메뉴 건너뛰기




Volumn 125, Issue 2, 2012, Pages 509-521

Mixed inhibition of adenosine deaminase activity by 1,3-dinitrobenzene: A Model for understanding cell-selective neurotoxicity in chemically-induced energy deprivation syndromes in brain

Author keywords

1,3 dinitrobenzene; Adenosine; Adenosine deaminase; Astrocytes

Indexed keywords

1,3 DINITROBENZENE; ADENOSINE; ADENOSINE DEAMINASE;

EID: 84862937411     PISSN: 10966080     EISSN: 10960929     Source Type: Journal    
DOI: 10.1093/toxsci/kfr317     Document Type: Article
Times cited : (6)

References (49)
  • 1
    • 40949109275 scopus 로고    scopus 로고
    • A study on the inhibition of adenosine deaminase
    • Alunni, S., Orru, M., and Ottavi, L. (2008). A study on the inhibition of adenosine deaminase. J. Enzyme Inhib. Med. Chem. 23, 182-189.
    • (2008) J. Enzyme Inhib. Med. Chem. , vol.23 , pp. 182-189
    • Alunni, S.1    Orru, M.2    Ottavi, L.3
  • 2
    • 0023835080 scopus 로고
    • A comparison of the effects of the three isomers of dinitrobenzene on the testis in the rat
    • Blackburn, D. M., Gray, A. J., Lloyd, S. C., Sheard, C. M., and Foster, P. M. (1988). A comparison of the effects of the three isomers of dinitrobenzene on the testis in the rat. Toxicol. Appl. Pharmacol. 92, 54-64.
    • (1988) Toxicol. Appl. Pharmacol. , vol.92 , pp. 54-64
    • Blackburn, D.M.1    Gray, A.J.2    Lloyd, S.C.3    Sheard, C.M.4    Foster, P.M.5
  • 3
    • 0019619130 scopus 로고
    • Induction of hepatic and testicular lesions in Fischer-344 rats by single oral doses of nitrobenzene
    • Bond, J. A., Chism, J. P., Rickert, D. E., and Popp, J. A. (1981). Induction of hepatic and testicular lesions in Fischer-344 rats by single oral doses of nitrobenzene. Fundam. Appl. Toxicol. 1, 389-394.
    • (1981) Fundam. Appl. Toxicol. , vol.1 , pp. 389-394
    • Bond, J.A.1    Chism, J.P.2    Rickert, D.E.3    Popp, J.A.4
  • 4
    • 0025848345 scopus 로고
    • Effect of culture age on 1,3-dinitrobenzene metabolism and indicators of cellular toxicity in rat testicular cells
    • Brown, C. D., and Miller, M. G. (1991). Effect of culture age on 1,3-dinitrobenzene metabolism and indicators of cellular toxicity in rat testicular cells. Toxicol. In Vitro 5, 269-275.
    • (1991) Toxicol. In Vitro , vol.5 , pp. 269-275
    • Brown, C.D.1    Miller, M.G.2
  • 5
    • 33645106684 scopus 로고    scopus 로고
    • Historical review: ATP as a neurotransmitter
    • Burnstock, G. (2006). Historical review: ATP as a neurotransmitter. Trends Pharmacol. Sci. 27, 166-176.
    • (2006) Trends Pharmacol. Sci. , vol.27 , pp. 166-176
    • Burnstock, G.1
  • 6
    • 0032671931 scopus 로고    scopus 로고
    • Unsupervised data base clustering based on Daylight's ngerprint and Tanimoto similarity: A fast and automated way to cluster small and large data sets
    • Butina, D. (1999). Unsupervised data base clustering based on Daylight's ngerprint and Tanimoto similarity: A fast and automated way to cluster small and large data sets. J. Chem. Inf. Comput. Sci. 39, 747-750.
