메뉴 건너뛰기




Volumn 269, Issue 22, 2002, Pages 5547-5556

DNA and RNA damage by Cu(II)-amikacin complex

Author keywords

2 deoxyguanosine oxidation; Amikacin; Copper(II) complexes; Plasmid DNA damage; tRNA cleavage

Indexed keywords

AMIKACIN; AMINOGLYCOSIDE ANTIBIOTIC AGENT; COPPER COMPLEX; DEOXYGUANOSINE; HYDROGEN PEROXIDE; HYDROPEROXIDE; HYDROXYL RADICAL; OXIDIZING AGENT; PLASMID DNA; RNA; TRANSFER RNA;

EID: 0036441031     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03260.x     Document Type: Article
Times cited : (35)

References (53)
  • 1
    • 33749104744 scopus 로고    scopus 로고
    • Co-ordination of copper (II) by amikacin. Complexation equilibria in solution and oxygen activation by resulting complexes
    • Jezowska-Bojczuk, M. & Bal, W. (1998) Co-ordination of copper (II) by amikacin. Complexation equilibria in solution and oxygen activation by resulting complexes. J. Chem. Soc. Dalton Trans. 153-159.
    • (1998) J. Chem. Soc. Dalton Trans. , pp. 153-159
    • Jezowska-Bojczuk, M.1    Bal, W.2
  • 3
    • 0001321440 scopus 로고
    • Carbon-NMR studies of the initial binding of Cu (II) to aminoglycoside antibiotics - A useful structural and functional probe
    • Hanessian, S. & Patil, G. (1978) Carbon-NMR studies of the initial binding of Cu (II) to aminoglycoside antibiotics - A useful structural and functional probe. Tetrahedron Lett. 12, 1031-1034.
    • (1978) Tetrahedron Lett. , vol.12 , pp. 1031-1034
    • Hanessian, S.1    Patil, G.2
  • 4
    • 0017873602 scopus 로고
    • Aminoglycoside antibiotics - A method for selective N-acylation based on the temporary protection of amino alcohol functions as copper chelates
    • Hanessian, S. & Patil, G. (1978) Aminoglycoside antibiotics - A method for selective N-acylation based on the temporary protection of amino alcohol functions as copper chelates. Tetrahedron Lett. 12, 1035-1038.
    • (1978) Tetrahedron Lett. , vol.12 , pp. 1035-1038
    • Hanessian, S.1    Patil, G.2
  • 6
    • 0024949776 scopus 로고
    • Coordination chemical studies of some polymeric transition metal complexes with neomycin and their biological activity uses. Indirect determination of neomycin by atomic absorption spectroscopy
    • Abu-El-Wafa, S.M., El-Ries, M.A., Abou-Attica, F.M. & Issa, R.M. (1989) Coordination chemical studies of some polymeric transition metal complexes with neomycin and their biological activity uses. Indirect determination of neomycin by atomic absorption spectroscopy. Anal. Lett. 22, 2703-2716.
    • (1989) Anal. Lett. , vol.22 , pp. 2703-2716
    • Abu-El-Wafa, S.M.1    El-Ries, M.A.2    Abou-Attica, F.M.3    Issa, R.M.4
  • 7
    • 0000990234 scopus 로고    scopus 로고
    • Kanamycin revisited: A combined potentiometric and spectroscopic study of copper (II) binding to kanamycin B
    • Jezowska-Bojczuk, M., Bal, W. & Kozlowski, H. (1998) Kanamycin revisited: A combined potentiometric and spectroscopic study of copper (II) binding to kanamycin B. Inorg. Chim. Acta 275/276, 541-545.
    • (1998) Inorg. Chim. Acta , vol.275-276 , pp. 541-545
    • Jezowska-Bojczuk, M.1    Bal, W.2    Kozlowski, H.3
  • 8
    • 0032464060 scopus 로고    scopus 로고
    • Copper (II) binding to tobramycin. Potentiometric and spectroscopic studies
    • Jezowska-Bojczuk, M., Karaczyn, A. & Kozlowski, H. (1998) Copper (II) binding to tobramycin. Potentiometric and spectroscopic studies. Carbohydr. Res. 313, 265-269.
