메뉴 건너뛰기




Volumn 51, Issue 11, 2011, Pages 2082-2089

Glyceraldehyde-3-phosphate dehydrogenase as a quinone reductase in the suppression of 1,2-naphthoquinone protein adduct formation

Author keywords

1,2 Napthoquinone; Covalent modification; Free radicals; GAPDH; Two electron reduction

Indexed keywords

1,2 NAPHTHOQUINONE; ANTIBODY; CIBACRON BLUE F3GA; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCOLYTIC ENZYME; HYDROQUINONE; OXYGEN; PYRIDINE NUCLEOTIDE; RECOMBINANT ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 80255127462     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2011.09.008     Document Type: Article
Times cited : (10)

References (27)
  • 2
    • 0030592950 scopus 로고    scopus 로고
    • Characterisation of the toxic metabolite(s) of naphthalene
    • DOI 10.1016/S0300-483X(96)03515-9, PII S0300483X96035159
    • A.S. Wilson, C.D. Davis, D.P. Williams, A.R. Buckpitt, M. Pirmohamed, and B.K. Park Characterisation of the toxic metabolite(s) of naphthalene Toxicology 114 1996 233 242 (Pubitemid 26421936)
    • (1996) Toxicology , vol.114 , Issue.3 , pp. 233-242
    • Wilson, A.S.1    Davis, C.D.2    Williams, D.P.3    Buckpitt, A.R.4    Pirmohamed, M.5    Park, B.K.6
  • 4
    • 36349037272 scopus 로고    scopus 로고
    • Chemical knockdown of protein-tyrosine phosphatase 1B by 1,2-naphthoquinone through covalent modification causes persistent transactivation of epidermal growth factor receptor
    • DOI 10.1074/jbc.M705224200
    • N. Iwamoto, D. Sumi, T. Ishii, K. Uchida, A.K. Cho, J.R. Froines, and Y. Kumagai Chemical knockdown of protein-tyrosine phosphatase 1B by 1,2-naphthoquinone through covalent modification causes persistent transactivation of epidermal growth factor receptor J. Biol. Chem. 282 2007 33396 33404 (Pubitemid 350159512)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.46 , pp. 33396-33404
    • Iwamoto, N.1    Sumi, D.2    Ishii, T.3    Uchida, K.4    Cho, A.K.5    Froines, J.R.6    Kumagai, Y.7
  • 5
    • 34547133038 scopus 로고    scopus 로고
    • 1,2-Naphthoquinone disrupts the function of cAMP response element-binding protein through covalent modification
    • DOI 10.1016/j.bbrc.2007.07.024, PII S0006291X07014854
    • A. Endo, D. Sumi, and Y. Kumagai 1,2-Naphthoquinone disrupts the function of cAMP response element-binding protein through covalent modification Biochem. Biophys. Res. Commun. 361 2007 243 248 (Pubitemid 47102292)
    • (2007) Biochemical and Biophysical Research Communications , vol.361 , Issue.1 , pp. 243-248
    • Endo, A.1    Sumi, D.2    Kumagai, Y.3
  • 9
    • 33745897902 scopus 로고    scopus 로고
    • Transport of glutathione and glutathione conjugates by MRP1
    • DOI 10.1016/j.tips.2006.06.008, PII S0165614706001568
    • S.P. Cole, and R.G. Deeley Transport of glutathione and glutathione conjugates by MRP1 Trends Pharmacol. Sci. 27 2006 438 446 (Pubitemid 44051570)
    • (2006) Trends in Pharmacological Sciences , vol.27 , Issue.8 , pp. 438-446
    • Cole, S.P.C.1    Deeley, R.G.2
  • 10
    • 80255131167 scopus 로고    scopus 로고
    • GSH-mediated S-transarylation of a quinone glyceraldehyde-3-phosphate dehydrogenase conjugate
    • [Electronic publication ahead of print]. doi.
    • Miura, T.; Kakehashi, H.; Shinkai, Y.; Egara, Y.; Hirose, R.; Cho, A. K.; Kumagai, Y. GSH-mediated S-transarylation of a quinone glyceraldehyde-3- phosphate dehydrogenase conjugate. Chem. Res. Toxicol.; 2011 [Electronic publication ahead of print]. doi: 10.1021/tx200025y.