    • (1999) J. Chem. Inf. Comput. Sci. , vol.39 , pp. 747-750
    • Butina, D.1
  • 8
    • 0001740590 scopus 로고    scopus 로고
    • One-dimensional electrophoresis using nondenaturing conditions
    • (J. Coligan, B. Dunn, H. Ploegh, D. Speicher and P. Wingeld, Eds.), John Wiley and Sons, New York, NY
    • Coligan, J. E. (1996). One-dimensional electrophoresis using nondenaturing conditions. In Current Protocols in Protein Science (J. Coligan, B. Dunn, H. Ploegh, D. Speicher and P. Wingeld, Eds.), pp. 10.3.1-10.3.11. John Wiley and Sons, New York, NY.
    • (1996) Current Protocols in Protein Science
    • Coligan, J.E.1
  • 10
    • 0242663237 scopus 로고    scopus 로고
    • A point-charge force eld for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations
    • Duan, Y.,Wu, C., Chowdhury, S., Lee, M. C., Xiong, G., Zhang,W., Yang, R., Cieplak, P., Luo, R., Lee, T., et al. (2003). A point-charge force eld for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations. J. Comput. Chem. 24, 1999-2012.
    • (2003) J. Comput. Chem. , vol.24 , pp. 1999-2012
    • Duan, Y.1    Wu, C.2    Chowdhury, S.3    Lee, M.C.4    Xiong, G.5    Zhang, W.6    Yang, R.7    Cieplak, P.8    Luo, R.9    Lee, T.10
  • 11
    • 1942471391 scopus 로고    scopus 로고
    • Assessing scoring functions for protein-ligand interactions
    • Ferrara, P., Gohlke, H., Price, D. J., Klebe, G., and Brooks, C. L. (2004). Assessing scoring functions for protein-ligand interactions. J. Med. Chem. 47, 3032-3047.
    • (2004) J. Med. Chem. , vol.47 , pp. 3032-3047
    • Ferrara, P.1    Gohlke, H.2    Price, D.J.3    Klebe, G.4    Brooks, C.L.5
  • 12
    • 34250770500 scopus 로고    scopus 로고
    • Adenosine, an endogenous distress signal, modulates tissue damage and repair
    • Fredholm, B. B. (2007). Adenosine, an endogenous distress signal, modulates tissue damage and repair. Cell Death Differ. 14, 1315-1323.
    • (2007) Cell Death Differ , vol.14 , pp. 1315-1323
    • Fredholm, B.B.1
  • 13
    • 13844315635 scopus 로고    scopus 로고
    • Actions of adenosine at its receptors in the CNS: Insights from knockouts and drugs
    • Fredholm, B. B., Chen, J. F., Masino, S. A., and Vaugeois, J. M. (2005). Actions of adenosine at its receptors in the CNS: Insights from knockouts and drugs. Annu. Rev. Pharmacol. Toxicol. 45, 385-412.
    • (2005) Annu. Rev. Pharmacol. Toxicol. , vol.45 , pp. 385-412
    • Fredholm, B.B.1    Chen, J.F.2    Masino, S.A.3    Vaugeois, J.M.4
  • 14
    • 0141655168 scopus 로고    scopus 로고
    • High-resolution real-time recording with microelectrode biosensors reveals novel aspects of adenosine release during hypoxia in rat hippocampal slices
    • Frenguelli, B. G., Llaudet, E., and Dale, N. (2003). High-resolution real-time recording with microelectrode biosensors reveals novel aspects of adenosine release during hypoxia in rat hippocampal slices. J. Neurochem. 86, 1506-1515.
    • (2003) J. Neurochem. , vol.86 , pp. 1506-1515
    • Frenguelli, B.G.1    Llaudet, E.2    Dale, N.3
  • 15
    • 0022497287 scopus 로고
    • Transition-state stabilization by adenosine deaminase: Structural studies of its inhibitory complex with deoxycoformycin
    • Frick, L., Wolfenden, R., Smal, E., and Baker, D. C. (1986). Transition-state stabilization by adenosine deaminase: Structural studies of its inhibitory complex with deoxycoformycin. Biochemistry 25, 1616-1621.