    • (1998) Carbohydr. Res. , vol.313 , pp. 265-269
    • Jezowska-Bojczuk, M.1    Karaczyn, A.2    Kozlowski, H.3
  • 9
    • 0031772698 scopus 로고    scopus 로고
    • Binding of Cu (II) ions to geneticin, a gentamicin analog
    • Jezowska-Bojczuk, M., Karaczyn, A. & Bal, W. (1998) Binding of Cu (II) ions to geneticin, a gentamicin analog. J. Inorg. Biochem. 71, 129-134.
    • (1998) J. Inorg. Biochem. , vol.71 , pp. 129-134
    • Jezowska-Bojczuk, M.1    Karaczyn, A.2    Bal, W.3
  • 10
    • 0032474723 scopus 로고    scopus 로고
    • 1H-NMR analysis of copper-aminoglycoside complexes in solution and its implication for regioselective modification of multifunctional aminoglycoside antibiotics
    • 1H-NMR analysis of copper-aminoglycoside complexes in solution and its implication for regioselective modification of multifunctional aminoglycoside antibiotics. Tetrahedron 54, 7705-7720.
    • (1998) Tetrahedron , vol.54 , pp. 7705-7720
    • Grapsas, I.1    Massova, I.2    Mobashery, S.3
  • 11
    • 0034692369 scopus 로고    scopus 로고
    • Efficient deoxy ribonucleases. Greater than 50-million-fold rate enhancement in enzyme-like DNA cleavage
    • Sreedhara, A., Freed, J.D. & Cowan, J.A. (2000) Efficient deoxy ribonucleases. Greater than 50-million-fold rate enhancement in enzyme-like DNA cleavage. J. Am. Chem. Soc. 122, 8814-8824.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8814-8824
    • Sreedhara, A.1    Freed, J.D.2    Cowan, J.A.3
  • 13
    • 0016817089 scopus 로고
    • Amikacin therapy for severe gram-negative sepsis. Emphasis on infections with gentamicin-resistant organisms
    • Tally, F.P., Louie, T.J., Weinstein, W.M., Bartlett, J.G. & Gorbach, S.L. (1975) Amikacin therapy for severe gram-negative sepsis. Emphasis on infections with gentamicin-resistant organisms. Ann. Intern. Med. 83, 484-488.
    • (1975) Ann. Intern. Med. , vol.83 , pp. 484-488
    • Tally, F.P.1    Louie, T.J.2    Weinstein, W.M.3    Bartlett, J.G.4    Gorbach, S.L.5
  • 14
    • 0023615466 scopus 로고
    • Mechanism of bactericidal action of aminoglycosides
    • Davis, B.D. (1987) Mechanism of bactericidal action of amino-glycosides. Microbiol. Rev. 51, 341-350.
    • (1987) Microbiol. Rev. , vol.51 , pp. 341-350
    • Davis, B.D.1
  • 15
    • 0026525894 scopus 로고
    • The bactericidal action of streptomycin: Membrane permeabilization caused by the insertion of mistranslated proteins into the cytoplasmic membrane of Escherichia coli and subsequent caging of the antibiotic inside the cells due to degradation of these proteins
    • Busse, H.J., Wostmann, C. & Bakker, E.P. (1992) The bactericidal action of streptomycin: Membrane permeabilization caused by the insertion of mistranslated proteins into the cytoplasmic membrane of Escherichia coli and subsequent caging of the antibiotic inside the cells due to degradation of these proteins. J. General Bacteriol. 138, 551-561.
    • (1992) J. General Bacteriol. , vol.138 , pp. 551-561
    • Busse, H.J.1    Wostmann, C.2    Bakker, E.P.3
  • 16
    • 0031013486 scopus 로고    scopus 로고
    • Aminoglycoside nephrotoxicity
    • Swan, S.K. (1997) Aminoglycoside nephrotoxicity. Semin. Nephrol. 17, 27-33.
    • (1997) Semin. Nephrol. , vol.17 , pp. 27-33
    • Swan, S.K.1
  • 17
    • 0032779362 scopus 로고    scopus 로고
    • Insights into ototoxicity. Analogies to nephrotoxicity
    • Humes, H.D. (1999) Insights into ototoxicity. Analogies to nephrotoxicity. Ann. N Y Acad. Sci. 884, 15-18.
