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Volumn 13, Issue 2, 2014, Pages 786-795

Overexpression of CD38 decreases cellular NAD levels and alters the expression of proteins involved in energy metabolism and antioxidant defense

Author keywords

CD38; chaperones; glycolytic enzymes; oxidative stress; proteomics

Indexed keywords

ANTIGENS, CD38; ANTIOXIDANTS; BLOTTING, WESTERN; DNA REPAIR; ENERGY METABOLISM; HEK293 CELLS; HUMANS; NAD; OXIDATIVE STRESS; POLYMERASE CHAIN REACTION;

EID: 84893854576     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr4010597     Document Type: Article
Times cited : (42)

References (51)
  • 1
    • 1542346420 scopus 로고    scopus 로고
    • The new life of a centenarian: Signalling functions of NAD (P)
    • Berger, F.; RamIrez-Hernandez, M. H.; Ziegler, M. The new life of a centenarian: signalling functions of NAD (P) Trends Biochem. Sci. 2004, 29 (3) 111-118
    • (2004) Trends Biochem. Sci. , vol.29 , Issue.3 , pp. 111-118
    • Berger, F.1    Ramirez-Hernandez, M.H.2    Ziegler, M.3
  • 3
    • 84867877340 scopus 로고    scopus 로고
    • The NAD metabolome - A key determinant of cancer cell biology
    • Chiarugi, A.; Dölle, C.; Felici, R.; Ziegler, M. The NAD metabolome-a key determinant of cancer cell biology Nat. Rev. Cancer 2012, 12 (11) 741-752
    • (2012) Nat. Rev. Cancer , vol.12 , Issue.11 , pp. 741-752
    • Chiarugi, A.1    Dölle, C.2    Felici, R.3    Ziegler, M.4
  • 4
    • 34547607850 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide: Beyond a redox coenzyme
    • Lin, H. Nicotinamide adenine dinucleotide: beyond a redox coenzyme Org. Biomol. Chem. 2007, 5 (16) 2541-2554
    • (2007) Org. Biomol. Chem. , vol.5 , Issue.16 , pp. 2541-2554
    • Lin, H.1
  • 5
    • 37549068090 scopus 로고    scopus 로고
    • NAD+/NADH and NADP+/NADPH in cellular functions and cell death: Regulation and biological consequences
    • Ying, W. NAD+/NADH and NADP+/NADPH in cellular functions and cell death: regulation and biological consequences Antioxid. Redox Signaling 2008, 10 (2) 179-206
    • (2008) Antioxid. Redox Signaling , vol.10 , Issue.2 , pp. 179-206
    • Ying, W.1
  • 7
    • 0040518650 scopus 로고    scopus 로고
    • A covalent intermediate in CD38 is responsible for ADP-ribosylation and cyclization reactions
    • Sauve, A. A.; Deng, H.; Angeletti, R. H.; Schramm, V. L. A covalent intermediate in CD38 is responsible for ADP-ribosylation and cyclization reactions J. Am. Chem. Soc. 2000, 122 (33) 7855-7859
    • (2000) J. Am. Chem. Soc. , vol.122 , Issue.33 , pp. 7855-7859
    • Sauve, A.A.1    Deng, H.2    Angeletti, R.H.3    Schramm, V.L.4
  • 9
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander, G.; Guarente, L. The Sir2 family of protein deacetylases Annu. Rev. Biochem. 2004, 73 (1) 417-435
    • (2004) Annu. Rev. Biochem. , vol.73 , Issue.1 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 10
    • 0035313756 scopus 로고    scopus 로고
    • Enzymatic activities of Sir2 and chromatin silencing
    • Moazed, D. Enzymatic activities of Sir2 and chromatin silencing Curr. Opin. Cell Biol. 2001, 13 (2) 232-238
    • (2001) Curr. Opin. Cell Biol. , vol.13 , Issue.2 , pp. 232-238
    • Moazed, D.1
  • 11
    • 0035951072 scopus 로고    scopus 로고
    • Chemistry of gene silencing: The mechanism of NAD+-dependent deacetylation reactions
    • Sauve, A. A.; Celic, I.; Avalos, J.; Deng, H.; Boeke, J. D.; Schramm, V. L. Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions Biochemistry 2001, 40 (51) 15456-15463
    • (2001) Biochemistry , vol.40 , Issue.51 , pp. 15456-15463
    • Sauve, A.A.1    Celic, I.2    Avalos, J.3    Deng, H.4    Boeke, J.D.5    Schramm, V.L.6
