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Volumn 327, Issue 1-2, 2009, Pages 39-45

The activity of erythrocyte and brain Na+/K+ and Mg2+-ATPases in rats subjected to acute homocysteine and homocysteine thiolactone administration

Author keywords

Brain; Erythrocyte; Homocysteine; Homocysteine thiolactone; Mg2+ ATPase; Na+ K+ ATPase; Rat

Indexed keywords

ANIMALS; BRAIN; CA(2+) MG(2+)-ATPASE; ERYTHROCYTES; HOMOCYSTEINE; MALE; RATS; RATS, WISTAR; SODIUM-POTASSIUM-EXCHANGING ATPASE;

EID: 67349267983     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-009-0040-6     Document Type: Article
Times cited : (46)

References (51)
  • 1
    • 17844378176 scopus 로고    scopus 로고
    • Homocysteine, the bad thiol
    • doi: 10.1002/hep.20708
    • Mato JM, Lu SC (2005) Homocysteine, the bad thiol. Hepatology 41:976-979. doi: 10.1002/hep.20708
    • (2005) Hepatology , vol.41 , pp. 976-979
    • Mato, J.M.1    Lu, S.C.2
  • 2
    • 0034116129 scopus 로고    scopus 로고
    • Plasma total homocysteine and cognitive performance in a volunteer elderly population
    • doi: 10.1111/j.1749-6632.2000.tb06392.x
    • Budge J, Johnston C, Hogervorst E et al (2000) Plasma total homocysteine and cognitive performance in a volunteer elderly population. Ann N Y Acad Sci 903:407-410. doi: 10.1111/j.1749-6632.2000.tb06392.x
    • (2000) Ann N Y Acad Sci , vol.903 , pp. 407-410
    • Budge, J.1    Johnston, C.2    Hogervorst, E.3
  • 3
    • 12244287634 scopus 로고    scopus 로고
    • Homocysteine as a risk factor for cognitive impairment in stroke patients
    • doi: 10.1159/000068481
    • Sachdev PS, Valenzuela M, Brodaty H et al (2003) Homocysteine as a risk factor for cognitive impairment in stroke patients. Dement Geriatr Cogn Disord 15:155-162. doi: 10.1159/000068481
    • (2003) Dement Geriatr Cogn Disord , vol.15 , pp. 155-162
    • Sachdev, P.S.1    Valenzuela, M.2    Brodaty, H.3
  • 6
    • 36549074220 scopus 로고    scopus 로고
    • + -ATPase activity inhibition and memory impairments caused by chronic hyperhomocysteinemia during rat development
    • doi: 10.1016/j.ijdevneu.2007.10.003
    • +-ATPase activity inhibition and memory impairments caused by chronic hyperhomocysteinemia during rat development. Int J Dev Neurosci 25:545-552. doi: 10.1016/ j.ijdevneu.2007.10.003
    • (2007) Int J Dev Neurosci , vol.25 , pp. 545-552
    • Matte, C.1    Scherer, E.B.S.2    Stefanello, F.M.3
  • 8
    • 0034666267 scopus 로고    scopus 로고
    • Homocysteine elicits a DNA damage response in neurons that promotes apoptosis and hypersensitivity to excitotoxicity
    • Kruman II, Culmsee C, Chan SL et al (2000) Homocysteine elicits a DNA damage response in neurons that promotes apoptosis and hypersensitivity to excitotoxicity. J Neurosci 20:6920-6926
    • (2000) J Neurosci , vol.20 , pp. 6920-6926
    • Kruman, I.I.1    Culmsee, C.2    Chan, S.L.3
  • 9
    • 0034092782 scopus 로고    scopus 로고
    • Behavioral and metabolic changes in immature rats during seizures induced by homocysteic acid: The protective effect of NMDA and non-NMDA receptor antagonists
    • doi: 10.1006/exnr.1999.7264
    • Folbergová J, Haugvicová R, Mareš P (2000) Behavioral and metabolic changes in immature rats during seizures induced by homocysteic acid: The protective effect of NMDA and non-NMDA receptor antagonists. Exp Neurol 161:336-345. doi: 10.1006/exnr.1999.7264
    • (2000) Exp Neurol , vol.161 , pp. 336-345
    • Folbergová, J.1    Haugvicová, R.2    Mareš, P.3
  • 10
    • 33646788784 scopus 로고    scopus 로고
