufalino, R.; Zurrida, S.; Collini, P.; Cascinelli, N. Prognostic value of tumor infiltrating lymphocytes in the vertical growth phase of primary cutaneous melanoma, Cancer, 1996, 77, 1303-1310.
    • (1996) Cancer , vol.77 , pp. 1303-1310
    • Clemente, C.G.1    Mihm Jr., M.C.2    Bufalino, R.3    Zurrida, S.4    Collini, P.5    Cascinelli, N.6
  • 53
    • 24344466882 scopus 로고    scopus 로고
    • DNA methylation and histone modifications: Teaming up to silence genes
    • Fuks, F. DNA methylation and histone modifications: teaming up to silence genes, Curr. Opin. Genet. Dev., 2005, 15, 490-495.
    • (2005) Curr. Opin. Genet. Dev , vol.15 , pp. 490-495
    • Fuks, F.1
  • 54
    • 37149010874 scopus 로고    scopus 로고
    • Oxidative stress modulates DNA methylation during melanocyte anchorage blockade associated with malignant transformation
    • Campos, A. C.; Molognoni, F.; Melo, F. H.; Galdieri, L. C.; Carneiro, C. R.; D'Almeida, V.; Correa, M.; Jasiulionis, M. G. Oxidative stress modulates DNA methylation during melanocyte anchorage blockade associated with malignant transformation, Neoplasia, 2007, 9, 1111-1121.
    • (2007) Neoplasia , vol.9 , pp. 1111-1121
    • Campos, A.C.1    Molognoni, F.2    Melo, F.H.3    Galdieri, L.C.4    Carneiro, C.R.5    D'Almeida, V.6    Correa, M.7    Jasiulionis, M.G.8
  • 56
    • 33644884949 scopus 로고    scopus 로고
    • The role of DNA hypomethylation in the control of stromelysin gene expression
    • Couillard, J.; Demers, M.; Lavoie, G.; St-Pierre, Y. The role of DNA hypomethylation in the control of stromelysin gene expression, Biochem. Biophys. Res. Commun., 2006, 342, 1233-1239.
    • (2006) Biochem. Biophys. Res. Commun , vol.342 , pp. 1233-1239
    • Couillard, J.1    Demers, M.2    Lavoie, G.3    St-Pierre, Y.4
  • 57
    • 79955872504 scopus 로고    scopus 로고
    • Epigenetic regulation of proMMP-1 expression in the HT1080 human fibrosarcoma cell line
    • Poplineau, M.; Dufer, J.; Antonicelli, F.; Trussardi-Regnier, A. Epigenetic regulation of proMMP-1 expression in the HT1080 human fibrosarcoma cell line, Int. J. Oncol., 2011, 38(6):1713-1718.
    • (2011) Int. J. Oncol , vol.38 , Issue.6 , pp. 1713-1718
    • Poplineau, M.1    Dufer, J.2    Antonicelli, F.3    Trussardi-Regnier, A.4
  • 58
    • 77953424645 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase 1 expression associated with gene demethylation confers anoikis resistance in early phases of melanocyte malignant transformation
    • Ricca, T. I.; Liang, G.; Suenaga, A. P.; Han, S. W.; Jones, P. A.; Jasiulionis, M. G. Tissue inhibitor of metalloproteinase 1 expression associated with gene demethylation confers anoikis resistance in early phases of melanocyte malignant transformation, Transl. Oncol., 2009, 2, 329-340.
    • (2009) Transl. Oncol , vol.2 , pp. 329-340
    • Ricca, T.I.1    Liang, G.2    Suenaga, A.P.3    Han, S.W.4    Jones, P.A.5    Jasiulionis, M.G.6
  • 59
    • 0034255298 scopus 로고    scopus 로고
    • The Swi/Snf family nucleosomeremodeling complexes and transcriptional control
    • Sudarsanam, P.; Winston, F. The Swi/Snf family nucleosomeremodeling complexes and transcriptional control, Trends Genet., 2000, 16, 345-351.
