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Volumn 290, Issue 25, 2015, Pages 15812-15824

Inhibition of nicotinamide phosphoribosyltransferase (NAMPT), an enzyme essential for NAD+ biosynthesis, leads to altered carbohydrate metabolism in cancer cells

Author keywords

[No Author keywords available]

Indexed keywords

AMIDES; BIOCHEMISTRY; BIOSYNTHESIS; CARBOHYDRATES; CELLS; CYTOLOGY; DISEASES; ENZYMES; FRUCTOSE; GLUCOSE; METABOLISM; PATHOLOGY; PHYSIOLOGY;

EID: 84940055387     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.632141     Document Type: Article
Times cited : (43)

References (39)
  • 3
    • 62149150332 scopus 로고    scopus 로고
    • Niacin status, NAD distribution and ADP-ribose metabolism
    • Kirkland, J. B. (2009) Niacin status, NAD distribution and ADP-ribose metabolism. Curr. Pharm. Des. 15, 3-11
    • (2009) Curr. Pharm. Des. , vol.15 , pp. 3-11
    • Kirkland, J.B.1
  • 5
    • 40849119972 scopus 로고    scopus 로고
    • + and vitamin B3: From metabolism to therapies
    • + and vitamin B3: from metabolism to therapies. J. Pharmacol. Exp. Ther. 324, 883-893
    • (2008) J. Pharmacol. Exp. Ther. , vol.324 , pp. 883-893
    • Sauve, A.A.1
  • 6
    • 77953408297 scopus 로고    scopus 로고
    • A preclinical study on the rescue of normal tissue by nicotinic acid in highdose treatment with APO866, a specific nicotinamide phosphoribosyltransferase inhibitor
    • Olesen, U. H., Thougaard, A. V., Jensen, P. B., and Sehested, M. (2010) A preclinical study on the rescue of normal tissue by nicotinic acid in highdose treatment with APO866, a specific nicotinamide phosphoribosyltransferase inhibitor. Mol. Cancer Ther. 9, 1609-1617
    • (2010) Mol. Cancer Ther. , vol.9 , pp. 1609-1617
    • Olesen, U.H.1    Thougaard, A.V.2    Jensen, P.B.3    Sehested, M.4
  • 9
    • 10944270187 scopus 로고    scopus 로고
    • The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells
    • Revollo, J. R., Grimm, A. A., and Imai, S. (2004) The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells. J. Biol. Chem. 279, 50754-50763
    • (2004) J. Biol. Chem. , vol.279 , pp. 50754-50763
    • Revollo, J.R.1    Grimm, A.A.2    Imai, S.3
  • 10
    • 58149316660 scopus 로고    scopus 로고
    • Nicotinamide phosphoribosyl transferase/pre-B cell colony-enhancing factor/visfatin is required for lymphocyte development and cellular resistance to genotoxic stress
    • Rongvaux, A., Galli, M., Denanglaire, S., Van Gool, F., Drèze, P. L., Szpirer, C., Bureau, F., Andris, F., and Leo, O. (2008) Nicotinamide phosphoribosyl transferase/pre-B cell colony-enhancing factor/visfatin is required for lymphocyte development and cellular resistance to genotoxic stress. J. Immunol. 181, 4685-4695
    • (2008) J. Immunol. , vol.181 , pp. 4685-4695
    • Rongvaux, A.1    Galli, M.2    Denanglaire, S.3    Van Gool, F.4    Drèze, P.L.5    Szpirer, C.6    Bureau, F.7    Andris, F.8    Leo, O.9
  • 11
    • 62149148872 scopus 로고    scopus 로고
    • Nicotinamide phosphoribosyltransferase (NAMPT): A link between NAD biology, metabolism, and diseases
    • Imai, S. (2009) Nicotinamide phosphoribosyltransferase (NAMPT): A link between NAD biology, metabolism, and diseases. Curr. Pharm. Des. 15, 20-28
    • (2009) Curr. Pharm. Des. , vol.15 , pp. 20-28
    • Imai, S.1
  • 12
    • 34248357083 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide metabolism as an attractive target for drug discovery
    • Khan, J. A., Forouhar, F., Tao, X., and Tong, L. (2007) Nicotinamide adenine dinucleotide metabolism as an attractive target for drug discovery. Expert Opin. Ther. Targets 11, 695-705
    • (2007) Expert Opin. Ther. Targets , vol.11 , pp. 695-705
    • Khan, J.A.1    Forouhar, F.2    Tao, X.3    Tong, L.4
  • 13
    • 44449124774 scopus 로고    scopus 로고
    • Pre-B cell colony-enhancing factor (PBEF)/visfatin: A novel mediator of innate immunity
    • Luk, T., Malam, Z., and Marshall, J. C. (2008) Pre-B cell colony-enhancing factor (PBEF)/visfatin: a novel mediator of innate immunity. J. Leukoc. Biol. 83, 804-816