    • Pathophysiological consequences of homocysteine excess
    • Jakubowski H (2006) Pathophysiological consequences of homocysteine excess. J Nutr 136:1741S-1749S
    • (2006) J Nutr , vol.136
    • Jakubowski, H.1
  • 12
    • 0028217760 scopus 로고
    • Ions and energy in mammalian brain
    • doi: 10.1016/0301-0082(94)90015-9
    • Erecinska M, Silver IA (1994) Ions and energy in mammalian brain. Prog Neurobiol 43:37-71. doi: 10.1016/0301-0082(94)90015-9
    • (1994) Prog Neurobiol , vol.43 , pp. 37-71
    • Erecinska, M.1    Silver, I.A.2
  • 13
    • 0031758268 scopus 로고    scopus 로고
    • Isozymes of the Na-K-ATPase: Heterogeneity in structure, diversity in function
    • Blanco G, Mercer RW (1998) Isozymes of the Na-K-ATPase: Heterogeneity in structure, diversity in function. Am J Physiol 275:F633-F650
    • (1998) Am J Physiol , vol.275
    • Blanco, G.1    Mercer, R.W.2
  • 14
    • 0002527806 scopus 로고
    • The role of magnesium in cell proliferation and transformation
    • In: Boynton AL, MacKeehan WL, Winitfield JP (eds) Academic Press, New York
    • Sanui H, Rubin H (1982) The role of magnesium in cell proliferation and transformation. In: Boynton AL, MacKeehan WL, Winitfield JP (eds) Ions, cell proliferation and cancer. Academic Press, New York, pp 517-537
    • (1982) Ions, Cell Proliferation and Cancer , pp. 517-537
    • Sanui, H.1    Rubin, H.2
  • 15
    • 0032589572 scopus 로고    scopus 로고
    • +-ATPase in rat brain synaptosomes by EDTA
    • doi: 10.1016/S0378-4274(99)00144-7
    • +-ATPase in rat brain synaptosomes by EDTA. Toxicol Lett 110:95-104. doi: 10.1016/S0378-4274(99)00144-7
    • (1999) Toxicol Lett , vol.110 , pp. 95-104
    • Vasić, V.1    Jovanović, D.2    Krstić, D.3
  • 16
    • 0027523160 scopus 로고
    • Coupling of cellular energy state and ion homeostasis during recovery following brain ischemia
    • doi: 10.1016/0006-8993(93)90367-V
    • Ekholm A, Katsura K, Kristián T, Liu M, Folbergrová J, Siesjö BK (1993) Coupling of cellular energy state and ion homeostasis during recovery following brain ischemia. Brain Res 604:185-191. doi: 10.1016/0006-8993(93)90367-V
    • (1993) Brain Res , vol.604 , pp. 185-191
    • Ekholm, A.1    Katsura, K.2    Kristián, T.3    Liu, M.4    Folbergrová, J.5    Siesjö, B.K.6
  • 18
    • 0027252546 scopus 로고
    • Contributory mechanisms in the causation of neurodegenerative disorders
    • doi: 10.1016/0306-4522(93)90254-D
    • Lees GJ (1993) Contributory mechanisms in the causation of neurodegenerative disorders. Neuroscience 54:287-322. doi: 10.1016/ 0306-4522(93)90254-D
    • (1993) Neuroscience , vol.54 , pp. 287-322
    • Lees, G.J.1
  • 19
    • 0013905002 scopus 로고
    • Effect of cardiazol on sodium-potassium adenosine triphosphatase of the rat brain in vivo
    • doi: 10.1016/0006-8993(66)90134-X
    • Bingami A, Palladini C, Venturini G (1966) Effect of cardiazol on sodium-potassium adenosine triphosphatase of the rat brain in vivo. Brain Res 1:413-414. doi: 10.1016/0006-8993(66)90134-X
    • (1966) Brain Res , vol.1 , pp. 413-414
    • Bingami, A.1    Palladini, C.2    Venturini, G.3
  • 20
    • 0037451890 scopus 로고    scopus 로고
    • Impairment of energy metabolism in hippocampus of rats subjected to chemically-induced hyperhomocysteinaemia
    • Streck EL, Matte C, Vieira PS et al (2003) Impairment of energy metabolism in hippocampus of rats subjected to chemically-induced hyperhomocysteinaemia. Biochim Biophys Acta 1637:187-192
    • (2003) Biochim Biophys Acta , vol.1637 , pp. 187-192
