메뉴 건너뛰기




Volumn 288, Issue 43, 2013, Pages 30904-30916

Protection of a ceramide synthase 2 null mouse from drug-induced liver injury role of gap junction dysfunction and connexin 32 mislocalization

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL CHANGES; CERAMIDE SYNTHASE; D-GALACTOSAMINE; DETERGENT-RESISTANT MEMBRANES; GAP JUNCTION PROTEINS; LYSOSOMAL DEGRADATION; MEMBRANE PROPERTIES; RECOMBINANT ADENO-ASSOCIATED VIRUS;

EID: 84886687848     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.448852     Document Type: Article
Times cited : (32)

References (47)
  • 2
    • 33645799020 scopus 로고    scopus 로고
    • Mechanisms of drug-induced liver injury
    • Holt, M. P., and Ju, C. (2006) Mechanisms of drug-induced liver injury. AAPS J. 8, E48-E54
    • (2006) AAPS J. , vol.8
    • Holt, M.P.1    Ju, C.2
  • 4
    • 84865049615 scopus 로고    scopus 로고
    • Sphingolipids. Critical players in Alzheimer's disease
    • van Echten-Deckert, G., and Walter, J. (2012) Sphingolipids. Critical players in Alzheimer's disease. Prog. Lipid Res. 51, 378-393
    • (2012) Prog. Lipid Res. , vol.51 , pp. 378-393
    • Van Echten-Deckert, G.1    Walter, J.2
  • 5
    • 84860482342 scopus 로고    scopus 로고
    • A ceramide-centric view of insulin resistance
    • Chavez, J. A., and Summers, S. A. (2012) A ceramide-centric view of insulin resistance. Cell Metab. 15, 585-594
    • (2012) Cell Metab. , vol.15 , pp. 585-594
    • Chavez, J.A.1    Summers, S.A.2
  • 6
    • 33748746334 scopus 로고    scopus 로고
    • When do Lasses (longevity assurance genes) become CerS (ceramide synthases) ? Insights into the regulation of ceramide synthesis
    • Pewzner-Jung, Y., Ben-Dor, S., and Futerman, A. H. (2006) When do Lasses (longevity assurance genes) become CerS (ceramide synthases) ? Insights into the regulation of ceramide synthesis. J. Biol. Chem. 281, 25001-25005
    • (2006) J. Biol. Chem. , vol.281 , pp. 25001-25005
    • Pewzner-Jung, Y.1    Ben-Dor, S.2    Futerman, A.H.3
  • 7
    • 84855918312 scopus 로고    scopus 로고
    • Ceramide synthases at the centre of sphingolipid metabolism and biology
    • Mullen, T. D., Hannun, Y. A., and Obeid, L. M. (2012) Ceramide synthases at the centre of sphingolipid metabolism and biology. Biochem. J. 441, 789-802
    • (2012) Biochem. J. , vol.441 , pp. 789-802
    • Mullen, T.D.1    Hannun, Y.A.2    Obeid, L.M.3
  • 8
    • 77953561361 scopus 로고    scopus 로고
    • Mammalian ceramide synthases
    • Levy, M., and Futerman, A. H. (2010) Mammalian ceramide synthases. IUBMB Life 62, 347-356
    • (2010) IUBMB Life , vol.62 , pp. 347-356
    • Levy, M.1    Futerman, A.H.2
  • 12
    • 84873295041 scopus 로고    scopus 로고
    • Ablation of very long acyl chain sphingolipids causes hepatic insulin resistance in mice due to altered detergentresistant membranes
    • Park, J.-W., Park, W.-J., Kuperman, Y., Boura-Halfon, S., Pewzner-Jung, Y., and Futerman, A. H. (2013) Ablation of very long acyl chain sphingolipids causes hepatic insulin resistance in mice due to altered detergentresistant membranes. Hepatology 57, 525-532
    • (2013) Hepatology , vol.57 , pp. 525-532
    • Park, J.-W.1    Park, W.-J.2    Kuperman, Y.3    Boura-Halfon, S.4    Pewzner-Jung, Y.5    Futerman, A.H.6
  • 16
  • 17
    • 0031635960 scopus 로고    scopus 로고
    • Early fumonisin B1 toxicity in relation to disrupted sphingolipid metabolism in male BALB/c mice
    • Tsunoda, M., Sharma, R. P., and Riley, R. T. (1998) Early fumonisin B1 toxicity in relation to disrupted sphingolipid metabolism in male BALB/c mice. J. Biochem. Mol. Toxicol. 12, 281-289
    • (1998) J. Biochem. Mol. Toxicol. , vol.12 , pp. 281-289
    • Tsunoda, M.1    Sharma, R.P.2    Riley, R.T.3
  • 18
    • 0029845402 scopus 로고    scopus 로고
