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Volumn 2 SEP, Issue , 2012, Pages

MAP17, a ROS-dependent oncogene

Author keywords

Cancer; MAP17; Oncogene; Reactive oxygen species; Tumorigenesis

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; MAP 17; MEMBRANE PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG;

EID: 84891656589     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2012.00112     Document Type: Short Survey
Times cited : (16)

References (66)
  • 1
    • 0034695441 scopus 로고    scopus 로고
    • Reactive oxygen species activate p90 ribosomal S6 kinase via Fyn and Ras
    • Abe, J., Okuda, M., Huang, Q., Yoshizumi, M., and Berk, B. C. (2000). Reactive oxygen species activate p90 ribosomal S6 kinase via Fyn and Ras. J. Biol. Chem. 275, 1739-1748.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1739-1748
    • Abe, J.1    Okuda, M.2    Huang, Q.3    Yoshizumi, M.4    Berk, B.C.5
  • 2
    • 0033963704 scopus 로고    scopus 로고
    • Oxidative stress and gene regulation
    • Allen, R. G., and Tresini, M. (2000). Oxidative stress and gene regulation. Free Radic. Biol. Med. 28, 463-499.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 463-499
    • Allen, R.G.1    Tresini, M.2
  • 5
    • 84861422324 scopus 로고    scopus 로고
    • Rethinking glycolysis: on the biochemical logic of metabolic pathways
    • Bar-Even, A., Flamholz, A., Noor, E., and Milo, R. (2012). Rethinking glycolysis: on the biochemical logic of metabolic pathways. Nat. Chem. Biol. 8, 509-517.
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 509-517
    • Bar-Even, A.1    Flamholz, A.2    Noor, E.3    Milo, R.4
  • 8
    • 0029902928 scopus 로고    scopus 로고
    • Control of cell proliferation by reactive oxygen species
    • Burdon, R. H. (1996). Control of cell proliferation by reactive oxygen species. Biochem. Soc. Trans. 24, 1028-1032.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 1028-1032
    • Burdon, R.H.1
  • 10
    • 25844528025 scopus 로고    scopus 로고
    • The role of disturbed pH dynamics and the Na+/H+ exchanger in metastasis
    • Cardone, R. A., Casavola, V., and Reshkin, S. J. (2005). The role of disturbed pH dynamics and the Na+/H+ exchanger in metastasis. Nat. Rev. Cancer 5, 786-795.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 786-795
    • Cardone, R.A.1    Casavola, V.2    Reshkin, S.J.3
  • 11
    • 84859497390 scopus 로고    scopus 로고
    • MAP17 and the double-edged sword of ROS
    • Carnero, A. (2012). MAP17 and the double-edged sword of ROS. Biochim. Biophys. Acta 1826, 44-52.
    • (2012) Biochim. Biophys. Acta , vol.1826 , pp. 44-52
    • Carnero, A.1
  • 12
    • 0034209908 scopus 로고    scopus 로고
    • Loss-of-function genetics in mammalian cells: the p53 tumor suppressor model
    • Carnero, A., Hudson, J. D., Hannon, G. J., and Beach, D. H. (2000). Loss-of-function genetics in mammalian cells: the p53 tumor suppressor model. Nucleic Acids Res. 28, 2234-2241.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2234-2241
    • Carnero, A.1    Hudson, J.D.2    Hannon, G.J.3    Beach, D.H.4
  • 13
    • 77953935500 scopus 로고    scopus 로고
    • Tumour hypoxia induces a metabolic shift causing acidosis: a common feature in cancer
    • Chiche, J., Brahimi-Horn, M. C., and Pouyssegur, J. (2010). Tumour hypoxia induces a metabolic shift causing acidosis: a common feature in cancer. J. Cell. Mol. Med. 14, 771-794.
    • (2010) J. Cell. Mol. Med. , vol.14 , pp. 771-794
    • Chiche, J.1    Brahimi-Horn, M.C.2    Pouyssegur, J.3
  • 15
    • 34250022861 scopus 로고    scopus 로고
    • NHE3 inhibition by cAMP and Ca2+ is abolished in PDZ-domain protein PDZK1-deficient murine enterocytes
    • Cinar, A., Chen, M., Riederer, B., Bachmann, O., Wiemann, M., Manns, M., Kocher, O., and Seidler, U. (2007). NHE3 inhibition by cAMP and Ca2+ is abolished in PDZ-domain protein PDZK1-deficient murine enterocytes. J. Physiol. 581, 1235-1246.
