메뉴 건너뛰기




Volumn 25, Issue 6, 2007, Pages 381-386

The effect of aluminium on NTPDase and 5′-nucleotidase activities from rat synaptosomes and platelets

Author keywords

5 Nucleotidase; Aluminium; Cerebral cortex; Hippocampus; NTPDase; Platelets; Synaptosomes

Indexed keywords

5' NUCLEOTIDASE; ALUMINUM; ALUMINUM CHLORIDE; CALCIUM ION; CITRIC ACID; NUCLEOSIDE TRIPHOSPHATE; NUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE; NUCLEOTIDASE; UNCLASSIFIED DRUG;

EID: 35748967616     PISSN: 07365748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijdevneu.2007.06.002     Document Type: Article
Times cited : (15)

References (43)
  • 1
    • 0031770379 scopus 로고    scopus 로고
    • Purinergic signaling: pathophysiological roles
    • Abbracchio M.P., and Burnstock G. Purinergic signaling: pathophysiological roles. Jpn. J. Pharmacol. 78 (1998) 113-145
    • (1998) Jpn. J. Pharmacol. , vol.78 , pp. 113-145
    • Abbracchio, M.P.1    Burnstock, G.2
  • 2
    • 0023873585 scopus 로고
    • Differential effect of aluminium on the blood-brain barrier transport of peptides, technetium and albumin
    • Banks W.A., Kastin A.J., and Fasold M.B. Differential effect of aluminium on the blood-brain barrier transport of peptides, technetium and albumin. J. Pharmacol. Exp. Ther. 244 (1988) 579-585
    • (1988) J. Pharmacol. Exp. Ther. , vol.244 , pp. 579-585
    • Banks, W.A.1    Kastin, A.J.2    Fasold, M.B.3
  • 3
    • 0026321837 scopus 로고
    • Characterization of an ATP diphosphohydrolase (EC 3.6.1.5) in synaptosomes from cerebral cortex of adult rats
    • Battastini A.M.O., Rocha J.B.T., Barcellos C.K., Dias R.D., and Sarkis J.J.F. Characterization of an ATP diphosphohydrolase (EC 3.6.1.5) in synaptosomes from cerebral cortex of adult rats. Neurochem. Res. 16 (1991) 1303-1310
    • (1991) Neurochem. Res. , vol.16 , pp. 1303-1310
    • Battastini, A.M.O.1    Rocha, J.B.T.2    Barcellos, C.K.3    Dias, R.D.4    Sarkis, J.J.F.5
  • 4
    • 84984585749 scopus 로고    scopus 로고
    • Organochalcogens affect the glutamatergic neurotransmission in human platelets
    • Borges V.C., Nogueira C.W., Zeni G., and Rocha J.B.T. Organochalcogens affect the glutamatergic neurotransmission in human platelets. Neurochem. Res. 29 (2004) 1497-1501
    • (2004) Neurochem. Res. , vol.29 , pp. 1497-1501
    • Borges, V.C.1    Nogueira, C.W.2    Zeni, G.3    Rocha, J.B.T.4
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M.A. A rapid and sensitive method for the quantification of 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.A.1
  • 6
    • 13644266898 scopus 로고    scopus 로고
    • Age- and region-dependent alterations in Abeta-degrading enzymes: implications for Abeta-induced disorders
    • Caccamo A., Oddo S., Sugarman M.C., Akbarri Y., and LaFerla F.M. Age- and region-dependent alterations in Abeta-degrading enzymes: implications for Abeta-induced disorders. Neurobiol. Aging 26 (2005) 645-654
    • (2005) Neurobiol. Aging , vol.26 , pp. 645-654
    • Caccamo, A.1    Oddo, S.2    Sugarman, M.C.3    Akbarri, Y.4    LaFerla, F.M.5
  • 7
    • 0031981162 scopus 로고    scopus 로고
    • Modulation of monoamine oxidase activity in different brain regions and platelets following exposure of rats to methylmercury
