메뉴 건너뛰기




Volumn 381, Issue 1-2, 2013, Pages 1-8

Neuroprotective effect of quercetin in ectoenzymes and acetylcholinesterase activities in cerebral cortex synaptosomes of cadmium-exposed rats

Author keywords

5 Nucleotidase; AChE; ADA; Cadmium; NTPDase; Quercetin

Indexed keywords

5' NUCLEOTIDASE; ACETYLCHOLINESTERASE; ADENOSINE DEAMINASE; CADMIUM; HYDROLASE; NUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE; QUERCETIN; UNCLASSIFIED DRUG;

EID: 84879237016     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-013-1659-x     Document Type: Article
Times cited : (52)

References (66)
  • 1
    • 0346014856 scopus 로고    scopus 로고
    • Nephrotoxicity and the proximal tubule. Insights from cadmium
    • doi:70241
    • Thevenod F (2003) Nephrotoxicity and the proximal tubule. Insights from cadmium. Nephron Physiol 93:p87-p93. doi:70241
    • (2003) Nephron Physiol , vol.93
    • Thevenod, F.1
  • 2
  • 3
    • 0017873582 scopus 로고
    • The biological half-time of heavy metals. The existence of a third, slowest component
    • Sugita M (1978) The biological half-time of heavy metals. The existence of a third, slowest component. Int Arch Occup Environ Health 41:25-40
    • (1978) Int Arch Occup Environ Health , vol.41 , pp. 25-40
    • Sugita, M.1
  • 5
    • 33646840637 scopus 로고    scopus 로고
    • The influence of curcumin and manganese complex of curcumin on cadmium-induced oxidative damage and trace elements status in tissues of mice
    • doi: 10.1002/jat.1124
    • Eybl V, Kotyzova D, Leseticky L, Bludovska M, Koutensky J (2006) The influence of curcumin and manganese complex of curcumin on cadmium-induced oxidative damage and trace elements status in tissues of mice. J Appl Toxicol 26:207-212. doi: 10.1002/jat.1124
    • (2006) J Appl Toxicol , vol.26 , pp. 207-212
    • Eybl, V.1    Kotyzova, D.2    Leseticky, L.3    Bludovska, M.4    Koutensky, J.5
  • 6
    • 0031963384 scopus 로고    scopus 로고
    • Effect of cadmium chelating agents on organ cadmium and trace element levels in mice
    • Eybl V, Kotyzova D, Koutensky J, Mickova V, Jones MM, Singh PK (1998) Effect of cadmium chelating agents on organ cadmium and trace element levels in mice. Analyst 123:25-26
    • (1998) Analyst , vol.123 , pp. 25-26
    • Eybl, V.1    Kotyzova, D.2    Koutensky, J.3    Mickova, V.4    Jones, M.M.5    Singh, P.K.6
  • 7
    • 69949102834 scopus 로고    scopus 로고
    • Induction of necrosis in cadmium-induced hepatic oxidative stress and its prevention by the prophylactic properties of taurine
    • doi:10.1016/j.jtemb.2009.03.010
    • Sinha M, Manna P, Sil PC (2009) Induction of necrosis in cadmium-induced hepatic oxidative stress and its prevention by the prophylactic properties of taurine. J Trace Elem Med Biol 23:300-313. doi:10.1016/j.jtemb.2009.03.010
    • (2009) J Trace Elem Med Biol , vol.23 , pp. 300-313
    • Sinha, M.1    Manna, P.2    Sil, P.C.3
  • 8
    • 0024639421 scopus 로고
    • The effect of cadmium on the body under conditions of various protein content in the diet
    • Veranian OA, Volkova NA, Karpliuk IA (1989) The effect of cadmium on the body under conditions of various protein content in the diet. Vopr Pitan 2:33-37
    • (1989) Vopr Pitan , vol.2 , pp. 33-37