    • (2007) J. Physiol. , vol.581 , pp. 1235-1246
    • Cinar, A.1    Chen, M.2    Riederer, B.3    Bachmann, O.4    Wiemann, M.5    Manns, M.6    Kocher, O.7    Seidler, U.8
  • 18
    • 77956181523 scopus 로고    scopus 로고
    • Role of NHERF and scaffolding proteins in proximal tubule transport
    • Cunningham, R., Biswas, R., Steplock, D., Shenolikar, S., and Weinman, E. (2010). Role of NHERF and scaffolding proteins in proximal tubule transport. Urol. Res. 38, 257-262.
    • (2010) Urol. Res. , vol.38 , pp. 257-262
    • Cunningham, R.1    Biswas, R.2    Steplock, D.3    Shenolikar, S.4    Weinman, E.5
  • 20
    • 20344385528 scopus 로고    scopus 로고
    • Transcriptional regulation of the SCL locus: identification of an enhancer that targets the primitive erythroid lineage in vivo
    • Delabesse, E., Ogilvy, S., Chapman, M. A., Piltz, S. G., Gottgens, B., and Green, A. R. (2005). Transcriptional regulation of the SCL locus: identification of an enhancer that targets the primitive erythroid lineage in vivo. Mol. Cell. Biol. 25, 5215-5225.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5215-5225
    • Delabesse, E.1    Ogilvy, S.2    Chapman, M.A.3    Piltz, S.G.4    Gottgens, B.5    Green, A.R.6
  • 21
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge, W. (2002). Free radicals in the physiological control of cell function. Physiol. Rev. 82, 47-95.
    • (2002) Physiol. Rev. , vol.82 , pp. 47-95
    • Droge, W.1
  • 22
    • 33646853458 scopus 로고    scopus 로고
    • Direct oxidative modifications of signalling proteins in mammalian cells and their effects on apoptosis
    • England, K., and Cotter, T. G. (2005). Direct oxidative modifications of signalling proteins in mammalian cells and their effects on apoptosis. Redox Rep. 10, 237-245.
    • (2005) Redox Rep. , vol.10 , pp. 237-245
    • England, K.1    Cotter, T.G.2
  • 23
    • 0020057408 scopus 로고
    • Correlation between the loss of the transformed phenotype and an increase in superoxide dismutase activity in a revertant subclone of sarcoma virus-infected mammalian cells
    • Fernandez-Pol, J. A., Hamilton, P. D., and Klos, D. J. (1982). Correlation between the loss of the transformed phenotype and an increase in superoxide dismutase activity in a revertant subclone of sarcoma virus-infected mammalian cells. Cancer Res. 42, 609-617.
    • (1982) Cancer Res. , vol.42 , pp. 609-617
    • Fernandez-Pol, J.A.1    Hamilton, P.D.2    Klos, D.J.3
  • 24
    • 0032053707 scopus 로고    scopus 로고
    • Oxygen radicals and signaling
    • Finkel, T. (1998). Oxygen radicals and signaling. Curr. Opin. Cell Biol. 10, 248-253.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 248-253
    • Finkel, T.1
  • 26
    • 0037458667 scopus 로고    scopus 로고
    • The PDZ-binding chloride channel ClC-3B localizes to the Golgi and associates with cystic fibrosis transmembrane conductance regulator-interacting PDZ proteins
    • Gentzsch, M., Cui, L., Mengos, A., Chang, X. B., Chen, J. H., and Riordan, J. R. (2003). The PDZ-binding chloride channel ClC-3B localizes to the Golgi and associates with cystic fibrosis transmembrane conductance regulator-interacting PDZ proteins. J. Biol. Chem. 278, 6440-6449.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6440-6449
    • Gentzsch, M.1    Cui, L.2    Mengos, A.3    Chang, X.B.4    Chen, J.H.5    Riordan, J.R.6
  • 29
    • 34247541694 scopus 로고    scopus 로고
    • Large scale genetic screen identifies MAP17 as protein bypassing TNF-induced growth arrest
    • Guijarro, M. V., Castro, M. E., Romero, L., Moneo, V., and Carnero, A. (2007a). Large scale genetic screen identifies MAP17 as protein bypassing TNF-induced growth arrest. J. Cell. Biochem. 101, 112-121.