    • Chakrabarti S.K., Loua K.M., Bai C., Durham H., and Panisset J.C. Modulation of monoamine oxidase activity in different brain regions and platelets following exposure of rats to methylmercury. Neurotoxicol. Teratol. 20 (1998) 161-168
    • (1998) Neurotoxicol. Teratol. , vol.20 , pp. 161-168
    • Chakrabarti, S.K.1    Loua, K.M.2    Bai, C.3    Durham, H.4    Panisset, J.C.5
  • 9
    • 0015913994 scopus 로고
    • Brain aluminium distribution in Alzheimer's disease and experimental neurofibrillary degeneration
    • Crapper D.R., Krishnan S.S., and Dalton A.J. Brain aluminium distribution in Alzheimer's disease and experimental neurofibrillary degeneration. Science 180 (1973) 511-513
    • (1973) Science , vol.180 , pp. 511-513
    • Crapper, D.R.1    Krishnan, S.S.2    Dalton, A.J.3
  • 10
    • 0034554789 scopus 로고    scopus 로고
    • ATP as a presynaptic modulator
    • Cunha R.A., and Ribeiro J.A. ATP as a presynaptic modulator. Life Sci. 68 (2000) 119-137
    • (2000) Life Sci. , vol.68 , pp. 119-137
    • Cunha, R.A.1    Ribeiro, J.A.2
  • 11
    • 33746893419 scopus 로고    scopus 로고
    • In vitro exposure of heavy metals on nucleotidase and cholinesterase activities from the digestive gland of Helix aspersa
    • Dahm K.C.S., Rückert C., Tonial E.M., and Bonan C.D. In vitro exposure of heavy metals on nucleotidase and cholinesterase activities from the digestive gland of Helix aspersa. Comp. Biochem. Physiol. C 143 (2006) 316-320
    • (2006) Comp. Biochem. Physiol. C , vol.143 , pp. 316-320
    • Dahm, K.C.S.1    Rückert, C.2    Tonial, E.M.3    Bonan, C.D.4
  • 12
    • 0027264923 scopus 로고
    • ATP-a fast neurotransmitter
    • Edwards F.A., and Gibb A.J. ATP-a fast neurotransmitter. FEBS Lett. 325 (1993) 86-89
    • (1993) FEBS Lett. , vol.325 , pp. 86-89
    • Edwards, F.A.1    Gibb, A.J.2
  • 13
    • 4644285299 scopus 로고    scopus 로고
    • Antioxidant effect of vitamin E and selenium on lipid peroxidation, enzyme activities and biochemical parameters in rats exposed to aluminium
    • El-Demerdash F.M. Antioxidant effect of vitamin E and selenium on lipid peroxidation, enzyme activities and biochemical parameters in rats exposed to aluminium. J. Trace Elem. Med. Biol. 18 (2004) 113-121
    • (2004) J. Trace Elem. Med. Biol. , vol.18 , pp. 113-121
    • El-Demerdash, F.M.1
  • 14
    • 1642481207 scopus 로고    scopus 로고
    • The pro-oxidant activity of aluminium
    • Exley C. The pro-oxidant activity of aluminium. Free Radic. Biol. Med. 36 (2004) 380-387
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 380-387
    • Exley, C.1
  • 16
    • 0028859662 scopus 로고
    • Astra Award Lecture. Adenosine, adenosine receptors and the actions of caffeine
    • Fredholm B.B. Astra Award Lecture. Adenosine, adenosine receptors and the actions of caffeine. Pharmacol. Toxicol. 76 (1995) 93-101
    • (1995) Pharmacol. Toxicol. , vol.76 , pp. 93-101
    • Fredholm, B.B.1
  • 18
    • 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
  • 19
    • 0025952271 scopus 로고
    • Pharmacological receptors on blood-platelets
    • Hourani S.M.O., and Cusak N.J. Pharmacological receptors on blood-platelets. Pharmacol. Rev. 43 (1991) 243-298
    • (1991) Pharmacol. Rev. , vol.43 , pp. 243-298
    • Hourani, S.M.O.1    Cusak, N.J.2
  • 20
    • 0030051506 scopus 로고    scopus 로고
    • Altered calcium homeostasis: a possible mechanism of aluminium-induced neurotoxicity