    • (2000) Trends Genet , vol.16 , pp. 345-351
    • Sudarsanam, P.1    Winston, F.2
  • 60
    • 0036532026 scopus 로고    scopus 로고
    • Histone modifications in transcriptional regulation
    • Berger, S. L. Histone modifications in transcriptional regulation, Curr. Opin. Genet. Dev., 2002, 12, 142-148.
    • (2002) Curr. Opin. Genet. Dev , vol.12 , pp. 142-148
    • Berger, S.L.1
  • 61
    • 0036008097 scopus 로고    scopus 로고
    • Deacetylase enzymes: Biological functions and the use of small-molecule inhibitors
    • Grozinger, C. M.; Schreiber, S. L. Deacetylase enzymes: biological functions and the use of small-molecule inhibitors, Chem. Biol., 2002, 9, 3-16.
    • (2002) Chem. Biol , vol.9 , pp. 3-16
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 62
    • 10644277123 scopus 로고    scopus 로고
    • Structure and chemistry of the Sir2 family of NAD+-dependent histone/protein deactylases
    • Marmorstein, R. Structure and chemistry of the Sir2 family of NAD+-dependent histone/protein deactylases, Biochem. Soc. Trans., 2004, 32, 904-909.
    • (2004) Biochem. Soc. Trans , vol.32 , pp. 904-909
    • Marmorstein, R.1
  • 63
    • 0035662888 scopus 로고    scopus 로고
    • Structure of histone deacetylases: Insights into substrate recognition and catalysis
    • Marmorstein, R. Structure of histone deacetylases: insights into substrate recognition and catalysis, Structure, 2001, 9, 1127-1133.
    • (2001) Structure , vol.9 , pp. 1127-1133
    • Marmorstein, R.1
  • 64
    • 49349098483 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Mechanisms of cell death and promise in combination cancer therapy
    • Carew, J. S.; Giles, F. J.; Nawrocki, S. T. Histone deacetylase inhibitors: mechanisms of cell death and promise in combination cancer therapy, Cancer Lett., 2008, 269, 7-17.
    • (2008) Cancer Lett , vol.269 , pp. 7-17
    • Carew, J.S.1    Giles, F.J.2    Nawrocki, S.T.3
  • 65
    • 79952932076 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Molecular mechanisms of action and clinical trials as anti-cancer drugs
    • Kim, H. J.; Bae, S. C. Histone deacetylase inhibitors: molecular mechanisms of action and clinical trials as anti-cancer drugs, Am. J. Transl. Res., 2011, 3, 166-179.
    • (2011) Am. J. Transl. Res , vol.3 , pp. 166-179
    • Kim, H.J.1    Bae, S.C.2
  • 67
    • 20544473454 scopus 로고    scopus 로고
    • Depsipeptide inhibits migration of primary and metastatic uveal melanoma cell lines in vitro: A potential strategy for uveal melanoma
    • Klisovic, D. D.; Klisovic, M. I.; Effron, D.; Liu, S.; Marcucci, G.; Katz, S. E. Depsipeptide inhibits migration of primary and metastatic uveal melanoma cell lines in vitro: a potential strategy for uveal melanoma, Melanoma Res., 2005, 15, 147-153.
    • (2005) Melanoma Res , vol.15 , pp. 147-153
    • Klisovic, D.D.1    Klisovic, M.I.2    Effron, D.3    Liu, S.4    Marcucci, G.5    Katz, S.E.6
  • 68
    • 77950543254 scopus 로고    scopus 로고
    • Epigenetic modifiers as anticancer drugs: Effectiveness of valproic acid in neural crest-derived tumor cells
    • Papi, A.; Ferreri, A. M.; Rocchi, P.; Guerra, F.; Orlandi, M. Epigenetic modifiers as anticancer drugs: effectiveness of valproic acid in neural crest-derived tumor cells, Anticancer Res., 2010, 30, 535-540.