    • (1999) Ann. N Y Acad. Sci. , vol.884 , pp. 15-18
    • Humes, H.D.1
  • 19
    • 0001929417 scopus 로고    scopus 로고
    • NMR studies of iron-gentamycin complexes and the implications for aminoglycoside toxicity
    • Priuska, E.M., Clark-Baldwin, K., Pecoraro, V.L. & Schacht, J. (1998) NMR studies of iron-gentamycin complexes and the implications for aminoglycoside toxicity. Inorg. Chim. Acta 273, 85-91.
    • (1998) Inorg. Chim. Acta , vol.273 , pp. 85-91
    • Priuska, E.M.1    Clark-Baldwin, K.2    Pecoraro, V.L.3    Schacht, J.4
  • 20
    • 0025145596 scopus 로고
    • Direct voltammetry of the Chromatium vinosum enzyme, sulfide: Cytochrome c oxidoreductase (flavocy-tochrome c552)
    • Guo, L.H., Hill, H.A.O., Hopper, D.J., Lawrance, G.A. & Sanghera, G.S. (1990) Direct voltammetry of the Chromatium vinosum enzyme, sulfide: cytochrome c oxidoreductase (flavocy-tochrome c552). J. Biol. Chem. 265, 1958-1963.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1958-1963
    • Guo, L.H.1    Hill, H.A.O.2    Hopper, D.J.3    Lawrance, G.A.4    Sanghera, G.S.5
  • 21
    • 0033617578 scopus 로고    scopus 로고
    • Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase
    • Rae, T.D., Schmidt, P.J., Pufahl, R.A., Culotta, V.C. & O'Halloran, T.V. (1999) Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase. Science 284, 805-808.
    • (1999) Science , vol.284 , pp. 805-808
    • Rae, T.D.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'Halloran, T.V.5
  • 26
    • 21844436527 scopus 로고    scopus 로고
    • Efficient catalytic cleavage of DNA mediated by metalloaminoglycosides
    • Sreedhara, A. & Cowan, J.A. (1998) Efficient catalytic cleavage of DNA mediated by metalloaminoglycosides. Chem. Commun. 1737-1738.
    • (1998) Chem. Commun. , pp. 1737-1738
    • Sreedhara, A.1    Cowan, J.A.2
  • 27
    • 0033591642 scopus 로고    scopus 로고
    • Novel reagents for targeted cleavage of RNA sequences: Towards a new family of inorganic pharmaceuticals
    • Sreedhara, A., Patwardhan, A. & Cowan, J.A. (1999) Novel reagents for targeted cleavage of RNA sequences: Towards a new family of inorganic pharmaceuticals. Chem. Commun. 1147-1148.
    • (1999) Chem. Commun. , pp. 1147-1148
    • Sreedhara, A.1    Patwardhan, A.2    Cowan, J.A.3
  • 28
    • 0032125614 scopus 로고    scopus 로고
    • A novel assay of 8-oxo-2′-deoxyguanosine 5′-triphosphate pyrophosphohydrolase (8-oxo-dGTPase) activity in cultured cells and its use for evaluation of cadmium (II) inhibition of this activity
    • Białkowski, K. & Kasprzak, K.S. (1998) A novel assay of 8-oxo-2′-deoxyguanosine 5′-triphosphate pyrophosphohydrolase (8-oxo-dGTPase) activity in cultured cells and its use for evaluation of cadmium (II) inhibition of this activity. Nucleic Acids Res. 26, 3194-3201.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3194-3201
    • Białkowski, K.1    Kasprzak, K.S.2
  • 29
    • 0029099472 scopus 로고
    • Possible role of oxidative damage in metal-induced carcinogenesis
    • Kasprzak, K.S. (1995) Possible role of oxidative damage in metal-induced carcinogenesis. Cancer Invest. 13, 411-430.
    • (1995) Cancer Invest. , vol.13 , pp. 411-430
    • Kasprzak, K.S.1
  • 30
    • 0025045198 scopus 로고
    • The role of 8-hydroxyguanosine in carcinogenesis
    • Floyd, R.A. (1990) The role of 8-hydroxyguanosine in carcinogenesis. Carcinogenesis 11, 1447-1450.
