메뉴 건너뛰기




Volumn 86, Issue 19-20, 2010, Pages 726-732

Inhibition of mitochondrial membrane bound-glutathione transferase by mitochondrial permeability transition inhibitors including cyclosporin A

Author keywords

Adenine nucleotide translocator; Cyclophilin D; Cyclosporin A; Glutathione transferase; Mitochondria; Mitochondrial permeability transition

Indexed keywords

BONGKREKIC ACID; CIBACRON BLUE F3GA; CYCLOPHILIN D; CYCLOSPORIN A; ENZYME INHIBITOR; GLUTATHIONE TRANSFERASE; GLUTATHIONE TRANSFERASE INHIBITOR; HEXYLGLUTATHIONE; MITOCHONDRIAL PERMEABILITY TRANSITION INHIBITOR; PROTEIN INHIBITOR; TRITON X 100; UNCLASSIFIED DRUG; ADENINE NUCLEOTIDE TRANSLOCASE; ADENOSINE DIPHOSPHATE; CARRIER PROTEIN; CYCLOPHILIN; CYCLOSPORIN; MICROSOMAL GLUTATHIONE S TRANSFERASE I; MICROSOMAL GLUTATHIONE S-TRANSFERASE-I; MITOCHONDRIAL PERMEABILITY TRANSITION PORE;

EID: 77951899737     PISSN: 00243205     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lfs.2010.03.002     Document Type: Article
Times cited : (14)