    • Effect of buthionine sulfoximine, a synthesis inhibitor of the antioxidant glutathione, on the murine nigrostriatal neurons
    • Andersen, J. K., Mo, J. Q., Hom, D. G., Lee, F. Y., Harnish, P., Hamill, R. W., and McNeill, T. H. (1996) Effect of buthionine sulfoximine, a synthesis inhibitor of the antioxidant glutathione, on the murine nigrostriatal neurons. J. Neurochem. 67, 2164-2171
    • (1996) J. Neurochem. , vol.67 , pp. 2164-2171
    • Andersen, J.K.1    Mo, J.Q.2    Hom, D.G.3    Lee, F.Y.4    Harnish, P.5    Hamill, R.W.6    McNeill, T.H.7
  • 19
    • 0034012890 scopus 로고    scopus 로고
    • Connexin and gap junction degradation
    • Berthoud, V. M., Tadros, P. N., and Beyer, E. C. (2000) Connexin and gap junction degradation. Methods 20, 180-187
    • (2000) Methods , vol.20 , pp. 180-187
    • Berthoud, V.M.1    Tadros, P.N.2    Beyer, E.C.3
  • 20
    • 80255132948 scopus 로고    scopus 로고
    • Analysis of mammalian sphingolipids by liquid chromatography tandem mass spectrometry (LC-MS/MS) and tissue imaging mass spectrometry (TIMS)
    • Sullards, M. C., Liu, Y., Chen, Y., and Merrill, A. H. (2011) Analysis of mammalian sphingolipids by liquid chromatography tandem mass spectrometry (LC-MS/MS) and tissue imaging mass spectrometry (TIMS). Biochim. Biophys. Acta 1811, 838-853
    • (2011) Biochim. Biophys. Acta , vol.1811 , pp. 838-853
    • Sullards, M.C.1    Liu, Y.2    Chen, Y.3    Merrill, A.H.4
  • 21
    • 68349095535 scopus 로고    scopus 로고
    • Quantitative analysis of sphingolipids for lipidomics using triple quadrupole and quadrupole linear ion trap mass spectrometers
    • Shaner, R. L., Allegood, J. C., Park, H., Wang, E., Kelly, S., Haynes, C. A., Sullards, M. C., and Merrill, A. H. (2009) Quantitative analysis of sphingolipids for lipidomics using triple quadrupole and quadrupole linear ion trap mass spectrometers. J. Lipid Res. 50, 1692-1707
    • (2009) J. Lipid Res. , vol.50 , pp. 1692-1707
    • Shaner, R.L.1    Allegood, J.C.2    Park, H.3    Wang, E.4    Kelly, S.5    Haynes, C.A.6    Sullards, M.C.7    Merrill, A.H.8
  • 22
    • 79953292299 scopus 로고    scopus 로고
    • Role of integrative signaling through gap junctions in toxicology
    • Chapter 2, Unit 2.18
    • Upham, B. L. (2011) Role of integrative signaling through gap junctions in toxicology. Curr. Protoc. Toxicol. Chapter 2, Unit 2.18
    • (2011) Curr. Protoc. Toxicol.
    • Upham, B.L.1
  • 23
    • 0034682799 scopus 로고    scopus 로고
    • Regulation of connexin degradation as a mechanism to increase gap junction assembly and function
    • Musil, L. S., Le, A. C., Van Slyke, J. K., and Roberts, L. M. (2000) Regulation of connexin degradation as a mechanism to increase gap junction assembly and function. J. Biol. Chem. 275, 25207-25215
    • (2000) J. Biol. Chem. , vol.275 , pp. 25207-25215
    • Musil, L.S.1    Le, A.C.2    Van Slyke, J.K.3    Roberts, L.M.4
  • 24
    • 0032396517 scopus 로고    scopus 로고
    • Normal differentiation of cultured lens cells after inhibition of gap junction-mediated intercellular communication
    • Le, A. C., and Musil, L. S. (1998) Normal differentiation of cultured lens cells after inhibition of gap junction-mediated intercellular communication. Dev. Biol. 204, 80-96
    • (1998) Dev. Biol. , vol.204 , pp. 80-96
    • Le, A.C.1    Musil, L.S.2
  • 25
  • 27
    • 3242778717 scopus 로고    scopus 로고
    • Long-term enzymatic and phenotypic correction in the phenylketonuria mouse model by adeno-associated virus vector-mediated gene transfer
    • Oh, H.-J., Park, E.-S., Kang, S., Jo, I., and Jung, S.-C. (2004) Long-term enzymatic and phenotypic correction in the phenylketonuria mouse model by adeno-associated virus vector-mediated gene transfer. Pediatr. Res. 56, 278-284
