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Volumn 83, Issue 11, 2012, Pages 1507-1513

Covalent binding of cisplatin impairs the function of Na +/K +-ATPase by binding to its cytoplasmic part

Author keywords

Cisplatin; Cysteine; Na +,K + ATPase; Nephrotoxicity; Sodium pump

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ASPARTIC ACID; CARBOPLATIN; CISPLATIN; CYSTEINE; OXALIPLATIN;

EID: 84859495833     PISSN: 00062952     EISSN: 18732968     Source Type: Journal    
DOI: 10.1016/j.bcp.2012.02.015     Document Type: Article
Times cited : (40)

References (47)
  • 1
    • 61549087775 scopus 로고    scopus 로고
    • Cisplatin: A review of toxicities and therapeutic applications
    • K. Barabas, R. Milner, D. Lurie, and C. Adin Cisplatin: a review of toxicities and therapeutic applications Vet Comp Oncol 6 2008 1 18
    • (2008) Vet Comp Oncol , vol.6 , pp. 1-18
    • Barabas, K.1    Milner, R.2    Lurie, D.3    Adin, C.4
  • 2
    • 33644767850 scopus 로고    scopus 로고
    • Role of copper transporters in the uptake and efflux of platinum containing drugs
    • R. Safaei Role of copper transporters in the uptake and efflux of platinum containing drugs Cancer Lett 234 2006 34 39
    • (2006) Cancer Lett , vol.234 , pp. 34-39
    • Safaei, R.1
  • 3
    • 79551489546 scopus 로고    scopus 로고
    • Organic cation transporter OCT/SLC22A and H(+)/organic cation antiporter MATE/SLC47A are key molecules for nephrotoxicity of platinum agents
    • A. Yonezawa, and K. Inui Organic cation transporter OCT/SLC22A and H(+)/organic cation antiporter MATE/SLC47A are key molecules for nephrotoxicity of platinum agents Biochem Pharmacol 81 2011 563 568
    • (2011) Biochem Pharmacol , vol.81 , pp. 563-568
    • Yonezawa, A.1    Inui, K.2
  • 4
    • 0018633891 scopus 로고
    • Anti-cancer activity of cis-dichloroammineplatinum(II) and some relevant chemistry
    • B. Rosenberg Anti-cancer activity of cis-dichloroammineplatinum(II) and some relevant chemistry Cancer Treat Rep 63 1979 1433 1438
    • (1979) Cancer Treat Rep , vol.63 , pp. 1433-1438
    • Rosenberg, B.1
  • 5
    • 34548455064 scopus 로고    scopus 로고
    • Repair capacity for platinum-DNA adducts determines the severity of cisplatin-induced peripheral neuropathy
    • A. Dzagnidze, Z. Katsarava, J. Makhalova, B. Liedert, M.S. Yoon, and H. Kaube Repair capacity for platinum-DNA adducts determines the severity of cisplatin-induced peripheral neuropathy J Neurosci 27 2007 9451 9457
    • (2007) J Neurosci , vol.27 , pp. 9451-9457
    • Dzagnidze, A.1    Katsarava, Z.2    Makhalova, J.3    Liedert, B.4    Yoon, M.S.5    Kaube, H.6
  • 7
    • 0022879127 scopus 로고
    • Nephrotoxicity induced by cancer-chemotherapy with special emphasis on cisplatin toxicity
    • F. Ries, and J. Klastersky Nephrotoxicity induced by cancer-chemotherapy with special emphasis on cisplatin toxicity Am J Kidney Dis 8 1986 368 379
    • (1986) Am J Kidney Dis , vol.8 , pp. 368-379
    • Ries, F.1    Klastersky, J.2
  • 8
    • 42149187768 scopus 로고    scopus 로고
    • Cisplatin nephrotoxicity: Mechanisms and renoprotective strategies
    • N. Pabla, and Z. Dong Cisplatin nephrotoxicity: mechanisms and renoprotective strategies Kidney Int 73 2008 994 1007
    • (2008) Kidney Int , vol.73 , pp. 994-1007
    • Pabla, N.1    Dong, Z.2
  • 9
    • 28644437521 scopus 로고    scopus 로고
    • Hormonal and nonhormonal mechanisms of regulation of the Na,K-pump in collecting duct principal cells
    • M. Vinciguerra, D. Mordasini, A. Vandewalle, and E. Feraille Hormonal and nonhormonal mechanisms of regulation of the Na,K-pump in collecting duct principal cells Semin Nephrol 25 2005 312 321
