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Volumn 21, Issue 3, 1996, Pages 175-191

Microvesicle-mediated exocytosis of glutamate is a novel paracrine-like chemical transduction mechanism and inhibits melatonin secretion in rat pinealocytes

Author keywords

Chemical transaction; Glutamate receptors; L glutamate; Melatonin; Microvestcles; Paracrine; Paraneuron; Pineal gland

Indexed keywords

ALPHA ADRENERGIC RECEPTOR STIMULATING AGENT; CALCIUM; GLUTAMATE RECEPTOR; GLUTAMIC ACID; MELATONIN; NEUROTOXIN; NORADRENALIN; PEPTIDE FRAGMENT; POTASSIUM CHLORIDE;

EID: 0030254346     PISSN: 07423098     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-079X.1996.tb00285.x     Document Type: Article
Times cited : (54)

References (68)
  • 1
    • 0026526404 scopus 로고
    • The amphicrine pancreatic cell line, AR42J, secretes GABA and amylase by separate regulated pathways
    • AHNERT-HILGER, G., B. WEIDENMANN (1992) The amphicrine pancreatic cell line, AR42J, secretes GABA and amylase by separate regulated pathways. FEBS Lett. 314:41-44.
    • (1992) FEBS Lett. , vol.314 , pp. 41-44
    • Ahnert-Hilger, G.1    Weidenmann, B.2
  • 2
    • 0027322820 scopus 로고
    • Catecholamines are present in a synaptic-like microvesicle-enriched fraction from bovine adrenal medulla
    • ANNAERT, W.G., L. LLONA, A.C. BACKER, W.A. JACOB, W.P. DE POTTER (1993) Catecholamines are present in a synaptic-like microvesicle-enriched fraction from bovine adrenal medulla. J. Neurochem. 60:1746-1754.
    • (1993) J. Neurochem. , vol.60 , pp. 1746-1754
    • Annaert, W.G.1    Llona, L.2    Backer, A.C.3    Jacob, W.A.4    De Potter, W.P.5
  • 3
    • 0026501650 scopus 로고
    • Cellular mechanism for norepinephrine suppression of pineal photoreceptor-like cell differentiation in rat pineal cultures
    • ARAKI, M (1992) Cellular mechanism for norepinephrine suppression of pineal photoreceptor-like cell differentiation in rat pineal cultures. Dev. Biol. 149:440-447.
    • (1992) Dev. Biol. , vol.149 , pp. 440-447
    • Araki, M.1
  • 4
    • 0016256663 scopus 로고
    • The pineal gland: A neurochemical transducer
    • AXELROD, J (1974) The pineal gland: A neurochemical transducer. Science 184:1341-1348.
    • (1974) Science , vol.184 , pp. 1341-1348
    • Axelrod, J.1
  • 5
    • 0027179911 scopus 로고
    • Selective storage of acetylcholine, but not catecholamines, in neuroendocrine synaptic-like microvesicles of early endosomal origin
    • BAUERFEIND, R., A. REGNIER-VIGOUROUX, T. FLATMARK, W. B. HUTTNER (1993) Selective storage of acetylcholine, but not catecholamines, in neuroendocrine synaptic-like microvesicles of early endosomal origin. Neuron 11:105-121.
    • (1993) Neuron , vol.11 , pp. 105-121
    • Bauerfeind, R.1    Regnier-Vigouroux, A.2    Flatmark, T.3    Huttner, W.B.4
  • 6
    • 0024453294 scopus 로고
    • Inositol phosphates and cell signaling
    • BERRIDGE, M.J., R.F. IRVINE (1989) Inositol phosphates and cell signaling. Nature 341:197-205.
    • (1989) Nature , vol.341 , pp. 197-205
    • Berridge, M.J.1    Irvine, R.F.2
  • 9
    • 0027934987 scopus 로고
    • Secretory and synaptic vesicle membrane proteins and their possible roles in regulated exocytosis
    • DAMER, C.K., C.E. CREUTZ (1994) Secretory and synaptic vesicle membrane proteins and their possible roles in regulated exocytosis. Prog. Neurobiol. 43:511-536.
