메뉴 건너뛰기




Volumn 42, Issue 2, 2003, Pages 179-188

Genistein inhibits Ca2+ influx and glutamate release from hippocampal synaptosomes: Putative non-specific effects

Author keywords

Ca2+ influx; Glutamate release; Hippocampal synaptosomes; Tyrosine phosphorylation

Indexed keywords

CALCIUM CHANNEL BLOCKING AGENT; CALCIUM ION; DEPHOSTATIN; GENISTEIN; GLUTAMIC ACID; HERBIMYCIN A; ISOFLAVONE DERIVATIVE; LAVENDUSTIN A; NITRENDIPINE; OMEGA CONOTOXIN GVIA; OMEGA CONOTOXIN IVA; POTASSIUM CHLORIDE; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR; PROTEIN TYROSINE PHOSPHATASE INHIBITOR; UNCLASSIFIED DRUG; VANADATE SODIUM; CALCIUM; ENZYME INHIBITOR; OMEGA AGATOXIN IVA; PROTEIN TYROSINE PHOSPHATASE;

EID: 0037207465     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0197-0186(02)00071-2     Document Type: Article
Times cited : (11)

References (61)
  • 2
    • 0026075305 scopus 로고
    • Use and specificity of genistein as inhibitor of protein-tyrosine kinases
    • Akiwama T., Ogawara H. Use and specificity of genistein as inhibitor of protein-tyrosine kinases. Methods Enzymol. 201:1991;362-370.
    • (1991) Methods Enzymol. , vol.201 , pp. 362-370
    • Akiwama, T.1    Ogawara, H.2
  • 4
    • 0029968294 scopus 로고    scopus 로고
    • Epidermal growth factor-mediated inhibition of neurotransmitter glutamate release from rat forebrain synaptosomes
    • Barrie A., Chieregatti E., Miloso M., Benfenati F., Valtorta F. Epidermal growth factor-mediated inhibition of neurotransmitter glutamate release from rat forebrain synaptosomes. Mol. Pharmacol. 49:1996;399-403.
    • (1996) Mol. Pharmacol. , vol.49 , pp. 399-403
    • Barrie, A.1    Chieregatti, E.2    Miloso, M.3    Benfenati, F.4    Valtorta, F.5
  • 5
    • 0029929415 scopus 로고    scopus 로고
    • Protein-tyrosine kinases activate while protein-tyrosine phosphatases inhibit L-type calcium channel activity in pituitary GH3 cells
    • Cataldi M., Taglialatela M., Guerriero S., Amoroso S., Lombardi G., di Renzo G., Annunziato L. Protein-tyrosine kinases activate while protein-tyrosine phosphatases inhibit L-type calcium channel activity in pituitary GH3 cells. J. Biol. Chem. 271:1996;1039-1044.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1039-1044
    • Cataldi, M.1    Taglialatela, M.2    Guerriero, S.3    Amoroso, S.4    Lombardi, G.5    Di Renzo, G.6    Annunziato, L.7
  • 6
    • 0030601087 scopus 로고    scopus 로고
    • Genistein directly inhibits L-type calcium currents but potentiates cAMP-dependent chloride currents in cardiomyocytes
    • Chiang C.-E., Chen S.-A., Chang M.-S., Lin C.-I., Luk H.-N. Genistein directly inhibits L-type calcium currents but potentiates cAMP-dependent chloride currents in cardiomyocytes. Biochem. Biophys. Res. Commun. 223:1996;598-603.
    • (1996) Biochem. Biophys. Res. Commun. , vol.223 , pp. 598-603
    • Chiang, C.-E.1    Chen, S.-A.2    Chang, M.-S.3    Lin, C.-I.4    Luk, H.-N.5
  • 7
    • 0030020444 scopus 로고    scopus 로고
    • Tyrosine kinases are required for catecholamine secretion and mitogen-activated protein kinase activation in bovine adrenal chromaffin cells
    • Cox M.E., Ely C.M., Catling A.D., Weber M.J., Parsons S.J. Tyrosine kinases are required for catecholamine secretion and mitogen-activated protein kinase activation in bovine adrenal chromaffin cells. J. Neurochem. 66:1996;1103-1112.
    • (1996) J. Neurochem. , vol.66 , pp. 1103-1112
    • Cox, M.E.1    Ely, C.M.2    Catling, A.D.3    Weber, M.J.4    Parsons, S.J.5
  • 9
    • 0023868787 scopus 로고
    • A rapid Percoll gradient procedure for isolation of synaptosomes directly from an S1 fraction: Homogeneity and morphology of subcellular fractions
    • Dunkley P.R., Heath J.W., Harrison S.M., Jarvie P.E., Glenfield P.J., Rostas J.A.P. A rapid Percoll gradient procedure for isolation of synaptosomes directly from an S1 fraction: homogeneity and morphology of subcellular fractions. Brain Res. 441:1988;59-71.