    • (2005) Semin Nephrol , vol.25 , pp. 312-321
    • Vinciguerra, M.1    Mordasini, D.2    Vandewalle, A.3    Feraille, E.4
  • 10
    • 0036434869 scopus 로고    scopus 로고
    • Large-scale preparation of sodium-potassium ATPase from kidney outer medulla
    • I. Klodos, M. Esmann, and R.L. Post Large-scale preparation of sodium-potassium ATPase from kidney outer medulla Kidney Int 62 2002 2097 2100
    • (2002) Kidney Int , vol.62 , pp. 2097-2100
    • Klodos, I.1    Esmann, M.2    Post, R.L.3
  • 12
    • 66249147196 scopus 로고    scopus 로고
    • Crystal structure of the sodium-potassium pump at 2.4 angstrom resolution
    • T. Shinoda, H. Ogawa, F. Cornelius, and C. Toyoshima Crystal structure of the sodium-potassium pump at 2.4 angstrom resolution Nature 459 2009 446 450
    • (2009) Nature , vol.459 , pp. 446-450
    • Shinoda, T.1    Ogawa, H.2    Cornelius, F.3    Toyoshima, C.4
  • 13
    • 0034773778 scopus 로고    scopus 로고
    • The functional role of beta subunits in oligomeric P-type ATPases
    • K. Geering The functional role of beta subunits in oligomeric P-type ATPases J Bioenerg Biomembr 33 2001 425 438
    • (2001) J Bioenerg Biomembr , vol.33 , pp. 425-438
    • Geering, K.1
  • 14
    • 0032562606 scopus 로고    scopus 로고
    • The M4M5 cytoplasmic loop of the Na,K-ATPase, overexpressed in Escherichia coli, binds nucleoside triphosphates with the same selectivity as the intact native protein
    • C. Gatto, A.X. Wang, and J.H. Kaplan The M4M5 cytoplasmic loop of the Na,K-ATPase, overexpressed in Escherichia coli, binds nucleoside triphosphates with the same selectivity as the intact native protein J Biol Chem 273 1998 10578 10585
    • (1998) J Biol Chem , vol.273 , pp. 10578-10585
    • Gatto, C.1    Wang, A.X.2    Kaplan, J.H.3
  • 15
    • 0032975040 scopus 로고    scopus 로고
    • Catalytic activity of an isolated domain of Na,K-ATPase expressed in Escherichia coli
    • C.M. Tran, and R.A. Farley Catalytic activity of an isolated domain of Na,K-ATPase expressed in Escherichia coli Biophys J 77 1999 258 266
    • (1999) Biophys J , vol.77 , pp. 258-266
    • Tran, C.M.1    Farley, R.A.2
  • 17
    • 70350031203 scopus 로고    scopus 로고
    • Changes in electrostatic surface potential of Na(+)/K(+)-ATPase cytoplasmic headpiece induced by cytoplasmic ligand(s) binding
    • M. Kubala, L. Grycova, Z. Lansky, P. Sklenovsky, M. Janovska, and M. Otyepka Changes in electrostatic surface potential of Na(+)/K(+)-ATPase cytoplasmic headpiece induced by cytoplasmic ligand(s) binding Biophys J 97 2009 1756 1764
    • (2009) Biophys J , vol.97 , pp. 1756-1764
    • Kubala, M.1    Grycova, L.2    Lansky, Z.3    Sklenovsky, P.4    Janovska, M.5    Otyepka, M.6
  • 18
    • 0043208929 scopus 로고    scopus 로고
    • Limitations in linearized analyses of binding equilibria: Binding of TNP-ATP to the H-4-H-5 loop of Na/K-ATPase
    • M. Kubala, J. Plasek, and E. Amler Limitations in linearized analyses of binding equilibria: binding of TNP-ATP to the H-4-H-5 loop of Na/K-ATPase Eur Biophys J Biophys Lett 32 2003 363 369
    • (2003) Eur Biophys J Biophys Lett , vol.32 , pp. 363-369
    • Kubala, M.1    Plasek, J.2    Amler, E.3
  • 21
    • 34547436392 scopus 로고    scopus 로고
    • Mass spectrometric analysis of ubiquitin-platinum interactions of leading anticancer drugs: MALDI versus ESI
    • C.G. Hartinger, W.H. Ang, A. Casini, L. Messori, B.K. Keppler, and P.J. Dyson Mass spectrometric analysis of ubiquitin-platinum interactions of leading anticancer drugs: MALDI versus ESI J Anal Atomic Spectrom 22 2007 960 967