    • Veranian, O.A.1    Volkova, N.A.2    Karpliuk, I.A.3
  • 9
    • 0038121657 scopus 로고    scopus 로고
    • Study of the activity of several brain enzymes like markers of the neurotoxicity induced by perinatal exposure to lead and/or cadmium
    • Antonio MT, Corredor L, Leret ML (2003) Study of the activity of several brain enzymes like markers of the neurotoxicity induced by perinatal exposure to lead and/or cadmium. Toxicol Lett 143:331-340
    • (2003) Toxicol Lett , vol.143 , pp. 331-340
    • Antonio, M.T.1    Corredor, L.2    Leret, M.L.3
  • 10
    • 0037447621 scopus 로고    scopus 로고
    • Perinatal exposure to lead and cadmium affects anxiety-like behaviour
    • Leret ML, Millan JA, Antonio MT (2003) Perinatal exposure to lead and cadmium affects anxiety-like behaviour. Toxicology 186:125-130
    • (2003) Toxicology , vol.186 , pp. 125-130
    • Leret, M.L.1    Millan, J.A.2    Antonio, M.T.3
  • 11
    • 0343580526 scopus 로고    scopus 로고
    • The effect of developmental exposure to cadmium (Cd) on visual evoked potentials (VEPs) and lipid peroxidation
    • Yargiçoglu P, Agar A, Oguz Y, Izgüt-Uysal V, Sentürk U, Oner G (1997) The effect of developmental exposure to cadmium (Cd) on visual evoked potentials (VEPs) and lipid peroxidation. Neurotoxicol Teratol 19:213-219
    • (1997) Neurotoxicol Teratol , vol.19 , pp. 213-219
    • Yargiçoglu, P.1    Agar, A.2    Oguz, Y.3    Izgüt-Uysal, V.4    Sentürk, U.5    Oner, G.6
  • 12
    • 0035961993 scopus 로고    scopus 로고
    • Histopathological alterations in the brain regions of rats after perinatal combined treatment with cadmium and dexamethasone
    • Mendez-Armenta M, Barroso-Moguel R, Villeda-Hernandez J, Nava-Ruiz C, Rios C (2001) Histopathological alterations in the brain regions of rats after perinatal combined treatment with cadmium and dexamethasone. Toxicology 161:189-199
    • (2001) Toxicology , vol.161 , pp. 189-199
    • Mendez-Armenta, M.1    Barroso-Moguel, R.2    Villeda-Hernandez, J.3    Nava-Ruiz, C.4    Rios, C.5
  • 14
    • 0027993419 scopus 로고
    • Cadmium encephalopathy: A report with elemental analysis and pathological findings
    • Provias JP, Ackerley CA, Smith C, Becker LE (1994) Cadmium encephalopathy: a report with elemental analysis and pathological findings. Acta Neuropathol 88:583-586
    • (1994) Acta Neuropathol , vol.88 , pp. 583-586
    • Provias, J.P.1    Ackerley, C.A.2    Smith, C.3    Becker, L.E.4
  • 15
    • 1542265817 scopus 로고    scopus 로고
    • In vivo and in vitro effects of cadmium on adult rat brain total antioxidant status, acetylcholinesterase, (Na?, K?)-ATPase and Mg2+-ATPase activities: Protection by L-cys-teine
    • Carageorgiou H, Tzotzes V, Pantos C, Mourouzis C, Zarros A, Tsakiris S (2004) In vivo and in vitro effects of cadmium on adult rat brain total antioxidant status, acetylcholinesterase, (Na?, K?)-ATPase and Mg2+-ATPase activities: protection by L-cys-teine. Basic Clin Pharmacol Toxicol 94:112-118
    • (2004) Basic Clin Pharmacol Toxicol , vol.94 , pp. 112-118
    • Carageorgiou, H.1    Tzotzes, V.2    Pantos, C.3    Mourouzis, C.4    Zarros, A.5    Tsakiris, S.6
  • 16
    • 34548579028 scopus 로고    scopus 로고
