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Volumn 287, Issue 10, 2012, Pages 7692-7700

Ethanol suppresses ureagenesis in rat hepatocytes: Role of acetaldehyde

Author keywords

[No Author keywords available]

Indexed keywords

3-AMINO-1; ALCOHOL DEHYDROGENASE; ALDEHYDE DEHYDROGENASE; BASE LINE; CELLULAR RESPIRATION; CYTOCHROME P450; ETHANOL OXIDATION; HEPATOCYTES; INHIBITORY EFFECT; INTERMEDIATE PRODUCT; INTERMEMBRANE SPACE; ISOTHIOCYANATES; METABOLITE EXCHANGES; OUTER MEMBRANE; RAT HEPATOCYTES; TRANS-1 ,2-DICHLOROETHYLENE; VOLTAGE-DEPENDENT ANION CHANNELS;

EID: 84857757376     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.293399     Document Type: Article
Times cited : (46)

References (62)
  • 1
    • 77953807486 scopus 로고    scopus 로고
    • Mitochondrial carriers function as monomers
    • Kunji, E. R., and Crichton, P. G. (2010) Mitochondrial carriers function as monomers. Biochim. Biophys. Acta 1797, 817-831
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 817-831
    • Kunji, E.R.1    Crichton, P.G.2
  • 2
    • 79953249623 scopus 로고    scopus 로고
    • Evolution, structure and function of mitochondrial carriers. A review with new insights
    • Palmieri, F., Pierri, C. L., De Grassi, A., Nunes-Nesi, A., and Fernie, A. R. (2011) Evolution, structure and function of mitochondrial carriers. A review with new insights. Plant J. 66, 161-181
    • (2011) Plant J. , vol.66 , pp. 161-181
    • Palmieri, F.1    Pierri, C.L.2    De Grassi, A.3    Nunes-Nesi, A.4    Fernie, A.R.5
  • 3
    • 28544436922 scopus 로고    scopus 로고
    • Activation of glycogen synthase kinase 3β disrupts the binding of hexokinase II to mitochondria by phosphorylating voltage-dependent anion channel and potentiates chemotherapy-induced cytotoxicity
    • DOI 10.1158/0008-5472.CAN-05-1925
    • Pastorino, J. G., Hoek, J. B., and Shulga, N. (2005) Activation of glycogen synthase kinase 3β disrupts the binding of hexokinase II to mitochondria by phosphorylating voltage-dependent anion channel and potentiates chemotherapy-induced cytotoxicity. Cancer Res. 65, 10545-10554 (Pubitemid 41743749)
    • (2005) Cancer Research , vol.65 , Issue.22 , pp. 10545-10554
    • Pastorino, J.G.1    Hoek, J.B.2    Shulga, N.3
  • 6
    • 29344468832 scopus 로고    scopus 로고
    • Voltage-dependent anion channel (VDAC) as mitochondrial governator - Thinking outside the box
    • DOI 10.1016/j.bbadis.2005.10.006, PII S0925443905001523, Mitochondria in Diseases and Therapeutics
    • Lemasters, J. J., and Holmuhamedov, E. (2006) Voltage-dependent anion channel (VDAC) as mitochondrial governator. Thinking outside the box. Biochim. Biophys. Acta 1762, 181-190 (Pubitemid 43006024)
    • (2006) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1762 , Issue.2 , pp. 181-190
    • Lemasters, J.J.1    Holmuhamedov, E.2
  • 7
  • 9
    • 58049093976 scopus 로고    scopus 로고
    • Ethanol exposure decreases mitochondrial outer membrane permeability in cultured rat hepatocytes
    • Holmuhamedov, E., and Lemasters, J. J. (2009) Ethanol exposure decreases mitochondrial outer membrane permeability in cultured rat hepatocytes. Arch. Biochem. Biophys. 481, 226-233
    • (2009) Arch. Biochem. Biophys. , vol.481 , pp. 226-233
    • Holmuhamedov, E.1    Lemasters, J.J.2
  • 10