  • 12
    • 25144496904 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Denu, J. M. The Sir2 family of protein deacetylases Curr. Opin. Chem. Biol. 2005, 9 (5) 431-440
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , Issue.5 , pp. 431-440
    • Denu, J.M.1
  • 13
    • 84858797015 scopus 로고    scopus 로고
    • Sirtuins and calorie restriction
    • Guarente, L. Sirtuins and calorie restriction Nat. Rev. Mol. Cell Biol. 2012, 13 (4) 207
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , Issue.4 , pp. 207
    • Guarente, L.1
  • 14
    • 84859977895 scopus 로고    scopus 로고
    • Sirtuins mediate mammalian metabolic responses to nutrient availability
    • Chalkiadaki, A.; Guarente, L. Sirtuins mediate mammalian metabolic responses to nutrient availability Nat. Rev. Endocrinol. 2012, 8 (5) 287-296
    • (2012) Nat. Rev. Endocrinol. , vol.8 , Issue.5 , pp. 287-296
    • Chalkiadaki, A.1    Guarente, L.2
  • 15
    • 33750445309 scopus 로고    scopus 로고
    • NAD metabolism and sirtuins: Metabolic regulation of protein deacetylation in stress and toxicity
    • Yang, T.; Sauve, A. A. NAD metabolism and sirtuins: metabolic regulation of protein deacetylation in stress and toxicity AAPS J. 2006, 8 (4) E632-E643
    • (2006) AAPS J. , vol.8 , Issue.4
    • Yang, T.1    Sauve, A.A.2
  • 16
    • 78649482634 scopus 로고    scopus 로고
    • SIRT1: Recent lessons from mouse models
    • Herranz, D.; Serrano, M. SIRT1: recent lessons from mouse models Nat. Rev. Cancer 2010, 10 (12) 819-823
    • (2010) Nat. Rev. Cancer , vol.10 , Issue.12 , pp. 819-823
    • Herranz, D.1    Serrano, M.2
  • 17
    • 79955661471 scopus 로고    scopus 로고
    • Mammalian Sirt1: Insights on its biological functions
    • Rahman, S.; Islam, R. Mammalian Sirt1: insights on its biological functions Cell Commun. Signal 2011, 9 (11) 11
    • (2011) Cell Commun. Signal , vol.9 , Issue.11 , pp. 11
    • Rahman, S.1    Islam, R.2
  • 18
    • 77953290752 scopus 로고    scopus 로고
    • SIRT1-dependent regulation of chromatin and transcription: Linking NAD+ metabolism and signaling to the control of cellular functions
    • Zhang, T.; Kraus, W. L. SIRT1-dependent regulation of chromatin and transcription: Linking NAD+ metabolism and signaling to the control of cellular functions Biochim. Biophys Acta, Proteins Proteomics 2010, 1804 (8) 1666-1675
    • (2010) Biochim. Biophys Acta, Proteins Proteomics , vol.1804 , Issue.8 , pp. 1666-1675
    • Zhang, T.1    Kraus, W.L.2
  • 19
    • 62149130110 scopus 로고    scopus 로고
    • Cellular regulation of SIRT1
    • Milner, J. Cellular regulation of SIRT1 Curr. Pharm. Des. 2009, 15 (1) 39-44
    • (2009) Curr. Pharm. Des. , vol.15 , Issue.1 , pp. 39-44
    • Milner, J.1
  • 20
    • 34547875773 scopus 로고    scopus 로고
    • Sirtuins: Critical regulators at the crossroads between cancer and aging
    • Saunders, L.; Verdin, E. Sirtuins: critical regulators at the crossroads between cancer and aging Oncogene 2007, 26 (37) 5489-5504
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5489-5504
    • Saunders, L.1    Verdin, E.2
  • 21
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: Biological insights and disease relevance
    • Haigis, M. C.; Sinclair, D. A. Mammalian sirtuins: biological insights and disease relevance Annu. Rev. Pathol. 2010, 5, 253-295
    • (2010) Annu. Rev. Pathol. , vol.5 , pp. 253-295
    • Haigis, M.C.1    Sinclair, D.A.2
  • 23
    • 33746824192 scopus 로고    scopus 로고
    • Neuronal SIRT1 activation as a novel mechanism underlying the prevention of Alzheimer disease amyloid neuropathology by calorie restriction