    • Efficacy of diphenyl diselenide against cerebral and pulmonary damage induced by cadmium in mice
    • doi:10.1016/j.toxlet.2007.07.011
    • Luchese C, Brandao R, de Oliveira R, Nogueira CW, Santos FW (2007) Efficacy of diphenyl diselenide against cerebral and pulmonary damage induced by cadmium in mice. Toxicol Lett 173:181-190. doi:10.1016/j.toxlet.2007.07.011
    • (2007) Toxicol Lett , vol.173 , pp. 181-190
    • Luchese, C.1    Brandao, R.2    De Oliveira, R.3    Nogueira, C.W.4    Santos, F.W.5
  • 17
    • 34047182492 scopus 로고    scopus 로고
    • Diallyl tetrasulfide improves cadmium induced alterations of acetylcholinesterase, ATPases and oxidative stress in brain of rats
    • doi: 10.1016/j.tox.2007.01.021
    • Pari L, Murugavel P (2007) Diallyl tetrasulfide improves cadmium induced alterations of acetylcholinesterase, ATPases and oxidative stress in brain of rats. Toxicology 234:44-50. doi: 10.1016/j.tox.2007.01.021
    • (2007) Toxicology , vol.234 , pp. 44-50
    • Pari, L.1    Murugavel, P.2
  • 20
    • 33744901157 scopus 로고    scopus 로고
    • Locomotor circuits in the mammalian spinal cord
    • doi:10.1146/annurev.neuro. 29.051605.112910
    • Kiehn O (2006) Locomotor circuits in the mammalian spinal cord. Annu Rev Neurosci 29:279-306. doi:10.1146/annurev.neuro. 29.051605.112910
    • (2006) Annu Rev Neurosci , vol.29 , pp. 279-306
    • Kiehn, O.1
  • 21
    • 0037012468 scopus 로고    scopus 로고
    • Acetylcholinesterase knockouts establish central cholinergic pathways and can use butyrylcholinesterase to hydrolyze acetylcholine
    • Mesulam MM, Guillozet A, Shaw P, Levey A, Duysen EG, Lockridge O (2002) Acetylcholinesterase knockouts establish central cholinergic pathways and can use butyrylcholinesterase to hydrolyze acetylcholine. Neuroscience 110:627-639
    • (2002) Neuroscience , vol.110 , pp. 627-639
    • Mesulam, M.M.1    Guillozet, A.2    Shaw, P.3    Levey, A.4    Duysen, E.G.5    Lockridge, O.6
  • 23
    • 0031936369 scopus 로고    scopus 로고
    • Behavioural and neu-rotoxicological changes caused by cadmium treatment of rats during development
    • Desi I, Nagymajtenyi L, Schulz H (1998) Behavioural and neu-rotoxicological changes caused by cadmium treatment of rats during development. J Appl Toxicol 18:63-70
    • (1998) J Appl Toxicol , vol.18 , pp. 63-70
    • Desi, I.1    Nagymajtenyi, L.2    Schulz, H.3
  • 24
    • 0344255794 scopus 로고    scopus 로고
    • The lymphocytic cholinergic system and its contribution to the regulation of immune activity
    • Kawashima K, Fujii T (2003) The lymphocytic cholinergic system and its contribution to the regulation of immune activity. Life Sci 74:675-696
    • (2003) Life Sci , vol.74 , pp. 675-696
    • Kawashima, K.1    Fujii, T.2
  • 25
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • doi:10.1152/physrev.00015.2002
    • North RA (2002) Molecular physiology of P2X receptors. Physiol Rev 82:1013-1067. doi:10.1152/physrev.00015.2002
    • (2002) Physiol Rev , vol.82 , pp. 1013-1067
    • North, R.A.1
  • 26
    • 20444368420 scopus 로고    scopus 로고
    • 0-nucleoti-dases as regulators of nucleotide and drug metabolism
    • doi:10.1016/j.pharmthera.2005.01.003
    • 0-nucleoti- dases as regulators of nucleotide and drug metabolism. Pharmacol Ther 107:1-30. doi:10.1016/j.pharmthera.2005.01.003