    • Julka D., and Gill K.D. Altered calcium homeostasis: a possible mechanism of aluminium-induced neurotoxicity. Biochim. Biophys. Acta 1315 (1996) 47-54
    • (1996) Biochim. Biophys. Acta , vol.1315 , pp. 47-54
    • Julka, D.1    Gill, K.D.2
  • 21
    • 24344442031 scopus 로고    scopus 로고
    • Acetylcholinesterase activation and enhanced lipid peroxidation after long-term exposure to low levels of aluminium on different mouse brain regions
    • Kaizer R.R., Corrêa M.C., Spanevello R.M., Morsch V.M., Mazzanti C.M., Gonçalves J.F., and Schetinger M.R.C. Acetylcholinesterase activation and enhanced lipid peroxidation after long-term exposure to low levels of aluminium on different mouse brain regions. J. Inorg. Biochem. 99 (2005) 1865-1870
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 1865-1870
    • Kaizer, R.R.1    Corrêa, M.C.2    Spanevello, R.M.3    Morsch, V.M.4    Mazzanti, C.M.5    Gonçalves, J.F.6    Schetinger, M.R.C.7
  • 25
    • 0027453673 scopus 로고
    • Postnatal development of ATPase-ADPase activities in synaptosomal fraction from cerebral cortex of rats
    • Muller J., Rocha J.B.T., Battastini A.M.O., Sarkis J.J.F., and Dias R.D. Postnatal development of ATPase-ADPase activities in synaptosomal fraction from cerebral cortex of rats. Neurochem. Int. 23 (1993) 471-477
    • (1993) Neurochem. Int. , vol.23 , pp. 471-477
    • Muller, J.1    Rocha, J.B.T.2    Battastini, A.M.O.3    Sarkis, J.J.F.4    Dias, R.D.5
  • 26
    • 0021219280 scopus 로고
    • Rapid preparation of synaptosomes from mammalian brain using nontoxic isoosmotic gradient material (Percoll)
    • Nagy A., and Delgado-Escueta A.V. Rapid preparation of synaptosomes from mammalian brain using nontoxic isoosmotic 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
  • 27
    • 0037057966 scopus 로고    scopus 로고
    • Epinephrine- and thrombin-stimulated high-affinity GTPase activity in platelet membranes from patients with psychiatric disorders
    • Odagaki Y., and Koyama T. Epinephrine- and thrombin-stimulated high-affinity GTPase activity in platelet membranes from patients with psychiatric disorders. Psychiat. Res. 112 (2002) 111-119
    • (2002) Psychiat. Res. , vol.112 , pp. 111-119
    • Odagaki, Y.1    Koyama, T.2
  • 29
  • 33
    • 0027322977 scopus 로고
    • Aluminium impacts elements of the phosphoinositide signalling pathway in neuroblastoma cells
    • Shi B., Chou K., and Haug A. Aluminium impacts elements of the phosphoinositide signalling pathway in neuroblastoma cells. Mol. Cell Biochem. 21 (1993) 109-118
    • (1993) Mol. Cell Biochem. , vol.21 , pp. 109-118
    • Shi, B.1    Chou, K.2    Haug, A.3
  • 34
    • 0036779577 scopus 로고    scopus 로고
    • Aluminium accumulation and membrane fluidity alteration in synaptosomes isolated from rat brain cortex following aluminium ingestion: effect of cholesterol
    • Silva V.S., Cordeiro J.M., Matos M.J., Oliveira C.R., and Gonçalves P.P. Aluminium accumulation and membrane fluidity alteration in synaptosomes isolated from rat brain cortex following aluminium ingestion: effect of cholesterol. Neurosci. Res. 44 (2002) 181-193
    • (2002) Neurosci. Res. , vol.44 , pp. 181-193
    • Silva, V.S.1    Cordeiro, J.M.2    Matos, M.J.3    Oliveira, C.R.4    Gonçalves, P.P.5
  • 35
    • 0026771360 scopus 로고