    • 84857733340 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 11
    • 33747605553 scopus 로고    scopus 로고
    • Cytochrome P450 2E1-dependent oxidant stress and up-regulation of anti-oxidant defense in liver cells
    • Cederbaum, A. I. (2006) Cytochrome P450 2E1-dependent oxidant stress and up-regulation of anti-oxidant defense in liver cells. J. Gastroenterol. Hepatol. 21, S22-S25
    • (2006) J. Gastroenterol. Hepatol. , vol.21
    • Cederbaum, A.I.1
  • 12
    • 38149016706 scopus 로고    scopus 로고
    • Acetaldehyde-generating enzyme systems. Roles of alcohol dehydrogenase, CYP2E1 and catalase, and speculations on the role of other enzymes and processes
    • discussion 16-22, 198-199
    • Crabb, D. W., and Liangpunsakul, S. (2007) Acetaldehyde-generating enzyme systems. Roles of alcohol dehydrogenase, CYP2E1 and catalase, and speculations on the role of other enzymes and processes. Novartis Found.Symp. 285, 4-16; discussion 16-22, 198-199
    • (2007) Novartis Found.Symp. , vol.285 , pp. 4-16
    • Crabb, D.W.1    Liangpunsakul, S.2
  • 14
    • 7544222395 scopus 로고    scopus 로고
    • The discovery of the microsomal ethanol oxidizing system and its physiologic and pathologic role
    • Lieber, C. S. (2004) The discovery of the microsomal ethanol oxidizing system and its physiologic and pathologic role. Drug Metab. Rev. 36, 511-529
    • (2004) Drug Metab. Rev. , vol.36 , pp. 511-529
    • Lieber, C.S.1
  • 15
    • 33845927120 scopus 로고    scopus 로고
    • Alcohol, oxidative stress and free radical damage
    • Albano, E. (2006) Alcohol, oxidative stress and free radical damage. Proc. Nutr. Soc. 65, 278-290
    • (2006) Proc. Nutr. Soc. , vol.65 , pp. 278-290
    • Albano, E.1
  • 16
    • 0036137559 scopus 로고    scopus 로고
    • Contribution of mitochondria to oxidative stress associated with alcoholic liver disease
    • DOI 10.1016/S0891-5849(01)00769-9, PII S0891584901007699
    • Bailey, S. M., and Cunningham, C. C. (2002) Contribution of mitochondria to oxidative stress associated with alcoholic liver disease. Free Radic. Biol. Med. 32, 11-16 (Pubitemid 34045132)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.1 , pp. 11-16
    • Bailey, S.M.1    Cunningham, C.C.2
  • 17
    • 0027739805 scopus 로고
    • Mitochondrial glutathione depletion in alcoholic liver disease
    • DOI 10.1016/0741-8329(93)90067-X
    • Fernández-Checa, J. C., Hirano, T., Tsukamoto, H., and Kaplowitz, N. (1993) Mitochondrial glutathione depletion in alcoholic liver disease. Alcohol 10, 469-475 (Pubitemid 24012670)
    • (1993) Alcohol , vol.10 , Issue.6 , pp. 469-475
    • Fernandez-Checa, J.C.1    Hirano, T.2    Tsukamoto, H.3    Kaplowitz, N.4
  • 19
    • 0141494281 scopus 로고    scopus 로고
    • CYP2E1: Biochemistry, toxicology, regulation and function in ethanol-induced liver injury
    • DOI 10.2174/1566524033479609
    • Kessova, I., and Cederbaum, A. I. (2003) CYP2E1. Biochemistry, toxicology, regulation and function in ethanol-induced liver injury. Curr. Mol. Med. 3, 509-518 (Pubitemid 37168595)
    • (2003) Current Molecular Medicine , vol.3 , Issue.6 , pp. 509-518
    • Kessova, I.1    Cederbaum, A.I.2
  • 20
    • 39149123560 scopus 로고    scopus 로고
    • CYP2E1 and oxidative liver injury by alcohol