    • (1990) Carcinogenesis , vol.11 , pp. 1447-1450
    • Floyd, R.A.1
  • 31
    • 0000401465 scopus 로고    scopus 로고
    • Comparison of the mutagenic properties of 8-oxo-7,8-dihydro-2′-deoxyadenosine and 8-oxo-7,8-dihydro-2′-deoxyguanosine DNA lesions in mammalian cells
    • Tan, X., Grollman, A.P. & Shibutani, S. (1999) Comparison of the mutagenic properties of 8-oxo-7,8-dihydro-2′-deoxyadenosine and 8-oxo-7,8-dihydro-2′-deoxyguanosine DNA lesions in mammalian cells. Carcinogenesis 11, 1447-1450.
    • (1999) Carcinogenesis , vol.11 , pp. 1447-1450
    • Tan, X.1    Grollman, A.P.2    Shibutani, S.3
  • 32
    • 4243545125 scopus 로고    scopus 로고
    • Oxidative nucleobase modifications leading to strand scission
    • Burrows, C.J. & Muller, J.G. (1998) Oxidative nucleobase modifications leading to strand scission. Chem. Rev. 98, 1109-1151.
    • (1998) Chem. Rev. , vol.98 , pp. 1109-1151
    • Burrows, C.J.1    Muller, J.G.2
  • 33
    • 0031027125 scopus 로고    scopus 로고
    • How easily oxidizable is DNA? One-electron reduction potentials of adenosine and guanosine radicals in aqueous solution
    • Steenken, S. & Jovanovic, S. (1997) How easily oxidizable is DNA? One-electron reduction potentials of adenosine and guanosine radicals in aqueous solution. J. Am. Chem. Soc. 119, 617-618.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 617-618
    • Steenken, S.1    Jovanovic, S.2
  • 34
    • 0026772501 scopus 로고
    • Redox ribonucleosides. Isolation and characterization of 5-ydroxyuridine, 8-hydroxyguanosine & 8-hydroxyadenosine from Torula yeast RNA
    • Yanagawa, H., Ogawa, Y. & Ueno, M. (1992) Redox ribonucleosides. Isolation and characterization of 5-ydroxyuridine, 8-hydroxyguanosine & 8-hydroxyadenosine from Torula yeast RNA. J. Biol. Chem. 267, 13320-13326.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13320-13326
    • Yanagawa, H.1    Ogawa, Y.2    Ueno, M.3
  • 35
    • 0029990148 scopus 로고    scopus 로고
    • Photosensitized reaction of 8-oxo-7,8-dihydro-2′-deoxyguanosine: Identification of 1-(2-deoxy-b-D-erythro-pentofuranosyl) cyanuric acid as the major singlet oxygen oxidation product
    • Raoul, S. & Cadet, J. (1996) Photosensitized reaction of 8-oxo-7,8-dihydro-2′-deoxyguanosine: Identification of 1-(2-deoxy-b-D-erythro-pentofuranosyl) cyanuric acid as the major singlet oxygen oxidation product. J. Am. Chem. Soc. 118, 1892-1898.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 1892-1898
    • Raoul, S.1    Cadet, J.2
  • 36
    • 0024458564 scopus 로고
    • Hydroxyl free radical is not the main active species in site-specific DNA damage induced by copper (II) ion and hydrogen peroxide
    • Yamamoto, K. & Kawanishi, S. (1989) Hydroxyl free radical is not the main active species in site-specific DNA damage induced by copper (II) ion and hydrogen peroxide. J. Biol. Chem. 264, 15435-15440.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15435-15440
    • Yamamoto, K.1    Kawanishi, S.2
  • 37
    • 0029920828 scopus 로고    scopus 로고
    • Site-specific DNA damage induced by NADH in the presence of copper (II): Role of active oxygen species
    • Oikawa, S. & Kawanishi, S. (1996) Site-specific DNA damage induced by NADH in the presence of copper (II): Role of active oxygen species. Biochemistry 35, 4584-4590.
    • (1996) Biochemistry , vol.35 , pp. 4584-4590
    • Oikawa, S.1    Kawanishi, S.2
  • 38
    • 0034602848 scopus 로고    scopus 로고
    • Modulation of RNA function by aminoglycoside antibiotics
    • Schroeder, R., Waldsich, C. & Wank, H. (2000) Modulation of RNA function by aminoglycoside antibiotics. EMBO J. 19, 1-9.
