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Volumn 80, Issue 6, 2009, Pages 371-376

Ectonucleotidase and acetylcholinesterase activities in synaptosomes from the cerebral cortex of streptozotocin-induced diabetic rats and treated with resveratrol

Author keywords

Acetylcholinesterase; Diabetes; Ectonucleotidases; Resveratrol; Streptozotocin; Synaptosomes

Indexed keywords

5' NUCLEOTIDASE; ACETYLCHOLINESTERASE; ECTONUCLEOTIDASE; NUCLEOTIDASE; PURINE; RESVERATROL; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

EID: 70349947111     PISSN: 03619230     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainresbull.2009.08.019     Document Type: Article
Times cited : (33)

References (55)
  • 1
    • 0032814775 scopus 로고    scopus 로고
    • Adenosine triphosphate: established and potential clinical applications
    • Agteresch H.J., Dagnelie P.C., and Paul J.H.W. Adenosine triphosphate: established and potential clinical applications. Drugs 58 (1999) 211-232
    • (1999) Drugs , vol.58 , pp. 211-232
    • Agteresch, H.J.1    Dagnelie, P.C.2    Paul, J.H.W.3
  • 2
    • 0026447003 scopus 로고
    • Secreted acetylcholinesterase: non-classical aspects of a classical enzyme
    • Appleyard M.E. Secreted acetylcholinesterase: non-classical aspects of a classical enzyme. Trends Neurosci. 15 (1992) 485-490
    • (1992) Trends Neurosci. , vol.15 , pp. 485-490
    • Appleyard, M.E.1
  • 3
    • 0028105940 scopus 로고
    • Non-cholinergic functions of acetylcholinesterase
    • Appleyard M.E. Non-cholinergic functions of acetylcholinesterase. Biochem. Soc. Trans. 22 (1994) 749-755
    • (1994) Biochem. Soc. Trans. , vol.22 , pp. 749-755
    • Appleyard, M.E.1
  • 4
    • 14744303952 scopus 로고    scopus 로고
    • Polyphenols and disease risk in epidemiologic studies
    • Arts I.C.W., and Hollman P.C.H. Polyphenols and disease risk in epidemiologic studies. Am. J. Clin. Nutr. 81 (2005) 156-162
    • (2005) Am. J. Clin. Nutr. , vol.81 , pp. 156-162
    • Arts, I.C.W.1    Hollman, P.C.H.2
  • 5
    • 2442424380 scopus 로고    scopus 로고
    • Diabetes mellitus and risk of Alzheimer disease and decline in cognitive function
    • Arvanitakis Z., Wilson R.S., Bienias J.L., Evans D.A., and Bennett D.A. Diabetes mellitus and risk of Alzheimer disease and decline in cognitive function. Arch. Neurol. 61 (2004) 661-666
    • (2004) Arch. Neurol. , vol.61 , pp. 661-666
    • Arvanitakis, Z.1    Wilson, R.S.2    Bienias, J.L.3    Evans, D.A.4    Bennett, D.A.5
  • 7
    • 0036752553 scopus 로고    scopus 로고
    • Natural extracts as possible protective agents of brain aging
    • Bastianetto S., and Quirion R. Natural extracts as possible protective agents of brain aging. Neurobiol. Aging 23 (2002) 891-897
    • (2002) Neurobiol. Aging , vol.23 , pp. 891-897
    • Bastianetto, S.1    Quirion, R.2
  • 8
    • 33745962138 scopus 로고    scopus 로고
    • Therapeutic potential of resveratrol: the in vivo evidence
    • Baur J.A., and Sinclair D.A. Therapeutic potential of resveratrol: the in vivo evidence. Nat. Rev. Drug Discov. 5 (2006) 493-506
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 493-506
    • Baur, J.A.1    Sinclair, D.A.2
  • 9