    • Lu, Y., and Cederbaum, A. I. (2008) CYP2E1 and oxidative liver injury by alcohol. Free Radic. Biol. Med. 44, 723-738
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 723-738
    • Lu, Y.1    Cederbaum, A.I.2
  • 21
    • 38449102937 scopus 로고    scopus 로고
    • Removal of acetaldehyde from the body
    • discussion 40-51, 198-199
    • Deitrich, R. A., Petersen, D., and Vasiliou, V. (2007) Removal of acetaldehyde from the body. Novartis Found. Symp. 285, 23-40; discussion 40-51, 198-199
    • (2007) Novartis Found. Symp. , vol.285 , pp. 23-40
    • Deitrich, R.A.1    Petersen, D.2    Vasiliou, V.3
  • 22
    • 0033649270 scopus 로고    scopus 로고
    • Mechanisms of liver cell injury
    • Kaplowitz, N. (2000) Mechanisms of liver cell injury. J. Hepatol. 32, 39-47
    • (2000) J. Hepatol. , vol.32 , pp. 39-47
    • Kaplowitz, N.1
  • 25
    • 16544373246 scopus 로고    scopus 로고
    • Dangerous byproducts of alcohol breakdown - Focus on adducts
    • Tuma, D. J., and Casey, C. A. (2003) Dangerous byproducts of alcohol breakdown. Focus on adducts. Alcohol Res. Health 27, 285-290 (Pubitemid 40685567)
    • (2003) Alcohol Research and Health , vol.27 , Issue.4 , pp. 285-290
    • Tuma, D.J.1    Casey, C.A.2
  • 26
    • 0038000608 scopus 로고    scopus 로고
    • N-acetylglutamate and its changing role through evolution
    • DOI 10.1042/BJ20030002
    • Caldovic, L., and Tuchman, M. (2003)N-acetylglutamate and its changing role through evolution. Biochem. J. 372, 279-290 (Pubitemid 36723874)
    • (2003) Biochemical Journal , vol.372 , Issue.2 , pp. 279-290
    • Caldovic, L.1    Tuchman, M.2
  • 28
    • 33745700811 scopus 로고    scopus 로고
    • Arginine challenge unravels persistent disturbances of urea cycle and gluconeogenesis in abstinent alcoholics
    • DOI 10.1093/alcalc/agl032
    • Hasselblatt, M., Krampe, H., Jacobs, S., Sindram, H., Armstrong, V. W., Hecker, M., and Ehrenreich, H. (2006) Arginine challenge unravels persistent disturbances of urea cycle and gluconeogenesis in abstinent alcoholics. Alcohol 41, 372-378 (Pubitemid 43997266)
    • (2006) Alcohol and Alcoholism , vol.41 , Issue.4 , pp. 372-378
    • Hasselblatt, M.1    Krampe, H.2    Jacobs, S.3    Sindram, H.4    Armstrong, V.W.5    Hecker, M.6    Ehrenreich, H.7
  • 29
    • 33646893457 scopus 로고    scopus 로고
    • Inborn errors of metabolism: The flux from Mendelian to complex diseases
    • DOI 10.1038/nrg1880, PII N1880
    • Lanpher, B., Brunetti-Pierri, N., and Lee, B. (2006) Inborn errors of metabolism. The flux from Mendelian to complex diseases. Nat. Rev. Genet. 7, 449-460 (Pubitemid 43780488)
    • (2006) Nature Reviews Genetics , vol.7 , Issue.6 , pp. 449-460
    • Lanpher, B.1    Brunetti-Pierri, N.2    Lee, B.3
  • 30
    • 0031691175 scopus 로고    scopus 로고
    • Urea. Diverse functions of a "waste" product
    • Withers, P. C. (1998) Urea. Diverse functions of a "waste" product. Clin. Exp. Pharmacol. Physiol. 25, 722-727
    • (1998) Clin. Exp. Pharmacol. Physiol. , vol.25 , pp. 722-727
    • Withers, P.C.1
  • 31
    • 84857695483 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 32
    • 0003633755 scopus 로고    scopus 로고
    • Institute of Laboratory Research, Commission on Life Sciences, National Research Council, The National Academies Press, Washington, D.C.