    • (1994) Prog. Neurobiol. , vol.43 , pp. 511-536
    • Damer, C.K.1    Creutz, C.E.2
  • 10
    • 0029057212 scopus 로고
    • Blockade by botulinum neurotoxin B of catecholamine release from adrenochromaffin cells correlates with its cleavage of synaptobrevin and a homologue present on the granules
    • FORAN, P., G. LAWRENCE, J.O. DOLLY (1995) Blockade by botulinum neurotoxin B of catecholamine release from adrenochromaffin cells correlates with its cleavage of synaptobrevin and a homologue present on the granules. Biochemistry 34:5495-5503.
    • (1995) Biochemistry , vol.34 , pp. 5495-5503
    • Foran, P.1    Lawrence, G.2    Dolly, J.O.3
  • 11
    • 0021434352 scopus 로고
    • Acidic amino acid binding sites in mammalian neuronal membranes: Their characteristics and relationship to synaptic receptors
    • FOSTER, A., G. FAGG (1984) Acidic amino acid binding sites in mammalian neuronal membranes: Their characteristics and relationship to synaptic receptors. Brain Res. Rev. 7:103-164.
    • (1984) Brain Res. Rev. , vol.7 , pp. 103-164
    • Foster, A.1    Fagg, G.2
  • 13
    • 0021284732 scopus 로고
    • Measurements of free amino acids in human biological fluids by high-performance liquid chromatography
    • GODEL, H., T. GRASER, P. FOELDI, P. FUERST (1984) Measurements of free amino acids in human biological fluids by high-performance liquid chromatography. J. Chromatography 297:49-61.
    • (1984) J. Chromatography , vol.297 , pp. 49-61
    • Godel, H.1    Graser, T.2    Foeldi, P.3    Fuerst, P.4
  • 14
    • 0022929899 scopus 로고
    • 2+-dependent glutamate (quisqualate) binding site in the bovine pineal organ
    • 2+-dependent glutamate (quisqualate) binding site in the bovine pineal organ. J. Pineal Res. 3:223-234.
    • (1986) J. Pineal Res. , vol.3 , pp. 223-234
    • Govitrapong, P.1    Ebadi, M.2    Murrin, J.L.3
  • 15
    • 0023816385 scopus 로고
    • The inhibition of pineal arylalkylamine N-acetyltransferase by glutamic acid and its analogues
    • GOVITRAPONG, P., M. EBADI (1988) The inhibition of pineal arylalkylamine N-acetyltransferase by glutamic acid and its analogues. Neurochem. Int. 13:223-230.
    • (1988) Neurochem. Int. , vol.13 , pp. 223-230
    • Govitrapong, P.1    Ebadi, M.2
  • 16
    • 0028023444 scopus 로고
    • Calcium dependence of the rate of exocytosis in a synaptic terminal
    • HEIDERBERGER, R., C. HEINEMANN, E. NEHR, G. MATTEWS (1994) Calcium dependence of the rate of exocytosis in a synaptic terminal. Nature 371:513-515.
    • (1994) Nature , vol.371 , pp. 513-515
    • Heiderberger, R.1    Heinemann, C.2    Nehr, E.3    Mattews, G.4
  • 18
    • 0027516462 scopus 로고
    • Purification and characterization of the ganglioside-binding fragment of Clostridium botulinum type E neurotoxin. Biochim
    • KAMATA, Y., Y. KIMURA, T. HIROI, G. SAKAGUCHI, S. KOZAKI (1993) Purification and characterization of the ganglioside-binding fragment of Clostridium botulinum type E neurotoxin. Biochim. Biophys. Acta 1156:213-218.
    • (1993) Biophys. Acta , vol.1156 , pp. 213-218
    • Kamata, Y.1    Kimura, Y.2    Hiroi, T.3    Sakaguchi, G.4    Kozaki, S.5
  • 19
    • 0023074631 scopus 로고
    • Mechanism of transport and storage of neurotransmitters
    • KANNER, B., S. SCHULDINER (1987) Mechanism of transport and storage of neurotransmitters. CRC Crit. Rev. Biochem. 22:1-38.
