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Volumn 1640, Issue 2-3, 2003, Pages 105-112

Effect of tributyltin on trout blood cells: Changes in mitochondrial morphology and functionality

Author keywords

Organotin compound; Rainbow trout; Tributyltin chloride

Indexed keywords

CASPASE 3; CYTOCHROME C; DNA; TRIBUTYLTIN CHLORIDE;

EID: 0037687858     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4889(03)00025-9     Document Type: Article
Times cited : (38)

References (43)
  • 1
    • 84990494317 scopus 로고
    • Review: Environmental aspects of tributyltin
    • Maguire R.J. Review: environmental aspects of tributyltin. Appl. Organomet. Chem. 1:1987;475-490.
    • (1987) Appl. Organomet. Chem. , vol.1 , pp. 475-490
    • Maguire, R.J.1
  • 2
    • 0026392835 scopus 로고
    • Aquatic environmental aspects of non-pesticidal organotin compounds
    • Maguire R.J. Aquatic environmental aspects of non-pesticidal organotin compounds. Water Pollut. Res. J. Can. 26:1991;243-248.
    • (1991) Water Pollut. Res. J. Can. , vol.26 , pp. 243-248
    • Maguire, R.J.1
  • 4
    • 0030039627 scopus 로고    scopus 로고
    • Ecotoxicology of organotin compounds
    • Fent K. Ecotoxicology of organotin compounds. Crit. Rev. Toxicol. 26:1996;1-117.
    • (1996) Crit. Rev. Toxicol. , vol.26 , pp. 1-117
    • Fent, K.1
  • 6
    • 0001383438 scopus 로고    scopus 로고
    • Plasma membrane perturbation induced by tributyltin chloride on density separated trout erythrocytes
    • Santroni A.M., Fedeli D., Zolese G., Gabbianelli R., Falcioni G. Plasma membrane perturbation induced by tributyltin chloride on density separated trout erythrocytes. Appl. Organomet. Chem. 13:1999;777-781.
    • (1999) Appl. Organomet. Chem. , vol.13 , pp. 777-781
    • Santroni, A.M.1    Fedeli, D.2    Zolese, G.3    Gabbianelli, R.4    Falcioni, G.5
  • 7
    • 0016416337 scopus 로고
    • Molecular adaptation to physiological requirements: The hemoglobin system of trout
    • Brunori M. Molecular adaptation to physiological requirements: the hemoglobin system of trout. Curr. Top. Cell. Regul. 9:1975;1-39.
    • (1975) Curr. Top. Cell. Regul. , vol.9 , pp. 1-39
    • Brunori, M.1
  • 8
    • 0034955744 scopus 로고    scopus 로고
    • DNA damage induced by organotins on trout-nucleated erythrocytes
    • Tiano L., Fedeli D., Moretti M., Falcioni G. DNA damage induced by organotins on trout-nucleated erythrocytes. Appl. Organomet. Chem. 15:2001;575-580.
    • (2001) Appl. Organomet. Chem. , vol.15 , pp. 575-580
    • Tiano, L.1    Fedeli, D.2    Moretti, M.3    Falcioni, G.4
  • 9
    • 0032077880 scopus 로고    scopus 로고
    • Detection of DNA damage in stressed trout nucleated erythrocytes using the comet assay: Protection by nitroxide radicals
    • Villarini M., Moretti M., Damiani E., Greci L., Santroni A.M., Fedeli D., Falcioni G. Detection of DNA damage in stressed trout nucleated erythrocytes using the comet assay: protection by nitroxide radicals. Free Radic. Biol. Med. 24:1998;1310-1315.
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 1310-1315
    • Villarini, M.1    Moretti, M.2    Damiani, E.3    Greci, L.4    Santroni, A.M.5    Fedeli, D.6    Falcioni, G.7
  • 10
    • 0032504575 scopus 로고    scopus 로고
    • Mitochondria as regulators of apoptosis: Doubt no more
    • Susin S.A., Zamzami N., Kroemer G. Mitochondria as regulators of apoptosis: doubt no more. Biochim. Biophys. Acta. 1366:1998;151-165.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 151-165
    • Susin, S.A.1    Zamzami, N.2    Kroemer, G.3
  • 11
    • 0032504657 scopus 로고    scopus 로고