    • Guide for the Care and Use of Laboratory Animals (1996) Institute of Laboratory Research, Commission on Life Sciences, National Research Council, The National Academies Press, Washington, D.C.
    • (1996) Guide for the Care and Use of Laboratory Animals
  • 33
    • 0031407680 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in pH-dependent reperfusion injury to rat hepatocytes
    • Qian, T., Nieminen, A. L., Herman, B., and Lemasters, J. J. (1997) Mitochondrial permeability transition in pH-dependent reperfusion injury to rat hepatocytes. Am. J. Physiol. 273, C1783-C1792
    • (1997) Am. J. Physiol. , vol.273
    • Qian, T.1    Nieminen, A.L.2    Herman, B.3    Lemasters, J.J.4
  • 34
    • 56149121299 scopus 로고    scopus 로고
    • Translocation of iron from lysosomes into mitochondria is a key event during oxidative stress-induced hepatocellular injury
    • Uchiyama, A., Kim, J. S., Kon, K., Jaeschke, H., Ikejima, K., Watanabe, S., and Lemasters, J. J. (2008) Translocation of iron from lysosomes into mitochondria is a key event during oxidative stress-induced hepatocellular injury. Hepatology 48, 1644-1654
    • (2008) Hepatology , vol.48 , pp. 1644-1654
    • Uchiyama, A.1    Kim, J.S.2    Kon, K.3    Jaeschke, H.4    Ikejima, K.5    Watanabe, S.6    Lemasters, J.J.7
  • 36
    • 0019963026 scopus 로고
    • A simple, rapid method for the determination of glucose, lactate, pyruvate, alanine, 3-hydroxybutyrate and acetoacetate on a single 20-mul blood sample
    • Maughan, R. J. (1982) A simple, rapid method for the determination of glucose, lactate, pyruvate, alanine, 3-hydroxybutyrate and acetoacetate on a single 20-mul blood sample. Clin. Chim. Acta 122, 231-240
    • (1982) Clin. Chim. Acta , vol.122 , pp. 231-240
    • Maughan, R.J.1
  • 37
    • 77249093012 scopus 로고    scopus 로고
    • The role of ethanol metabolism in development of alcoholic steatohepatitis in the rat
    • Ronis, M. J., Korourian, S., Blackburn, M. L., Badeaux, J., and Badger, T. M. (2010) The role of ethanol metabolism in development of alcoholic steatohepatitis in the rat. Alcohol 44, 157-169
    • (2010) Alcohol , vol.44 , pp. 157-169
    • Ronis, M.J.1    Korourian, S.2    Blackburn, M.L.3    Badeaux, J.4    Badger, T.M.5
  • 39
    • 33847232240 scopus 로고    scopus 로고
    • Inhibiting catalase activity sensitizes 36B10 rat glioma cells to oxidative stress
    • Smith, P. S., Zhao, W., Spitz, D. R., and Robbins, M. E. (2007) Inhibiting catalase activity sensitizes 36B10 rat glioma cells to oxidative stress. Free Radic. Biol. Med. 42, 787-797
    • (2007) Free Radic. Biol. Med. , vol.42 , pp. 787-797
    • Smith, P.S.1    Zhao, W.2    Spitz, D.R.3    Robbins, M.E.4
  • 40
    • 0035036987 scopus 로고    scopus 로고
    • Ethanol consumption and liver mitochondria function
    • Cunningham, C. C., and Bailey, S. M. (2001) Ethanol consumption and liver mitochondria function. Biol. Signals Recept. 10, 271-282 (Pubitemid 32449005)
    • (2001) Biological Signals and Receptors , vol.10 , Issue.3-4 , pp. 271-282
    • Cunningham, C.C.1    Bailey, S.M.2
  • 41
    • 40949141493 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in the pathogenesis of alcohol- And obesity-induced fatty liver diseases