    • Streck, E.L.1    Matte, C.2    Vieira, P.S.3
  • 22
    • 1542373560 scopus 로고    scopus 로고
    • Molecular basis of homocysteine toxicity in humans
    • doi: 10.1007/s00018-003-3204-7
    • Jakubowski H (2004) Molecular basis of homocysteine toxicity in humans. Cell Mol Life Sci 61:470-487. doi: 10.1007/s00018-003-3204-7
    • (2004) Cell Mol Life Sci , vol.61 , pp. 470-487
    • Jakubowski, H.1
  • 23
    • 0001195135 scopus 로고
    • Membrane adenosine triphosphatase as a participant in the active transport of sodium and potassium in the human erythrocyte
    • Post RI, Merit CR, Kosolving CR, Albbright CD (1960) Membrane adenosine triphosphatase as a participant in the active transport of sodium and potassium in the human erythrocyte. J Biol Chem 235:1796-1802
    • (1960) J Biol Chem , vol.235 , pp. 1796-1802
    • Post, R.I.1    Merit, C.R.2    Kosolving, C.R.3    Albbright, C.D.4
  • 25
    • 0017396421 scopus 로고
    • The structure of postsynaptic densities isolated from dog cerebral cortex: I. Overall morphology and protein composition
    • doi: 10.1083/jcb.74.1.181
    • Cohen RS, Blomber F, Berzins K, Siekevitz P (1977) The structure of postsynaptic densities isolated from dog cerebral cortex: I. Overall morphology and protein composition. J Cell Biol 74:181-203. doi: 10.1083/ jcb.74.1.181
    • (1977) J Cell Biol , vol.74 , pp. 181-203
    • Cohen, R.S.1    Blomber, F.2    Berzins, K.3    Siekevitz, P.4
  • 26
    • 0020695007 scopus 로고
    • Steroid binding to synaptic plasma membrane: Differential binding of glucocorticoids and gonadal steroids
    • doi: 10.1016/0022-4731(83)90079-1
    • Towle AC, Sze PY (1983) Steroid binding to synaptic plasma membrane: differential binding of glucocorticoids and gonadal steroids. J Steroid Biochem 18:135-143. doi: 10.1016/0022-4731(83)90079-1
    • (1983) J Steroid Biochem , vol.18 , pp. 135-143
    • Towle, A.C.1    Sze, P.Y.2
  • 27
    • 0028815456 scopus 로고
    • Estradiol binding to synaptosomal plasma membranes of rat brain regions
    • Horvat A, Nikezić G, Martinović JV (1995) Estradiol binding to synaptosomal plasma membranes of rat brain regions. Experientia 51(1):11-15
    • (1995) Experientia , vol.51 , Issue.1 , pp. 11-15
    • Horvat, A.1    Nikezić, G.2    Martinović, J.V.3
  • 29
    • 0036912033 scopus 로고    scopus 로고
    • +-ATPase activity in hippocampus of rats subjected to acute administration of homocysteine is prevented by vitamins E and C treatment
    • doi: 10.1023/A:1021647329937
    • +-ATPase activity in hippocampus of rats subjected to acute administration of homocysteine is prevented by vitamins E and C treatment. Neurochem Res 27:1685-1689. doi: 10.1023/A:1021647329937
    • (2002) Neurochem Res , vol.27 , pp. 1685-1689
    • Wyse, A.T.1    Zugno, A.I.2    Streck, E.L.3
  • 31
    • 0020662493 scopus 로고
    • In vivo elevation of mouse brain S-adenosil-l-homocysteine after treatment with l -homocysteine
    • doi: 10.1111/j.1471-4159.1983.tb08100.x
    • Gharib A, Chabennes B, Sarda N, Pacheco H (1983) In vivo elevation of mouse brain S-adenosil-l-homocysteine after treatment with l-homocysteine. J Neurochem 40:1110-1112. doi: 10.1111/ j.1471-4159.1983.tb08100.x
    • (1983) J Neurochem , vol.40 , pp. 1110-1112
    • Gharib, A.1    Chabennes, B.2    Sarda, N.3    Pacheco, H.4
  • 33
    • 33645783026 scopus 로고    scopus 로고
    • 2+-ATPase activities in subjects with methylenetetrahydrofolate reductase (MTHFR) 677 C → T genotype and moderate hyperhomocysteinemia. The role of L-phenylalanine and L-alanine