    • (2005) Pharmacol Ther , vol.107 , pp. 1-30
    • Hunsucker, S.A.1    Mitchell, B.S.2    Spychala, J.3
  • 27
    • 0036798380 scopus 로고    scopus 로고
    • The evidence for two opposite, ATP-generating and ATP-consuming, extracellular pathways on endothelial and lymphoid cells
    • doi:10.1042/BJ20020439
    • Yegutkin G, Henttinen T, Samburski S, Spychala J, Jalkanen S (2002) The evidence for two opposite, ATP-generating and ATP-consuming, extracellular pathways on endothelial and lymphoid cells. Biochem J 367:121-128. doi:10.1042/BJ20020439
    • (2002) Biochem J , vol.367 , pp. 121-128
    • Yegutkin, G.1    Henttinen, T.2    Samburski, S.3    Spychala, J.4    Jalkanen, S.5
  • 28
    • 52449105495 scopus 로고    scopus 로고
    • 0-nucleotidase activities in physiological and disease conditions: New perspectives for human health
    • 0-nucleotidase activities in physiological and disease conditions: new perspectives for human health. BioFactors 31:77-98
    • (2007) BioFactors , vol.31 , pp. 77-98
    • Schetinger, M.R.1    Morsch, V.M.2    Bonan, C.D.3    Wyse, A.T.4
  • 31
    • 34250814456 scopus 로고    scopus 로고
    • Previous treatment with ebselen and vitamin e alters adenine nucleotide hydrolysis in platelets from adult rats experimentally demyelinated with ethidium bromide
    • doi:10.1016/j.lfs.2007.05.008
    • Mazzanti CM, Spanevello RM, Morsch A, Zanin R, Battisti V, Ahmed M, Goncalves JF, Mazzanti A, Graca DL, Morsch VM, Schetinger MR (2007) Previous treatment with ebselen and vitamin E alters adenine nucleotide hydrolysis in platelets from adult rats experimentally demyelinated with ethidium bromide. Life Sci 81:241-248. doi:10.1016/j.lfs.2007.05.008
    • (2007) Life Sci , vol.81 , pp. 241-248
    • Mazzanti, C.M.1    Spanevello, R.M.2    Morsch, A.3    Zanin, R.4    Battisti, V.5    Ahmed, M.6    Goncalves, J.F.7    Mazzanti, A.8    Graca, D.L.9    Morsch, V.M.10    Schetinger, M.R.11
  • 34
    • 84984555347 scopus 로고    scopus 로고
    • In vitro and in vivo interactions of aluminum on NTPDase and AChE activities in lymphocytes of rats
    • doi:10.1016/j.cellimm.2010.08.001
    • Kaizer RR, Gutierres JM, Schmatz R, Spanevello RM, Morsch VM, Schetinger MR, Rocha JB (2010) In vitro and in vivo interactions of aluminum on NTPDase and AChE activities in lymphocytes of rats. Cell Immunol 265:133-138. doi:10.1016/j.cellimm.2010.08.001
    • (2010) Cell Immunol , vol.265 , pp. 133-138
    • Kaizer, R.R.1    Gutierres, J.M.2    Schmatz, R.3    Spanevello, R.M.4    Morsch, V.M.5    Schetinger, M.R.6    Rocha, J.B.7
  • 36
    • 0033631609 scopus 로고    scopus 로고
    • Mechanisms of cadmium-mediated acute hepatotoxicity
    • Rikans LE, Yamano T (2000) Mechanisms of cadmium-mediated acute hepatotoxicity. J Biochem Mol Toxicol 14:110-117
    • (2000) J Biochem Mol Toxicol , vol.14 , pp. 110-117
    • Rikans, L.E.1    Yamano, T.2
  • 37
    • 0035809068 scopus 로고    scopus 로고
    • Modulation of the stress response during apoptosis and necrosis induction in cadmium-treated U-937 human promono-cytic cells