    • (1987) CRC Crit. Rev. Biochem. , vol.22 , pp. 1-38
    • Kanner, B.1    Schuldiner, S.2
  • 20
    • 0022210967 scopus 로고
    • Photoneural regulation of the mammalian pineal gland
    • Photoperiodism, melatonin, and the pineal gland. Evered D., and Clark, S., eds. Pitman, London
    • KLEIN, D.C. (1985) Photoneural regulation of the mammalian pineal gland. In: Ciba Foundation Symposium 117: Photoperiodism, melatonin, and the pineal gland. Evered D., and Clark, S., eds. Pitman, London, pp. 38-56.
    • (1985) Ciba Foundation Symposium , vol.117 , pp. 38-56
    • Klein, D.C.1
  • 21
    • 0027336323 scopus 로고
    • 3H]glutamate binding site in rat pineal gland: Enhanced affinity following superior cervical ganglionectomy
    • 3H]glutamate binding site in rat pineal gland: enhanced affinity following superior cervical ganglionectomy. J. Pineal Res. 14:39-44.
    • (1993) J. Pineal Res. , vol.14 , pp. 39-44
    • Kus, L.1    Handa, R.J.2    Mcnulty, J.A.3
  • 22
    • 0028247171 scopus 로고
    • Glutamate inhibition of the adrenergic-stimulated production of melatonin in rat pineal gland in vitro
    • KUS, L., R.J. HANDA, J.A. MCNULTY (1994) Glutamate inhibition of the adrenergic-stimulated production of melatonin in rat pineal gland in vitro. J. Neurochem. 62: 2241-2245.
    • (1994) J. Neurochem. , vol.62 , pp. 2241-2245
    • Kus, L.1    Handa, R.J.2    Mcnulty, J.A.3
  • 23
    • 0023125256 scopus 로고
    • The physiology of excitatory amino acids in the vertebrate central nervous system
    • MAYER, M.L., G. WESTBROOK (1987) The physiology of excitatory amino acids in the vertebrate central nervous system. Prog. Neurobiol. 28:197-276.
    • (1987) Prog. Neurobiol. , vol.28 , pp. 197-276
    • Mayer, M.L.1    Westbrook, G.2
  • 24
    • 0026706712 scopus 로고
    • Immunocytochemical and circadian biochemical analysis of neuroactive amino acids in the pineal gland of the rat: Effect of superior cervical ganglionectomy
    • MCNULTY, J.A., L. Kus, O.P. OTTERSEN (1992) Immunocytochemical and circadian biochemical analysis of neuroactive amino acids in the pineal gland of the rat: Effect of superior cervical ganglionectomy. Cell Tissue Res. 269:515-523.
    • (1992) Cell Tissue Res. , vol.269 , pp. 515-523
    • Mcnulty, J.A.1    Kus, L.2    Ottersen, O.P.3
  • 25
    • 0007054606 scopus 로고
    • Biochemical evidence that vesicles are the source of the acetylcholine released from stimulated PC12 cells
    • MELGA, W.P., B.D. HOWARD (1984) Biochemical evidence that vesicles are the source of the acetylcholine released from stimulated PC12 cells. Proc. Natl. Acad. Sci. U.S.A. 81:6535-6538.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 6535-6538
    • Melga, W.P.1    Howard, B.D.2
  • 28
    • 0023645189 scopus 로고
    • The purified ATPase from chromaffin granule membranes is an anion-dependent proton pump
    • MORIYAM, Y, N. NELSON (1987) The purified ATPase from chromaffin granule membranes is an anion-dependent proton pump. J. Biol. Chem. 262:9175-9180.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9175-9180
    • Moriyam, Y.1    Nelson, N.2
  • 30
    • 0029077242 scopus 로고
    • Localization of N-ethylmaleimide-sensitive fusion protein in pinealocytes
    • MORIYAMA, Y., A. YAMAMOTO, M. TAGAYA, Y. TASHIRO, H. MICHIBATA (1995b) Localization of N-ethylmaleimide-sensitive fusion protein in pinealocytes. NeuroReport 6:1757-1760.