    • (2011) Chem. Res. Toxicol.
    • Miura, T.1    Kakehashi, H.2    Shinkai, Y.3    Egara, Y.4    Hirose, R.5    Cho, A.K.6    Kumagai, Y.7
  • 11
    • 78649878916 scopus 로고    scopus 로고
    • Immunochemical method to detect proteins that undergo selective modification by 1,2-naphthoquinone derived from naphthalene through metabolic activation
    • T. Miura, and Y. Kumagai Immunochemical method to detect proteins that undergo selective modification by 1,2-naphthoquinone derived from naphthalene through metabolic activation J. Toxicol. Sci. 35 2010 843 852
    • (2010) J. Toxicol. Sci. , vol.35 , pp. 843-852
    • Miura, T.1    Kumagai, Y.2
  • 12
    • 34547093431 scopus 로고    scopus 로고
    • An approach to evaluate two-electron reduction of 9,10-phenanthraquinone and redox activity of the hydroquinone associated with oxidative stress
    • DOI 10.1016/j.freeradbiomed.2007.05.021, PII S0891584907003528
    • K. Taguchi, S. Fujii, S. Yamano, A.K. Cho, S. Kamisuki, Y. Nakai, F. Sugawara, J.R. Froines, and Y. Kumagai An approach to evaluate two-electron reduction of 9,10-phenanthraquinone and redox activity of the hydroquinone associated with oxidative stress Free Radic. Biol. Med. 43 2007 789 799 (Pubitemid 47102127)
    • (2007) Free Radical Biology and Medicine , vol.43 , Issue.5 , pp. 789-799
    • Taguchi, K.1    Fujii, S.2    Yamano, S.3    Cho, A.K.4    Kamisuki, S.5    Nakai, Y.6    Sugawara, F.7    Froines, J.R.8    Kumagai, Y.9
  • 13
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • DOI 10.1016/0165-022X(84)90040-X
    • J. Kyhse-Andersen Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose J. Biochem. Biophys. Methods 10 1984 203 209 (Pubitemid 15171298)
    • (1984) Journal of Biochemical and Biophysical Methods , vol.10 , Issue.3-4 , pp. 203-209
    • Kyhse-Andersen, J.1
  • 16
    • 38049100668 scopus 로고    scopus 로고
    • On the interaction between glyceraldehyde-3-phosphate dehydrogenase and airborne particles: Evidence for electrophilic species
    • M. Shinyashiki, C. Rodriguez, E. Di Stefano, C. Sioutas, R. Delfino, Y. Kumagai, J. Froines, and A. Cho On the interaction between glyceraldehyde-3- phosphate dehydrogenase and airborne particles: evidence for electrophilic species Atmos. Environ. 42 2008 517 529
    • (2008) Atmos. Environ. , vol.42 , pp. 517-529
    • Shinyashiki, M.1    Rodriguez, C.2    Di Stefano, E.3    Sioutas, C.4    Delfino, R.5    Kumagai, Y.6    Froines, J.7    Cho, A.8
  • 17
    • 20644457548 scopus 로고    scopus 로고
    • The interactions of 9,10-phenanthrenequinone with glyceraldehyde-3- phosphate dehydrogenase (GAPDH), a potential site for toxic actions
    • DOI 10.1016/j.cbi.2005.05.002, PII S0009279705001511
    • C.E. Rodriguez, J.M. Fukuto, K. Taguchi, J. Froines, and A.K. Cho The interactions of 9,10-phenanthrenequinone with glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a potential site for toxic actions Chem. Biol. Interact. 155 2005 97 110 (Pubitemid 40835993)
    • (2005) Chemico-Biological Interactions , vol.155 , Issue.1-2 , pp. 97-110
    • Rodriguez, C.E.1    Fukuto, J.M.2    Taguchi, K.3    Froines, J.4    Cho, A.K.5
  • 18
    • 0027480753 scopus 로고
    • Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase. A possible involvement of intra- and intermolecular cross- linking reaction
    • K. Uchida, and E.R. Stadtman Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase: a possible involvement of intra- and intermolecular cross-linking reaction J. Biol. Chem. 268 1993 6388 6393 (Pubitemid 23099334)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.9 , pp. 6388-6393