References (31)
  • 1
    • 0029021811 scopus 로고
    • Evidence for the involvement of a membrane-associated cyclosporin-A-binding protein in the Ca(2+)-activated inner membrane pore of heart mitochondria
    • Andreeva L., Tanveer A., Crompton M. Evidence for the involvement of a membrane-associated cyclosporin-A-binding protein in the Ca(2+)-activated inner membrane pore of heart mitochondria. European Journal of Biochemistry 1995, 230(3):1125-1132.
    • (1995) European Journal of Biochemistry , vol.230 , Issue.3 , pp. 1125-1132
    • Andreeva, L.1    Tanveer, A.2    Crompton, M.3
  • 2
    • 0026726105 scopus 로고
    • Activation of rat liver microsomal glutathione S-transferase by hydrogen peroxide: role for protein-dimer formation
    • Aniya Y., Anders M. Activation of rat liver microsomal glutathione S-transferase by hydrogen peroxide: role for protein-dimer formation. Archives of Biochemistry and Biophysics 1992, 296(2):611-616.
    • (1992) Archives of Biochemistry and Biophysics , vol.296 , Issue.2 , pp. 611-616
    • Aniya, Y.1    Anders, M.2
  • 3
    • 67349285823 scopus 로고    scopus 로고
    • The molecular composition of the mitochondrial permeability transition pore
    • Baines C. The molecular composition of the mitochondrial permeability transition pore. Journal of Molecular and Cellular Cardiology 2009, 46(6):850-857.
    • (2009) Journal of Molecular and Cellular Cardiology , vol.46 , Issue.6 , pp. 850-857
    • Baines, C.1
  • 6
    • 0026696585 scopus 로고
    • Purification and N-terminal sequencing of peptidyl-prolyl cis-trans-isomerase from rat liver mitochondrial matrix reveals the existence of a distinct mitochondrial cyclophilin
    • Connern C., Halestrap A. Purification and N-terminal sequencing of peptidyl-prolyl cis-trans-isomerase from rat liver mitochondrial matrix reveals the existence of a distinct mitochondrial cyclophilin. Biochemical Journal 1992, 284(Pt 2):381-385.
    • (1992) Biochemical Journal , vol.284 , Issue.PART 2 , pp. 381-385
    • Connern, C.1    Halestrap, A.2
  • 9
    • 0034983918 scopus 로고    scopus 로고
    • Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase
    • Gottlob K., Majewski N., Kennedy S., Kandel E., Robey R., Hay N. Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase. Genes & Development 2001, 15(11):1406-1418.
    • (2001) Genes & Development , vol.15 , Issue.11 , pp. 1406-1418
    • Gottlob, K.1    Majewski, N.2    Kennedy, S.3    Kandel, E.4    Robey, R.5    Hay, N.6
  • 10
    • 0016275313 scopus 로고
    • Glutathione S-transferases. The first enzymatic step in mercapturic acid formation
    • Habig W., Pabst M., Jakoby W. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. Journal of Biological Chemistry 1974, 249(22):7130-7139.
    • (1974) Journal of Biological Chemistry , vol.249 , Issue.22 , pp. 7130-7139
    • Habig, W.1    Pabst, M.2    Jakoby, W.3
  • 11
    • 67349117275 scopus 로고    scopus 로고
    • What is the mitochondrial permeability transition pore ?
    • Halestrap A. What is the mitochondrial permeability transition pore ?. Journal of Molecular and Cellular Cardiology 2009, 46(6):821-831.
    • (2009) Journal of Molecular and Cellular Cardiology , vol.46 , Issue.6 , pp. 821-831
    • Halestrap, A.1
  • 13
    • 59149085002 scopus 로고    scopus 로고
    • Contribution of liver mitochondrial membrane-bound glutathione transferase to mitochondrial permeability transition pores
    • Hossain Q.S., Ulziikhishig E., Lee K.K., Yamamoto H., Aniya Y. Contribution of liver mitochondrial membrane-bound glutathione transferase to mitochondrial permeability transition pores. Toxicology and Applied Pharmacology 2009, 235(1):77-85.
    • (2009) Toxicology and Applied Pharmacology , vol.235 , Issue.1 , pp. 77-85
    • Hossain, Q.S.1    Ulziikhishig, E.2    Lee, K.K.3    Yamamoto, H.4    Aniya, Y.5
  • 14
    • 33646187917 scopus 로고    scopus 로고
    • Reactive nitrogen species derived activation of rat liver microsomal glutathione S-transferase
    • Imaizumi N., Miyagi S., Aniya Y. Reactive nitrogen species derived activation of rat liver microsomal glutathione S-transferase. Life Sciences 2006, 78(26):2998-3006.
    • (2006) Life Sciences , vol.78 , Issue.26 , pp. 2998-3006
    • Imaizumi, N.1    Miyagi, S.2    Aniya, Y.3
  • 17
    • 0017897434 scopus 로고
    • Glutathione transferases. Catalysis of nucleophilic reactions of glutathione
    • Keen J., Jakoby W. Glutathione transferases. Catalysis of nucleophilic reactions of glutathione. Journal of Biological Chemistry 1978, 253(16):5654-5657.
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.16 , pp. 5654-5657
    • Keen, J.1    Jakoby, W.2
  • 18
    • 0842307483 scopus 로고    scopus 로고
    • The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore
    • Kokoszka J., Waymire K., Levy S., Sligh J., Cai J., Jones D., et al. The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore. Nature 2004, 427(6973):461-465.
    • (2004) Nature , vol.427 , Issue.6973 , pp. 461-465
    • Kokoszka, J.1    Waymire, K.2    Levy, S.3    Sligh, J.4    Cai, J.5    Jones, D.6
  • 19
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer G., Galluzzi L., Brenner C. Mitochondrial membrane permeabilization in cell death. Physiological Reviews 2007, 87(1):99-163.
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 20
    • 51549090341 scopus 로고    scopus 로고
    • Novel function of glutathione transferase in rat liver mitochondrial membrane: role for cytochrome c release from mitochondria
    • Lee K.K., Shimoji M., Hossain Q.S., Sunakawa H., Aniya Y. Novel function of glutathione transferase in rat liver mitochondrial membrane: role for cytochrome c release from mitochondria. Toxicology and Applied Pharmacology 2008, 232(1):109-118.
    • (2008) Toxicology and Applied Pharmacology , vol.232 , Issue.1 , pp. 109-118
    • Lee, K.K.1    Shimoji, M.2    Hossain, Q.S.3    Sunakawa, H.4    Aniya, Y.5
  • 22
    • 0041316988 scopus 로고    scopus 로고
    • Novel class of bivalent glutathione S-transferase inhibitors
    • Lyon R.P., Hill J.J., Atkins W.M. Novel class of bivalent glutathione S-transferase inhibitors. Biochemistry 2003, 42(35):10418-10428.
    • (2003) Biochemistry , vol.42 , Issue.35 , pp. 10418-10428
    • Lyon, R.P.1    Hill, J.J.2    Atkins, W.M.3
  • 23
    • 21144440291 scopus 로고    scopus 로고
    • The chemistry and biology of inhibitors and pro-drugs targeted to glutathione S-transferases
    • Mahajan S., Atkins W. The chemistry and biology of inhibitors and pro-drugs targeted to glutathione S-transferases. Cellular and Molecular Life Sciences 2005, 62(11):1221-1233.
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.11 , pp. 1221-1233
    • Mahajan, S.1    Atkins, W.2
  • 24
    • 37349002016 scopus 로고    scopus 로고
    • Dithiothreitol abrogates the effect of arsenic trioxide on normal rat liver mitochondria and human hepatocellular carcinoma cells
    • Paul M., Kumar R., Mukhopadhyay A. Dithiothreitol abrogates the effect of arsenic trioxide on normal rat liver mitochondria and human hepatocellular carcinoma cells. Toxicology and Applied Pharmacology 2008, 226(2):140-152.
    • (2008) Toxicology and Applied Pharmacology , vol.226 , Issue.2 , pp. 140-152
    • Paul, M.1    Kumar, R.2    Mukhopadhyay, A.3
  • 25
    • 0008930305 scopus 로고    scopus 로고
    • Mechanisms of allograft rejection
    • Lippincott-Raven, Philadelphia, E.G. Neilson, W.G. Couser (Eds.)
    • Pattison J.M., Sibley R.K., Krensky A.M. Mechanisms of allograft rejection. Immunologic renal Diseases 1997, 331-354. Lippincott-Raven, Philadelphia. E.G. Neilson, W.G. Couser (Eds.).
    • (1997) Immunologic renal Diseases , pp. 331-354
    • Pattison, J.M.1    Sibley, R.K.2    Krensky, A.M.3
  • 28
    • 51549112254 scopus 로고    scopus 로고
    • Activation of microsomal glutathione transferase 1 in toxicology
    • Taylor & Francis, New York, Y.C. Awasthi (Ed.)
    • Shimoji M., Aniya Y., Morgenstern R. Activation of microsomal glutathione transferase 1 in toxicology. Toxicology of glutathione transferases 2007, 293-319. Taylor & Francis, New York. Y.C. Awasthi (Ed.).
    • (2007) Toxicology of glutathione transferases , pp. 293-319
    • Shimoji, M.1    Aniya, Y.2    Morgenstern, R.3
  • 31


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.