    • (1986) Biochemistry , vol.25 , pp. 1616-1621
    • Frick, L.1    Wolfenden, R.2    Smal, E.3    Baker, D.C.4
  • 16
    • 51849117273 scopus 로고    scopus 로고
    • Human adenosine deaminase as an allosteric modulator of human A(1) adenosine receptor: Abolishment of negative cooperativity for [H-3](R)-pia binding to the caudate nucleus
    • Gracia, E., Cortés, A., Meana, J. J., García-Sevilla, J., Hersheld, M. S., Canela, E. I., Mallol, J., Lluis, C., Franco, R., and Casadó, V. (2008). Human adenosine deaminase as an allosteric modulator of human A(1) adenosine receptor: Abolishment of negative cooperativity for [H-3](R)-pia binding to the caudate nucleus. J. Neurochem. 107, 161-170.
    • (2008) J. Neurochem. , vol.107 , pp. 161-170
    • Gracia, E.1    Cortés, A.2    Meana, J.J.3    García-Sevilla, J.4    Hersheld, M.S.5    Canela, E.I.6    Mallol, J.7    Lluis, C.8    Franco, R.9    Casadó, V.10
  • 19
    • 0000267781 scopus 로고
    • Specic adenosine deaminase from intestine
    • Kaplan, N. O. (1955). Specic adenosine deaminase from intestine. Methods Enzymol. 2, 473-475.
    • (1955) Methods Enzymol , vol.2 , pp. 473-475
    • Kaplan, N.O.1
  • 21
    • 45849138147 scopus 로고    scopus 로고
    • Conformational change of adenosine deaminase during ligand-exchange in a crystal
    • Kinoshita, T., Tada, T., and Nakanishi, I. (2008). Conformational change of adenosine deaminase during ligand-exchange in a crystal. Biochem. Biophys. Res. Commun. 373, 53-57.
    • (2008) Biochem. Biophys. Res. Commun. , vol.373 , pp. 53-57
    • Kinoshita, T.1    Tada, T.2    Nakanishi, I.3
  • 22
    • 10344223464 scopus 로고    scopus 로고
    • Making optimal use of empirical energy functions: Force-eld parameter-ization in crystal space
    • Krieger, E., Darden, T., Nabuurs, S. B., Finkelstein, A., and Vriend, G. (2004). Making optimal use of empirical energy functions: Force-eld parameter-ization in crystal space. Proteins 57, 678-683.
    • (2004) Proteins , vol.57 , pp. 678-683
    • Krieger, E.1    Darden, T.2    Nabuurs, S.B.3    Finkelstein, A.4    Vriend, G.5
  • 23
    • 0026499905 scopus 로고
    • The rate of formation of transition-state analogues in the active site of adenosine deaminase is encounter-controlled: Implications for the mechanism
    • Kurz, L. C., Moix, L., Riley, M. C., and Frieden, C. (1992). The rate of formation of transition-state analogues in the active site of adenosine deaminase is encounter-controlled: Implications for the mechanism. Biochemistry 31, 39-48.
    • (1992) Biochemistry , vol.31 , pp. 39-48
    • Kurz, L.C.1    Moix, L.2    Riley, M.C.3    Frieden, C.4
  • 24
    • 0034765853 scopus 로고    scopus 로고
    • Adenosine in the central nervous system: Release mechanisms and extracellular concentrations
    • Latini, S., and Pedata, F. (2001). Adenosine in the central nervous system: Release mechanisms and extracellular concentrations. J. Neurochem. 79, 463-484.
    • (2001) J. Neurochem. , vol.79 , pp. 463-484
    • Latini, S.1    Pedata, F.2
  • 25
    • 0021961581 scopus 로고
    • Blood volume in the rat
    • Lee, H. B., and Blaufox, M. D. (1985). Blood volume in the rat. J. Nucl. Med. 26, 72-76.