    • Qin, W.; Yang, T.; Ho, L.; Zhao, Z.; Wang, J.; Chen, L.; Zhao, W.; Thiyagarajan, M.; MacGrogan, D.; Rodgers, J. T. Neuronal SIRT1 activation as a novel mechanism underlying the prevention of Alzheimer disease amyloid neuropathology by calorie restriction J. Biol. Chem. 2006, 281 (31) 21745-21754
    • (2006) J. Biol. Chem. , vol.281 , Issue.31 , pp. 21745-21754
    • Qin, W.1    Yang, T.2    Ho, L.3    Zhao, Z.4    Wang, J.5    Chen, L.6    Zhao, W.7    Thiyagarajan, M.8    MacGrogan, D.9    Rodgers, J.T.10
  • 24
    • 62149085241 scopus 로고    scopus 로고
    • Pharmaceutical strategies for activating sirtuins
    • Sauve, A. A. Pharmaceutical strategies for activating sirtuins Curr. Pharm. Des. 2009, 15 (1) 45-56
    • (2009) Curr. Pharm. Des. , vol.15 , Issue.1 , pp. 45-56
    • Sauve, A.A.1
  • 25
    • 53249121556 scopus 로고    scopus 로고
    • Sirtuins - Novel therapeutic targets to treat age-associated diseases
    • Lavu, S.; Boss, O.; Elliott, P. J.; Lambert, P. D. Sirtuins-novel therapeutic targets to treat age-associated diseases Nat. Rev. Drug Discovery 2008, 7 (10) 841-853
    • (2008) Nat. Rev. Drug Discovery , vol.7 , Issue.10 , pp. 841-853
    • Lavu, S.1    Boss, O.2    Elliott, P.J.3    Lambert, P.D.4
  • 28
    • 79952590211 scopus 로고    scopus 로고
    • A role for SIRT1 in the hypoxic response
    • Leiser, S. F.; Kaeberlein, M. A role for SIRT1 in the hypoxic response Mol. Cell 2010, 38 (6) 779-780
    • (2010) Mol. Cell , vol.38 , Issue.6 , pp. 779-780
    • Leiser, S.F.1    Kaeberlein, M.2
  • 29
    • 79960141848 scopus 로고    scopus 로고
    • Mammalian sirtuins and energy metabolism
    • Li, X.; Kazgan, N. Mammalian sirtuins and energy metabolism Int. J. Biol. Sci. 2011, 7 (5) 575-587
    • (2011) Int. J. Biol. Sci. , vol.7 , Issue.5 , pp. 575-587
    • Li, X.1    Kazgan, N.2
  • 30
    • 78649328799 scopus 로고    scopus 로고
    • Sirtuin regulation of mitochondria: Energy production, apoptosis, and signaling
    • Verdin, E.; Hirschey, M. D.; Finley, L. W.; Haigis, M. C. Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling Trends Biochem. Sci. 2010, 35 (12) 669-675
    • (2010) Trends Biochem. Sci. , vol.35 , Issue.12 , pp. 669-675
    • Verdin, E.1    Hirschey, M.D.2    Finley, L.W.3    Haigis, M.C.4
  • 31
    • 58849158388 scopus 로고    scopus 로고
    • How does SIRT1 affect metabolism, senescence and cancer?
    • Brooks, C. L.; Gu, W. How does SIRT1 affect metabolism, senescence and cancer? Nat. Rev. Cancer 2008, 9 (2) 123-128
    • (2008) Nat. Rev. Cancer , vol.9 , Issue.2 , pp. 123-128
    • Brooks, C.L.1    Gu, W.2
  • 33
    • 84879391795 scopus 로고    scopus 로고
    • SIRT1Mediates Central Circadian Control in the SCN by a Mechanism that Decays with Aging
    • Chang, H.; Guarente, L. SIRT1Mediates Central Circadian Control in the SCN by a Mechanism that Decays with Aging Cell 2013, 153 (7) 1448-1460
    • (2013) Cell , vol.153 , Issue.7 , pp. 1448-1460
    • Chang, H.1    Guarente, L.2
  • 34
    • 84857891632 scopus 로고    scopus 로고
    • On PAR with PARP: Cellular stress signaling through poly (ADP-ribose) and PARP-1
    • Luo, X.; Kraus, W. L. On PAR with PARP: cellular stress signaling through poly (ADP-ribose) and PARP-1 Genes Dev. 2012, 26 (5) 417-432
    • (2012) Genes Dev. , vol.26 , Issue.5 , pp. 417-432
    • Luo, X.1    Kraus, W.L.2
  • 35
    • 84886717428 scopus 로고    scopus 로고
    • Crosstalk between poly (ADP-ribose) polymerase and sirtuin enzymes
    • Cantó, C.; Sauve, A. A.; Bai, P. Crosstalk between poly (ADP-ribose) polymerase and sirtuin enzymes Mol. Aspects Med. 2013, 34 (6) 1168-1201
    • (2013) Mol. Aspects Med. , vol.34 , Issue.6 , pp. 1168-1201
    • Cantó, C.1    Sauve, A.A.2    Bai, P.3
  • 36
    • 33744509311 scopus 로고    scopus 로고