    • (2000) EMBO J. , vol.19 , pp. 1-9
    • Schroeder, R.1    Waldsich, C.2    Wank, H.3
  • 41
    • 0032860283 scopus 로고    scopus 로고
    • tRNA (Phe) binds aminoglycoside antibiotics
    • Kirk, S.R. & Tor, Y. (1999) tRNA (Phe) binds aminoglycoside antibiotics. Bioorg. Med. Chem. 7, 1979-1991.
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 1979-1991
    • Kirk, S.R.1    Tor, Y.2
  • 43
    • 0008875663 scopus 로고
    • Structural analysis of spermine and magnesium ion binding to yeast phenylalanine transfer RNA
    • Quigley, G.J., Teeter, M.M. & Rich, A. (1978) Structural analysis of spermine and magnesium ion binding to yeast phenylalanine transfer RNA. Proc. Natl. Acad. Sci. USA 75, 64-68.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 64-68
    • Quigley, G.J.1    Teeter, M.M.2    Rich, A.3
  • 44
    • 0024319347 scopus 로고
    • Probing the environment of lanthanide binding sites in yeast tRNA (Phe) by specific metal-ion-promoted cleavages
    • Ciesiolka, J., Marciniec, T. & Krzyzosiak, W. (1989) Probing the environment of lanthanide binding sites in yeast tRNA (Phe) by specific metal-ion-promoted cleavages. Eur. J. Biochem. 182, 445-450.
    • (1989) Eur. J. Biochem. , vol.182 , pp. 445-450
    • Ciesiolka, J.1    Marciniec, T.2    Krzyzosiak, W.3
  • 49
    • 0035882247 scopus 로고    scopus 로고
    • Intracellular iron, but not copper, plays critical role in hydrogen peroxide - Induced DNA damage
    • Barbouti, A., Doulias, P.-T., Zhu, B.-Z., Frei, B. & Galaris, D. (2001) Intracellular iron, but not copper, plays critical role in hydrogen peroxide - Induced DNA damage. Free Rad. Biol. Med. 31, 490-498.
    • (2001) Free Rad. Biol. Med. , vol.31 , pp. 490-498
    • Barbouti, A.1    Doulias, P.-T.2    Zhu, B.-Z.3    Frei, B.4    Galaris, D.5
  • 50
    • 0037081366 scopus 로고    scopus 로고
    • Copper is involved in hydrogen - peroxide - induced DNA damage
    • Bar-Or, D. & Winkler, J.V. (2002) Copper is involved in hydrogen - peroxide - induced DNA damage. Free Rad. Biol. Med. 32, 197-198.
    • (2002) Free Rad. Biol. Med. , vol.32 , pp. 197-198
    • Bar-Or, D.1    Winkler, J.V.2
  • 51
    • 0037081442 scopus 로고    scopus 로고
    • On the role of iron and copper ions in hydrogen peroxide - Induced cellular DNA damage
    • Galaris, D. & Zhu, B.-Z. (2002) On the role of iron and copper ions in hydrogen peroxide - Induced cellular DNA damage. Free Rad. Biol. Med. 32, 198-199.
    • (2002) Free Rad. Biol. Med. , vol.32 , pp. 198-199
    • Galaris, D.1    Zhu, B.-Z.2
  • 52
    • 0027456505 scopus 로고
    • Enzyme function of copper, zinc superoxide dismutase as a free radical generator
    • Yim, M.B., Chock, P.B. & Stadtman, E.R. (1993) Enzyme function of copper, zinc superoxide dismutase as a free radical generator. J. Biol. Chem. 268, 4099-4105.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4099-4105
    • Yim, M.B.1    Chock, P.B.2    Stadtman, E.R.3
  • 53
    • 0001792286 scopus 로고
    • Roles of amines in the action of antibiotics - Bleomycin, spergualin & aminoglycosides
    • Umezawa, H. (1983) Roles of amines in the action of antibiotics - Bleomycin, spergualin & aminoglycosides. Adv. Polyamine Res. 4, 1-15.
    • (1983) Adv. Polyamine Res. , vol.4 , pp. 1-15
    • Umezawa, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.