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Volumn 82, Issue 1, 1997, Pages 161-170

Reduction of tyrosine kinase activity and protein tyrosine dephosphorylation by anoxic stimulation in vitro

Author keywords

Cerebral ischemia; Excitatory amino acid receptors; N methyl D aspartate receptor subunits; Protein tyrosine kinase; Protein tyrosine phosphatase; Protein tyrosine phosphorylation

Indexed keywords

2 AMINO 5 PHOSPHONOVALERIC ACID; 6,7 DINITRO 2,3 QUINOXALINEDIONE; CALCIUM; DEPHOSTATIN; EGTAZIC ACID; ETHYLENE GLYCOL 1,2 BIS(2 AMINOPHENYL) ETHER N,N,N',N' TETRAACETIC ACID; GLUTAMATE RECEPTOR ANTAGONIST; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PHOSPHOSERINE; PHOSPHOTHREONINE; PHOSPHOTYROSINE; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE INHIBITOR; TYROSINE; UNCLASSIFIED DRUG;

EID: 0030921159     PISSN: 03064522     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0306-4522(97)00286-8     Document Type: Article
Times cited : (20)

References (54)
  • 1
    • 0029118793 scopus 로고
    • Tyrosine phosphorylation in a model of ischemia using the rat hippocampal slice: Specific, long-term decrease in the tyrosine phosphorylation of the postsynaptic glycoprotein PSD-GP180
    • Au K. N., Gurd J. W. Tyrosine phosphorylation in a model of ischemia using the rat hippocampal slice: specific, long-term decrease in the tyrosine phosphorylation of the postsynaptic glycoprotein PSD-GP180. J. Neurochem. 65:1995;1834-1841.
    • (1995) J. Neurochem. , vol.65 , pp. 1834-1841
    • Au, K.N.1    Gurd, J.W.2
  • 2
    • 0027379946 scopus 로고
    • Postischaemic changes in protein synthesis in the rat brain: Effect of hypothermia
    • Bergstedt K., Hu B. R., Wieloch T. Postischaemic changes in protein synthesis in the rat brain: effect of hypothermia. Expl Brain Res. 95:1993;91-99.
    • (1993) Expl Brain Res. , vol.95 , pp. 91-99
    • Bergstedt, K.1    Hu, B.R.2    Wieloch, T.3
  • 4
    • 0026730122 scopus 로고
    • Tyrosine phosphorylation of microtubule-associated protein kinase after transient ischemia in the gerbil brain
    • Campos-Gonzalez R., Kindy M. S. Tyrosine phosphorylation of microtubule-associated protein kinase after transient ischemia in the gerbil brain. J. Neurochem. 59:1992;1955-1958.
    • (1992) J. Neurochem. , vol.59 , pp. 1955-1958
    • Campos-Gonzalez, R.1    Kindy, M.S.2
  • 5
    • 0027160239 scopus 로고
    • Tyrosine kinase-dependent selection of transmitter responses induced by neuronal contact
    • Catarsi S., Drapeau P. Tyrosine kinase-dependent selection of transmitter responses induced by neuronal contact. Nature. 363:1993;353-355.
    • (1993) Nature , vol.363 , pp. 353-355
    • Catarsi, S.1    Drapeau, P.2
  • 6
    • 0029890005 scopus 로고    scopus 로고
    • Protein tyrosine kinase-mediated potentiation of currents from cloned NMDA receptors
    • Chen C., Leonard J. P. Protein tyrosine kinase-mediated potentiation of currents from cloned NMDA receptors. J. Neurochem. 67:1996;194-200.