    • (1995) NeuroReport , vol.6 , pp. 1757-1760
    • Moriyama, Y.1    Yamamoto, A.2    Tagaya, M.3    Tashiro, Y.4    Michibata, H.5
  • 31
    • 0029020844 scopus 로고
    • Microvesicles isolated from bovine pineal gland specifically accumulate L-glutamate
    • MORIYAM, Y, A. YAMAMOTO (1995a) Microvesicles isolated from bovine pineal gland specifically accumulate L-glutamate. FEBS Lett. 367:233-236.
    • (1995) FEBS Lett. , vol.367 , pp. 233-236
    • Moriyam, Y.1    Yamamoto, A.2
  • 32
    • 0029121814 scopus 로고
    • Vesicular L-glutamate transporter in microvesicles from bovine pineal glands: Driving force, mechanism of chloride anion-activation, and substrate specificity
    • MORIYAMA, Y., A. YAMAMOTO (1995b) Vesicular L-glutamate transporter in microvesicles from bovine pineal glands: Driving force, mechanism of chloride anion-activation, and substrate specificity. J. Biol. Chem. 270:22314-22320.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22314-22320
    • Moriyama, Y.1    Yamamoto, A.2
  • 34
    • 0027938848 scopus 로고
    • Metabolic glutamate receptors: Synaptic transmission, modulation, and plasticity
    • NAKANISHI, S. (1994) Metabolic glutamate receptors: synaptic transmission, modulation, and plasticity. Neuron 13:1031-1037.
    • (1994) Neuron , vol.13 , pp. 1031-1037
    • Nakanishi, S.1
  • 35
    • 0023032310 scopus 로고
    • Protein p38: An intergral membrane protein specific for small vesicles of neurons and neuroendocrine cells
    • NAVONE, F., R. JAHN, G. DI GOIA, H. STUKENBROK, P. GREENGARD, P. DE CAMILLI (1986) Protein p38: An intergral membrane protein specific for small vesicles of neurons and neuroendocrine cells. J. Cell Biol. 103:2511-2527.
    • (1986) J. Cell Biol. , vol.103 , pp. 2511-2527
    • Navone, F.1    Jahn, R.2    Di Goia, G.3    Stukenbrok, H.4    Greengard, P.5    De Camilli, P.6
  • 36
    • 0024534115 scopus 로고
    • The release of glutamate, aspartate, and GABA from isolated nerve terminals
    • NICHOLLS, D.G (1989) The release of glutamate, aspartate, and GABA from isolated nerve terminals. J. Neurochem. 52:331-341.
    • (1989) J. Neurochem. , vol.52 , pp. 331-341
    • Nicholls, D.G.1
  • 37
    • 0028341442 scopus 로고
    • Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes
    • NISHIKI, T., Y. KAMATA, Y. NEMOTO, A. OMORI, T. ITO, M. TAKAHASHI, S. KOZAKI (1994) Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes. J. Biol. Chem. 269:10498-10503.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10498-10503
    • Nishiki, T.1    Kamata, Y.2    Nemoto, Y.3    Omori, A.4    Ito, T.5    Takahashi, M.6    Kozaki, S.7
  • 38
    • 0022642415 scopus 로고
    • Identification of a synaptic vesicle-specific 38,000-dalton protein by monoclonal antibodies
    • OBATA, K., H. NISHIYA, S.C. FUJITA, T. SHIRAO, H. INOUE. K. UCHIZONO (1986) Identification of a synaptic vesicle-specific 38,000-dalton protein by monoclonal antibodies. Brain Res. 375:37-48.
    • (1986) Brain Res. , vol.375 , pp. 37-48
    • Obata, K.1    Nishiya, H.2    Fujita, S.C.3    Shirao, T.4    Inoue, H.5    Uchizono, K.6
  • 39
    • 0028966170 scopus 로고
    • Expression and complex formation of SNAP, soluble N-ethylmaleimide-sensitive factor attachment protein, receptor in 'clonal rat endocrine cells
    • OHO, C., S. SEISO, M. TAKAHASHI (1995) Expression and complex formation of SNAP, soluble N-ethylmaleimide-sensitive factor attachment protein, receptor in 'clonal rat endocrine cells. Neurosci. Lett. 186:208-210.