    • Galan A, Troyano A, Vilaboa NE, Fernandez C, de Blas E, Aller P (2001) Modulation of the stress response during apoptosis and necrosis induction in cadmium-treated U-937 human promono-cytic cells. Biochim Biophys Acta 1538:38-46
    • (2001) Biochim Biophys Acta , vol.1538 , pp. 38-46
    • Galan, A.1    Troyano, A.2    Vilaboa, N.E.3    Fernandez, C.4    De Blas, E.5    Aller, P.6
  • 40
    • 84866045756 scopus 로고    scopus 로고
    • Life or death: Neuroprotective and anticancer effects of quercetin
    • doi:10.1016/j.jep.2012.07.005
    • Dajas F (2012) Life or death: neuroprotective and anticancer effects of quercetin. J Ethnopharmacol 143:383-396. doi:10.1016/j.jep.2012.07.005
    • (2012) J Ethnopharmacol , vol.143 , pp. 383-396
    • Dajas, F.1
  • 41
    • 0037292433 scopus 로고    scopus 로고
    • Molecular handling of cadmium in transporting epithelia
    • Zalups R, Ahmad S (2003) Molecular handling of cadmium in transporting epithelia. Toxicol Appl Pharmacol 186:163-188
    • (2003) Toxicol Appl Pharmacol , vol.186 , pp. 163-188
    • Zalups, R.1    Ahmad, S.2
  • 42
    • 33745377482 scopus 로고    scopus 로고
    • Quercetin reverses D-galactose induced neurotoxicity in mouse brain
    • doi:10.1016/j.bbr.2006. 03.043
    • Lu J, Zheng YL, Luo L, Wu DM, Sun DX, Feng YJ (2006) Quercetin reverses D-galactose induced neurotoxicity in mouse brain. Behav Brain Res 171:251-260. doi:10.1016/j.bbr.2006. 03.043
    • (2006) Behav Brain Res , vol.171 , pp. 251-260
    • Lu, J.1    Zheng, Y.L.2    Luo, L.3    Wu, D.M.4    Sun, D.X.5    Feng, Y.J.6
  • 43
    • 34548471990 scopus 로고    scopus 로고
    • Neuroprotective effects of quercetin and rutin on spatial memory impairment in an 8-arm radial maze task and neuronal death induced by repeated cerebral ischemia in rats
    • Pu F, Mishima K, Irie K, Motohashi K, Tanaka Y, Orito K, Egawa T, Kitamura Y, Egashira N, Iwasaki K, Fujiwara M (2007) Neuroprotective effects of quercetin and rutin on spatial memory impairment in an 8-arm radial maze task and neuronal death induced by repeated cerebral ischemia in rats. J Pharmacol Sci 104:329-334
    • (2007) J Pharmacol Sci , vol.104 , pp. 329-334
    • Pu, F.1    Mishima, K.2    Irie, K.3    Motohashi, K.4    Tanaka, Y.5    Orito, K.6    Egawa, T.7    Kitamura, Y.8    Egashira, N.9    Iwasaki, K.10    Fujiwara, M.11
  • 44
    • 0021219280 scopus 로고
    • Rapid preparation of syn-aptosomes from mammalian brain using nontoxic isoosmotic gradient material (Percoll)
    • Nagy A, Delgado-Escueta A (1984) Rapid preparation of syn-aptosomes from mammalian brain using nontoxic isoosmotic gradient material (Percoll). J Neurochem 43:1114-1123
    • (1984) J Neurochem , vol.43 , pp. 1114-1123
    • Nagy, A.1    Delgado-Escueta, A.2
  • 45
    • 33644811612 scopus 로고
    • A new and rapid colorimetric determination of acetylcholinesterase activity
    • Ellman G, Courtney K, Andres VJ, Feather-Stone R (1961) A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem Pharmacol 7:88-95
    • (1961) Biochem Pharmacol , vol.7 , pp. 88-95
    • Ellman, G.1    Courtney, K.2    Andres, V.J.3    Feather-Stone, R.4
  • 46
    • 84984571922 scopus 로고
    • Effects of early undernutrition on kinetic parameters of brain acetylcholinesterase from adult rats