    • (1988) Brain Res. , vol.441 , pp. 59-71
    • Dunkley, P.R.1    Heath, J.W.2    Harrison, S.M.3    Jarvie, P.E.4    Glenfield, P.J.5    Rostas, J.A.P.6
  • 10
    • 0031593392 scopus 로고    scopus 로고
    • A receptor function by tyrosine kinase inhibitors and their inactive analogues
    • A receptor function by tyrosine kinase inhibitors and their inactive analogues. Mol. Cell. Neurosci. 12:1998;300-310.
    • (1998) Mol. Cell. Neurosci. , vol.12 , pp. 300-310
    • Dunne, E.L.1    Moss, S.J.2    Smart, T.G.3
  • 11
    • 0023680002 scopus 로고    scopus 로고
    • Synaptic protein-tyrosine kinase: Partial characterization and identification of endogenous substrates
    • Ellis P.D., Bisson N., Gurd J.W. Synaptic protein-tyrosine kinase: partial characterization and identification of endogenous substrates. J. Neurochem. 51:2000;611-620.
    • (2000) J. Neurochem. , vol.51 , pp. 611-620
    • Ellis, P.D.1    Bisson, N.2    Gurd, J.W.3
  • 13
  • 14
    • 0030847355 scopus 로고    scopus 로고
    • Protein-tyrosine phosphorylation - Implication for synaptic function
    • Gurd J.W. Protein-tyrosine phosphorylation - implication for synaptic function. Neurochem. Int. 31:1997;635-649.
    • (1997) Neurochem. Int. , vol.31 , pp. 635-649
    • Gurd, J.W.1
  • 15
    • 0031972834 scopus 로고    scopus 로고
    • Growth factor receptor tyrosine kinases acutely regulate neuronal sodium channels through the src signaling pathway
    • Hilborn M.D., Vaillancourt R.R., Rane S.G. Growth factor receptor tyrosine kinases acutely regulate neuronal sodium channels through the src signaling pathway. J. Neurosci. 18:1998;590-600.
    • (1998) J. Neurosci. , vol.18 , pp. 590-600
    • Hilborn, M.D.1    Vaillancourt, R.R.2    Rane, S.G.3
  • 16
    • 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
    • 0029916913 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the Kv1.3 potassium channel
    • Holmes T.C., Fadool D.A., Levitan I.B. Tyrosine phosphorylation of the Kv1.3 potassium channel. J. Neurosci. 16:1996;1581-1590.
    • (1996) J. Neurosci. , vol.16 , pp. 1581-1590
    • Holmes, T.C.1    Fadool, D.A.2    Levitan, I.B.3
  • 18
    • 0242571496 scopus 로고    scopus 로고
    • Protein-tyrosine kinase is required for the induction of long-term potentiation in the rat hippocampus
    • Huang C.C., Hsu K.S. Protein-tyrosine kinase is required for the induction of long-term potentiation in the rat hippocampus. J. Physiol. Lond. 520:1999;783-796.
    • (1999) J. Physiol. Lond. , vol.520 , pp. 783-796
    • Huang, C.C.1    Hsu, K.S.2
  • 19
    • 0033846403 scopus 로고    scopus 로고
    • Direct inhibition of glycine receptors by genistein, a tyrosine kinase inhibitor
    • Huang R.Q., Dillon G.H. Direct inhibition of glycine receptors by genistein, a tyrosine kinase inhibitor. Neuropharmacol. 39:2000;2195-2204.
    • (2000) Neuropharmacol. , vol.39 , pp. 2195-2204
    • Huang, R.Q.1    Dillon, G.H.2
  • 20
    • 0027146670 scopus 로고
    • Tyrosine kinase-dependent suppression of a potassium channel by the G protein-coupled m1 muscarinic acetylcholine receptor
    • Huang X.Y., Morielli A.D., Peralta E.G. Tyrosine kinase-dependent suppression of a potassium channel by the G protein-coupled m1 muscarinic acetylcholine receptor. Cell. 75:1993;1145-1156.
    • (1993) Cell , vol.75 , pp. 1145-1156
    • Huang, X.Y.1    Morielli, A.D.2    Peralta, E.G.3
  • 21
    • 0027373866 scopus 로고
    • Dephostatin, a novel protein-tyrosine phosphatase inhibitor produced by Streptomyces. I. Taxonomy, isolation, and characterization
    • 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. J. Antibiotics. 46:1993;1342-1346.