    • (1995) Neurosci. Lett. , vol.186 , pp. 208-210
    • Oho, C.1    Seiso, S.2    Takahashi, M.3
  • 40
    • 0021749660 scopus 로고
    • Purification and sequence of a presynaptic peptide toxin from Conus geographus venom
    • OLIVERA, B.M., J.M. MCLINTOSH, L.J. CRUZ, F.A. LUQUE, W.R. GRAY (1984) Purification and sequence of a presynaptic peptide toxin from Conus geographus venom. Biochemistry 23:5087-5090.
    • (1984) Biochemistry , vol.23 , pp. 5087-5090
    • Olivera, B.M.1    Mclintosh, J.M.2    Cruz, L.J.3    Luque, F.A.4    Gray, W.R.5
  • 41
    • 0027505663 scopus 로고
    • Synaptophysin - A common constituent of presumptive secretory microvesicles in the mammalian pinealocyte: A study of rat and gerbil pineal glands
    • REDECKER, P., G. BARGSTEN (1993) Synaptophysin - a common constituent of presumptive secretory microvesicles in the mammalian pinealocyte: A study of rat and gerbil pineal glands. J. Neurosci. Res. 34:79-96.
    • (1993) J. Neurosci. Res. , vol.34 , pp. 79-96
    • Redecker, P.1    Bargsten, G.2
  • 42
    • 0028829924 scopus 로고
    • The ras-like rab3A protein is present in pinealocytes of the gerbil pineal gland
    • REDECKE, P. (1995) The ras-like rab3A protein is present in pinealocytes of the gerbil pineal gland. Neurosci. Lett. 184:117-120.
    • (1995) Neurosci. Lett. , vol.184 , pp. 117-120
    • Redecke, P.1
  • 43
    • 0019781433 scopus 로고
    • The mammalian pineal gland: Structure and function
    • REITER, R.J. (1981) The mammalian pineal gland: Structure and function. Am. J. Anat. 162:287-313.
    • (1981) Am. J. Anat. , vol.162 , pp. 287-313
    • Reiter, R.J.1
  • 44
    • 0025758136 scopus 로고
    • Pineal melatonin:cell biology of its synthesis and of its physiological interactions
    • REITER, R.J. (1991) Pineal melatonin:cell biology of its synthesis and of its physiological interactions. Endocrine Rev. 12:151-180.
    • (1991) Endocrine Rev. , vol.12 , pp. 151-180
    • Reiter, R.J.1
  • 45
    • 0024470349 scopus 로고
    • Glucose-inhibition of glucagon secretion involves activation of GABAA-receptor chloride channels
    • RORSMAN, P., P.-O. BERGGREN, K. BOKVIST, H. ERICSON, H. MOHLER, C.-G. OTENSON, P.A. SMITH (1989) Glucose-inhibition of glucagon secretion involves activation of GABAA-receptor chloride channels. Nature 341:233-236.
    • (1989) Nature , vol.341 , pp. 233-236
    • Rorsman, P.1    Berggren, P.-O.2    Bokvist, K.3    Ericson, H.4    Mohler, H.5    Otenson, C.-G.6    Smith, P.A.7
  • 46
    • 0024311618 scopus 로고
    • Inositol 1,4,5-trisphosphate receptor localized to endoplasmic reticulum in cerebellar Purkinje neurons
    • ROSS, C.A., J. MELDOLESI, T.A., MILNER, T. SATOH, S. SUPATTAPONE, S.H. SNYDER (1989) Inositol 1,4,5-trisphosphate receptor localized to endoplasmic reticulum in cerebellar Purkinje neurons. Nature 339:468-470.