    • (2007) J. Cell. Biochem. , vol.101 , pp. 112-121
    • Guijarro, M.V.1    Castro, M.E.2    Romero, L.3    Moneo, V.4    Carnero, A.5
  • 32
    • 36949008406 scopus 로고    scopus 로고
    • MAP17 inhibits Myc-induced apoptosis through PI3K/AKT pathway activation
    • Guijarro, M. V., Link, W., Rosado, A., Leal, J. F., and Carnero, A. (2007d). MAP17 inhibits Myc-induced apoptosis through PI3K/AKT pathway activation. Carcinogenesis 28, 2443-2450.
    • (2007) Carcinogenesis , vol.28 , pp. 2443-2450
    • Guijarro, M.V.1    Link, W.2    Rosado, A.3    Leal, J.F.4    Carnero, A.5
  • 34
    • 0027361046 scopus 로고
    • Redox modulation of p53 conformation and sequence-specific DNA binding in vitro
    • Hainaut, P., and Milner, J. (1993). Redox modulation of p53 conformation and sequence-specific DNA binding in vitro. Cancer Res. 53, 4469-4473.
    • (1993) Cancer Res. , vol.53 , pp. 4469-4473
    • Hainaut, P.1    Milner, J.2
  • 35
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D., and Weinberg, R. (2000). The hallmarks of cancer. Cell 100, 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.2
  • 36
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: the next generation
    • Hanahan, D., and Weinberg, R. A. (2011). Hallmarks of cancer: the next generation. Cell 144, 646-674.
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 39
    • 3042683879 scopus 로고    scopus 로고
    • Overexpression of PDZK1 within the 1q12-q22 amplicon is likely to be associated with drug-resistance phenotype in multiple myeloma
    • Inoue, J., Otsuki, T., Hirasawa, A., Imoto, I., Matsuo, Y., Shimizu, S., Taniwaki, M., and Inazawa, J. (2004). Overexpression of PDZK1 within the 1q12-q22 amplicon is likely to be associated with drug-resistance phenotype in multiple myeloma. Am. J. Pathol. 165, 71-81.
    • (2004) Am. J. Pathol. , vol.165 , pp. 71-81
    • Inoue, J.1    Otsuki, T.2    Hirasawa, A.3    Imoto, I.4    Matsuo, Y.5    Shimizu, S.6    Taniwaki, M.7    Inazawa, J.8
  • 41
    • 0033832036 scopus 로고    scopus 로고
    • The membrane-associated protein pKe#192/MAP17 in human keratinocytes
    • Jaeger, C., Schaefer, B., Wallich, R., and Kramer, M. (2000). The membrane-associated protein pKe#192/MAP17 in human keratinocytes. J. Invest. Dermatol. 115, 375-380.
    • (2000) J. Invest. Dermatol. , vol.115 , pp. 375-380
    • Jaeger, C.1    Schaefer, B.2    Wallich, R.3    Kramer, M.4
  • 42
    • 84862271827 scopus 로고    scopus 로고
    • PDZ domain-containing 1 (PDZK1) protein regulates phospholipase C-beta3 (PLC-beta3)-specific activation of somatostatin by forming a ternary complex with PLC-beta3 and somatostatin receptors
    • Kim, J. K., Kwon, O., Kim, J., Kim, E. K., Park, H. K., Lee, J. E., Kim, K. L., Choi, J. W., Lim, S., Seok, H., Lee-Kwon, W., Choi, J. H., Kang, B. H., Kim, S., Ryu, S. H., and Suh, P. G. (2012). PDZ domain-containing 1 (PDZK1) protein regulates phospholipase C-beta3 (PLC-beta3)-specific activation of somatostatin by forming a ternary complex with PLC-beta3 and somatostatin receptors. J. Biol. Chem. 287, 21012-21024.
    • (2012) J. Biol. Chem. , vol.287 , pp. 21012-21024
    • Kim, J.K.1    Kwon, O.2    Kim, J.3    Kim, E.K.4    Park, H.K.5    Lee, J.E.6    Kim, K.L.7    Choi, J.W.8    Lim, S.9    Seok, H.10    Lee-Kwon, W.11    Choi, J.H.12    Kang, B.H.13    Kim, S.14    Ryu, S.H.15    Suh, P.G.16
  • 44
    • 0028871496 scopus 로고
    • Identification of a novel gene, selectively up-regulated in human carcinomas, using the differential display technique
    • Kocher, O., Cheresh, P., Brown, L. F., and Lee, S. W. (1995). Identification of a novel gene, selectively up-regulated in human carcinomas, using the differential display technique. Clin. Cancer Res. 1, 1209-1215.