    • (1996) J. Neurochem. , vol.67 , pp. 194-200
    • Chen, C.1    Leonard, J.P.2
  • 7
    • 0026612694 scopus 로고
    • A synthetic peptide derived from p34cdc2 is a specific and efficient substrate of src-family tyrosine kinases
    • Cheng H. C., Nishio H., Hatase O., Ralph S., Wang J. H. A synthetic peptide derived from p34cdc2 is a specific and efficient substrate of src-family tyrosine kinases. J. biol. Chem. 267:1992;9248-9256.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9248-9256
    • Cheng, H.C.1    Nishio, H.2    Hatase, O.3    Ralph, S.4    Wang, J.H.5
  • 8
    • 0028016077 scopus 로고
    • Glutamate receptors and the induction of excitotoxic neuronal death [Review]
    • Choi D. W. Glutamate receptors and the induction of excitotoxic neuronal death [Review]. Prog. Brain Res. 100:1994;47-51.
    • (1994) Prog. Brain Res. , vol.100 , pp. 47-51
    • Choi, D.W.1
  • 10
    • 0023680002 scopus 로고
    • Synaptic protein tyrosine kinase: Partial characterization and identification of endogenous substrates
    • Ellis P. D., Bissoon N., Gurd J. W. Synaptic protein tyrosine kinase: partial characterization and identification of endogenous substrates. J. Neurochem. 51:1988;611-620.
    • (1988) J. Neurochem. , vol.51 , pp. 611-620
    • Ellis, P.D.1    Bissoon, N.2    Gurd, J.W.3
  • 11
    • 0026324171 scopus 로고
    • Protein tyrosine phosphatases: A diverse family of intracellular and transmembrane enzymes
    • Fischer E. H., Charbonneau H., Tonks N. K. Protein tyrosine phosphatases: a diverse family of intracellular and transmembrane enzymes. Science. 253:1991;401-406.
    • (1991) Science , vol.253 , pp. 401-406
    • Fischer, E.H.1    Charbonneau, H.2    Tonks, N.K.3
  • 12
    • 0023425239 scopus 로고
    • Systemic administration of MK-801 protects against ischemia-induced hippocampal neurodegeneration in the gerbil
    • Gill R., Foster A. C., Woodruff G. N. Systemic administration of MK-801 protects against ischemia-induced hippocampal neurodegeneration in the gerbil. J. Neurosci. 7:1987;3343-3349.
    • (1987) J. Neurosci. , vol.7 , pp. 3343-3349
    • Gill, R.1    Foster, A.C.2    Woodruff, G.N.3
  • 13
    • 0026506360 scopus 로고
    • Stimulation of protein-tyrosine phosphorylation in rat striatum after lesion of dopamine neurons or chronic neuroleptic treatment
    • Girault J.-A., Siciliano J. C., Robel L., Herve D. Stimulation of protein-tyrosine phosphorylation in rat striatum after lesion of dopamine neurons or chronic neuroleptic treatment. Proc. natn. Acad. Sci. U.S.A. 89:1992;2769-2773.
    • (1992) Proc. Natn. Acad. Sci. U.S.A. , vol.89 , pp. 2769-2773
    • Girault, J.-A.1    Siciliano, J.C.2    Robel, L.3    Herve, D.4
  • 14
    • 0027092647 scopus 로고
    • Impaired long-term potentiation, spatial learning and hippocampal development in fyn mutant mice
    • Grant S. G. N., O'Dell T. J., Karl K. A., Stein P. L., Soriano P., Kandel E. R. Impaired long-term potentiation, spatial learning and hippocampal development in fyn mutant mice. Science. 258:1992;1903-1910.
    • (1992) Science , vol.258 , pp. 1903-1910
    • Grant, S.G.N.1    O'Dell, T.J.2    Karl, K.A.3    Stein, P.L.4    Soriano, P.5    Kandel, E.R.6
  • 15
    • 0023922799 scopus 로고
    • Protein tyrosine kinase activity and its endogenous substrates in rat brain: A subcellular and regional survey
    • Hirano A. A., Greengard P., Huganir R. L. Protein tyrosine kinase activity and its endogenous substrates in rat brain: a subcellular and regional survey. J. Neurochem. 50:1988;1447-1455.