    • (1989) Nature , vol.339 , pp. 468-470
    • Ross, C.A.1    Meldolesi, J.2    Milner, T.A.3    Satoh, T.4    Supattapone, S.5    Snyder, S.H.6
  • 47
    • 0028143698 scopus 로고
    • Mechanism of intracellular protein transport
    • ROTHMAN, J.E. (1994) Mechanism of intracellular protein transport. Nature 372:55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 48
    • 0027203938 scopus 로고
    • Expression of the metabolic glutamate receptor mGluR1α and the ionotropic glutamate receptor GluR1 in the brain during the postnatal development of normal mouse and in the cerebellum from the mutant mice
    • RYO, Y., A. MIYAWAKI, T. FURUICHI, K. MIKOSHIBA (1993) Expression of the metabolic glutamate receptor mGluR1α and the ionotropic glutamate receptor GluR1 in the brain during the postnatal development of normal mouse and in the cerebellum from the mutant mice. J. Neurosci. Res. 36:19-32.
    • (1993) J. Neurosci. Res. , vol.36 , pp. 19-32
    • Ryo, Y.1    Miyawaki, A.2    Furuichi, T.3    Mikoshiba, K.4
  • 50
    • 0023707538 scopus 로고
    • Determination of plasma 5-ydroxytryptophan, 5-hydroxytryptamine, 5-hydroxyindoleacetic acid, tryptophan, and melatonin by HPLC with electrochemical detection
    • SAGARA, Y., Y. OKATANI, S. YAMANAKA, T. KIRIYAMA (1988) Determination of plasma 5-ydroxytryptophan, 5-hydroxytryptamine, 5-hydroxyindoleacetic acid, tryptophan, and melatonin by HPLC with electrochemical detection. J. Chromatog. 431:170-176.
    • (1988) J. Chromatog. , vol.431 , pp. 170-176
    • Sagara, Y.1    Okatani, Y.2    Yamanaka, S.3    Kiriyama, T.4
  • 52
    • 0029078987 scopus 로고
    • Vasoactive intestinal peptide elevates pinealocyte intracellular calcium concentrations by enhancing influx: Evidence for involvement of a cyclic GMP-dependent mechanism
    • SCHAAD, N.C., J. VANECEK, I.R. RODRIGUEZ, D.C. KLEIN, L. HOLTZCLAW, J.T. RUSSEL (1995) Vasoactive intestinal peptide elevates pinealocyte intracellular calcium concentrations by enhancing influx: Evidence for involvement of a cyclic GMP-dependent mechanism. Mol. Pharmacol. 47:923-933.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 923-933
    • Schaad, N.C.1    Vanecek, J.2    Rodriguez, I.R.3    Klein, D.C.4    Holtzclaw, L.5    Russel, J.T.6
  • 53
    • 0029058492 scopus 로고
    • Membrane trafficking in the presynaptic nerve terminal
    • SCHELLER, R.H. (1995) Membrane trafficking in the presynaptic nerve terminal. Neuron 14:893-897.
    • (1995) Neuron , vol.14 , pp. 893-897
    • Scheller, R.H.1
  • 55
    • 0037934795 scopus 로고
    • Storage and release of acetylcholine by a clonal cell line
    • SCHUBERT, D., F.G. KLIER (1977) Storage and release of acetylcholine by a clonal cell line. Proc. Natl. Acad. Sci. U.S.A. 74:5184-5188.
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 5184-5188
    • Schubert, D.1    Klier, F.G.2
  • 57
    • 0024659539 scopus 로고
    • A synaptic vesicle membrane protein is conserved from mammals to Drosophila
    • SÜDHOF, T.C., M. BAUMERT, M.S. PERIN, R. JAHN (1989) A synaptic vesicle membrane protein is conserved from mammals to Drosophila. Neuron 2:1475-1481.
    • (1989) Neuron , vol.2 , pp. 1475-1481
    • Südhof, T.C.1    Baumert, M.2    Perin, M.S.3    Jahn, R.4
  • 58
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • SÜDHOF, T.C. (1995) The synaptic vesicle cycle: A cascade of protein-protein interactions. Nature 375:645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 59
    • 0022999960 scopus 로고
    • Essential role of calcium influx in the adrenergic regulation of cAMPand cGMP in rat pinealocytes
    • SUGDEN, L., D. SUGDEN, D.C. KLEIN (1986) Essential role of calcium influx in the adrenergic regulation of cAMPand cGMP in rat pinealocytes. J. Biol. Chem. 261:741-745.