    • Uchida, K.1    Stadtman, E.R.2
  • 19
    • 0026029166 scopus 로고
    • Identification of koningic acid (heptelidic acid)-modified site in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase
    • K. Sakai, K. Hasumi, and A. Endo Identification of koningic acid (heptelidic acid)-modified site in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase Biochim. Biophys. Acta 1077 1991 192 196
    • (1991) Biochim. Biophys. Acta , vol.1077 , pp. 192-196
    • Sakai, K.1    Hasumi, K.2    Endo, A.3
  • 22
    • 0024498044 scopus 로고
    • DT-diaphorase-catalysed reduction of 1,4-naphthoquinone derivatives and glutathionyl-quinone conjugates. Effect of substituents on autoxidation rates
    • G.D. Buffinton, K. Ollinger, A. Brunmark, and E. Cadenas DT-diaphorase-catalysed reduction of 1,4-naphthoquinone derivatives and glutathionyl-quinone conjugates: effect of substituents on autoxidation rates Biochem. J. 257 1989 561 571 (Pubitemid 19040932)
    • (1989) Biochemical Journal , vol.257 , Issue.2 , pp. 561-571
    • Buffinton, G.D.1    Ollinger, K.2    Brunmark, A.3    Cadenas, E.4
  • 23
    • 0033569574 scopus 로고    scopus 로고
    • 1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members
    • DOI 10.1042/0264-6021:3430487
    • T. O'Connor, L.S. Ireland, D.J. Harrison, and J.D. Hayes Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo-keto reductase AKR1 family members Biochem. J. 343 Pt 2 1999 487 504 (Pubitemid 29511786)
    • (1999) Biochemical Journal , vol.343 , Issue.2 , pp. 487-504
    • O'Connor, T.1    Ireland, L.S.2    Harrison, D.J.3    Hayes, J.D.4
  • 24
    • 0016802486 scopus 로고
    • The specificity of induced conformational changes: The case of yeast glyceraldehyde-3-phosphate dehydrogenase
    • L.D. Byers, and D.E. Koshland Jr. The specificity of induced conformational changes: the case of yeast glyceraldehyde-3-phosphate dehydrogenase Biochemistry 14 1975 3661 3669
    • (1975) Biochemistry , vol.14 , pp. 3661-3669
    • Byers, L.D.1    Koshland Jr., D.E.2
  • 25
    • 0034609535 scopus 로고    scopus 로고
    • Structural analysis of glyceraldehyde 3-phosphate dehydrogenase from Escherichia coli: Direct evidence of substrate binding and cofactor-induced conformational changes
    • M. Yun, C.G. Park, J.Y. Kim, and H.W. Park Structural analysis of glyceraldehyde 3-phosphate dehydrogenase from Escherichia coli: direct evidence of substrate binding and cofactor-induced conformational changes Biochemistry 39 2000 10702 10710
    • (2000) Biochemistry , vol.39 , pp. 10702-10710
    • Yun, M.1    Park, C.G.2    Kim, J.Y.3    Park, H.W.4
  • 26
    • 0013774083 scopus 로고
    • The mechanism of action of glyceraldehyde-3-phosphate dehydrogenase
    • L. Polgar The mechanism of action of glyceraldehyde-3-phosphate dehydrogenase Experientia 20 1964 408 413
    • (1964) Experientia , vol.20 , pp. 408-413
    • Polgar, L.1
  • 27
    • 0035471025 scopus 로고    scopus 로고
    • Study of the properties of phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase
    • DOI 10.1023/A:1012472627801
    • N.K. Nagradova Study of the properties of phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase Biochem. (Moscow) 66 2001 1067 1076 (Pubitemid 33099909)
    • (2001) Biochemistry (Moscow) , vol.66 , Issue.10 , pp. 1067-1076
    • Nagradova, N.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.