    • (1988) J. Neurochem. , vol.50 , pp. 1447-1455
    • Hirano, A.A.1    Greengard, P.2    Huganir, R.L.3
  • 17
    • 0028353865 scopus 로고
    • Tyrosine phosphorylation and activation of mitogen-activated protein kinase in the rat brain following transient cerebral ischemia
    • Hu B. R., Wieloch T. Tyrosine phosphorylation and activation of mitogen-activated protein kinase in the rat brain following transient cerebral ischemia. J. Neurochem. 62:1994;1357-1367.
    • (1994) J. Neurochem. , vol.62 , pp. 1357-1367
    • Hu, B.R.1    Wieloch, T.2
  • 18
    • 0026336662 scopus 로고
    • Protein kinase classification
    • Hunter T. Protein kinase classification. Meth. Enzym. 200:1991;3-37.
    • (1991) Meth. Enzym. , vol.200 , pp. 3-37
    • Hunter, T.1
  • 20
    • 0027373866 scopus 로고
    • Dephostatin, a novel protein tyrosine phosphatase inhibitor produced by Streptomyces. I. Taxonomy, isolation, and characterization [published erratum appears in J. Antibiot. (Tokyo) 1994 Feb; 47(2):C-1]
    • Imoto M., Kakeya H., Sawa T., Hayashi C., Hamada M., Takeuchi T., Umezawa K. Dephostatin, a novel protein tyrosine phosphatase inhibitor produced by Streptomyces. I. Taxonomy, isolation, and characterization [published erratum appears in J. Antibiot. (Tokyo) 1994 Feb; 47(2):C-1]. J. Antibiot. 46:1993;1342-1346.
    • (1993) J. Antibiot. , vol.46 , pp. 1342-1346
    • Imoto, M.1    Kakeya, H.2    Sawa, T.3    Hayashi, C.4    Hamada, M.5    Takeuchi, T.6    Umezawa, K.7
  • 22
    • 0028988240 scopus 로고
    • Long-lasting neurotrophin-induced enhancement of synaptic transmission in the adult hippocampus
    • Kang H., Schuman E. M. Long-lasting neurotrophin-induced enhancement of synaptic transmission in the adult hippocampus. Science. 267:1995;1658-1662.
    • (1995) Science , vol.267 , pp. 1658-1662
    • Kang, H.1    Schuman, E.M.2
  • 23
    • 0027223296 scopus 로고
    • Inhibition of tyrosine phosphorylation prevents delayed neuronal death following cerebral ischemia
    • Kindy M. S. Inhibition of tyrosine phosphorylation prevents delayed neuronal death following cerebral ischemia. J. cerebr. Blood Flow Metab. 13:1993;372-377.
    • (1993) J. Cerebr. Blood Flow Metab. , vol.13 , pp. 372-377
    • Kindy, M.S.1
  • 24
    • 0020051129 scopus 로고
    • Delayed neuronal death in the gerbil hippocampus following ischemia
    • Kirino T. Delayed neuronal death in the gerbil hippocampus following ischemia. Brain Res. 239:1982;57-69.
    • (1982) Brain Res. , vol.239 , pp. 57-69
    • Kirino, T.1
  • 25
    • 0024851534 scopus 로고
    • TrkB, a novel tyrosine protein kinase receptor expressed during mouse neural development
    • Klein R., Parada L. F., Coulier F., Barbacid M. TrkB, a novel tyrosine protein kinase receptor expressed during mouse neural development. Eur. molec. Biol. Org. J. 8:1989;3701-3709.
    • (1989) Eur. Molec. Biol. Org. J. , vol.8 , pp. 3701-3709
    • Klein, R.1    Parada, L.F.2    Coulier, F.3    Barbacid, M.4
  • 26
    • 0029887725 scopus 로고    scopus 로고
    • Subtype-specific regulation of recombinant NMDA receptor-channels by protein tyrosine kinases of the src family
    • Köhr G., Seeburg P. H. Subtype-specific regulation of recombinant NMDA receptor-channels by protein tyrosine kinases of the src family. J. Physiol. 492:1996;445-452.