    • Rocha JB, Emanuelli T, Pereira ME (1993) Effects of early undernutrition on kinetic parameters of brain acetylcholinesterase from adult rats. Acta Neurobiol Exp (Wars) 53:431-437
    • (1993) Acta Neurobiol Exp (Wars) , vol.53 , pp. 431-437
    • Rocha, J.B.1    Emanuelli, T.2    Pereira, M.E.3
  • 49
    • 0022549284 scopus 로고
    • A direct colorimetric assay for Ca2+-stimulated ATPase activity
    • Chan K, Delfert D, Junger K (1986) A direct colorimetric assay for Ca2+-stimulated ATPase activity. Anal Biochem 157:375-380
    • (1986) Anal Biochem , vol.157 , pp. 375-380
    • Chan, K.1    Delfert, D.2    Junger, K.3
  • 50
    • 0015180548 scopus 로고
    • Temperature conversion factors, activation energy, relative substrate specificity and optimum pH of adenosine deaminase from human serum and tissues
    • Giusti G, Gakis C (1971) Temperature conversion factors, activation energy, relative substrate specificity and optimum pH of adenosine deaminase from human serum and tissues. Enzyme 12:417-425
    • (1971) Enzyme , vol.12 , pp. 417-425
    • Giusti, G.1    Gakis, C.2
  • 51
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 52
    • 33745209198 scopus 로고    scopus 로고
    • In vitro effect of zinc and cadmium on acetylcholinesterase and ectonucleotidase activities in zebra-fish (Danio rerio) brain
    • doi: 10.1016/j.tiv.2005.12.002
    • Senger MR, Rosemberg DB, Rico EP, de Bem Arizi M, Dias RD, Bogo MR, Bonan CD (2006) In vitro effect of zinc and cadmium on acetylcholinesterase and ectonucleotidase activities in zebra-fish (Danio rerio) brain. Toxicol In Vitro 20:954-958. doi: 10.1016/j.tiv.2005.12.002
    • (2006) Toxicol in Vitro , vol.20 , pp. 954-958
    • Senger, M.R.1    Rosemberg, D.B.2    Rico, E.P.3    De Bem Arizi, M.4    Dias, R.D.5    Bogo, M.R.6    Bonan, C.D.7
  • 54
    • 23844501100 scopus 로고    scopus 로고
    • Cloning and characterization of the ecto-nucleotidase NTPDase3 from rat brain: Predicted secondary structure and relation to other members of the E-NTPDase family and actin
    • doi:10.1007/s11302-005-6314-x
    • Vorhoff T, Zimmermann H, Pelletier J, Sevigny J, Braun N (2005) Cloning and characterization of the ecto-nucleotidase NTPDase3 from rat brain: predicted secondary structure and relation to other members of the E-NTPDase family and actin. Purinergic Signal 1:259-270. doi:10.1007/s11302-005-6314-x
    • (2005) Purinergic Signal , vol.1 , pp. 259-270
    • Vorhoff, T.1    Zimmermann, H.2    Pelletier, J.3    Sevigny, J.4    Braun, N.5
  • 55
    • 0027515387 scopus 로고
    • Structure and functions of acetylcholinesterase and butyrylcholinesterase
    • Massoulie J, Sussman J, Bon S, Silman I (1993) Structure and functions of acetylcholinesterase and butyrylcholinesterase. Prog Brain Res 98:139-146
    • (1993) Prog Brain Res , vol.98 , pp. 139-146
    • Massoulie, J.1    Sussman, J.2    Bon, S.3    Silman, I.4
  • 57
    • 27744437463 scopus 로고    scopus 로고
    • Cadmium effects on brain acetylcholinesterase activity and antioxidant status of adult rats: Modulation by zinc, calcium and L-cysteine co-administration
    • doi:10.1111/j.1742-7843.2005.pto-174.x