    • (1993) J. Antibiotics , 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
  • 25
    • 0033624990 scopus 로고    scopus 로고
    • 2+-induced noradrenaline release by vanadate in PC12 cells: Possible involvement of tyrosine phosphorylation
    • 2+-induced noradrenaline release by vanadate in PC12 cells: possible involvement of tyrosine phosphorylation. Brain Res. 854:2000;165-171.
    • (2000) Brain Res. , vol.854 , pp. 165-171
    • Kitamura, T.1    Murayama, T.2    Nomura, Y.3
  • 26
    • 77957012032 scopus 로고
    • Spectrophotometric and turbidimetric methods for measuring proteins
    • Layne E. Spectrophotometric and turbidimetric methods for measuring proteins. Methods Enzymol. 3:1957;447-451.
    • (1957) Methods Enzymol. , vol.3 , pp. 447-451
    • Layne, E.1
  • 27
    • 0001555360 scopus 로고    scopus 로고
    • Modulation of unitary glutamatergic synapses by neurotrophin-4/5 or brain-derived neurotrophic factor in hippocampal microcultures - Presynaptic enhancement depends on pre-established paired-pulse facilitation
    • Leßmann V., Heumann R. Modulation of unitary glutamatergic synapses by neurotrophin-4/5 or brain-derived neurotrophic factor in hippocampal microcultures - presynaptic enhancement depends on pre-established paired-pulse facilitation. Neuroscience. 86:1998;399-413.
    • (1998) Neuroscience , vol.86 , pp. 399-413
    • Leßmann, V.1    Heumann, R.2
  • 29
    • 0029099174 scopus 로고
    • Brain-derived neurotrophic factor rapidly enhances synaptic transmission in hippocampal neurons via postsynaptic tyrosine kinase receptors
    • Levine, E.S., Dreyfus, C.F., Black, I.B., Plummer, M.R., 1995. Brain-derived neurotrophic factor rapidly enhances synaptic transmission in hippocampal neurons via postsynaptic tyrosine kinase receptors. Proc. Natl. Acad. Sci. U.S.A. 92, 8074-8077.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8074-8077
    • Levine, E.S.1    Dreyfus, C.F.2    Black, I.B.3    Plummer, M.R.4
  • 31
    • 0026795115 scopus 로고
    • Tetanus toxin and botulinun toxins types A and B inhibit glutamate, γ-aminobutyric acid, aspartate, and Met-enkephalin release from synaptosomes
    • McMahon H.T., Forman P., Dolly J.O., Verhage M., Wiegant V., Nicholls D.G. Tetanus toxin and botulinun toxins types A and B inhibit glutamate, γ-aminobutyric acid, aspartate, and Met-enkephalin release from synaptosomes. J. Biol. Chem. 267:1992;21338-21343.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21338-21343
    • McMahon, H.T.1    Forman, P.2    Dolly, J.O.3    Verhage, M.4    Wiegant, V.5    Nicholls, D.G.6
  • 34
    • 0024534115 scopus 로고
    • Release of glutamate, aspartate and γ-aminobutyric acid from isolated nerve terminals
    • Nicholls D.G. Release of glutamate, aspartate and γ-aminobutyric acid from isolated nerve terminals. J. Neurochem. 52:1989;331-341.
    • (1989) J. Neurochem. , vol.52 , pp. 331-341
    • Nicholls, D.G.1
  • 35
    • 0023370658 scopus 로고
    • Calcium-dependent and independent release of glutamate from synaptosomes monitored by continuous fluorimetry
    • Nicholls D.G., Sihra T.S., Sanchez-Prieto J. Calcium-dependent and independent release of glutamate from synaptosomes monitored by continuous fluorimetry. J. Neurochem. 47:1987;50-57.
    • (1987) J. Neurochem. , vol.47 , pp. 50-57
    • Nicholls, D.G.1    Sihra, T.S.2    Sanchez-Prieto, J.3
  • 36
    • 0033563868 scopus 로고    scopus 로고
    • Tyrosine kinase-independent inhibition of cyclic-AMP phosphodiesterase by genistein and tyrphostin 51
    • Nichols M.R., Morimoto B.H. Tyrosine kinase-independent inhibition of cyclic-AMP phosphodiesterase by genistein and tyrphostin 51. Arch. Biochem. Biophys. 366:1999;224-230.