    • Role of mitochondria in oxidative stress and ageing
    • Lenaz G. Role of mitochondria in oxidative stress and ageing. Biochim. Biophys. Acta. 1366:1998;53-67.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 53-67
    • Lenaz, G.1
  • 13
    • 0030580287 scopus 로고    scopus 로고
    • Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell
    • Skulachev V.P. Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell. FEBS Lett. 397:1996;7-10.
    • (1996) FEBS Lett. , vol.397 , pp. 7-10
    • Skulachev, V.P.1
  • 14
    • 0029036412 scopus 로고
    • Alterations in mitochondrial structure and function are early events of dexamethasone-induced thymocyte apoptosis
    • Petit P.X., Lecoeur H., Zorn E., Dauguet C., Mignotte B., Gougeon M.L. Alterations in mitochondrial structure and function are early events of dexamethasone-induced thymocyte apoptosis. J. Cell Biol. 130:1995;157-167.
    • (1995) J. Cell Biol. , vol.130 , pp. 157-167
    • Petit, P.X.1    Lecoeur, H.2    Zorn, E.3    Dauguet, C.4    Mignotte, B.5    Gougeon, M.L.6
  • 15
    • 0028903933 scopus 로고
    • Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo
    • Zamzami N., Marchetti P., Castedo M., Zanin C., Vayssiere J.L., Petit P.X., Kroemer G. Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo. J. Exp. Med. 181:1995;1661-1672.
    • (1995) J. Exp. Med. , vol.181 , pp. 1661-1672
    • Zamzami, N.1    Marchetti, P.2    Castedo, M.3    Zanin, C.4    Vayssiere, J.L.5    Petit, P.X.6    Kroemer, G.7
  • 17
    • 0030612749 scopus 로고    scopus 로고
    • JC-1, but not DiOC6(3) or rhodamine 123, is a reliable fluorescent probe to assess delta psi changes in intact cells: Implications for studies on mitochondrial functionality during apoptosis
    • Salvioli S., Ardizzoni A., Franceschi C., Cossarizza A. JC-1, but not DiOC6(3) or rhodamine 123, is a reliable fluorescent probe to assess delta psi changes in intact cells: implications for studies on mitochondrial functionality during apoptosis. FEBS Lett. 411:1997;77-82.
    • (1997) FEBS Lett. , vol.411 , pp. 77-82
    • Salvioli, S.1    Ardizzoni, A.2    Franceschi, C.3    Cossarizza, A.4
  • 19
    • 0025830873 scopus 로고
    • J-aggregate formation of a carbocyanine as a quantitative fluorescent indicator of membrane potential
    • Reers M., Smith T.W., Chen L.B. J-aggregate formation of a carbocyanine as a quantitative fluorescent indicator of membrane potential. Biochemistry. 30:1991;4480-4486.
    • (1991) Biochemistry , vol.30 , pp. 4480-4486
    • Reers, M.1    Smith, T.W.2    Chen, L.B.3
  • 20
    • 0027374638 scopus 로고
    • A new method for the cytofluorimetric analysis of mitochondrial membrane potential using the J-aggregate forming lipophilic cation 5,5′,6,6′-tetrachloro-1,1′,3,3′- tetraethylbenzimidazolcarbocyanine iodide (JC-1)
    • Cossarizza A., Baccarani-Contri M., Kalashnikova G., Franceschi C. A new method for the cytofluorimetric analysis of mitochondrial membrane potential using the J-aggregate forming lipophilic cation 5,5′,6,6′-tetrachloro-1,1′,3,3′- tetraethylbenzimidazolcarbocyanine iodide (JC-1). Biochem. Biophys. Res. Commun. 197:1993;40-45.
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 40-45
    • Cossarizza, A.1    Baccarani-Contri, M.2    Kalashnikova, G.3    Franceschi, C.4
  • 21
    • 0036290152 scopus 로고    scopus 로고
    • Tributyltin causes cytochrome C release from isolated mitochondria by two discrete mechanisms
    • Gogvadze V., Stridh H., Orrenius S., Cotgreave I. Tributyltin causes cytochrome C release from isolated mitochondria by two discrete mechanisms. Biochem. Biophys. Res. Commun. 292:2002;904-908.