    • 38149065205 scopus 로고    scopus 로고
    • Cognition and diabetes: a lifespan perspective
    • Biessels G.J., Deary I.J., and Ryan C.M. Cognition and diabetes: a lifespan perspective. Lancet Neurol. 7 (2008) 184-190
    • (2008) Lancet Neurol. , vol.7 , pp. 184-190
    • Biessels, G.J.1    Deary, I.J.2    Ryan, C.M.3
  • 11
    • 34147119739 scopus 로고    scopus 로고
    • Diabetic neuropathy
    • Bloomgarden Z.T. Diabetic neuropathy. Diabetes Care 30 (2007) 1027-1032
    • (2007) Diabetes Care , vol.30 , pp. 1027-1032
    • Bloomgarden, Z.T.1
  • 12
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantificationof microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for quantificationof microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 13
    • 1842785177 scopus 로고    scopus 로고
    • Cerebral dysfunction in type 1 diabetes: effects of insulin, vascular risk factors and blood-glucose levels
    • Brands A.M.A., Kessels R.P.C., de Haan E.H.F., Kappelle L.J., and Biessels G.J. Cerebral dysfunction in type 1 diabetes: effects of insulin, vascular risk factors and blood-glucose levels. Eur. J. Pharmacol. 490 (2004) 159-168
    • (2004) Eur. J. Pharmacol. , vol.490 , pp. 159-168
    • Brands, A.M.A.1    Kessels, R.P.C.2    de Haan, E.H.F.3    Kappelle, L.J.4    Biessels, G.J.5
  • 14
    • 33645106684 scopus 로고    scopus 로고
    • Historical review: ATP as a neurotransmitter
    • Burnstock G. Historical review: ATP as a neurotransmitter. Trends Pharmacol. Sci. 27 (2006) 166-176
    • (2006) Trends Pharmacol. Sci. , vol.27 , pp. 166-176
    • Burnstock, G.1
  • 15
    • 0141642240 scopus 로고    scopus 로고
    • Acetylcholinesterase induces neuronal cell loss, astrocyte hypertrophy and behavioral deficits in mammalian hippocampus
    • Chacón M.A., Reyes A.E., and Inestrosa N.C. Acetylcholinesterase induces neuronal cell loss, astrocyte hypertrophy and behavioral deficits in mammalian hippocampus. J. Neurochem. 87 (2003) 195-204
    • (2003) J. Neurochem. , vol.87 , pp. 195-204
    • Chacón, M.A.1    Reyes, A.E.2    Inestrosa, N.C.3
  • 17
    • 60249091672 scopus 로고    scopus 로고
    • Inhibitory effect of glutamate release from rat cerebrocortical nerve terminals by resveratrol
    • Chang Y., and Wang S.J. Inhibitory effect of glutamate release from rat cerebrocortical nerve terminals by resveratrol. Neurochem. Int. 54 2 (2009) 135-141
    • (2009) Neurochem. Int. , vol.54 , Issue.2 , pp. 135-141
    • Chang, Y.1    Wang, S.J.2
  • 18
    • 0034554789 scopus 로고    scopus 로고
    • ATP as presynaptic modulator
    • Cunha R.A., and Ribeiro J.A. ATP as presynaptic modulator. Life Sci. 68 (2000) 119-137
    • (2000) Life Sci. , vol.68 , pp. 119-137
    • Cunha, R.A.1    Ribeiro, J.A.2
  • 19
    • 0035255227 scopus 로고    scopus 로고
    • Adenosine as a neuromodulator and as homeostatic regulator in the nervous system: different role, different sources and different receptors
    • Cunha R.A. Adenosine as a neuromodulator and as homeostatic regulator in the nervous system: different role, different sources and different receptors. Neurochem. Int. 38 (2001) 107-125
    • (2001) Neurochem. Int. , vol.38 , pp. 107-125
    • Cunha, R.A.1
  • 20