    • (2004) Pediatr. Res. , vol.56 , pp. 278-284
    • Oh, H.-J.1    Park, E.-S.2    Kang, S.3    Jo, I.4    Jung, S.-C.5
  • 28
    • 56049091075 scopus 로고    scopus 로고
    • Protective effect of recombinant adeno-associated virus 2/8-mediated gene therapy from the maternal hyperphenylalaninemia in offsprings of a mouse model of phenylketonuria
    • Jung, S.-C., Park, J.-W., Oh, H.-J., Choi, J.-O., Seo, K.-I., Park, E.-S., and Park, H.-Y. (2008) Protective effect of recombinant adeno-associated virus 2/8-mediated gene therapy from the maternal hyperphenylalaninemia in offsprings of a mouse model of phenylketonuria. J. Korean Med. Sci. 23, 877-883
    • (2008) J. Korean Med. Sci. , vol.23 , pp. 877-883
    • Jung, S.-C.1    Park, J.-W.2    Oh, H.-J.3    Choi, J.-O.4    Seo, K.-I.5    Park, E.-S.6    Park, H.-Y.7
  • 31
    • 0034212136 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase kinase 4 (MKK4)
    • Cuenda, A. (2000) Mitogen-activated protein kinase kinase 4 (MKK4). Int. J. Biochem. Cell Biol. 32, 581-587
    • (2000) Int. J. Biochem. Cell Biol. , vol.32 , pp. 581-587
    • Cuenda, A.1
  • 32
    • 73449143152 scopus 로고    scopus 로고
    • Novel mechanisms of protection against acetaminophen hepatotoxicity in mice by glutathione and N-acetylcysteine
    • Saito, C., Zwingmann, C., and Jaeschke, H. (2010) Novel mechanisms of protection against acetaminophen hepatotoxicity in mice by glutathione and N-acetylcysteine. Hepatology 51, 246-254
    • (2010) Hepatology , vol.51 , pp. 246-254
    • Saito, C.1    Zwingmann, C.2    Jaeschke, H.3
  • 33
    • 33846589652 scopus 로고    scopus 로고
    • Mutations and polymorphisms in the bile salt export pump and the multidrug resistance protein 3 associated with drug-induced liver injury
    • Lang, C., Meier, Y., Stieger, B., Beuers, U., Lang, T., Kerb, R., Kullak-Ublick, G. A., Meier, P. J., and Pauli-Magnus, C. (2007) Mutations and polymorphisms in the bile salt export pump and the multidrug resistance protein 3 associated with drug-induced liver injury. Pharmacogen. Genomics 17, 47-60
    • (2007) Pharmacogen. Genomics , vol.17 , pp. 47-60
    • Lang, C.1    Meier, Y.2    Stieger, B.3    Beuers, U.4    Lang, T.5    Kerb, R.6    Kullak-Ublick, G.A.7    Meier, P.J.8    Pauli-Magnus, C.9
  • 34
    • 47849118785 scopus 로고    scopus 로고
    • Acquired resistance to acetaminophen hepatotoxicity is associated with induction of multidrug resistance-associated protein 4 (Mrp4) in proliferating hepatocytes
    • Aleksunes, L. M., Campion, S. N., Goedken, M. J., and Manautou, J. E. (2008) Acquired resistance to acetaminophen hepatotoxicity is associated with induction of multidrug resistance-associated protein 4 (Mrp4) in proliferating hepatocytes. Toxicol. Sci. 104, 261-273
    • (2008) Toxicol. Sci. , vol.104 , pp. 261-273
    • Aleksunes, L.M.1    Campion, S.N.2    Goedken, M.J.3    Manautou, J.E.4
  • 35
    • 31144459322 scopus 로고    scopus 로고
    • Coordinated expression of multidrug resistance-associated proteins (Mrps) in mouse liver during toxicant-induced injury
    • Aleksunes, L. M., Scheffer, G. L., Jakowski, A. B., Pruimboom-Brees, I. M., and Manautou, J. E. (2006) Coordinated expression of multidrug resistance-associated proteins (Mrps) in mouse liver during toxicant-induced injury. Toxicol. Sci. 89, 370-379
    • (2006) Toxicol. Sci. , vol.89 , pp. 370-379
    • Aleksunes, L.M.1    Scheffer, G.L.2    Jakowski, A.B.3    Pruimboom-Brees, I.M.4    Manautou, J.E.5
  • 37
    • 0038036657 scopus 로고    scopus 로고
    • Overexpression of thioredoxin prevents acute hepatitis caused by thioacetamide or lipopolysaccharide in mice