    • (1996) J. Physiol. , vol.492 , pp. 445-452
    • Köhr, G.1    Seeburg, P.H.2
  • 27
    • 0029093990 scopus 로고
    • Differential tyrosine phosphorylation of N-methyl-D-aspartate receptor subunits
    • Lau L. F., Huganir R. L. Differential tyrosine phosphorylation of N-methyl-D-aspartate receptor subunits. J. biol. Chem. 270:1995;20036-20041.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20036-20041
    • Lau, L.F.1    Huganir, R.L.2
  • 29
    • 0010297008 scopus 로고
    • Protein tyrosine kinases (TKs) in postsynaptic density (PSD) and phosphorylation of the NMDAR1 (Abstract)
    • Lin S. Y., Wu K., Kim T. W., Huang Y., Xu J. L., Suen P. C., Black I. B. Protein tyrosine kinases (TKs) in postsynaptic density (PSD) and phosphorylation of the NMDAR1 (Abstract). Soc. Neurosci. Abstr. 19(2):1993;1358.
    • (1993) Soc. Neurosci. Abstr. , vol.19 , Issue.2 , pp. 1358
    • Lin, S.Y.1    Wu, K.2    Kim, T.W.3    Huang, Y.4    Xu, J.L.5    Suen, P.C.6    Black, I.B.7
  • 31
    • 0030002941 scopus 로고    scopus 로고
    • src activation and translocation to cytoskeleton in fetal lung cells
    • src activation and translocation to cytoskeleton in fetal lung cells. J. biol. Chem. 271:1996;7066-7071.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7066-7071
    • Liu, M.1    Qiu, Y.2    Tanswell, A.K.3    Post, M.4
  • 32
    • 0023125256 scopus 로고
    • The physiology of excitatory amino acids in the vertebrate central nervous system
    • Mayer M. L., Westbrook G. L. The physiology of excitatory amino acids in the vertebrate central nervous system. Prog. Neurobiol. 28:1987;197-276.
    • (1987) Prog. Neurobiol. , vol.28 , pp. 197-276
    • Mayer, M.L.1    Westbrook, G.L.2
  • 33
    • 0029556408 scopus 로고
    • Tyrosine phosphorylation of NMDA receptor in rat striatum: Effects of 6-OH-dopamine lesions
    • Menegoz M., Lau L. F., Hervé D., Huganir R. L., Girault J. A. Tyrosine phosphorylation of NMDA receptor in rat striatum: effects of 6-OH-dopamine lesions. NeuroReport. 7:1995;125-128.
    • (1995) NeuroReport , vol.7 , pp. 125-128
    • Menegoz, M.1    Lau, L.F.2    Hervé, D.3    Huganir, R.L.4    Girault, J.A.5
  • 35
    • 0028343648 scopus 로고
    • Developmental and regional expression in the rat brain and functional properties of four NMDA receptors
    • Monyer H., Burnashev N., Laurie D. J., Sakmann B., Seeburg P. H. Developmental and regional expression in the rat brain and functional properties of four NMDA receptors. Neuron. 12:1994;529-540.
    • (1994) Neuron , vol.12 , pp. 529-540
    • Monyer, H.1    Burnashev, N.2    Laurie, D.J.3    Sakmann, B.4    Seeburg, P.H.5
  • 36
    • 0000927212 scopus 로고
    • The major tyrosine-phosphorylated protein in the postsynaptic density fraction is N-methyl-D-aspartate receptor subunit 2B
    • Moon I. S., Apperson M. L., Kennedy M. B. The major tyrosine-phosphorylated protein in the postsynaptic density fraction is N-methyl-D-aspartate receptor subunit 2B. Proc. natn. Acad. Sci. U.S.A. 91:1994;3954-3958.
    • (1994) Proc. Natn. Acad. Sci. U.S.A. , vol.91 , pp. 3954-3958
    • Moon, I.S.1    Apperson, M.L.2    Kennedy, M.B.3
  • 37
    • 0025995324 scopus 로고
    • Long-term potentiation in the hippocampus is blocked by tyrosine kinase inhibitors
    • O'Dell T. J., Kandel E. R., Grant S. G. Long-term potentiation in the hippocampus is blocked by tyrosine kinase inhibitors. Nature. 353:1991;558-560.