    • 35348895686 scopus 로고    scopus 로고
    • Modification of purinergic signaling in the hippocampus of streptozotocin-induced diabetic rats
    • Duarte J.M., Oses J.P., Rodrigues R.J., and Cunha R.A. Modification of purinergic signaling in the hippocampus of streptozotocin-induced diabetic rats. Neuroscience 149 (2007) 382-391
    • (2007) Neuroscience , vol.149 , pp. 382-391
    • Duarte, J.M.1    Oses, J.P.2    Rodrigues, R.J.3    Cunha, R.A.4
  • 21
    • 0034923094 scopus 로고    scopus 로고
    • The role and regulation of adenosine in the central nervous system
    • Dumwiddie T.V., and Masino S.A. The role and regulation of adenosine in the central nervous system. Annu. Rev. Neurosci. 24 (2001) 31-35
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 31-35
    • Dumwiddie, T.V.1    Masino, S.A.2
  • 22
  • 23
    • 0034531974 scopus 로고    scopus 로고
    • ATP: an extracellular signaling molecule between neurons and glia
    • Fields R.D., and Stevens B. ATP: an extracellular signaling molecule between neurons and glia. TINS 23 (2000) 625-633
    • (2000) TINS , vol.23 , pp. 625-633
    • Fields, R.D.1    Stevens, B.2
  • 24
    • 0030221064 scopus 로고    scopus 로고
    • Fast purinergic transmission in the central nervous system
    • Gibb A., and Halliday F.C. Fast purinergic transmission in the central nervous system. Neuroscience 8 (1996) 225-232
    • (1996) Neuroscience , vol.8 , pp. 225-232
    • Gibb, A.1    Halliday, F.C.2
  • 25
    • 0021162078 scopus 로고
    • Subcellular localization of 5′-nucleotidase in rat brain
    • Heymann D., Reddington M., and Kreutzberg G.W. Subcellular localization of 5′-nucleotidase in rat brain. J. Neurochem. 43 (1984) 971-978
    • (1984) J. Neurochem. , vol.43 , pp. 971-978
    • Heymann, D.1    Reddington, M.2    Kreutzberg, G.W.3
  • 26
    • 60249098801 scopus 로고    scopus 로고
    • Dietary supplementation with resveratrol reduces plaque pathology in a transgenic model of Alzheimer's disease
    • Karuppagounder S.S., Pinto J.T., Xu H., Chen H.L., Beal M.F., and Gibson G.E. Dietary supplementation with resveratrol reduces plaque pathology in a transgenic model of Alzheimer's disease. Neurochem. Int. 54 2 (2009) 111-118
    • (2009) Neurochem. Int. , vol.54 , Issue.2 , pp. 111-118
    • Karuppagounder, S.S.1    Pinto, J.T.2    Xu, H.3    Chen, H.L.4    Beal, M.F.5    Gibson, G.E.6
  • 27
    • 42949176731 scopus 로고    scopus 로고
    • Lycopene attenuates thermal hyperalgesia in a diabetic mouse model of neuropathic pain
    • Kuhad A., Sharma S., and Chopra K. Lycopene attenuates thermal hyperalgesia in a diabetic mouse model of neuropathic pain. Eur. J. Pharmacol. 12 (2008) 624-632
    • (2008) Eur. J. Pharmacol. , vol.12 , pp. 624-632
    • Kuhad, A.1    Sharma, S.2    Chopra, K.3
  • 28
    • 35348851411 scopus 로고    scopus 로고
    • Curcumin attenuates diabetic encephalopathy in rats: behavioral and biochemical evidences
    • Kuhad A., and Chopra K. Curcumin attenuates diabetic encephalopathy in rats: behavioral and biochemical evidences. Eur. J. Pharmacol. 576 (2007) 34-42
    • (2007) Eur. J. Pharmacol. , vol.576 , pp. 34-42
    • Kuhad, A.1    Chopra, K.2
  • 29
    • 33847334999 scopus 로고    scopus 로고