    • (1995) Clin. Cancer Res. , vol.1 , pp. 1209-1215
    • Kocher, O.1    Cheresh, P.2    Brown, L.F.3    Lee, S.W.4
  • 45
    • 0030017442 scopus 로고    scopus 로고
    • Identification and partial characterization of a novel mem-brane-associated protein (MAP17) up-regulated in human carcinomas and modulating cell replication and tumor growth
    • Kocher, O., Cheresh, P., and Lee, S. W. (1996). Identification and partial characterization of a novel mem-brane-associated protein (MAP17) up-regulated in human carcinomas and modulating cell replication and tumor growth. Am. J. Pathol. 149, 493-500.
    • (1996) Am. J. Pathol. , vol.149 , pp. 493-500
    • Kocher, O.1    Cheresh, P.2    Lee, S.W.3
  • 47
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • Lee, S. R., Kwon, K. S., Kim, S. R., and Rhee, S. G. (1998). Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J. Biol. Chem. 273, 15366-15372.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15366-15372
    • Lee, S.R.1    Kwon, K.S.2    Kim, S.R.3    Rhee, S.G.4
  • 50
    • 0027459024 scopus 로고
    • Activation of endothelial cell phospholipase D by hydrogen peroxide and fatty acid hydroperoxide
    • Natarajan, V., Taher, M. M., Roehm, B., Parinandi, N. L., Schmid, H. H., Kiss, Z., and Garcia, J. G. (1993). Activation of endothelial cell phospholipase D by hydrogen peroxide and fatty acid hydroperoxide. J. Biol. Chem. 268, 930-937.
    • (1993) J. Biol. Chem. , vol.268 , pp. 930-937
    • Natarajan, V.1    Taher, M.M.2    Roehm, B.3    Parinandi, N.L.4    Schmid, H.H.5    Kiss, Z.6    Garcia, J.G.7
  • 51
    • 78649659788 scopus 로고    scopus 로고
    • pH control mechanisms of tumor survival and growth
    • Parks, S. K., Chiche, J., and Pouyssegur, J. (2011). pH control mechanisms of tumor survival and growth. J. Cell. Physiol. 226, 299-308.
    • (2011) J. Cell. Physiol. , vol.226 , pp. 299-308
    • Parks, S.K.1    Chiche, J.2    Pouyssegur, J.3
  • 53
    • 84857116578 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
    • Ray, P. D., Huang, B. W., and Tsuji, Y. (2012). Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling. Cell. Signal. 24, 981-990.
    • (2012) Cell. Signal. , vol.24 , pp. 981-990
    • Ray, P.D.1    Huang, B.W.2    Tsuji, Y.3
  • 54
    • 0029170274 scopus 로고
    • The roles of hydrogen peroxide and superoxide as messengers in the activation of transcription factor NF-kappa B
    • Schmidt, K. N., Amstad, P., Cerutti, P., and Baeuerle, P. A. (1995). The roles of hydrogen peroxide and superoxide as messengers in the activation of transcription factor NF-kappa B. Chem. Biol. 2, 13-22.
    • (1995) Chem. Biol. , vol.2 , pp. 13-22
    • Schmidt, K.N.1    Amstad, P.2    Cerutti, P.3    Baeuerle, P.A.4
  • 56
    • 0041707710 scopus 로고    scopus 로고
    • Identification of small PDZK1-associated protein, DD96/MAP17, as a regulator of PDZK1 and plasma high density lipoprotein levels
    • Silver, D. L., Wang, N., and Vogel, S. (2003). Identification of small PDZK1-associated protein, DD96/MAP17, as a regulator of PDZK1 and plasma high density lipoprotein levels. J. Biol. Chem. 278, 28528-28532.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28528-28532
    • Silver, D.L.1    Wang, N.2    Vogel, S.3
  • 57
    • 38949105541 scopus 로고    scopus 로고
    • Independent activation of Akt and NF-kappaB pathways and their role in resistance to TNF-alpha mediated cytotoxicity in gliomas
    • Sudheerkumar, P., Shiras, A., Das, G., Jagtap, J. C., Prasad, V., and Shastry, P. (2008). Independent activation of Akt and NF-kappaB pathways and their role in resistance to TNF-alpha mediated cytotoxicity in gliomas. Mol. Carcinog. 47, 126-136.