    • Mantena, S. K., King, A. L., Andringa, K. K., Eccleston, H. B., and Bailey, S. M. (2008) Mitochondrial dysfunction and oxidative stress in the pathogenesis of alcohol- and obesity-induced fatty liver diseases. Free Radic. Biol. Med. 44, 1259-1272
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 1259-1272
    • Mantena, S.K.1    King, A.L.2    Andringa, K.K.3    Eccleston, H.B.4    Bailey, S.M.5
  • 44
    • 0024238668 scopus 로고
    • Genetic polymorphism of the alcohol metabolising enzymes as a basis for alcoholic liver disease
    • Grant, D. A. (1988) Genetic polymorphism of the alcohol metabolising enzymes as a basis for alcoholic liver disease. Br. J. Addict. 83, 1255-1259
    • (1988) Br. J. Addict. , vol.83 , pp. 1255-1259
    • Grant, D.A.1
  • 45
    • 0036083422 scopus 로고    scopus 로고
    • Alcohol and mitochondria. A dysfunctional relationship
    • Hoek, J. B., Cahill, A., and Pastorino, J. G. (2002) Alcohol and mitochondria. A dysfunctional relationship. Gastroenterology 122, 2049-2063
    • (2002) Gastroenterology , vol.122 , pp. 2049-2063
    • Hoek, J.B.1    Cahill, A.2    Pastorino, J.G.3
  • 47
    • 0027753777 scopus 로고
    • Oxidative stress, antioxidants, and alcoholic liver fibrogenesis
    • Tsukamoto, H. (1993) Oxidative stress, antioxidants, and alcoholic liver fibrogenesis. Alcohol 10, 465-467
    • (1993) Alcohol , vol.10 , pp. 465-467
    • Tsukamoto, H.1
  • 48
    • 0025160864 scopus 로고
    • Inhibition of ethanol-inducible cytochrome P450IIE1 by 3-amino-1,2,4-triazole
    • Koop, D. R. (1990) Inhibition of ethanol-inducible cytochrome P450IIE1 by 3-amino-1,2,4-triazole. Chem. Res. Toxicol. 3, 377-383
    • (1990) Chem. Res. Toxicol. , vol.3 , pp. 377-383
    • Koop, D.R.1
  • 49
    • 0027270728 scopus 로고
    • Evidence that catalase is a major pathway of ethanol oxidation in vivo: Dose-response studies in deer mice using methanol as a selective substrate
    • DOI 10.1006/abbi.1993.1269
    • Bradford, B. U., Seed, C. B., Handler, J. A., Forman, D. T., and Thurman, R. G. (1993) Evidence that catalase is a major pathway of ethanol oxidation in vivo. Dose-response studies in deer mice using methanol as a selective substrate. Arch. Biochem. Biophys. 303, 172-176 (Pubitemid 23212673)
    • (1993) Archives of Biochemistry and Biophysics , vol.303 , Issue.1 , pp. 172-176
    • Bradford, B.U.1    Seed, C.B.2    Handler, J.A.3    Forman, D.T.4    Thurman, R.G.5
  • 51
    • 19444369790 scopus 로고    scopus 로고
    • Swift increase in alcohol metabolism (SIAM): Understanding the phenomenon of hypermetabolism in liver
    • DOI 10.1016/j.alcohol.2004.12.001, PII S0741832905000534
    • Bradford, B. U., and Rusyn, I. (2005) Swift increase in alcohol metabolism (SIAM). Understanding the phenomenon of hypermetabolism in liver. Alcohol 35, 13-17 (Pubitemid 40726307)
    • (2005) Alcohol , vol.35 , Issue.1 , pp. 13-17
    • Bradford, B.U.1    Rusyn, I.2
  • 52
    • 34249824628 scopus 로고    scopus 로고
    • Modulation of mitochondrial membrane permeability in pathogenesis, autophagy and control of metabolism
    • Lemasters, J. J. (2007) Modulation of mitochondrial membrane permeability in pathogenesis, autophagy and control of metabolism. J. Gastroenterol. Hepatol. 22, S31-S37
    • (2007) J. Gastroenterol. Hepatol. , vol.22
    • Lemasters, J.J.1
  • 53
    • 34247485841 scopus 로고    scopus 로고
    • Role of the mitochondrial membrane permeability transition in cell death