    • Regulation of intracellular levels of NAD: A novel role for CD38
    • Aksoy, P.; White, T. A.; Thompson, M.; Chini, E. N. Regulation of intracellular levels of NAD: a novel role for CD38 Biochem. Biophys. Res. Commun. 2006, 345 (4) 1386-1392
    • (2006) Biochem. Biophys. Res. Commun. , vol.345 , Issue.4 , pp. 1386-1392
    • Aksoy, P.1    White, T.A.2    Thompson, M.3    Chini, E.N.4
  • 37
    • 62149151357 scopus 로고    scopus 로고
    • CD38 as a regulator of cellular NAD: A novel potential pharmacological target for metabolic conditions
    • Chini, E. N. CD38 as a regulator of cellular NAD: a novel potential pharmacological target for metabolic conditions Curr. Pharm. Des. 2009, 15 (1) 57-63
    • (2009) Curr. Pharm. Des. , vol.15 , Issue.1 , pp. 57-63
    • Chini, E.N.1
  • 38
    • 79953280488 scopus 로고    scopus 로고
    • Deletion or overexpression of mitochondrial NAD+ carriers in Saccharomyces cerevisiae alters cellular NAD and ATP contents and affects mitochondrial metabolism and the rate of glycolysis
    • Agrimi, G.; Brambilla, L.; Frascotti, G.; Pisano, I.; Porro, D.; Vai, M.; Palmieri, L. Deletion or overexpression of mitochondrial NAD+ carriers in Saccharomyces cerevisiae alters cellular NAD and ATP contents and affects mitochondrial metabolism and the rate of glycolysis Appl. Environ. Microbiol. 2011, 77 (7) 2239-2246
    • (2011) Appl. Environ. Microbiol. , vol.77 , Issue.7 , pp. 2239-2246
    • Agrimi, G.1    Brambilla, L.2    Frascotti, G.3    Pisano, I.4    Porro, D.5    Vai, M.6    Palmieri, L.7
  • 39
    • 34250666701 scopus 로고    scopus 로고
    • Production and purification of lentiviral vectors
    • Tiscornia, G.; Singer, O.; Verma, I. M. Production and purification of lentiviral vectors Nat. Protoc. 2006, 1 (1) 241-245
    • (2006) Nat. Protoc. , vol.1 , Issue.1 , pp. 241-245
    • Tiscornia, G.1    Singer, O.2    Verma, I.M.3
  • 40
    • 84860502652 scopus 로고    scopus 로고
    • Biochemical issues in estimation of cytosolic free NAD/NADH ratio
    • Sun, F.; Dai, C.; Xie, J.; Hu, X. Biochemical issues in estimation of cytosolic free NAD/NADH ratio PloS One 2012, 7 (5) e34525
    • (2012) PloS One , vol.7 , Issue.5 , pp. 34525
    • Sun, F.1    Dai, C.2    Xie, J.3    Hu, X.4
  • 41
    • 0037376665 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease
    • Lin, S. J.; Guarente, L. Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease Curr. Opin. Cell Biol. 2003, 15 (2) 241-246
    • (2003) Curr. Opin. Cell Biol. , vol.15 , Issue.2 , pp. 241-246
    • Lin, S.J.1    Guarente, L.2
  • 42
    • 84861722850 scopus 로고    scopus 로고
    • Nicotinamide-induced Mitophagy event mediated by high NAD+/NADH ratio and SIRT1 protein activation
    • Jang, S. Y.; Kang, H. T.; Hwang, E. S. Nicotinamide-induced Mitophagy event mediated by high NAD+/NADH ratio and SIRT1 protein activation J. Biol. Chem. 2012, 287 (23) 19304-19314
    • (2012) J. Biol. Chem. , vol.287 , Issue.23 , pp. 19304-19314
    • Jang, S.Y.1    Kang, H.T.2    Hwang, E.S.3
  • 44
    • 77955847017 scopus 로고    scopus 로고
    • Mouse embryonic fibroblasts from CD38 knockout mice are resistant to oxidative stresses through inhibition of reactive oxygen species production and Ca2+ overload
    • Ge, Y.; Jiang, W.; Gan, L.; Wang, L.; Sun, C.; Ni, P.; Liu, Y.; Wu, S.; Gu, L.; Zheng, W. Mouse embryonic fibroblasts from CD38 knockout mice are resistant to oxidative stresses through inhibition of reactive oxygen species production and Ca2+ overload Biochem. Biophys. Res. Commun. 2010, 399 (2) 167-172
    • (2010) Biochem. Biophys. Res. Commun. , vol.399 , Issue.2 , pp. 167-172
    • Ge, Y.1    Jiang, W.2    Gan, L.3    Wang, L.4    Sun, C.5    Ni, P.6    Liu, Y.7    Wu, S.8    Gu, L.9    Zheng, W.10