    • (2008) J. Leukoc. Biol. , vol.83 , pp. 804-816
    • Luk, T.1    Malam, Z.2    Marshall, J.C.3
  • 14
    • 80053142651 scopus 로고    scopus 로고
    • Overexpression of Nampt in gastric cancer and chemo-potentiating effects of the Nampt inhibitor FK866 in combination with fluorouracil
    • Bi, T. Q., Che, X. M., Liao, X. H., Zhang, D. J., Long, H. L., Li, H. J., and Zhao, W. (2011) Overexpression of Nampt in gastric cancer and chemo-potentiating effects of the Nampt inhibitor FK866 in combination with fluorouracil. Oncol. Rep. 26, 1251-1257
    • (2011) Oncol. Rep. , vol.26 , pp. 1251-1257
    • Bi, T.Q.1    Che, X.M.2    Liao, X.H.3    Zhang, D.J.4    Long, H.L.5    Li, H.J.6    Zhao, W.7
  • 15
    • 0033461164 scopus 로고    scopus 로고
    • A profile of differentially expressed genes in primary colorectal cancer using suppression subtractive hybridization
    • Hufton, S. E., Moerkerk, P. T., Brandwijk, R., de Bruïne, A. P., Arends, J. W., Hoogenboom, H. R. (1999) A profile of differentially expressed genes in primary colorectal cancer using suppression subtractive hybridization. FEBS Lett. 463, 77-82
    • (1999) FEBS Lett. , vol.463 , pp. 77-82
    • Hufton, S.E.1    Moerkerk, P.T.2    Brandwijk, R.3    De Bruïne, A.P.4    Arends, J.W.5    Hoogenboom, H.R.6
  • 16
    • 0037056219 scopus 로고    scopus 로고
    • Target validation for genomics using peptide-specific phage antibodies: A study of five gene products overexpressed in colorectal cancer
    • Van Beijnum, J. R., Moerkerk, P. T., Gerbers, A. J., De Bruïne, A. P., Arends, J. W., and Hoogenboom, H. R., and Hufton, S. E. (2002) Target validation for genomics using peptide-specific phage antibodies: a study of five gene products overexpressed in colorectal cancer. Int. J. Cancer 101, 118-127
    • (2002) Int. J. Cancer , vol.101 , pp. 118-127
    • Van Beijnum, J.R.1    Moerkerk, P.T.2    Gerbers, A.J.3    De Bruïne, A.P.4    Arends, J.W.5    Hoogenboom, H.R.6    Hufton, S.E.7
  • 17
    • 79952007931 scopus 로고    scopus 로고
    • NAMPT overexpression in prostate cancer and its contribution to tumor cell survival and stress response
    • Wang, B., Hasan, M. K., Alvarado, E., Yuan, H., Wu, H., and Chen, W. Y. (2011) NAMPT overexpression in prostate cancer and its contribution to tumor cell survival and stress response. Oncogene 30, 907-921
    • (2011) Oncogene , vol.30 , pp. 907-921
    • Wang, B.1    Hasan, M.K.2    Alvarado, E.3    Yuan, H.4    Wu, H.5    Chen, W.Y.6
  • 19
    • 48249105497 scopus 로고    scopus 로고
    • Pharmacological inhibition of nicotinamide phosphoribosyltransferase/visfatin enzymatic activity identifies a new inflammatory pathway linked to NAD
    • Busso, N., Karababa, M., Nobile, M., Rolaz, A., Van Gool, F., Galli, M., Leo, O., So, A., and De Smedt, T. (2008) Pharmacological inhibition of nicotinamide phosphoribosyltransferase/visfatin enzymatic activity identifies a new inflammatory pathway linked to NAD. PLoS One 3, e2267
    • (2008) PLoS One , vol.3
    • Busso, N.1    Karababa, M.2    Nobile, M.3    Rolaz, A.4    Van Gool, F.5    Galli, M.6    Leo, O.7    So, A.8    De Smedt, T.9
  • 20
    • 0242526050 scopus 로고    scopus 로고
    • FK866, a highly specific noncompetitive inhibitor of nicotinamide phosphoribosyltransferase, represents a novel mechanism for induction of tumor cell apoptosis
    • Hasmann, M., and Schemainda, I. (2003) FK866, a highly specific noncompetitive inhibitor of nicotinamide phosphoribosyltransferase, represents a novel mechanism for induction of tumor cell apoptosis. Cancer Res. 63, 7436-7442
    • (2003) Cancer Res. , vol.63 , pp. 7436-7442
    • Hasmann, M.1    Schemainda, I.2
  • 22
    • 0842333189 scopus 로고    scopus 로고
    • Antiangiogenic potency of FK866/K22.175, a new inhibitor of intracellular NAD biosynthesis, in murine renal cell carcinoma