    • (2002) Biochem. Biophys. Res. Commun. , vol.292 , pp. 904-908
    • Gogvadze, V.1    Stridh, H.2    Orrenius, S.3    Cotgreave, I.4
  • 22
    • 0033590122 scopus 로고    scopus 로고
    • The role of calcium in pre- and postmitochondrial events in tributyltin-induced T-cell apoptosis
    • Stridh H., Gigliotti D., Orrenius S., Cotgreave I. The role of calcium in pre- and postmitochondrial events in tributyltin-induced T-cell apoptosis. Biochem. Biophys. Res. Commun. 266:1999;460-465.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 460-465
    • Stridh, H.1    Gigliotti, D.2    Orrenius, S.3    Cotgreave, I.4
  • 24
    • 0015101615 scopus 로고
    • Oxidative phosphorylation. The relation between the specific binding of trimethylytin and triethyltin to mitochondria and their effects on various mitochondrial functions
    • Aldridge W.N., Street B.W. Oxidative phosphorylation. The relation between the specific binding of trimethylytin and triethyltin to mitochondria and their effects on various mitochondrial functions. Biochem. J. 124:1971;221-234.
    • (1971) Biochem. J. , vol.124 , pp. 221-234
    • Aldridge, W.N.1    Street, B.W.2
  • 25
    • 0014806273 scopus 로고
    • Oxidative phosphorylation. The specific binding of trimethyltin and triethyltin to rat liver mitochondria
    • Aldridge W.N., Street B.W. Oxidative phosphorylation. The specific binding of trimethyltin and triethyltin to rat liver mitochondria. Biochem. J. 118:1970;171-179.
    • (1970) Biochem. J. , vol.118 , pp. 171-179
    • Aldridge, W.N.1    Street, B.W.2
  • 26
    • 0013769940 scopus 로고
    • Oxidative phosphorylation. Biochemical effects and properties of trialkyltins
    • Aldridge W.N., Street B.W. Oxidative phosphorylation. Biochemical effects and properties of trialkyltins. Biochem. J. 91:1964;287-297.
    • (1964) Biochem. J. , vol.91 , pp. 287-297
    • Aldridge, W.N.1    Street, B.W.2
  • 27
    • 0034421920 scopus 로고    scopus 로고
    • Organotins induce apoptosis by disturbance of [Ca(2+)](i) and mitochondrial activity, causing oxidative stress and activation of caspases in rat thymocytes
    • Gennari A., Viviani B., Galli C.L., Marinovich M., Pieters R., Corsini E. Organotins induce apoptosis by disturbance of [Ca(2+)](i) and mitochondrial activity, causing oxidative stress and activation of caspases in rat thymocytes. Toxicol. Appl. Pharmacol. 169:2000;185-190.
    • (2000) Toxicol. Appl. Pharmacol. , vol.169 , pp. 185-190
    • Gennari, A.1    Viviani, B.2    Galli, C.L.3    Marinovich, M.4    Pieters, R.5    Corsini, E.6
  • 28
    • 0034468736 scopus 로고    scopus 로고
    • Role of reactive oxygen species (ROS) in apoptosis induction
    • Simon H.U., Haj-Yehia A., Levi-Schaffer F. Role of reactive oxygen species (ROS) in apoptosis induction. Apoptosis. 5:2000;415-418.
    • (2000) Apoptosis , vol.5 , pp. 415-418
    • Simon, H.U.1    Haj-Yehia, A.2    Levi-Schaffer, F.3
  • 29
    • 0028000903 scopus 로고
    • Immunotoxic organotins as possible model compounds in studying apoptosis and thymocyte differentiation
    • Pieters R., Bol M., Penninks A.H. Immunotoxic organotins as possible model compounds in studying apoptosis and thymocyte differentiation. Toxicology. 91:1994;189-202.
    • (1994) Toxicology , vol.91 , pp. 189-202
    • Pieters, R.1    Bol, M.2    Penninks, A.H.3
  • 31
    • 0003331966 scopus 로고    scopus 로고
    • TBT-induced apoptosis in tunicate haemocytes
    • Cima F., Ballarin L. TBT-induced apoptosis in tunicate haemocytes. Appl. Organomet. Chem. 13:1999;697-703.
    • (1999) Appl. Organomet. Chem. , vol.13 , pp. 697-703
    • Cima, F.1    Ballarin, L.2