    • doi: 10.1515/CCLM.2006.069
    • 2+-ATPase activities in subjects with methylenetetrahydrofolate reductase (MTHFR) 677 C → T genotype and moderate hyperhomocysteinemia. The role of L-phenylalanine and L-alanine. Clin Chem Lab Med 44:423-427. doi: 10.1515/CCLM.2006.069
    • (2006) Clin Chem Lab Med , vol.44 , pp. 423-427
    • Schulpis, K.H.1    Giannoulia-Karantana, A.2    Papaconstantinou, E.D.3    Parthimos, T.4    Tjamouranis, I.5    Tsakiris, S.6
  • 34
    • 38649094855 scopus 로고    scopus 로고
    • Modulations of rabbit erythrocyte ATPase activities induced by in vitro and in vivo exposure to ethanol
    • doi: 10.1007/s11010-007-9618-z
    • Rašić-Marković A, Krstić D, Vujović Z et al (2008) Modulations of rabbit erythrocyte ATPase activities induced by in vitro and in vivo exposure to ethanol. Mol Cell Biochem 308:111-116. doi: 10.1007/s11010-007-9618-z
    • (2008) Mol Cell Biochem , vol.308 , pp. 111-116
    • Rašić-Marković, A.1    Krstić, D.2    Vujović, Z.3
  • 35
    • 0028580746 scopus 로고
    • +-ATPase α subunit gene is expressed in testis
    • doi: 10.1073/pnas.91.26.12952
    • +-ATPase α subunit gene is expressed in testis. Proc Natl Acad Sci USA 91:12952-12956. doi: 10.1073/pnas.91.26.12952
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12952-12956
    • Shamraj, O.I.1    Lingrel, J.B.2
  • 38
    • 0026636168 scopus 로고
    • Na,K-ATPase: Isoform structure, function, and expression
    • Lingrel JB (1992) Na,K-ATPase: Isoform structure, function, and expression. J Bioenerg Biomembr 24:263-270
    • (1992) J Bioenerg Biomembr , vol.24 , pp. 263-270
    • Lingrel, J.B.1
  • 39
    • 0025138388 scopus 로고
    • The adhesion molecule on glia (AMOG) is a homologue of the beta subunit of the Na,K-ATPase
    • doi: 10.1083/jcb.110.1.165
    • Gloor S, Antonicek H, Sweadner KJ, Pagliusi S, Frank R, Moos M, Schachner M (1990) The adhesion molecule on glia (AMOG) is a homologue of the beta subunit of the Na,K-ATPase. J Cell Biol 110:165-174. doi: 10.1083/jcb.110.1.165
    • (1990) J Cell Biol , vol.110 , pp. 165-174
    • Gloor, S.1    Antonicek, H.2    Sweadner, K.J.3    Pagliusi, S.4    Frank, R.5    Moos, M.6    Schachner, M.7
  • 40
    • 0025734417 scopus 로고
    • + -ATPase alpha- and beta-subunit isoforms within the rat central nervous system
    • doi: 10.1073/pnas.88.16.7425
    • +-ATPase alpha- and beta-subunit isoforms within the rat central nervous system. Proc Natl Acad Sci USA 88:7425-7429. doi: 10.1073/pnas.88.16.7425
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7425-7429
    • Watts, A.G.1    Sanchez-Watts, G.2    Emanuel, J.R.3    Levenson, R.4
  • 41
    • 34250900920 scopus 로고    scopus 로고
    • +-ATPase isoforms: Different hypothalamus and mesencephalon response to acute desipramine treatment
    • doi: 10.1016/j.lfs.2007.05.011
    • +-ATPase isoforms: Different hypothalamus and mesencephalon response to acute desipramine treatment. Life Sci 81:228-233. doi: 10.1016/j.lfs.2007.05.011
    • (2007) Life Sci , vol.81 , pp. 228-233
    • Viola, M.S.1    Rodríguez de Lores Arnaiz, G.2
  • 42
    • 0028910630 scopus 로고
    • Modulation of ion gradients and glutamate release in cultured cerebellar granule cells by oubain
    • Cousin MA, Nicholls DG, Pocock JM (1995) Modulation of ion gradients and glutamate release in cultured cerebellar granule cells by oubain. J Neurochem 64:2097-2104
    • (1995) J Neurochem , vol.64 , pp. 2097-2104
    • Cousin, M.A.1    Nicholls, D.G.2    Pocock, J.M.3
  • 43
    • 0028306042 scopus 로고