    • (1991) Nature , vol.353 , pp. 558-560
    • O'Dell, T.J.1    Kandel, E.R.2    Grant, S.G.3
  • 39
    • 0028087773 scopus 로고
    • The NMDA receptor subunits NR2A and NR2B show histological and ultrastructural localization patterns similar to those of NR1
    • Petralia R. S., Wang Y. X., Wenthold R. J. The NMDA receptor subunits NR2A and NR2B show histological and ultrastructural localization patterns similar to those of NR1. J. Neurosci. 14:1994;6102-6120.
    • (1994) J. Neurosci. , vol.14 , pp. 6102-6120
    • Petralia, R.S.1    Wang, Y.X.2    Wenthold, R.J.3
  • 40
    • 0028157362 scopus 로고
    • Light and electron microscope distribution of the NMDA receptor subunit NMDAR1 in the rat nervous system using a selective anti-peptide antibody
    • Petralia R. S., Yokotani N., Wenthold R. J. Light and electron microscope distribution of the NMDA receptor subunit NMDAR1 in the rat nervous system using a selective anti-peptide antibody. J. Neurosci. 14:1994;667-696.
    • (1994) J. Neurosci. , vol.14 , pp. 667-696
    • Petralia, R.S.1    Yokotani, N.2    Wenthold, R.J.3
  • 41
    • 0023219060 scopus 로고
    • Excitotoxicity and the NMDA receptor
    • Rothman S. M., Olney J. W. Excitotoxicity and the NMDA receptor. Trends Neurosci. 7:1987;299-302.
    • (1987) Trends Neurosci. , vol.7 , pp. 299-302
    • Rothman, S.M.1    Olney, J.W.2
  • 42
    • 0028219211 scopus 로고
    • Changing subunit composition of heteromeric NMDA receptors during development of rat cortex
    • Sheng M., Cummings J., Roldan L. A., Jan Y. N., Jan L. Y. Changing subunit composition of heteromeric NMDA receptors during development of rat cortex. Nature. 368:1994;144-147.
    • (1994) Nature , vol.368 , pp. 144-147
    • Sheng, M.1    Cummings, J.2    Roldan, L.A.3    Jan, Y.N.4    Jan, L.Y.5
  • 43
    • 0027972713 scopus 로고
    • Depolarization and neurotransmitters increase neuronal protein tyrosine phosphorylation
    • Siciliano J. C., Gelman M., Girault J. A. Depolarization and neurotransmitters increase neuronal protein tyrosine phosphorylation. J. Neurochem. 62:1994;950-959.
    • (1994) J. Neurochem. , vol.62 , pp. 950-959
    • Siciliano, J.C.1    Gelman, M.2    Girault, J.A.3
  • 45
    • 0021743001 scopus 로고
    • Blockade of N-methyl-D-aspartate receptors may protect against ischemic damage in the brain
    • Simon R. P., Swan J. H., Griffiths T., Meldrum B. S. Blockade of N-methyl-D-aspartate receptors may protect against ischemic damage in the brain. Science. 226:1984;850-852.
    • (1984) Science , vol.226 , pp. 850-852
    • Simon, R.P.1    Swan, J.H.2    Griffiths, T.3    Meldrum, B.S.4
  • 46
    • 0023895343 scopus 로고
    • Differential developmental expression of cellular yes and cellular src proteins in cerebellum
    • Sudol M., Alvarez-Buylla A., Hanafusa H. Differential developmental expression of cellular yes and cellular src proteins in cerebellum. Oncogene Res. 2:1988;345-355.