    • (2010) Anticancer Res , vol.30 , pp. 535-540
    • Papi, A.1    Ferreri, A.M.2    Rocchi, P.3    Guerra, F.4    Orlandi, M.5
  • 71
    • 0036401604 scopus 로고    scopus 로고
    • Trichostatin A-histone deacetylase inhibitor with clinical therapeutic potential-is also a selective and potent inhibitor of gelatinase A expression
    • Ailenberg, M.; Silverman, M. Trichostatin A-histone deacetylase inhibitor with clinical therapeutic potential-is also a selective and potent inhibitor of gelatinase A expression, Biochem. Biophys. Res. Commun., 2002, 298, 110-115.
    • (2002) Biochem. Biophys. Res. Commun , vol.298 , pp. 110-115
    • Ailenberg, M.1    Silverman, M.2
  • 72
    • 0037428248 scopus 로고    scopus 로고
    • Differential effects of trichostatin A on gelatinase A expression in 3T3 fibroblasts and HT-1080 fibrosarcoma cells: Implications for use of TSA in cancer therapy
    • Ailenberg, M.; Silverman, M. Differential effects of trichostatin A on gelatinase A expression in 3T3 fibroblasts and HT-1080 fibrosarcoma cells: implications for use of TSA in cancer therapy, Biochem. Biophys. Res. Commun., 2003, 302, 181-185.
    • (2003) Biochem. Biophys. Res. Commun , vol.302 , pp. 181-185
    • Ailenberg, M.1    Silverman, M.2
  • 73
    • 34047170360 scopus 로고    scopus 로고
    • Valproate induces widespread epigenetic reprogramming which involves demethylation of specific genes
    • Milutinovic, S.; D'Alessio, A. C.; Detich, N.; Szyf, M. Valproate induces widespread epigenetic reprogramming which involves demethylation of specific genes, Carcinogenesis, 2007, 28, 560-571.
    • (2007) Carcinogenesis , vol.28 , pp. 560-571
    • Milutinovic, S.1    D'Alessio, A.C.2    Detich, N.3    Szyf, M.4
  • 74
    • 0035951802 scopus 로고    scopus 로고
    • Identification of SWI.SNF complex subunit BAF60a as a determinant of the transactivation potential of Fos/Jun dimers
    • Ito, T.; Yamauchi, M.; Nishina, M.; Yamamichi, N.; Mizutani, T.; Ui, M.; Murakami, M.; Iba, H. Identification of SWI.SNF complex subunit BAF60a as a determinant of the transactivation potential of Fos/Jun dimers, J. Biol. Chem., 2001, 276, 2852-2857.
    • (2001) J. Biol. Chem , vol.276 , pp. 2852-2857
    • Ito, T.1    Yamauchi, M.2    Nishina, M.3    Yamamichi, N.4    Mizutani, T.5    Ui, M.6    Murakami, M.7    Iba, H.8
  • 75
    • 77958035725 scopus 로고    scopus 로고
    • Modulation of extracellular matrix/adhesion molecule expression by BRG1 is associated with increased melanoma invasiveness
    • Saladi, S. V.; Keenen, B.; Marathe, H. G.; Qi, H.; Chin, K. V.; de la Serna, I. L. Modulation of extracellular matrix/adhesion molecule expression by BRG1 is associated with increased melanoma invasiveness, Mol. Cancer., 2010, 9, 280.
    • (2010) Mol. Cancer , vol.9 , pp. 280
    • Saladi, S.V.1    Keenen, B.2    Marathe, H.G.3    Qi, H.4    Chin, K.V.5    de la Serna, I.L.6
  • 76
    • 73849126977 scopus 로고    scopus 로고
    • Heterogeneous SWI/SNF chromatin remodeling complexes promote expression of microphthalmia-associated transcription factor target genes in melanoma
    • Keenen, B.; Qi, H.; Saladi, S. V.; Yeung, M.; de la Serna, I. L. Heterogeneous SWI/SNF chromatin remodeling complexes promote expression of microphthalmia-associated transcription factor target genes in melanoma, Oncogene, 2010, 29, 81-92.
    • (2010) Oncogene , vol.29 , pp. 81-92
    • Keenen, B.1    Qi, H.2    Saladi, S.V.3    Yeung, M.4    de la Serna, I.L.5
  • 77
    • 76349100965 scopus 로고    scopus 로고
    • SWI/SNF chromatin remodeling complex is critical for the expression of microphthalmia-associated transcription factor in melanoma cells
    • Vachtenheim, J.; Ondrusova, L.; Borovansky, J. SWI/SNF chromatin remodeling complex is critical for the expression of microphthalmia-associated transcription factor in melanoma cells, Biochem. Biophys. Res. Commun., 2010, 392, 454-459.
