메뉴 건너뛰기




Volumn 8, Issue 2, 2005, Pages 173-178

Activity-dependent liberation of synaptic neuropeptide vesicles

Author keywords

[No Author keywords available]

Indexed keywords

ATRIAL NATRIURETIC FACTOR; CALCIUM ION; GREEN FLUORESCENT PROTEIN; NEUROPEPTIDE;

EID: 13244291589     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/nn1377     Document Type: Article
Times cited : (101)

References (37)
  • 1
    • 0030075194 scopus 로고    scopus 로고
    • Peptidergic transmission: From morphological correlates to functional implications
    • Zupanc, G.K. Peptidergic transmission: from morphological correlates to functional implications. Micron. 27, 35-91 (1996).
    • (1996) Micron. , vol.27 , pp. 35-91
    • Zupanc, G.K.1
  • 3
    • 0041342066 scopus 로고    scopus 로고
    • Drosophila neuropeptide signaling
    • Taghert, P.H. & Veenstra, J.A. Drosophila neuropeptide signaling. Adv. Genet. 49, 1-65 (2003).
    • (2003) Adv. Genet. , vol.49 , pp. 1-65
    • Taghert, P.H.1    Veenstra, J.A.2
  • 4
    • 0024331496 scopus 로고
    • Frequency-dependent release of peptide cotransmitters from identified cholinergic motor neurons of Aplysia
    • Whim, M.D. & Lloyd, P.E. Frequency-dependent release of peptide cotransmitters from identified cholinergic motor neurons of Aplysia. Proc. Natl. Acad. Sci. USA 86, 9034-9038 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9034-9038
    • Whim, M.D.1    Lloyd, P.E.2
  • 5
    • 0028097540 scopus 로고
    • The molecular machinery for fast and slow neurosecretion
    • Martin, T.F. The molecular machinery for fast and slow neurosecretion. Curr. Opin. Neurobiol. 4, 626-632 (1994).
    • (1994) Curr. Opin. Neurobiol. , vol.4 , pp. 626-632
    • Martin, T.F.1
  • 6
    • 1242310783 scopus 로고    scopus 로고
    • High mobility of vesicles supports continuous exocytosis at a ribbon synapse
    • Holt, M., Cooke, A., Neef, A. & Lagnado, L. High mobility of vesicles supports continuous exocytosis at a ribbon synapse. Curr. Biol. 14, 173-183 (2004).
    • (2004) Curr. Biol. , vol.14 , pp. 173-183
    • Holt, M.1    Cooke, A.2    Neef, A.3    Lagnado, L.4
  • 7
    • 1542358809 scopus 로고    scopus 로고
    • Streamlined synaptic vesicle cycle in cone photoreceptor terminals
    • Rea, R. et al. Streamlined synaptic vesicle cycle in cone photoreceptor terminals. Neuron 41, 755-766 (2004).
    • (2004) Neuron , vol.41 , pp. 755-766
    • Rea, R.1
  • 8
    • 0029885396 scopus 로고    scopus 로고
    • Synaptic vesicle movements monitored by fluorescence recovery after photobleaching in nerve terminals stained with FM1-43
    • Henkel, A.W., Simpson, L.L., Ridge, R.M. & Betz, W.J. Synaptic vesicle movements monitored by fluorescence recovery after photobleaching in nerve terminals stained with FM1-43. J. Neurosci. 16, 3960-3967 (1996).
    • (1996) J. Neurosci. , vol.16 , pp. 3960-3967
    • Henkel, A.W.1    Simpson, L.L.2    Ridge, R.M.3    Betz, W.J.4
  • 9
    • 0029812769 scopus 로고    scopus 로고
    • Mobility of synaptic vesicles in nerve endings monitored by recovery from photobleaching of synaptic vesicle-associated fluorescence
    • Kraszewski, K., Daniell, L., Mundigl, O. & DeCamilli, P. Mobility of synaptic vesicles in nerve endings monitored by recovery from photobleaching of synaptic vesicle-associated fluorescence. J. Neurosci. 16, 5905-5913 (1996).
    • (1996) J. Neurosci. , vol.16 , pp. 5905-5913
    • Kraszewski, K.1    Daniell, L.2    Mundigl, O.3    DeCamilli, P.4
  • 10
    • 0037101566 scopus 로고    scopus 로고
    • Physical mobilization of secretory vesicles facilitates neuropeptide release by nerve growth factor-differentiated PC12 cells
    • Ng, Y.K., Lu, X. & Levitan, E.S. Physical mobilization of secretory vesicles facilitates neuropeptide release by nerve growth factor-differentiated PC12 cells. J. Physiol. 542, 395-402 (2002).
    • (2002) J. Physiol. , vol.542 , pp. 395-402
    • Ng, Y.K.1    Lu, X.2    Levitan, E.S.3
  • 11
    • 0043210732 scopus 로고    scopus 로고
    • Calcium regulates exocytosis at the level of single vesicles
    • Becherer, U., Moser, T., Stuhmer, W. & Oheim, M. Calcium regulates exocytosis at the level of single vesicles. Nat. Neurosci. 6, 846-853 (2003).