    • (1988) Oncogene Res. , vol.2 , pp. 345-355
    • Sudol, M.1    Alvarez-Buylla, A.2    Hanafusa, H.3
  • 47
    • 0025469313 scopus 로고
    • Immunocytochemical localization of the neuron-specific form of the c-src gene product, pp60c-src(+), in rat brain
    • Sugrue M. M., Brugge J. S., Marshak D. R., Greengard P., Gustafson E. L. Immunocytochemical localization of the neuron-specific form of the c-src gene product, pp60c-src(+), in rat brain. J. Neurosci. 10:1990;2513-2527.
    • (1990) J. Neurosci. , vol.10 , pp. 2513-2527
    • Sugrue, M.M.1    Brugge, J.S.2    Marshak, D.R.3    Greengard, P.4    Gustafson, E.L.5
  • 48
    • 0028889715 scopus 로고
    • NMDA receptor subunits ∈1 (NR2A) and ∈2 (NR2B) are substrates for Fyn in the postsynaptic density fraction isolated from the rat brain
    • Suzuki T., Okumura-Noji K. NMDA receptor subunits ∈1 (NR2A) and ∈2 (NR2B) are substrates for Fyn in the postsynaptic density fraction isolated from the rat brain. Biochem. biophys. Res. Commun. 216:1995;582-588.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 582-588
    • Suzuki, T.1    Okumura-Noji, K.2
  • 49
    • 0028024908 scopus 로고
    • Triggering and execution of neuronal death in brain ischaemia: Two phases of glutamate release by different mechanisms
    • Szatkowski M., Attwell D. Triggering and execution of neuronal death in brain ischaemia: two phases of glutamate release by different mechanisms. Trends Neurosci. 17:1994;359-365.
    • (1994) Trends Neurosci. , vol.17 , pp. 359-365
    • Szatkowski, M.1    Attwell, D.2
  • 50
    • 0024560780 scopus 로고
    • Influence of epidermal growth factor on long-term potentiation in the hippocampal slice
    • Terlau H., Seifert W. Influence of epidermal growth factor on long-term potentiation in the hippocampal slice. Brain Res. 484:1989;352-356.
    • (1989) Brain Res. , vol.484 , pp. 352-356
    • Terlau, H.1    Seifert, W.2
  • 51
    • 0028360327 scopus 로고
    • Regulation of NMDA receptors by protein-tyrosine kinases and phosphatases
    • Wang Y. T., Salter M. W. Regulation of NMDA receptors by protein-tyrosine kinases and phosphatases. Nature. 369:1994;233-235.
    • (1994) Nature , vol.369 , pp. 233-235
    • Wang, Y.T.1    Salter, M.W.2
  • 52
    • 0029919507 scopus 로고    scopus 로고
    • 2+-independent reduction of NMDA receptor-mediated currents by protein tyrosine phosphorylation
    • 2+-independent reduction of NMDA receptor-mediated currents by protein tyrosine phosphorylation. Proc. natn. Acad. Sci. U.S.A. 93:1996;1721-1725.
    • (1996) Proc. Natn. Acad. Sci. U.S.A. , vol.93 , pp. 1721-1725
    • Wang, Y.T.1    Yu, X.-M.2    Salter, M.W.3
  • 53
    • 0031053363 scopus 로고    scopus 로고
    • NMDA channel regulation by channel-associated protein tyrosine kinase src
    • Yu X.-M., Askalan R., Keil II G. J., Salter M. W. NMDA channel regulation by channel-associated protein tyrosine kinase src. Science. 275:1996;674-678.
    • (1996) Science , vol.275 , pp. 674-678
    • Yu, X.-M.1    Askalan, R.2    Keil G.J. II3    Salter, M.W.4
  • 54
    • 0027464656 scopus 로고
    • Purification and characterization of a protein tyrosine phosphatase containing SH2 domains
    • Zhao Z., Bouchard P., Diltz C. D., Shen S. H., Fischer E. H. Purification and characterization of a protein tyrosine phosphatase containing SH2 domains. J. biol. Chem. 268:1993;2816-2820.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2816-2820
    • Zhao, Z.1    Bouchard, P.2    Diltz, C.D.3    Shen, S.H.4    Fischer, E.H.5


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