    • (1986) J. Biol. Chem. , vol.261 , pp. 741-745
    • Sugden, L.1    Sugden, D.2    Klein, D.C.3
  • 60
    • 0027474007 scopus 로고
    • Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport
    • TAGAYA, M., D.W. WILSON, M. BRUNNER, N. ARANGO, J.M. ROTHMAN (1993) Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport. J. Biol. Chem. 268:2662-2666.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2662-2666
    • Tagaya, M.1    Wilson, D.W.2    Brunner, M.3    Arango, N.4    Rothman, J.M.5
  • 61
    • 0027265223 scopus 로고
    • A γ-aminobutyric acid transporter driven by a proton pump is present in synaptic-like microvesicles of pancreatic β cells
    • THOMAS-REETZ, A., J.W. HELL, M.J. DURING, C. WALCH-SOLIMENA, R. JAHN, P. DE CAMILLI (1993) A γ-aminobutyric acid transporter driven by a proton pump is present in synaptic-like microvesicles of pancreatic β cells. Proc. Natl. Acad. Sci. U.S.A. 90:5317-5321.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 5317-5321
    • Thomas-Reetz, A.1    Hell, J.W.2    During, M.J.3    Walch-Solimena, C.4    Jahn, R.5    De Camilli, P.6
  • 62
    • 0028014432 scopus 로고
    • A role for synaptic vesicles in non-neuronal cells: Clues from pancreatic β cells and from chromaffin cells
    • THOMAS-REETZ, A., P. DE CAMILLI (1994) A role for synaptic vesicles in non-neuronal cells: Clues from pancreatic β cells and from chromaffin cells. FASEB. J. 8:209-216.
    • (1994) FASEB. J. , vol.8 , pp. 209-216
    • Thomas-Reetz, A.1    De Camilli, P.2
  • 63
    • 0023778390 scopus 로고
    • Multiple types of neuronal calcium channels and their selective modulation
    • TSIEN, R.W., D. LIPSCOMBE, D.V. MADISON, K.R. BLEY, A.P. Fox (1988) Multiple types of neuronal calcium channels and their selective modulation. Trends Neurosci. 11:431-438.
    • (1988) Trends Neurosci. , vol.11 , pp. 431-438
    • Tsien, R.W.1    Lipscombe, D.2    Madison, D.V.3    Bley, K.R.4    Fox, A.P.5
  • 64
    • 0026448583 scopus 로고
    • Calcium channels coupled to glutamate release identified by ω-Aga-IVA
    • TURNER, T.J., M.E. ADAMS, K. DUNLAP (1992) Calcium channels coupled to glutamate release identified by ω-Aga-IVA. Science 258:310-313.
    • (1992) Science , vol.258 , pp. 310-313
    • Turner, T.J.1    Adams, M.E.2    Dunlap, K.3
  • 65
    • 0027969112 scopus 로고
    • Glutamate inhibits the isoprenaline-induced raise in melatonin synthesis by organ cultures of rat pineal glands
    • VAN WYK, E., S. DAYA (1994). Glutamate inhibits the isoprenaline-induced raise in melatonin synthesis by organ cultures of rat pineal glands. Med. Sci. Res. 22:635-636.
    • (1994) Med. Sci. Res. , vol.22 , pp. 635-636
    • Van Wyk, E.1    Daya, S.2
  • 67
    • 0025923431 scopus 로고
    • 2+ transients in norepinephrine-stimulated individual H-35 hepatoma cells: Fura-2 digital imaging microscopy and high time-resolution microspectrofluorometry
    • 2+ transients in norepinephrine-stimulated individual H-35 hepatoma cells: Fura-2 digital imaging microscopy and high time-resolution microspectrofluorometry. J. Histochem. Cytochem. 39:1311-1319.
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 1311-1319
    • Yodozawa, S.1    Tsunoda, Y.2    Funai, Y.3    Tashiro, Y.4


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