    • Effects of resveratrol on nerve functions, oxidative stress and DNA fragmentation in experimental diabetic neuropathy
    • Kumar A., Kaundal R.K., and Iyer S. Effects of resveratrol on nerve functions, oxidative stress and DNA fragmentation in experimental diabetic neuropathy. Life Sci. 80 (2007) 1236-1244
    • (2007) Life Sci. , vol.80 , pp. 1236-1244
    • Kumar, A.1    Kaundal, R.K.2    Iyer, S.3
  • 30
    • 42049100322 scopus 로고    scopus 로고
    • Nonsynaptic chemical transmission through nicotinic acetylcholine receptors
    • Lendvai B., and Vizi E.S. Nonsynaptic chemical transmission through nicotinic acetylcholine receptors. Physiol. Rev. 88 (2008) 333-349
    • (2008) Physiol. Rev. , vol.88 , pp. 333-349
    • Lendvai, B.1    Vizi, E.S.2
  • 33
    • 0037012468 scopus 로고    scopus 로고
    • Acetylcholinesterase knockouts establish central cholinergic pathways and can use butyrylcholinesterase to hydrolyze acetylcholine
    • Mesulam M.M., Guillozet A., Shaw P., Levey A., Duysen E.G., and Lockridge O. Acetylcholinesterase knockouts establish central cholinergic pathways and can use butyrylcholinesterase to hydrolyze acetylcholine. Neuroscience 110 (2002) 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
  • 35
    • 34248146970 scopus 로고    scopus 로고
    • Effect of resveratrol on antioxidant enzyme activities in the brain of healthy rat
    • Mokni M., Elkahoui S., Limam F., Amri M., and Aouani E. Effect of resveratrol on antioxidant enzyme activities in the brain of healthy rat. Neurochem. Res. 32 (2007) 981-987
    • (2007) Neurochem. Res. , vol.32 , pp. 981-987
    • Mokni, M.1    Elkahoui, S.2    Limam, F.3    Amri, M.4    Aouani, E.5
  • 36
    • 0021219280 scopus 로고
    • Rapid preparation of synaptosomes from mammalian brain using non-toxic isosmotic gradient material (Percoll)
    • Nagy A., and Delgado Escueta A.V. Rapid preparation of synaptosomes from mammalian brain using non-toxic isosmotic gradient material (Percoll). J. Neurochem. 43 (1984) 1114-1123
    • (1984) J. Neurochem. , vol.43 , pp. 1114-1123
    • Nagy, A.1    Delgado Escueta, A.V.2
  • 39
    • 33846436678 scopus 로고    scopus 로고
    • The E-NTPDase family of ectonucleotidases: structure function relationships and pathophysiological significance
    • Robson S., Sévigny J., and Zimmermann H. The E-NTPDase family of ectonucleotidases: structure function relationships and pathophysiological significance. Purinergic Signal. 2 (2006) 409-430
    • (2006) Purinergic Signal. , vol.2 , pp. 409-430
    • Robson, S.1    Sévigny, J.2    Zimmermann, H.3
  • 40
    • 84984571922 scopus 로고
    • Effects of early undernutrition on kinetic parameters of brain acetylcholinesterase from adult rats
    • Rocha J.B.T., Emanuelli T., and Pereira M.E. Effects of early undernutrition on kinetic parameters of brain acetylcholinesterase from adult rats. Acta Neurobiol. Exp. 53 (1993) 431-437
    • (1993) Acta Neurobiol. Exp. , vol.53 , pp. 431-437
    • Rocha, J.B.T.1    Emanuelli, T.2    Pereira, M.E.3
  • 41
    • 38649132291 scopus 로고    scopus 로고
    • Resveratrol and its analogs: defense against cancer, coronary disease and neurodegenerative maladies or just a fad?