    • Brain lesions induced by specific and non-specific inhibitors of sodium-potassium ATPase
    • doi: 10.1016/0006-8993(94)91068-5
    • Lees GJ, Leong W (1994) Brain lesions induced by specific and non-specific inhibitors of sodium-potassium ATPase. Brain Res 649:225-233. doi: 10.1016/0006-8993(94)91068-5
    • (1994) Brain Res , vol.649 , pp. 225-233
    • Lees, G.J.1    Leong, W.2
  • 44
    • 0036099882 scopus 로고    scopus 로고
    • + -ATPase activity caused by homocysteine
    • doi: 10.1016/S0736-5748(02)00043-6
    • +-ATPase activity caused by homocysteine. Int J Dev Neurosci 20:77-81. doi: 10.1016/ S0736-5748(02)00043-6
    • (2002) Int J Dev Neurosci , vol.20 , pp. 77-81
    • Streck, E.L.1    Zugno, A.I.2    Tagliari, B.3
  • 45
    • 0018765199 scopus 로고
    • Presynaptic modulation of neurochemical transmission
    • doi: 10.1016/0301-0082(79)90011-X
    • Vizi ES (1979) Presynaptic modulation of neurochemical transmission. Prog Neurobiol 12:181-290. doi: 10.1016/0301-0082(79)90011-X
    • (1979) Prog Neurobiol , vol.12 , pp. 181-290
    • Vizi, E.S.1
  • 47
    • 0038509956 scopus 로고    scopus 로고
    • In vitro effect of homocysteine on some parameters of oxidative stress in rat hippocampus
    • doi: 10.1023/A:1023815119931
    • Streck EL, Vieira PS, Clovis MD et al (2003) In vitro effect of homocysteine on some parameters of oxidative stress in rat hippocampus. Metab Brain Dis 18:147-154. doi: 10.1023/A:1023815119931
    • (2003) Metab Brain Dis , vol.18 , pp. 147-154
    • Streck, E.L.1    Vieira, P.S.2    Clovis, M.D.3
  • 48
    • 0032797368 scopus 로고    scopus 로고
    • The effect of cysteine on the auto-oxidation of homocysteine
    • doi: 10.1016/S0891-5849(99)00029-5
    • Hogg N (1999) The effect of cysteine on the auto-oxidation of homocysteine. Free Radic Biol Med 27:28-33. doi: 10.1016/ S0891-5849(99)00029-5
    • (1999) Free Radic Biol Med , vol.27 , pp. 28-33
    • Hogg, N.1
  • 49
    • 0028609667 scopus 로고
    • NMDA and not non-NMDA receptor antagonists are protective against seizures induced by homocysteine in neonatal rats
    • doi: 10.1006/exnr.1994.1213
    • Folbergrova J (1994) NMDA and not non-NMDA receptor antagonists are protective against seizures induced by homocysteine in neonatal rats. Exp Neurol 130:344-350. doi: 10.1006/exnr.1994.1213
    • (1994) Exp Neurol , vol.130 , pp. 344-350
    • Folbergrova, J.1
  • 50
    • 0029035707 scopus 로고
    • Toxicity, biodistribution and radioprotective capacity of L-homocysteine thiolactone in CNS tissues and tumors in rodents: Comparison with prior results with phosphorothioates
    • doi: 10.1016/0167-8140(95)01543-P
    • Spence AM, Rasey JS, Dwyer-Hansen L et al (1995) Toxicity, biodistribution and radioprotective capacity of L-homocysteine thiolactone in CNS tissues and tumors in rodents: Comparison with prior results with phosphorothioates. Radiother Oncol 35:216-226. doi: 10.1016/ 0167-8140(95)01543-P
    • (1995) Radiother Oncol , vol.35 , pp. 216-226
    • Spence, A.M.1    Rasey, J.S.2    Dwyer-Hansen, L.3
  • 51
    • 0014939901 scopus 로고
    • Brain adenosine triphosphate: Decreased concentration precedes convulsions
    • doi: 10.1126/science.169.3941.206
    • Sanders AP, Kramer RS, Woodhall B, Currie WD (1970) Brain adenosine triphosphate: Decreased concentration precedes convulsions. Science 169:206-208. doi: 10.1126/science.169.3941.206
    • (1970) Science , vol.169 , pp. 206-208
    • Sanders, A.P.1    Kramer, R.S.2    Woodhall, B.3    Currie, W.D.4


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