  • 45
    • 0026520064 scopus 로고
    • Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space
    • Koll, H.; Guiard, B.; Rassow, J.; Ostermann, J.; Horwich, A. L.; Neupert, W.; Hartl, F.-U. Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space Cell 1992, 68 (6) 1163-1175
    • (1992) Cell , vol.68 , Issue.6 , pp. 1163-1175
    • Koll, H.1    Guiard, B.2    Rassow, J.3    Ostermann, J.4    Horwich, A.L.5    Neupert, W.6    Hartl, F.-U.7
  • 46
    • 34247326430 scopus 로고    scopus 로고
    • In vivo induction of heat shock proteins in the substantia nigra following L-DOPA administration is associated with increased activity of mitochondrial complex i and nitrosative stress in rats: Regulation by glutathione redox state
    • Calabrese, V.; Mancuso, C.; Ravagna, A.; Perluigi, M.; Cini, C.; Marco, C. D.; Allan Butterfield, D.; Stella, A. M. G. In vivo induction of heat shock proteins in the substantia nigra following L-DOPA administration is associated with increased activity of mitochondrial complex I and nitrosative stress in rats: regulation by glutathione redox state J. Neurochem. 2007, 101 (3) 709-717
    • (2007) J. Neurochem. , vol.101 , Issue.3 , pp. 709-717
    • Calabrese, V.1    Mancuso, C.2    Ravagna, A.3    Perluigi, M.4    Cini, C.5    Marco, C.D.6    Allan Butterfield, D.7    Stella, A.M.G.8
  • 47
    • 0036913861 scopus 로고    scopus 로고
    • Expression of hsp 27, hsp 60, hsc 70, and hsp 70 stress response genes in cultured human urothelial cells (UROtsa) exposed to lethal and sublethal concentrations of sodium arsenite
    • Rossi, M. R.; Somji, S.; Garrett, S. H.; Sens, M. A.; Nath, J.; Sens, D. A. Expression of hsp 27, hsp 60, hsc 70, and hsp 70 stress response genes in cultured human urothelial cells (UROtsa) exposed to lethal and sublethal concentrations of sodium arsenite Environ. Health Perspect. 2002, 110 (12) 1225-1232
    • (2002) Environ. Health Perspect. , vol.110 , Issue.12 , pp. 1225-1232
    • Rossi, M.R.1    Somji, S.2    Garrett, S.H.3    Sens, M.A.4    Nath, J.5    Sens, D.A.6
  • 48
    • 35748929414 scopus 로고    scopus 로고
    • Cytosolic accumulation of hsp60 during apoptosis with or without apparent mitochondrial release: Evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase
    • Chandra, D.; Choy, G.; Tang, D. G. Cytosolic accumulation of hsp60 during apoptosis with or without apparent mitochondrial release: Evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase J. Biol. Chem. 2007, 282 (43) 31289-31301
    • (2007) J. Biol. Chem. , vol.282 , Issue.43 , pp. 31289-31301
    • Chandra, D.1    Choy, G.2    Tang, D.G.3
  • 49
    • 80052267874 scopus 로고    scopus 로고
    • Vimentin in cancer and its potential as a molecular target for cancer therapy
    • Satelli, A.; Li, S. Vimentin in cancer and its potential as a molecular target for cancer therapy Cell. Mol. Life Sci. 2011, 68 (18) 3033-3046
    • (2011) Cell. Mol. Life Sci. , vol.68 , Issue.18 , pp. 3033-3046
    • Satelli, A.1    Li, S.2
  • 50
    • 0242413674 scopus 로고    scopus 로고
    • Proteome analysis of vinca alkaloid response and resistance in acute lymphoblastic leukemia reveals novel cytoskeletal alterations
    • Verrills, N. M.; Walsh, B. J.; Cobon, G. S.; Hains, P. G.; Kavallaris, M. Proteome analysis of vinca alkaloid response and resistance in acute lymphoblastic leukemia reveals novel cytoskeletal alterations J. Biol. Chem. 2003, 278 (46) 45082-45093
    • (2003) J. Biol. Chem. , vol.278 , Issue.46 , pp. 45082-45093
    • Verrills, N.M.1    Walsh, B.J.2    Cobon, G.S.3    Hains, P.G.4    Kavallaris, M.5


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