    • (1985) J. Nucl. Med. , vol.26 , pp. 72-76
    • Lee, H.B.1    Blaufox, M.D.2
  • 26
    • 33747874700 scopus 로고    scopus 로고
    • Neurochemical and oedematous changes in 1,3-dinitrobenzene-induced astroglial injury in rat brain from a 1H-nuclear magnetic resonance perspective
    • Mavroudis, G., Prior, M. J., Lister, T., Nolan, C. C., and Ray, D. E. (2006). Neurochemical and oedematous changes in 1,3-dinitrobenzene-induced astroglial injury in rat brain from a 1H-nuclear magnetic resonance perspective. J. Neural Transm. 113, 1263-1278.
    • (2006) J. Neural Transm. , vol.113 , pp. 1263-1278
    • Mavroudis, G.1    Prior, M.J.2    Lister, T.3    Nolan, C.C.4    Ray, D.E.5
  • 27
    • 80051690825 scopus 로고    scopus 로고
    • 1,3-Dinitrobenzene induced metabolic impairment through selective inactivation of the pyruvate dehydrogenase complex
    • Miller, J. A., Runkle, S. A., Tjalkens, R. B., and Philbert, M. A. (2011). 1,3-Dinitrobenzene induced metabolic impairment through selective inactivation of the pyruvate dehydrogenase complex. Toxicol. Sci. 122, 502-511
    • (2011) Toxicol. Sci. , vol.122 , pp. 502-511
    • Miller, J.A.1    Runkle, S.A.2    Tjalkens, R.B.3    Philbert, M.A.4
  • 28
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K., and Olson, A. J. (1998). Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem. 19, 1639-1662.
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 29
    • 33745755958 scopus 로고    scopus 로고
    • Purinergic transmission in the central nervous system
    • North, R. A., and Verkhratsky, A. (2006). Purinergic transmission in the central nervous system. Pugers Arch. 452, 479-485.
    • (2006) Pugers Arch , vol.452 , pp. 479-485
    • North, R.A.1    Verkhratsky, A.2
  • 30
    • 0033584887 scopus 로고    scopus 로고
    • Cis peptide bonds in proteins: residues involved, their conformations, interactions and locations
    • Pal, D., and Chakrabarti, P. (1999). Cis peptide bonds in proteins: residues involved, their conformations, interactions and locations. J. Mol. Biol. 294, 271-288.
    • (1999) J. Mol. Biol. , vol.294 , pp. 271-288
    • Pal, D.1    Chakrabarti, P.2
  • 31
    • 0027935403 scopus 로고
    • Inhibition of adenosine kinase increases endogenous adenosine and depresses neuronal activity in hippocampal slices
    • Pak, M. A., Haas, H. L., Decking, U. K., and Schrader, J. (1994). Inhibition of adenosine kinase increases endogenous adenosine and depresses neuronal activity in hippocampal slices. Neuropharmacology 33, 1049-1053.
    • (1994) Neuropharmacology , vol.33 , pp. 1049-1053
    • Pak, M.A.1    Haas, H.L.2    Decking, U.K.3    Schrader, J.4
  • 32
    • 15244341323 scopus 로고    scopus 로고
    • Astrocytes and neurons: Different roles in regulating adenosine levels
    • Parkinson, F. E., Xiong,W., and Zamzow, C. R. (2005). Astrocytes and neurons: Different roles in regulating adenosine levels. Neurol. Res. 27, 153-160.
    • (2005) Neurol. Res. , vol.27 , pp. 153-160
    • Parkinson, F.E.1    Xiong, W.2    Zamzow, C.R.3
  • 33
    • 0038275916 scopus 로고    scopus 로고
    • 1,3-Dinitrobenzene inhibits mitochondrial complex II in rat and mouse brainstem and cortical astrocytes
    • Phelka, A. D., Beck, M. J., and Philbert, M. A. (2003). 1,3-Dinitrobenzene inhibits mitochondrial complex II in rat and mouse brainstem and cortical astrocytes. Neurotoxicology 24, 403-415.