    • (2008) Mol. Carcinog. , vol.47 , pp. 126-136
    • Sudheerkumar, P.1    Shiras, A.2    Das, G.3    Jagtap, J.C.4    Prasad, V.5    Shastry, P.6
  • 60
    • 34247262095 scopus 로고    scopus 로고
    • NHERF links the N-cadherin/catenin complex to the platelet-derived growth factor receptor to modulate the actin cytoskeleton and regulate cell motility
    • Theisen, C. S., Wahl, J. K. III, Johnson, K. R., and Wheelock, M. J. (2007). NHERF links the N-cadherin/catenin complex to the platelet-derived growth factor receptor to modulate the actin cytoskeleton and regulate cell motility. Mol. Biol. Cell 18, 1220-1232.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1220-1232
    • Theisen, C.S.1    Wahl III, J.K.2    Johnson, K.R.3    Wheelock, M.J.4
  • 61
    • 77955966139 scopus 로고    scopus 로고
    • Bypassing cellular senescence by genetic screening tools
    • Vergel, M., and Carnero, A. (2010). Bypassing cellular senescence by genetic screening tools. Clin. Transl. Oncol. 12, 410-417.
    • (2010) Clin. Transl. Oncol. , vol.12 , pp. 410-417
    • Vergel, M.1    Carnero, A.2
  • 62
    • 84655169936 scopus 로고    scopus 로고
    • Tumor suppressor genes and ROS: complex networks of interactions
    • Vurusaner, B., Poli, G., and Basaga, H. (2012). Tumor suppressor genes and ROS: complex networks of interactions. Free Radic. Biol. Med. 52, 7-18.
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 7-18
    • Vurusaner, B.1    Poli, G.2    Basaga, H.3
  • 63
    • 77951527059 scopus 로고    scopus 로고
    • Sodium-hydrogen exchanger regulatory factor 1 (NHERF-1) transduces signals that mediate dopamine inhibition of sodium-phosphate co-transport in mouse kidney
    • Weinman, E. J., Biswas, R., Steplock, D., Douglass, T. S., Cunningham, R., and Shenolikar, S. (2010). Sodium-hydrogen exchanger regulatory factor 1 (NHERF-1) transduces signals that mediate dopamine inhibition of sodium-phosphate co-transport in mouse kidney. J. Biol. Chem. 285, 13454-13460.
    • (2010) J. Biol. Chem. , vol.285 , pp. 13454-13460
    • Weinman, E.J.1    Biswas, R.2    Steplock, D.3    Douglass, T.S.4    Cunningham, R.5    Shenolikar, S.6
  • 64
    • 0033520497 scopus 로고    scopus 로고
    • Stable overexpression of manganese superoxide dismutase in mitochondria identifies hydrogen peroxide as a major oxidant in the AP-1-mediated induction of matrix-degrading metalloprotease-1
    • Wenk, J., Brenneisen, P., Wlaschek, M., Poswig, A., Briviba, K., Oberley, T. D., and Scharffetter-Kochanek, K. (1999). Stable overexpression of manganese superoxide dismutase in mitochondria identifies hydrogen peroxide as a major oxidant in the AP-1-mediated induction of matrix-degrading metalloprotease-1. J. Biol. Chem. 274, 25869-25876.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25869-25876
    • Wenk, J.1    Brenneisen, P.2    Wlaschek, M.3    Poswig, A.4    Briviba, K.5    Oberley, T.D.6    Scharffetter-Kochanek, K.7
  • 65
    • 84863287281 scopus 로고    scopus 로고
    • Bradykinin prevents the apoptosis of NIT-1 cells induced by TNF-alpha via the PI3K/Akt and MAPK signaling pathways
    • Xu, X., Tu, L., Jiang, W., Feng, W., Zhao, C. X., and Wang, D. W. (2012). Bradykinin prevents the apoptosis of NIT-1 cells induced by TNF-alpha via the PI3K/Akt and MAPK signaling pathways. Int. J. Mol. Med. 29, 891-898.
    • (2012) Int. J. Mol. Med. , vol.29 , pp. 891-898
    • Xu, X.1    Tu, L.2    Jiang, W.3    Feng, W.4    Zhao, C.X.5    Wang, D.W.6
  • 66
    • 0029886717 scopus 로고    scopus 로고
    • Manganese-containing superoxide dismutase overexpression causes phenotypic reversion in SV40-transformed human lung fibroblasts
    • Yan, T., Oberley, L. W., Zhong, W., and St Clair, D. K. (1996). Manganese-containing superoxide dismutase overexpression causes phenotypic reversion in SV40-transformed human lung fibroblasts. Cancer Res. 56, 2864-2871.
    • (1996) Cancer Res. , vol.56 , pp. 2864-2871
    • Yan, T.1    Oberley, L.W.2    Zhong, W.3    St Clair, D.K.4


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