    • Okuyama, H., Nakamura, H., Shimahara, Y., Araya, S., Kawada, N., Yamaoka, Y., and Yodoi, J. (2003) Overexpression of thioredoxin prevents acute hepatitis caused by thioacetamide or lipopolysaccharide in mice. Hepatology 37, 1015-1025
    • (2003) Hepatology , vol.37 , pp. 1015-1025
    • Okuyama, H.1    Nakamura, H.2    Shimahara, Y.3    Araya, S.4    Kawada, N.5    Yamaoka, Y.6    Yodoi, J.7
  • 39
    • 84864370670 scopus 로고    scopus 로고
    • Closing the gap on drug-induced liver injury
    • Maurel, M., and Rosenbaum, J. (2012) Closing the gap on drug-induced liver injury. Hepatology 56, 781-783
    • (2012) Hepatology , vol.56 , pp. 781-783
    • Maurel, M.1    Rosenbaum, J.2
  • 40
    • 3042821628 scopus 로고    scopus 로고
    • Connexin 32 dominant-negative mutant transgenic rats are resistant to hepatic damage by chemicals
    • Asamoto, M., Hokaiwado, N., Murasaki, T., and Shirai, T. (2004) Connexin 32 dominant-negative mutant transgenic rats are resistant to hepatic damage by chemicals. Hepatology 40, 205-210
    • (2004) Hepatology , vol.40 , pp. 205-210
    • Asamoto, M.1    Hokaiwado, N.2    Murasaki, T.3    Shirai, T.4
  • 41
    • 77952539714 scopus 로고    scopus 로고
    • Gap junction dysfunction reduces acetaminophen hepatotoxicity with impact on apoptotic signaling and connexin 43 protein induction in rat
    • Naiki-Ito, A., Asamoto, M., Naiki, T., Ogawa, K., Takahashi, S., Sato, S., and Shirai, T. (2010) Gap junction dysfunction reduces acetaminophen hepatotoxicity with impact on apoptotic signaling and connexin 43 protein induction in rat. Toxicol. Pathol. 38, 280-286
    • (2010) Toxicol. Pathol. , vol.38 , pp. 280-286
    • Naiki-Ito, A.1    Asamoto, M.2    Naiki, T.3    Ogawa, K.4    Takahashi, S.5    Sato, S.6    Shirai, T.7
  • 42
    • 25444475775 scopus 로고    scopus 로고
    • Lipid rafts prepared by different methods contain different connexin channels, but gap junctions are not lipid rafts
    • Locke, D., Liu, J., and Harris, A. L. (2005) Lipid rafts prepared by different methods contain different connexin channels, but gap junctions are not lipid rafts. Biochemistry 44, 13027-13042
    • (2005) Biochemistry , vol.44 , pp. 13027-13042
    • Locke, D.1    Liu, J.2    Harris, A.L.3
  • 43
    • 69149107146 scopus 로고    scopus 로고
    • DNA-triggered innate immune responses are propagated by gap junction communication
    • Patel, S. J., King, K. R., Casali, M., and Yarmush, M. L. (2009) DNA-triggered innate immune responses are propagated by gap junction communication. Proc. Natl. Acad. Sci. U. S. A. 106, 12867-12872
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 12867-12872
    • Patel, S.J.1    King, K.R.2    Casali, M.3    Yarmush, M.L.4
  • 44
  • 45
    • 0034122170 scopus 로고    scopus 로고
    • Taurine preserves gap junctional intercellular communication in rat hepatocytes under oxidative stress
    • Fukuda, T., Ikejima, K., Hirose, M., Takei, Y., Watanabe, S., and Sato, N. (2000) Taurine preserves gap junctional intercellular communication in rat hepatocytes under oxidative stress. J. Gastroenterol. 35, 361-368
    • (2000) J. Gastroenterol. , vol.35 , pp. 361-368
    • Fukuda, T.1    Ikejima, K.2    Hirose, M.3    Takei, Y.4    Watanabe, S.5    Sato, N.6
  • 47
    • 35349022491 scopus 로고    scopus 로고
    • Several dual specificity phosphatases coordinate to control the magnitude and duration of JNK activation in signaling response to oxidative stress
    • Teng, C.-H., Huang, W.-N., and Meng, T.-C. (2007) Several dual specificity phosphatases coordinate to control the magnitude and duration of JNK activation in signaling response to oxidative stress. J. Biol. Chem. 282, 28395-28407
    • (2007) J. Biol. Chem. , vol.282 , pp. 28395-28407
    • Teng, C.-H.1    Huang, W.-N.2    Meng, T.-C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.