    • (2003) Neurotoxicology , vol.24 , pp. 403-415
    • Phelka, A.D.1    Beck, M.J.2    Philbert, M.A.3
  • 35
    • 0018288468 scopus 로고
    • Maximum activities, properties and distribution of 5' nucleotidase, adenosine kinase and adenosine deaminase in rat and human brain
    • Phillips, E., and Newsholme, E. A. (1979). Maximum activities, properties and distribution of 5' nucleotidase, adenosine kinase and adenosine deaminase in rat and human brain. J. Neurochem. 33, 553-558.
    • (1979) J. Neurochem. , vol.33 , pp. 553-558
    • Phillips, E.1    Newsholme, E.A.2
  • 36
    • 76649142732 scopus 로고    scopus 로고
    • Hill coefcients, dose-response curves and allosteric mechanisms
    • Prinz, H. (2009). Hill coefcients, dose-response curves and allosteric mechanisms. J. Chem. Biol. 3, 37-44.
    • (2009) J. Chem. Biol. , vol.3 , pp. 37-44
    • Prinz, H.1
  • 37
    • 0036131027 scopus 로고    scopus 로고
    • 3-Dinitrobenzene metabolism and protein binding
    • Reeve, I. T., and Miller, M. G. (2002). 1,3-Dinitrobenzene metabolism and protein binding. Chem. Res. Toxicol. 15, 352-360.
    • (2002) Chem. Res. Toxicol. , vol.1 , pp. 352-360
    • Reeve, I.T.1    Miller, M.G.2
  • 38
    • 77951216441 scopus 로고    scopus 로고
    • Modulation and metamodulation of synapses by adenosine
    • Ribeiro, J. A., and Sebastiao, A. M. (2010). Modulation and metamodulation of synapses by adenosine. Acta Physiol. (Oxf.) 199, 161-169.
    • (2010) Acta Physiol. (Oxf.) , vol.199 , pp. 161-169
    • Ribeiro, J.A.1    Sebastiao, A.M.2
  • 39
    • 0028835805 scopus 로고
    • Early metabolic changes during m-dinitrobenzene neurotoxicity and the possible role of oxidative stress
    • Romero, I. A., Lister, T., Richards, H. K., Seville, M. P., Wylie, S. P., and Ray, D. E. (1995). Early metabolic changes during m-dinitrobenzene neurotoxicity and the possible role of oxidative stress. Free Radic. Biol. Med. 18, 311-319.
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 311-319
    • Romero, I.A.1    Lister, T.2    Richards, H.K.3    Seville, M.P.4    Wylie, S.P.5    Ray, D.E.6
  • 40
    • 0141923641 scopus 로고    scopus 로고
    • Identication and prediction of promiscuous aggregating inhibitors among known drugs
    • Seidler, J., McGovern, S. L., Doman, T. N., and Shoichet, B. K. (2003). Identication and prediction of promiscuous aggregating inhibitors among known drugs. J. Med. Chem. 46, 4477-4486.
    • (2003) J. Med. Chem. , vol.46 , pp. 4477-4486
    • Seidler, J.1    McGovern, S.L.2    Doman, T.N.3    Shoichet, B.K.4
  • 41
    • 79955114990 scopus 로고    scopus 로고
    • Proteomic identication of carbonylated proteins in 1,3-dinitrobenzene neurotoxicity
    • Steiner, S. R., and Philbert, M. A. (2011). Proteomic identication of carbonylated proteins in 1,3-dinitrobenzene neurotoxicity. Neurotoxicology 32, 362-373.