    • Membrane fluidity of platelets and erythrocytes in patients with Alzheimer's disease and the effect of small amounts of aluminium on platelet and erythrocyte membranes
    • Van Rensburg S.J., Carstens M.E., Potocnik F.C., Aucamp A.J., Taljaard J.J., and Koch K.R. Membrane fluidity of platelets and erythrocytes in patients with Alzheimer's disease and the effect of small amounts of aluminium on platelet and erythrocyte membranes. Neurochem. Res. 17 (1992) 825-829
    • (1992) Neurochem. Res. , vol.17 , pp. 825-829
    • Van Rensburg, S.J.1    Carstens, M.E.2    Potocnik, F.C.3    Aucamp, A.J.4    Taljaard, J.J.5    Koch, K.R.6
  • 37
    • 0027082739 scopus 로고
    • Brain aluminium in Alzheimer's disease using an improved GFAAS method
    • Xu N., Majidi V., Markesbery W.R., and Ehmann W.D. Brain aluminium in Alzheimer's disease using an improved GFAAS method. Neurotoxicology 13 (1992) 735-743
    • (1992) Neurotoxicology , vol.13 , pp. 735-743
    • Xu, N.1    Majidi, V.2    Markesbery, W.R.3    Ehmann, W.D.4
  • 38
    • 0035052636 scopus 로고    scopus 로고
    • Aluminium toxicokinetics: na updated minireview
    • Yokel R.A., and McNamara P.J. Aluminium toxicokinetics: na updated minireview. Pharmacol. Toxicol. 88 (2001) 159-167
    • (2001) Pharmacol. Toxicol. , vol.88 , pp. 159-167
    • Yokel, R.A.1    McNamara, P.J.2
  • 39
    • 0037107889 scopus 로고    scopus 로고
    • In vivo and in vitro effects of aluminium on the activity of mouse brain acetylcholinesterase.
    • Zatta P., Ibn-Lkhayat-Idrissi M., Zambenedetti P., Kilyen M., and Kiss T. In vivo and in vitro effects of aluminium on the activity of mouse brain acetylcholinesterase. Brain Res. Bull. 59 (2002) 41-45
    • (2002) Brain Res. Bull. , vol.59 , pp. 41-45
    • Zatta, P.1    Ibn-Lkhayat-Idrissi, M.2    Zambenedetti, P.3    Kilyen, M.4    Kiss, T.5
  • 40
    • 0030221465 scopus 로고    scopus 로고
    • Biochemistry, localization and functional roles of ecto-nucleotidases in the nervous system
    • Zimmermann H. Biochemistry, localization and functional roles of ecto-nucleotidases in the nervous system. Prog. Neurobiol. 49 (1996) 589-618
    • (1996) Prog. Neurobiol. , vol.49 , pp. 589-618
    • Zimmermann, H.1
  • 41
    • 0033152549 scopus 로고    scopus 로고
    • Two novel families of ectonucleotidases: molecular structures, catalytic properties and a search for function
    • Zimmermann H. Two novel families of ectonucleotidases: molecular structures, catalytic properties and a search for function. TiPS 20 (1999) 231-236
    • (1999) TiPS , vol.20 , pp. 231-236
    • Zimmermann, H.1
  • 42
    • 0035033156 scopus 로고    scopus 로고
    • Ectonucleotidases: some recent developments and a note on nomenclature
    • Zimmermann H. Ectonucleotidases: some recent developments and a note on nomenclature. Drug Dev. Res. 52 (2001) 44-56
    • (2001) Drug Dev. Res. , vol.52 , pp. 44-56
    • Zimmermann, H.1
  • 43
    • 0032077198 scopus 로고    scopus 로고
    • New insights into molecular structure and function of ecto-nucleotidases in the nervous system
    • Zimmermann H., Braun N., Kegel B., and Heine P. New insights into molecular structure and function of ecto-nucleotidases in the nervous system. Neurochem. Int. 32 (1998) 421-425
    • (1998) Neurochem. Int. , vol.32 , pp. 421-425
    • Zimmermann, H.1    Braun, N.2    Kegel, B.3    Heine, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.