    • (2007) J Anal Atomic Spectrom , vol.22 , pp. 960-967
    • Hartinger, C.G.1    Ang, W.H.2    Casini, A.3    Messori, L.4    Keppler, B.K.5    Dyson, P.J.6
  • 22
    • 38749084242 scopus 로고    scopus 로고
    • Characterization of platinum anticancer drug protein-binding sites using a top-down mass spectrometric approach
    • C.G. Hartinger, Y.O. Tsybin, J. Fuchser, and P.J. Dyson Characterization of platinum anticancer drug protein-binding sites using a top-down mass spectrometric approach Inorg Chem 47 2008 17 19
    • (2008) Inorg Chem , vol.47 , pp. 17-19
    • Hartinger, C.G.1    Tsybin, Y.O.2    Fuchser, J.3    Dyson, P.J.4
  • 23
    • 0027305406 scopus 로고
    • Glutathione-associated cis-diamminodichloroplatinum(II) metabolism and ATP-dependent efflux from leukemia-cells - Molecular characterization of glutathione-platinum complex and its biological significance
    • T. Ishikawa, and F. Aliosman Glutathione-associated cis- diamminodichloroplatinum(II) metabolism and ATP-dependent efflux from leukemia-cells - molecular characterization of glutathione-platinum complex and its biological significance J Biol Chem 268 1993 20116 20125
    • (1993) J Biol Chem , vol.268 , pp. 20116-20125
    • Ishikawa, T.1    Aliosman, F.2
  • 24
    • 0002304923 scopus 로고
    • Reactions of cisplatin with sulfur-containing amino-acids and peptides. 1. Cysteine and glutathione
    • B. Odenheimer, and W. Wolf Reactions of cisplatin with sulfur-containing amino-acids and peptides. 1. Cysteine and glutathione Inorg Chim Acta 66 1982 L41 L43
    • (1982) Inorg Chim Acta , vol.66
    • Odenheimer, B.1    Wolf, W.2
  • 25
    • 0013844613 scopus 로고
    • Highly specific sodium-potassium-activated adenosine triphosphatase from various tissues of rabbit
    • T. Nakao, Y. Tashima, K. Nagano, and M. Nakao Highly specific sodium-potassium-activated adenosine triphosphatase from various tissues of rabbit Biochem Biophys Res Commun 19 1965 755 758
    • (1965) Biochem Biophys Res Commun , vol.19 , pp. 755-758
    • Nakao, T.1    Tashima, Y.2    Nagano, K.3    Nakao, M.4
  • 26
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding
    • M.M. Bradford Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding Anal Biochem 72 1976 248 254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 9644266645 scopus 로고    scopus 로고
    • Staining of proteins on SDS polyacrylamide gels and on nitrocellulose membranes by Alta, a colour used as a cosmetic
    • J.K. Pal, D. Godbole, and K. Sharma Staining of proteins on SDS polyacrylamide gels and on nitrocellulose membranes by Alta, a colour used as a cosmetic J Biochem Biophys Methods 61 2004 339 347
    • (2004) J Biochem Biophys Methods , vol.61 , pp. 339-347
    • Pal, J.K.1    Godbole, D.2    Sharma, K.3
  • 28
    • 0025344156 scopus 로고
    • A continuous fluorimetric assay for ATPase activity
    • U. Banik, and S. Roy A continuous fluorimetric assay for ATPase activity Biochem J 266 1990 611 614
    • (1990) Biochem J , vol.266 , pp. 611-614
    • Banik, U.1    Roy, S.2
  • 29
    • 0037093907 scopus 로고    scopus 로고
    • Catalytic signal of rabbit liver metallothionein on a mercury electrode: A combination of derivative chronopotentiometry with adsorptive transfer stripping
    • L. Trnkova, R. Kizek, and J. Vacek Catalytic signal of rabbit liver metallothionein on a mercury electrode: a combination of derivative chronopotentiometry with adsorptive transfer stripping Bioelectrochemistry 56 2002 57 61
    • (2002) Bioelectrochemistry , vol.56 , pp. 57-61