    • (1999) Arch. Biochem. Biophys. , vol.366 , pp. 224-230
    • Nichols, M.R.1    Morimoto, B.H.2
  • 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.N. 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.N.3
  • 39
    • 0035371620 scopus 로고    scopus 로고
    • Regulation of receptor tyrosine kinase signaling by protein-tyrosine phosphatases
    • Ostman A., Bohmer F.D. Regulation of receptor tyrosine kinase signaling by protein-tyrosine phosphatases. Trends Cell Biol. 11:2001;258-266.
    • (2001) Trends Cell Biol. , vol.11 , pp. 258-266
    • Ostman, A.1    Bohmer, F.D.2
  • 40
    • 0030933913 scopus 로고    scopus 로고
    • Direct block of voltage-sensitive sodium channels by genistein, a tyrosine kinase inhibitor
    • Paillart C., Carlier E., Guedin D., Dargent B., Couraud F. Direct block of voltage-sensitive sodium channels by genistein, a tyrosine kinase inhibitor. J. Pharmacol. Exp. Therap. 280:1997;521-526.
    • (1997) J. Pharmacol. Exp. Therap. , vol.280 , pp. 521-526
    • Paillart, C.1    Carlier, E.2    Guedin, D.3    Dargent, B.4    Couraud, F.5
  • 42
    • 0030176079 scopus 로고    scopus 로고
    • Recombinant BDNF rescues deficits in basal synaptic transmission and hippocampal LTP in BDNF knockout mice
    • Patterson S.L., Abel T., Deuel T.A.S., Martin K.C., Rose J.C., Kandel E.R. Recombinant BDNF rescues deficits in basal synaptic transmission and hippocampal LTP in BDNF knockout mice. Neuron. 16:1996;1137-1145.
    • (1996) Neuron , vol.16 , pp. 1137-1145
    • Patterson, S.L.1    Abel, T.2    Deuel, T.A.S.3    Martin, K.C.4    Rose, J.C.5    Kandel, E.R.6
  • 43
    • 0003386218 scopus 로고    scopus 로고
    • Modulation of hippocampal synaptic plasticity by the ERK/MAPK pathway
    • Bos, J.L. (Ed).IOS Press, Amsterdam
    • Pereira, D.B., Carvalho, A.P., Duarte, C.B., 2000. Modulation of hippocampal synaptic plasticity by the ERK/MAPK pathway. In: Bos, J.L. (Ed), Molecular Mechanisms of Signal Transduction, Vol. A/316. IOS Press, Amsterdam, pp. 63-72.
    • Molecular Mechanisms of Signal Transduction , vol.A316 , pp. 63-72
    • Pereira, D.B.1    Carvalho, A.P.2    Duarte, C.B.3
  • 45
    • 0033858043 scopus 로고    scopus 로고
    • Emerging issues in receptor protein-tyrosine phosphatase function: Lifting fog or simply shifting?
    • Petrone A., Sap J. Emerging issues in receptor protein-tyrosine phosphatase function: lifting fog or simply shifting? J. Cell Sci. 113:2000;2345-2354.
    • (2000) J. Cell Sci. , vol.113 , pp. 2345-2354
    • Petrone, A.1    Sap, J.2
  • 46
    • 0033596590 scopus 로고    scopus 로고
    • Protein-tyrosine kinase inhibitors reduce high-voltage activating calcium currents in CA1 pyramidal neurones from rat hippocampal slices
    • Potier B., Rovira C. Protein-tyrosine kinase inhibitors reduce high-voltage activating calcium currents in CA1 pyramidal neurones from rat hippocampal slices. Brain Res. 816:1999;587-597.
    • (1999) Brain Res. , vol.816 , pp. 587-597
    • Potier, B.1    Rovira, C.2
  • 48
    • 0026806426 scopus 로고
    • Inhibition of interleukin 3 and granulocyte-macrophage colony-stimulating factor stimulated increase of active ras.GTP by herbimycin A, a specific inhibitor of tyrosine kinases
    • Satoh T., Uehara Y., Kaziro Y. Inhibition of interleukin 3 and granulocyte-macrophage colony-stimulating factor stimulated increase of active ras.GTP by herbimycin A, a specific inhibitor of tyrosine kinases. J. Biol. Chem. 267:1992;2537-2541.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2537-2541
    • Satoh, T.1    Uehara, Y.2    Kaziro, Y.3
  • 50
    • 0028386402 scopus 로고
    • Ion channel control by tyrosine phosphorylation
    • Siegelbaum S.A. Ion channel control by tyrosine phosphorylation. Cur. Biol. 4:1994;242-245.