    • DOI 10.1007/s10495-006-0525-7, Special Issue on Mitochondria in Apoptosis
    • Tsujimoto, Y., and Shimizu, S. (2007) Role of the mitochondrial membrane permeability transition in cell death. Apoptosis 12, 835-840 (Pubitemid 46653286)
    • (2007) Apoptosis , vol.12 , Issue.5 , pp. 835-840
    • Tsujimoto, Y.1    Shimizu, S.2
  • 54
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrial- dependent cell death
    • DOI 10.1038/ncb1575, PII NCB1575
    • Baines, C. P., Kaiser, R. A., Sheiko, T., Craigen, W. J., and Molkentin, J. D. (2007) Voltage-dependent anion channels are dispensable for mitochondrial- dependent cell death. Nat. Cell Biol. 9, 550-555 (Pubitemid 46696536)
    • (2007) Nature Cell Biology , vol.9 , Issue.5 , pp. 550-555
    • Baines, C.P.1    Kaiser, R.A.2    Sheiko, T.3    Craigen, W.J.4    Molkentin, J.D.5
  • 55
    • 0035842896 scopus 로고    scopus 로고
    • VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release
    • DOI 10.1083/jcb.200105057
    • Madesh, M., and Hajnóczky, G. (2001) VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release. J. Cell Biol. 155, 1003-1015 (Pubitemid 34286251)
    • (2001) Journal of Cell Biology , vol.155 , Issue.6 , pp. 1003-1015
    • Madesh, M.1    Hajnoczky, G.2
  • 58
    • 0035380462 scopus 로고    scopus 로고
    • Bcl-xL promotes the open configuration of the voltage-dependent anion channel and metabolite passage through the outer mitochondrial membrane
    • Vander Heiden, M. G., Li, X. X., Gottleib, E., Hill, R. B., Thompson, C. B., and Colombini, M. (2001) Bcl-xL promotes the open configuration of the voltage-dependent anion channel and metabolite passage through the outer mitochondrial membrane. J. Biol. Chem. 276, 19414-19419
    • (2001) J. Biol. Chem. , vol.276 , pp. 19414-19419
    • Vander Heiden, M.G.1    Li, X.X.2    Gottleib, E.3    Hill, R.B.4    Thompson, C.B.5    Colombini, M.6
  • 59
    • 78049278366 scopus 로고    scopus 로고
    • Inhibition of the mitochondrial permeability transition by protein kinase A in rat liver mitochondria and hepatocytes
    • Pediaditakis, P., Kim, J. S., He, L., Zhang, X., Graves, L. M., and Lemasters, J. J. (2010) Inhibition of the mitochondrial permeability transition by protein kinase A in rat liver mitochondria and hepatocytes. Biochem. J. 431, 411-421
    • (2010) Biochem. J. , vol.431 , pp. 411-421
    • Pediaditakis, P.1    Kim, J.S.2    He, L.3    Zhang, X.4    Graves, L.M.5    Lemasters, J.J.6
  • 60
    • 78650332649 scopus 로고    scopus 로고
    • Free tubulin modulates mitochondrial membrane potential in cancer cells
    • Maldonado, E. N., Patnaik, J., Mullins, M. R., and Lemasters, J. J. (2010) Free tubulin modulates mitochondrial membrane potential in cancer cells. Cancer Res. 70, 10192-10201
    • (2010) Cancer Res. , vol.70 , pp. 10192-10201
    • Maldonado, E.N.1    Patnaik, J.2    Mullins, M.R.3    Lemasters, J.J.4
  • 61
    • 52449104836 scopus 로고    scopus 로고
    • VDAC regulation. Role of cytosolic proteins and mitochondrial lipids
    • Rostovtseva, T. K., and Bezrukov, S. M. (2008) VDAC regulation. Role of cytosolic proteins and mitochondrial lipids. J. Bioenerg. Biomembr. 40, 163-170
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 163-170
    • Rostovtseva, T.K.1    Bezrukov, S.M.2


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