  • 32
    • 0033012407 scopus 로고    scopus 로고
    • Caspase involvement in the induction of apoptosis by the environmental toxicants tributyltin and triphenyltin
    • Stridh H., Orrenius S., Hampton M.B. Caspase involvement in the induction of apoptosis by the environmental toxicants tributyltin and triphenyltin. Toxicol. Appl. Pharmacol. 156:1999;141-146.
    • (1999) Toxicol. Appl. Pharmacol. , vol.156 , pp. 141-146
    • Stridh, H.1    Orrenius, S.2    Hampton, M.B.3
  • 33
    • 0033809856 scopus 로고    scopus 로고
    • Molecular mechanisms of apoptosis induced by cytotoxic chemicals
    • Robertson J.D., Orrenius S. Molecular mechanisms of apoptosis induced by cytotoxic chemicals. Crit. Rev. Toxicol. 30:2000;609-627.
    • (2000) Crit. Rev. Toxicol. , vol.30 , pp. 609-627
    • Robertson, J.D.1    Orrenius, S.2
  • 34
    • 0028986963 scopus 로고
    • Organotin compounds induce calcium overload and apoptosis in PC12 cells
    • Viviani B., Rossi A.D., Chow S.C., Nicotera P. Organotin compounds induce calcium overload and apoptosis in PC12 cells. Neurotoxicology. 16:1995;19-25.
    • (1995) Neurotoxicology , vol.16 , pp. 19-25
    • Viviani, B.1    Rossi, A.D.2    Chow, S.C.3    Nicotera, P.4
  • 35
    • 0034282238 scopus 로고    scopus 로고
    • Cytotoxicity of tributyltin in rat hippocampal slice cultures
    • Mizuhashi S., Ikegaya Y., Matsuki N. Cytotoxicity of tributyltin in rat hippocampal slice cultures. Neurosci. Res. 38:2000;35-42.
    • (2000) Neurosci. Res. , vol.38 , pp. 35-42
    • Mizuhashi, S.1    Ikegaya, Y.2    Matsuki, N.3
  • 37
    • 0036289055 scopus 로고    scopus 로고
    • Effect of different organotin compounds on DNA of gilthead sea bream (Sparus aurata) erythrocytes assessed by the comet assay
    • Gabbianelli R., Villarini M., Falcioni G., Lupidi G. Effect of different organotin compounds on DNA of gilthead sea bream (Sparus aurata) erythrocytes assessed by the comet assay. Appl. Organomet. Chem. 16:2002;163-168.
    • (2002) Appl. Organomet. Chem. , vol.16 , pp. 163-168
    • Gabbianelli, R.1    Villarini, M.2    Falcioni, G.3    Lupidi, G.4
  • 38
    • 0001383438 scopus 로고    scopus 로고
    • Plasma membrane perturbation induced by trubutyltin chloride on density separated trout erythrocytes
    • Santroni A.M., Fedeli D., Zolese G., Gabbianelli R., Falcioni G. Plasma membrane perturbation induced by trubutyltin chloride on density separated trout erythrocytes. Appl. Organomet. Chem. 13:1999;777-781.
    • (1999) Appl. Organomet. Chem. , vol.13 , pp. 777-781
    • Santroni, A.M.1    Fedeli, D.2    Zolese, G.3    Gabbianelli, R.4    Falcioni, G.5
  • 41
    • 0037181167 scopus 로고    scopus 로고
    • Caspase 3 regulates phosphatidylserine externalization and phagocytosis of oxidatively stressed erythrocytes
    • Mandal D., Moitra P.K., Saha S., Basu J. Caspase 3 regulates phosphatidylserine externalization and phagocytosis of oxidatively stressed erythrocytes. FEBS Lett. 513:2002;184-188.
    • (2002) FEBS Lett. , vol.513 , pp. 184-188
    • Mandal, D.1    Moitra, P.K.2    Saha, S.3    Basu, J.4
  • 42
    • 0031752746 scopus 로고    scopus 로고
    • Are caspases involved in the death of cells with a transcriptionally inactive nucleus? Sperm and chicken erythrocytes
    • Weil M., Jacobson M.D., Raff M.C. Are caspases involved in the death of cells with a transcriptionally inactive nucleus? Sperm and chicken erythrocytes. J. Cell Sci. 111(Pt. 18):1998;2707-2715.
    • (1998) J. Cell Sci. , vol.111 , Issue.PART 18 , pp. 2707-2715
    • Weil, M.1    Jacobson, M.D.2    Raff, M.C.3


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