    • (1994) Cur. Biol. , vol.4 , pp. 242-245
    • Siegelbaum, S.A.1
  • 52
    • 0029609408 scopus 로고
    • Structure of synaptogyrin (p29) defines a novel synaptic vesicle protein
    • Stenius K., Janz R., Sudhof T.C., Jahn R. Structure of synaptogyrin (p29) defines a novel synaptic vesicle protein. J. Cell Biol. 131:1995;1801-1809.
    • (1995) J. Cell Biol. , vol.131 , pp. 1801-1809
    • Stenius, K.1    Janz, R.2    Sudhof, T.C.3    Jahn, R.4
  • 53
    • 0030800864 scopus 로고    scopus 로고
    • Regulation of L-type calcium channels by protein-tyrosine kinase and protein kinase C in cultured rat and human retinal pigment epithelial cells
    • Strauss O., Mergler S., Wiederholt M. Regulation of L-type calcium channels by protein-tyrosine kinase and protein kinase C in cultured rat and human retinal pigment epithelial cells. FASEB J. 11:1997;859-867.
    • (1997) FASEB J. , vol.11 , pp. 859-867
    • Strauss, O.1    Mergler, S.2    Wiederholt, M.3
  • 54
    • 0020463759 scopus 로고
    • Inhibition of membrane phosphotyrosyl-protein phosphatase activity by vanadate
    • Swarup G., Cohen S., Garbers D.L. Inhibition of membrane phosphotyrosyl-protein phosphatase activity by vanadate. Biochem. Biophys. Res. Commun. 107:1982;1104-1109.
    • (1982) Biochem. Biophys. Res. Commun. , vol.107 , pp. 1104-1109
    • Swarup, G.1    Cohen, S.2    Garbers, D.L.3
  • 56
    • 0025947138 scopus 로고
    • Use and selectivity of herbimycin A as inhibitor of protein-tyrosine kinases
    • Uehara Y., Fukazawa H. Use and selectivity of herbimycin A as inhibitor of protein-tyrosine kinases. Methods Enzymol. 201:1991;370-379.
    • (1991) Methods Enzymol. , vol.201 , pp. 370-379
    • Uehara, Y.1    Fukazawa, H.2
  • 57
    • 0032053706 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases in the developing nervous system
    • Van Vactor D. Protein-tyrosine phosphatases in the developing nervous system. Cur. Opin. Cell Biol. 10:1998;174-181.
    • (1998) Cur. Opin. Cell Biol. , vol.10 , pp. 174-181
    • Van Vactor, D.1
  • 58
    • 0028360327 scopus 로고
    • Regulation of NMDA receptors by tyrosine kinases and phosphatases
    • Wang Y.T., Salter M.W. Regulation of NMDA receptors by tyrosine kinases and phosphatases. Nature. 369:1994;233-235.
    • (1994) Nature , vol.369 , pp. 233-235
    • Wang, Y.T.1    Salter, M.W.2
  • 59
    • 0032414792 scopus 로고    scopus 로고
    • Genistein inhibits slow component delayed-rectifier K currents via a tyrosine kinase-independent pathway
    • Washizuka T., Horie M., Obayashi K., Sasayama S. Genistein inhibits slow component delayed-rectifier K currents via a tyrosine kinase-independent pathway. J. Mol. Cell. Cardiol. 30:1998;2577-2590.
    • (1998) J. Mol. Cell. Cardiol. , vol.30 , pp. 2577-2590
    • Washizuka, T.1    Horie, M.2    Obayashi, K.3    Sasayama, S.4
  • 60
    • 0031836041 scopus 로고    scopus 로고
    • Effect of inhibition of tyrosine phosphatases on voltage-operated calcium channel currents in rabbit isolated ear artery cells
    • Wijetunge S., Lymn J.S., Hughes A.D. Effect of inhibition of tyrosine phosphatases on voltage-operated calcium channel currents in rabbit isolated ear artery cells. Br. J. Pharmacol. 124:1998;307-316.
    • (1998) Br. J. Pharmacol. , vol.124 , pp. 307-316
    • Wijetunge, S.1    Lymn, J.S.2    Hughes, A.D.3
  • 61
    • 0026686956 scopus 로고
    • Depolarization-dependent tyrosine phosphorylation in rat brain synaptosomes
    • Woodrow S., Bisson N., Gurd J.W. Depolarization-dependent tyrosine phosphorylation in rat brain synaptosomes. J. Neurochem. 59:1992;857-862.
    • (1992) J. Neurochem. , vol.59 , pp. 857-862
    • Woodrow, S.1    Bisson, N.2    Gurd, J.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.