    • Trnkova, L.1    Kizek, R.2    Vacek, J.3
  • 30
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • A. Shevchenko, H. Tomas, J. Havlis, J.V. Olsen, and M. Mann In-gel digestion for mass spectrometric characterization of proteins and proteomes Nat Protoc 1 2006 2856 2860
    • (2006) Nat Protoc , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 31
    • 0000094029 scopus 로고
    • Improved resolutionand very high-sensitivity in MALDI TOF of matrix surfaces made by fast evaporation
    • O. Vorm, P. Roepstorff, and M. Mann Improved resolutionand very high-sensitivity in MALDI TOF of matrix surfaces made by fast evaporation Anal Chem 66 1994 3281 3287
    • (1994) Anal Chem , vol.66 , pp. 3281-3287
    • Vorm, O.1    Roepstorff, P.2    Mann, M.3
  • 32
    • 77950631490 scopus 로고    scopus 로고
    • From DC polarographic presodium wave of proteins to electrochemistry of biomacromolecules
    • E. Palecek, M. Heyrovsky, B. Janik, D. Kalab, and Z. Pechan From DC polarographic presodium wave of proteins to electrochemistry of biomacromolecules Collect Czech Chem Commun 74 2009 1739 1755
    • (2009) Collect Czech Chem Commun , vol.74 , pp. 1739-1755
    • Palecek, E.1    Heyrovsky, M.2    Janik, B.3    Kalab, D.4    Pechan, Z.5
  • 33
    • 62349121113 scopus 로고    scopus 로고
    • Electrochemical determination of thioredoxin redox states
    • V. Dorcak, and E. Palecek Electrochemical determination of thioredoxin redox states Anal Chem 81 2009 1543 1548
    • (2009) Anal Chem , vol.81 , pp. 1543-1548
    • Dorcak, V.1    Palecek, E.2
  • 34
    • 0033673144 scopus 로고    scopus 로고
    • The presodium catalysis of electroreduction of hydrogen ions on mercury electrodes by metallothionein. An investigation by constant current derivative stripping chronopotentiometry
    • M. Tomschik, L. Havran, E. Palecek, and M. Heyrovsky The presodium catalysis of electroreduction of hydrogen ions on mercury electrodes by metallothionein. An investigation by constant current derivative stripping chronopotentiometry Electroanalysis 12 2000 274 279
    • (2000) Electroanalysis , vol.12 , pp. 274-279
    • Tomschik, M.1    Havran, L.2    Palecek, E.3    Heyrovsky, M.4
  • 35
    • 79955784193 scopus 로고    scopus 로고
    • Mass-spectrometric characterization of cisplatin binding sites on native and denatured ubiquitin
    • T. Zhao, and F.L. King Mass-spectrometric characterization of cisplatin binding sites on native and denatured ubiquitin J Biol Inorg Chem 16 2011 633 639
    • (2011) J Biol Inorg Chem , vol.16 , pp. 633-639
    • Zhao, T.1    King, F.L.2
  • 36
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • G.L. Ellman Tissue sulfhydryl groups Arch Biochem Biophys 82 1959 70 77
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 37
    • 0019983423 scopus 로고
    • The inhibition of renal ATPase by cisplatin and some biotransformation products
    • P.T. Daley-Yates, and D.C.H. McBrien The inhibition of renal ATPase by cisplatin and some biotransformation products Chem Biol Interact 40 1982 325 334
    • (1982) Chem Biol Interact , vol.40 , pp. 325-334
    • Daley-Yates, P.T.1    McBrien, D.C.H.2
  • 38
    • 79960981382 scopus 로고    scopus 로고
    • Necrotic concentrations of cisplatin activate the apoptotic machinery but inhibit effector caspases and interfere with the execution of apoptosis
    • S.M. Sancho-Martinez, F.J. Piedrafita, J.B. Cannata-Andia, J.M. Lopez-Novoa, and F.J. Lopez-Hernandez Necrotic concentrations of cisplatin activate the apoptotic machinery but inhibit effector caspases and interfere with the execution of apoptosis Toxicol Sci 122 2011 73 85