    • Carageorgiou H, Tzotzes V, Sideris A, Zarros A, Tsakiris S (2005) Cadmium effects on brain acetylcholinesterase activity and antioxidant status of adult rats: modulation by zinc, calcium and L-cysteine co-administration. Basic Clin Pharmacol Toxicol 97:320-324. doi:10.1111/j.1742-7843.2005.pto-174.x
    • (2005) Basic Clin Pharmacol Toxicol , vol.97 , pp. 320-324
    • Carageorgiou, H.1    Tzotzes, V.2    Sideris, A.3    Zarros, A.4    Tsakiris, S.5
  • 58
    • 0029967268 scopus 로고    scopus 로고
    • Cadmium-induced alterations in blood-brain barrier permeability and its possible correlation with decreased microvessel antioxidant potential in rat
    • Shukla A, Shukla GS, Srimal RC (1996) Cadmium-induced alterations in blood-brain barrier permeability and its possible correlation with decreased microvessel antioxidant potential in rat. Hum Exp Toxicol 15:400-405
    • (1996) Hum Exp Toxicol , vol.15 , pp. 400-405
    • Shukla, A.1    Shukla, G.S.2    Srimal, R.C.3
  • 59
    • 0348222661 scopus 로고    scopus 로고
    • Adenosine: An endogenous regulator of innate immunity
    • Hasko G, Cronstein BN (2004) Adenosine: an endogenous regulator of innate immunity. Trends Immunol 25:33-39
    • (2004) Trends Immunol , vol.25 , pp. 33-39
    • Hasko, G.1    Cronstein, B.N.2
  • 61
    • 0029010019 scopus 로고
    • ATP acts as fast neurotransmitter in rat habenula: Neurochemical and enzymecy-tochemical evidence
    • Sperlagh B, Kittel A, Lajtha A, Vizi ES (1995) ATP acts as fast neurotransmitter in rat habenula: neurochemical and enzymecy-tochemical evidence. Neuroscience 66:915-920
    • (1995) Neuroscience , vol.66 , pp. 915-920
    • Sperlagh, B.1    Kittel, A.2    Lajtha, A.3    Vizi, E.S.4
  • 62
    • 33645106684 scopus 로고    scopus 로고
    • Historical review: ATP as a neurotransmitter
    • doi:10.1016/j.tips.2006.01.005
    • Burnstock G (2006) Historical review: ATP as a neurotransmitter. Trends Pharmacol Sci 27:166-176. doi:10.1016/j.tips.2006.01.005
    • (2006) Trends Pharmacol Sci , vol.27 , pp. 166-176
    • Burnstock, G.1
  • 63
    • 0034554789 scopus 로고    scopus 로고
    • ATP as a presynaptic modulator
    • Cunha RA, Ribeiro JA (2000) ATP as a presynaptic modulator. Life Sci 68:119-137
    • (2000) Life Sci , vol.68 , pp. 119-137
    • Cunha, R.A.1    Ribeiro, J.A.2
  • 64
    • 0037401680 scopus 로고    scopus 로고
    • Distribution and expression of A1 adenosine receptors, adenosine deaminase and adenosine deaminase-binding protein (CD26) in goldfish brain
    • Beraudi A, Traversa U, Villani L, Sekino Y, Nagy JI, Poli A (2003) Distribution and expression of A1 adenosine receptors, adenosine deaminase and adenosine deaminase-binding protein (CD26) in goldfish brain. Neurochem Int 42:455-464
    • (2003) Neurochem Int , vol.42 , pp. 455-464
    • Beraudi, A.1    Traversa, U.2    Villani, L.3    Sekino, Y.4    Nagy, J.I.5    Poli, A.6
  • 66
    • 19544391973 scopus 로고    scopus 로고
    • The 'danger' sensors that STOP the immune response: The A2 adenosine receptors?
    • doi:10.1016/j.it.2005.04.004
    • Sitkovsky MV, Ohta A (2005) The 'danger' sensors that STOP the immune response: the A2 adenosine receptors? Trends Immunol 26:299-304. doi:10.1016/j.it.2005.04.004
    • (2005) Trends Immunol , vol.26 , pp. 299-304
    • Sitkovsky, M.V.1    Ohta, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.