    • (2003) Nat. Neurosci. , vol.6 , pp. 846-853
    • Becherer, U.1    Moser, T.2    Stuhmer, W.3    Oheim, M.4
  • 12
  • 13
    • 0029048850 scopus 로고
    • Exocytosis in peptidergic nerve terminals exhibits two calcium-sensitive phases during pulsatile calcium entry
    • Seward, E.P., Chernevskaya, N.I. & Nowycky, M.C. Exocytosis in peptidergic nerve terminals exhibits two calcium-sensitive phases during pulsatile calcium entry. J. Neurosci. 15, 3390-3399 (1995).
    • (1995) J. Neurosci. , vol.15 , pp. 3390-3399
    • Seward, E.P.1    Chernevskaya, N.I.2    Nowycky, M.C.3
  • 14
    • 0034666115 scopus 로고    scopus 로고
    • Temporal pattern dependence of neuronal peptide transmitter release: Models and experiments
    • Brezina, V., Church, P.J. & Weiss, K.R. Temporal pattern dependence of neuronal peptide transmitter release: models and experiments. J. Neurosci. 20, 6760-6772 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 6760-6772
    • Brezina, V.1    Church, P.J.2    Weiss, K.R.3
  • 15
    • 0037019296 scopus 로고    scopus 로고
    • Intracellular calcium stores regulate activity-dependent neuropeptide release from dendrites
    • Ludwig, M. et al. Intracellular calcium stores regulate activity-dependent neuropeptide release from dendrites. Nature 418, 85-89 (2002).
    • (2002) Nature , vol.418 , pp. 85-89
    • Ludwig, M.1
  • 16
    • 0030855088 scopus 로고    scopus 로고
    • Transport, docking and exocytosis of single secretory granules in live chromaffin cells
    • Steyer, J.A., Horstmann, H. & Almers, W. Transport, docking and exocytosis of single secretory granules in live chromaffin cells. Nature 388, 474-478 (1997).
    • (1997) Nature , vol.388 , pp. 474-478
    • Steyer, J.A.1    Horstmann, H.2    Almers, W.3
  • 17
    • 0036261251 scopus 로고    scopus 로고
    • Fast insulin secretion reflects exocytosis of docked granules in mouse pancreatic B-cells
    • Olofsson, C.S. et al. Fast insulin secretion reflects exocytosis of docked granules in mouse pancreatic B-cells. Pflugers Arch. 444, 43-51 (2002).
    • (2002) Pflugers Arch. , vol.444 , pp. 43-51
    • Olofsson, C.S.1
  • 18
    • 0037435034 scopus 로고    scopus 로고
    • Functional and spatial segregation of secretory vesicle pools according to vesicle age
    • Duncan, R.R. et al. Functional and spatial segregation of secretory vesicle pools according to vesicle age. Nature 422, 176-180 (2003).
    • (2003) Nature , vol.422 , pp. 176-180
    • Duncan, R.R.1
  • 19
    • 0033460188 scopus 로고    scopus 로고
    • Neuropeptide release by efficient recruitment of diffusing cytoplasmic secretory vesicles
    • Han, W., Ng, Y.K., Axelrod, D. & Levitan, E.S. Neuropeptide release by efficient recruitment of diffusing cytoplasmic secretory vesicles. Proc. Natl. Acad. Sci. USA 96, 14577-14582 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14577-14582
    • Han, W.1    Ng, Y.K.2    Axelrod, D.3    Levitan, E.S.4
  • 20
    • 0038101465 scopus 로고    scopus 로고
    • Unexpected mobility variation among individual secretory vesicles produces an apparent refractory neuropeptide pool
    • Ng, Y.K. et al. Unexpected mobility variation among individual secretory vesicles produces an apparent refractory neuropeptide pool. Biophys. J. 84, 4127-4134 (2003).
    • (2003) Biophys. J. , vol.84 , pp. 4127-4134
    • Ng, Y.K.1
  • 21
    • 0030830742 scopus 로고    scopus 로고
    • Neuronal peptide release is limited by secretory granule mobility
    • Burke, N.V. et al. Neuronal peptide release is limited by secretory granule mobility. Neuron 19, 1095-1102 (1997).
    • (1997) Neuron , vol.19 , pp. 1095-1102
    • Burke, N.V.1
  • 22
    • 2942558730 scopus 로고    scopus 로고
    • Using GFP to image peptide hormone and neuropeptide release in vitro and in vivo
    • Levitan, E.S. Using GFP to image peptide hormone and neuropeptide release in vitro and in vivo. Methods 33, 281-286 (2004).
    • (2004) Methods , vol.33 , pp. 281-286
    • Levitan, E.S.1
  • 23
    • 0035889713 scopus 로고    scopus 로고
    • Visualization of neuropeptide expression, transport, and exocytosis in Drosophila melanogaster