    • Drevs, J., Löser, R., Rattel, B., and Esser, N. (2003) Antiangiogenic potency of FK866/K22.175, a new inhibitor of intracellular NAD biosynthesis, in murine renal cell carcinoma. Anticancer Res. 23, 4853-4858
    • (2003) Anticancer Res. , vol.23 , pp. 4853-4858
    • Drevs, J.1    Löser, R.2    Rattel, B.3    Esser, N.4
  • 30
    • 0033979904 scopus 로고    scopus 로고
    • Expression, purification, and characterization of natural mutants of human aldolase B: Role of quaternary structure in catalysis
    • Rellos, P., Sygusch, J., and Cox, T M. (2000) Expression, purification, and characterization of natural mutants of human aldolase B: role of quaternary structure in catalysis. J. Biol. Chem. 275, 1145-1151
    • (2000) J. Biol. Chem. , vol.275 , pp. 1145-1151
    • Rellos, P.1    Sygusch, J.2    Cox, T.M.3
  • 31
    • 0025085911 scopus 로고
    • Construction and properties of active chimeric enzymes between human aldolases A and B: Analysis of molecular regions which determine isozyme-specific functions
    • Kitajima, Y., Takasaki, Y., Takahashi, I., and Hori, K. (1990) Construction and properties of active chimeric enzymes between human aldolases A and B: analysis of molecular regions which determine isozyme-specific functions. J. Biol. Chem. 265, 17493-17498
    • (1990) J. Biol. Chem. , vol.265 , pp. 17493-17498
    • Kitajima, Y.1    Takasaki, Y.2    Takahashi, I.3    Hori, K.4
  • 32
    • 0028359507 scopus 로고
    • Human aldolase C: Characterization of the recombinant enzyme expressed in E. coli
    • Kusakabe, T., Motoki, K., and Hori, K. (1994) Human aldolase C: characterization of the recombinant enzyme expressed in E. coli. J. Biochem. 115, 1172-1177
    • (1994) J. Biochem. , vol.115 , pp. 1172-1177
    • Kusakabe, T.1    Motoki, K.2    Hori, K.3
  • 33
    • 0022244506 scopus 로고
    • The purification and properties of human liver ketohexokinase: A role for ketohexokinase and fructose-bisphosphate aldolase in the metabolic production of oxalate from xylitol
    • Bais, R., James, H. M., Rofe, A. M., and Conyers, R. A. (1985) The purification and properties of human liver ketohexokinase: a role for ketohexokinase and fructose-bisphosphate aldolase in the metabolic production of oxalate from xylitol. Biochem. J. 230, 53-60
    • (1985) Biochem. J. , vol.230 , pp. 53-60
    • Bais, R.1    James, H.M.2    Rofe, A.M.3    Conyers, R.A.4
  • 34
    • 53049096537 scopus 로고    scopus 로고
    • Characterization of mammalian sedoheptulokinase and mechanism of formation of erythritol in sedoheptulokinase deficiency
    • Kardon, T., Stroobant, V., Veiga-da-Cunha, M., and Schaftingen, E. V. (2008) Characterization of mammalian sedoheptulokinase and mechanism of formation of erythritol in sedoheptulokinase deficiency. FEBS Lett. 582, 3330-3334
    • (2008) FEBS Lett. , vol.582 , pp. 3330-3334
    • Kardon, T.1    Stroobant, V.2    Veiga-da-Cunha, M.3    Schaftingen, E.V.4
  • 36
    • 0017058392 scopus 로고
    • Evolution of enzyme function and the development of catalytic efficiency
    • Albery, W. J., and Knowles, J. R. (1976) Evolution of enzyme function and the development of catalytic efficiency. Biochemistry 15, 5631-5640
    • (1976) Biochemistry , vol.15 , pp. 5631-5640
    • Albery, W.J.1    Knowles, J.R.2
  • 37
    • 78651330006 scopus 로고    scopus 로고
    • Triosephosphate isomerase: A highly evolved biocatalyst
    • Wierenga, R. K., Kapetaniou, E. G., and Venkatesan, R. (2010) Triosephosphate isomerase: a highly evolved biocatalyst. Cell Mol. Life Sci. 67, 3961-3982
    • (2010) Cell Mol. Life Sci. , vol.67 , pp. 3961-3982
    • Wierenga, R.K.1    Kapetaniou, E.G.2    Venkatesan, R.3
  • 39
    • 84884239694 scopus 로고    scopus 로고
    • Structural basis for regulation of human glucokinase by glucokinase regulatory protein
    • Beck, T., and Miller, B. G. (2013) Structural basis for regulation of human glucokinase by glucokinase regulatory protein. Biochemistry 52, 6232-6239
    • (2013) Biochemistry , vol.52 , pp. 6232-6239
    • Beck, T.1    Miller, B.G.2


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