    • (2011) Toxicol Sci , vol.122 , pp. 73-85
    • Sancho-Martinez, S.M.1    Piedrafita, F.J.2    Cannata-Andia, J.B.3    Lopez-Novoa, J.M.4    Lopez-Hernandez, F.J.5
  • 39
    • 78649976515 scopus 로고    scopus 로고
    • Ouabain-induced apoptosis and Rho kinase: A novel caspase-2 cleavage site and fragment of Rock-2
    • M. Ark, A. Ozdemir, and B. Polat Ouabain-induced apoptosis and Rho kinase: a novel caspase-2 cleavage site and fragment of Rock-2 Apoptosis 15 2010 1494 1506
    • (2010) Apoptosis , vol.15 , pp. 1494-1506
    • Ark, M.1    Ozdemir, A.2    Polat, B.3
  • 40
    • 77952327427 scopus 로고    scopus 로고
    • Targeting the Na(+)/K(+)-ATPase alpha 1 subunit of hepatoma HepG2 cell line to induce apoptosis and cell cycle arresting
    • Z.W. Xu, F.M. Wang, M.J. Gao, X.Y. Chen, W.L. Hu, and R.C. Xu Targeting the Na(+)/K(+)-ATPase alpha 1 subunit of hepatoma HepG2 cell line to induce apoptosis and cell cycle arresting Biol Pharm Bull 33 2010 743 751
    • (2010) Biol Pharm Bull , vol.33 , pp. 743-751
    • Xu, Z.W.1    Wang, F.M.2    Gao, M.J.3    Chen, X.Y.4    Hu, W.L.5    Xu, R.C.6
  • 41
    • 58849142986 scopus 로고    scopus 로고
    • Cisplatin sensitivity of oral squamous carcinoma cells is regulated by Na(+),K(+)-ATPase activity rather than copper-transporting P-type ATPases, ATP7A and ATP7B
    • Z. Ahmed, Y. Deyama, Y. Yoshimura, and K. Suzuki Cisplatin sensitivity of oral squamous carcinoma cells is regulated by Na(+),K(+)-ATPase activity rather than copper-transporting P-type ATPases, ATP7A and ATP7B Cancer Chemother Pharmacol 63 2009 643 650
    • (2009) Cancer Chemother Pharmacol , vol.63 , pp. 643-650
    • Ahmed, Z.1    Deyama, Y.2    Yoshimura, Y.3    Suzuki, K.4
  • 42
    • 70349905225 scopus 로고    scopus 로고
    • Crystal structures of cisplatin bound to a human copper chaperone
    • A.K. Boal, and A.C. Rosenzweig Crystal structures of cisplatin bound to a human copper chaperone J Am Chem Soc 131 2009 14196 14197
    • (2009) J Am Chem Soc , vol.131 , pp. 14196-14197
    • Boal, A.K.1    Rosenzweig, A.C.2
  • 45
    • 68949144979 scopus 로고    scopus 로고
    • NaKtide, a Na/K-ATPase-derived peptide Src inhibitor, antagonizes ouabain-activated signal transduction in cultured cells
    • Z.C. Li, T. Cai, J. Tian, J.X. Xie, X.C. Zhao, and L.J. Liu NaKtide, a Na/K-ATPase-derived peptide Src inhibitor, antagonizes ouabain-activated signal transduction in cultured cells J Biol Chem 284 2009 21066 21076
    • (2009) J Biol Chem , vol.284 , pp. 21066-21076
    • Li, Z.C.1    Cai, T.2    Tian, J.3    Xie, J.X.4    Zhao, X.C.5    Liu, L.J.6
  • 46
    • 79953770711 scopus 로고    scopus 로고
    • Interactions between proteins and platinum-containing anti-cancer drugs
    • C. Bischin, A. Lupan, V. Taciuc, and R. Silaghi-Dumitrescu Interactions between proteins and platinum-containing anti-cancer drugs Mini Rev Med Chem 11 2011 214 224
    • (2011) Mini Rev Med Chem , vol.11 , pp. 214-224
    • Bischin, C.1    Lupan, A.2    Taciuc, V.3    Silaghi-Dumitrescu, R.4
  • 47
    • 0030027897 scopus 로고    scopus 로고
    • Expression in high yield of pig alpha 1 beta 1 Na,K-ATPase and inactive mutants D369N and D807N in Saccharomyces cerevisiae
    • P.A. Pedersen, J.H. Rasmussen, and P.L. Jorgensen Expression in high yield of pig alpha 1 beta 1 Na,K-ATPase and inactive mutants D369N and D807N in Saccharomyces cerevisiae J Biol Chem 271 1996 2514 2522
    • (1996) J Biol Chem , vol.271 , pp. 2514-2522
    • Pedersen, P.A.1    Rasmussen, J.H.2    Jorgensen, P.L.3


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