    • (2010) Biochem. Biophys. Res. Commun , vol.392 , pp. 454-459
    • Vachtenheim, J.1    Ondrusova, L.2    Borovansky, J.3
  • 78
    • 2942617294 scopus 로고    scopus 로고
    • Coordination of cell signaling, chromatin remodeling, histone modifications, and regulator recruitment in human matrix metalloproteinase 9 gene transcription
    • Ma, Z.; Shah, R. C.; Chang, M. J.; Benveniste, E. N. Coordination of cell signaling, chromatin remodeling, histone modifications, and regulator recruitment in human matrix metalloproteinase 9 gene transcription, Mol. Cell. Biol., 2004, 24, 5496-5509.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 5496-5509
    • Ma, Z.1    Shah, R.C.2    Chang, M.J.3    Benveniste, E.N.4
  • 80
    • 45749116898 scopus 로고    scopus 로고
    • Protein kinase D-dependent phosphorylation and nuclear export of histone deacetylase 5 mediates vascular endothelial growth factor-induced gene expression and angiogenesis
    • Ha, C. H.; Wang, W.; Jhun, B. S.; Wong, C.; Hausser, A.; Pfizenmaier, K.; McKinsey, T. A.; Olson, E. N.; Jin, Z. G. Protein kinase D-dependent phosphorylation and nuclear export of histone deacetylase 5 mediates vascular endothelial growth factor-induced gene expression and angiogenesis, J. Biol. Chem., 2008, 283, 14590-14599.
    • (2008) J. Biol. Chem , vol.283 , pp. 14590-14599
    • Ha, C.H.1    Wang, W.2    Jhun, B.S.3    Wong, C.4    Hausser, A.5    Pfizenmaier, K.6    McKinsey, T.A.7    Olson, E.N.8    Jin, Z.G.9
  • 81
    • 33746228132 scopus 로고    scopus 로고
    • Histone deacetylase 7 maintains vascular integrity by repressing matrix metalloproteinase 10
    • Chang, S.; Young, B. D.; Li, S.; Qi, X.; Richardson, J. A.; Olson, E. N. Histone deacetylase 7 maintains vascular integrity by repressing matrix metalloproteinase 10, Cell, 2006, 126, 321-334.
    • (2006) Cell , vol.126 , pp. 321-334
    • Chang, S.1    Young, B.D.2    Li, S.3    Qi, X.4    Richardson, J.A.5    Olson, E.N.6
  • 82
    • 53449086522 scopus 로고    scopus 로고
    • VEGF stimulates HDAC7 phosphorylation and cytoplasmic accumulation modulating matrix metalloproteinase expression and angiogenesis
    • Ha, C. H.; Jhun, B. S.; Kao, H. Y.; Jin, Z. G. VEGF stimulates HDAC7 phosphorylation and cytoplasmic accumulation modulating matrix metalloproteinase expression and angiogenesis, Arterioscler. Thromb. Vasc. Biol., 2008, 28, 1782-1788.
    • (2008) Arterioscler. Thromb. Vasc. Biol , vol.28 , pp. 1782-1788
    • Ha, C.H.1    Jhun, B.S.2    Kao, H.Y.3    Jin, Z.G.4
  • 85
    • 11144221007 scopus 로고    scopus 로고
    • Apoptotic and autophagic cell death induced by histone deacetylase inhibitors
    • Shao, Y.; Gao, Z.; Marks, P. A.; Jiang, X. Apoptotic and autophagic cell death induced by histone deacetylase inhibitors, Proc. Natl. Acad. Sci. U S A, 2004, 101, 18030-18035.
    • (2004) Proc. Natl. Acad. Sci. U S A , vol.101 , pp. 18030-18035
    • Shao, Y.1    Gao, Z.2    Marks, P.A.3    Jiang, X.4


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