    • Saiko P., Szakmary A., Jaeger W., and Szekeres T. Resveratrol and its analogs: defense against cancer, coronary disease and neurodegenerative maladies or just a fad?. Mutat Res. Rev. 658 (2008) 68-94
    • (2008) Mutat Res. Rev. , vol.658 , pp. 68-94
    • Saiko, P.1    Szakmary, A.2    Jaeger, W.3    Szekeres, T.4
  • 42
    • 0343962228 scopus 로고    scopus 로고
    • Effect of streptozotocin-induced diabetes on activities of cholinesterases in the rat retina
    • Sanchez-Chavez G., and Salceda R. Effect of streptozotocin-induced diabetes on activities of cholinesterases in the rat retina. IUBMB Life 49 (2000) 283-287
    • (2000) IUBMB Life , vol.49 , pp. 283-287
    • Sanchez-Chavez, G.1    Salceda, R.2
  • 44
    • 52449105495 scopus 로고    scopus 로고
    • NTPDase and 5′-nucleotidase activities in physiological and disease conditions: new perspectives for human health
    • Schetinger M.R., Morsch V.M., Bonan C., and Wyse A. NTPDase and 5′-nucleotidase activities in physiological and disease conditions: new perspectives for human health. Biofactors 31 (2008) 77-98
    • (2008) Biofactors , vol.31 , pp. 77-98
    • Schetinger, M.R.1    Morsch, V.M.2    Bonan, C.3    Wyse, A.4
  • 46
    • 18744414554 scopus 로고    scopus 로고
    • Acetylcholinesterase: classical and non classical functions and pharmacology
    • Silman I., and Sussman J. Acetylcholinesterase: classical and non classical functions and pharmacology. Curr. Opin. Pharmacol. 5 (2005) 293-302
    • (2005) Curr. Opin. Pharmacol. , vol.5 , pp. 293-302
    • Silman, I.1    Sussman, J.2
  • 47
    • 1842785176 scopus 로고    scopus 로고
    • Insulin, C-peptide, hyperglycemia, and central nervous system complications in diabetes
    • Sima A.A.F., Kamiya H., and Lia Z.G. Insulin, C-peptide, hyperglycemia, and central nervous system complications in diabetes. Eur. J. Pharmacol. 490 (2004) 187-197
    • (2004) Eur. J. Pharmacol. , vol.490 , pp. 187-197
    • Sima, A.A.F.1    Kamiya, H.2    Lia, Z.G.3
  • 48
    • 0035320772 scopus 로고    scopus 로고
    • Acetylcholinesterase-new roles for and old actor
    • Soreq H., and Seidman S. Acetylcholinesterase-new roles for and old actor. Nat. Rev. Neurosci. 2 (2001) 294-302
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 294-302
    • Soreq, H.1    Seidman, S.2
  • 50
    • 0029010019 scopus 로고
    • ATP acts as fast neurotransmitter in rat habenula: neurochemical and enzymecytochemical evidence
    • Sperlágh B., Kittel A., Lajtha A., and Vizi E.S. ATP acts as fast neurotransmitter in rat habenula: neurochemical and enzymecytochemical evidence. Neuroscience 66 (1995) 915-920
    • (1995) Neuroscience , vol.66 , pp. 915-920
    • Sperlágh, B.1    Kittel, A.2    Lajtha, A.3    Vizi, E.S.4
  • 51
  • 52
    • 34047250594 scopus 로고    scopus 로고
    • Ecto-5′-nucleotidase: structure function relationships
    • Sträter N. Ecto-5′-nucleotidase: structure function relationships. Purinergic Signal. 2 (2006) 243-350
    • (2006) Purinergic Signal. , vol.2 , pp. 243-350
    • Sträter, N.1
  • 53
    • 0030583727 scopus 로고    scopus 로고
    • Role of ionic interactions in cholinesterase catalysis
    • Tõugu V., and Kesvatera T. Role of ionic interactions in cholinesterase catalysis. Biochim. Biophys. Acta 1298 (1996) 12-30
    • (1996) Biochim. Biophys. Acta , vol.1298 , pp. 12-30
    • Tõugu, V.1    Kesvatera, T.2
  • 54
    • 41949083203 scopus 로고    scopus 로고
    • Nucleotide- and nucleoside-converting ectoenzymes: Important modulators of purinergic signalling cascade
    • Yegutkin G.G. Nucleotide- and nucleoside-converting ectoenzymes: Important modulators of purinergic signalling cascade. Biochim. Biophys. Acta 1783 (2008) 673-694
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 673-694
    • Yegutkin, G.G.1
  • 55
    • 38349101862 scopus 로고    scopus 로고
    • ATP and acetylcholine, equal brethren
    • Zimmermann H. ATP and acetylcholine, equal brethren. Neurochem. Int. 52 (2008) 634-648
    • (2008) Neurochem. Int. , vol.52 , pp. 634-648
    • Zimmermann, H.1


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