    • (2011) Neurotoxicology , vol.32 , pp. 362-373
    • Steiner, S.R.1    Philbert, M.A.2
  • 42
    • 70349331090 scopus 로고    scopus 로고
    • Adenosine receptors and neurological disease: Neuroprotection and neurodegeneration
    • Stone, T. W., Ceruti, S., and Abbracchio, M. P. (2009). Adenosine receptors and neurological disease: Neuroprotection and neurodegeneration. Handb. Exp. Pharmacol. 193, 535-587.
    • (2009) Handb. Exp. Pharmacol. , vol.193 , pp. 535-587
    • Stone, T.W.1    Ceruti, S.2    Abbracchio, M.P.3
  • 43
    • 78649423015 scopus 로고    scopus 로고
    • Adenosine and inosine release during hypoxia in the isolated spinal cord of neonatal rats
    • Takahashi, T., Otsuguro, K., Ohta, T., and Ito, S. (2010). Adenosine and inosine release during hypoxia in the isolated spinal cord of neonatal rats. Br. J. Pharmacol. 161, 1806-1816.
    • (2010) Br. J. Pharmacol. , vol.161 , pp. 1806-1816
    • Takahashi, T.1    Otsuguro, K.2    Ohta, T.3    Ito, S.4
  • 44
    • 0034714297 scopus 로고    scopus 로고
    • Differential cellular regulation of the mitochondrial permeability transition in an in vitro model of 1,3-dinitrobenzene-induced encephalopathy
    • Tjalkens, R. B., Ewing, M. M., and Philbert, M. A. (2000). Differential cellular regulation of the mitochondrial permeability transition in an in vitro model of 1,3-dinitrobenzene-induced encephalopathy. Brain Res. 874, 165-177.
    • (2000) Brain Res , vol.874 , pp. 165-177
    • Tjalkens, R.B.1    Ewing, M.M.2    Philbert, M.A.3
  • 45
    • 41849088116 scopus 로고    scopus 로고
    • Nitro as a novel zinc-binding group in the inhibition of carboxypeptidase A
    • Wang, S. H., Wang, S. F., Xuan, W., Zeng, Z. H., Jin, J. Y., Ma, J., and Tian, G. R. (2008). Nitro as a novel zinc-binding group in the inhibition of carboxypeptidase A. Bioorg. Med. Chem. 16, 3596-3601.
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 3596-3601
    • Wang, S.H.1    Wang, S.F.2    Xuan, W.3    Zeng, Z.H.4    Jin, J.Y.5    Ma, J.6    Tian, G.R.7
  • 47
    • 0035543093 scopus 로고    scopus 로고
    • The depth of chemical time and the power of enzymes as catalysts
    • Wolfenden, R., and Snider, M. J. (2001). The depth of chemical time and the power of enzymes as catalysts. Acc. Chem. Res. 34, 938-945.
    • (2001) Acc. Chem. Res. , vol.34 , pp. 938-945
    • Wolfenden, R.1    Snider, M.J.2
  • 48
    • 0033572657 scopus 로고    scopus 로고
    • Pharmacokinetic factors and concentration-time threshold in m-dinitroben-zene-induced neurotoxicity
    • Xu, J., Nolan, C. C., Lister, T., Purcell, W. M., and Ray, D. E. (1999). Pharmacokinetic factors and concentration-time threshold in m-dinitroben-zene-induced neurotoxicity. Toxicol. Appl. Pharmacol. 161, 267-273.
    • (1999) Toxicol. Appl. Pharmacol. , vol.161 , pp. 267-273
    • Xu, J.1    Nolan, C.C.2    Lister, T.3    Purcell, W.M.4    Ray, D.E.5
  • 49
    • 77955916880 scopus 로고    scopus 로고
    • Rapid determination of adenosine deaminase kinetics using fast-scan cyclic voltammetry
    • Xu, Y. D., and Venton, B. J. (2010). Rapid determination of adenosine deaminase kinetics using fast-scan cyclic voltammetry. Phys. Chem. Chem. Phys. 12, 10027-10032.
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 10027-10032
    • Xu, Y.D.1    Venton, B.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.