    • Rao, S., Lang, C., Levitan, E.S. & Deitcher, D.L. Visualization of neuropeptide expression, transport, and exocytosis in Drosophila melanogaster. J. Neurobiol. 49, 159-172 (2001).
    • (2001) J. Neurobiol. , vol.49 , pp. 159-172
    • Rao, S.1    Lang, C.2    Levitan, E.S.3    Deitcher, D.L.4
  • 24
    • 0027325492 scopus 로고
    • Differential ultrastructure of synaptic terminals on ventral longitudinal abdominal muscles in Drosophila larvae
    • Atwood, H.L., Govind, C.K. & Wu, C.F. Differential ultrastructure of synaptic terminals on ventral longitudinal abdominal muscles in Drosophila larvae. J. Neurobiol. 24, 1008-1024 (1993).
    • (1993) J. Neurobiol. , vol.24 , pp. 1008-1024
    • Atwood, H.L.1    Govind, C.K.2    Wu, C.F.3
  • 25
    • 0027301138 scopus 로고
    • Ultrastructure of neuromuscular junctions in Drosophila: Comparison of wild type and mutants with increased excitability
    • Jia, X.X., Gorczyca, M. & Budnik, V. Ultrastructure of neuromuscular junctions in Drosophila: comparison of wild type and mutants with increased excitability. J. Neurobiol. 24, 1025-1044 (1993).
    • (1993) J. Neurobiol. , vol.24 , pp. 1025-1044
    • Jia, X.X.1    Gorczyca, M.2    Budnik, V.3
  • 26
    • 1942485371 scopus 로고    scopus 로고
    • Use of targetable GFP-tagged neuropeptide for visualizing neuropeptide release following execution of a behavior
    • Husain, Q.M. & Ewer, J. Use of targetable GFP-tagged neuropeptide for visualizing neuropeptide release following execution of a behavior. J. Neurobiol. 59, 181-191 (2004).
    • (2004) J. Neurobiol. , vol.59 , pp. 181-191
    • Husain, Q.M.1    Ewer, J.2
  • 27
    • 1942437414 scopus 로고    scopus 로고
    • Mating, seminal fluid components, and sperm cause changes in vesicle release in the Drosophila female reproductive tract
    • Heifetz, Y. & Wolfner, M.F. Mating, seminal fluid components, and sperm cause changes in vesicle release in the Drosophila female reproductive tract. Proc. Natl. Acad. Sci. USA 101, 6261-6266 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6261-6266
    • Heifetz, Y.1    Wolfner, M.F.2
  • 28
    • 0017089101 scopus 로고
    • Properties of the larval neuromuscular junction in Drosophila melanogaster
    • Jan, L.Y. & Jan, Y.N. Properties of the larval neuromuscular junction in Drosophila melanogaster. J. Physiol. 262, 189-214 (1976).
    • (1976) J. Physiol. , vol.262 , pp. 189-214
    • Jan, L.Y.1    Jan, Y.N.2
  • 29
    • 0028483237 scopus 로고
    • Improved stability of Drosophila larval neuromuscular preparations in haemolymph-like physiological solutions
    • Stewart, B.A., Atwood, H.L., Renger, J.J., Wang, J. & Wu, C.F. Improved stability of Drosophila larval neuromuscular preparations in haemolymph-like physiological solutions. J. Comp. Physiol. A 175, 179-191 (1994).
    • (1994) J. Comp. Physiol. A , vol.175 , pp. 179-191
    • Stewart, B.A.1    Atwood, H.L.2    Renger, J.J.3    Wang, J.4    Wu, C.F.5
  • 30
    • 0036488823 scopus 로고    scopus 로고
    • Impairment of central pattern generation in Drosophila cysteine string protein mutants
    • Barclay, J.W., Atwood, H.L. & Robertson, R.M. Impairment of central pattern generation in Drosophila cysteine string protein mutants. J. Comp. Physiol A. 188, 71-78 (2002).
    • (2002) J. Comp. Physiol A , vol.188 , pp. 71-78
    • Barclay, J.W.1    Atwood, H.L.2    Robertson, R.M.3
  • 31
    • 0034970918 scopus 로고    scopus 로고
    • Blockade of the central generator of locomotor rhythm by noncompetitive NMDA receptor antagonists in Drosophila larvae
    • Cattaert, D. & Birman, S. Blockade of the central generator of locomotor rhythm by noncompetitive NMDA receptor antagonists in Drosophila larvae. J. Neurobiol. 48, 58-73 (2001).
    • (2001) J. Neurobiol. , vol.48 , pp. 58-73
    • Cattaert, D.1    Birman, S.2
  • 32
    • 0024425922 scopus 로고
    • Modification of the microtubule-binding and ATPase activities of kinesin by N-ethylmaleimide (NEM) suggests a role for sulfhydryls in fast axonal transport
    • Pfister, K.K., Wagner, M.C., Bloom, G.S. & Brady, S.T. Modification of the microtubule-binding and ATPase activities of kinesin by N-ethylmaleimide (NEM) suggests a role for sulfhydryls in fast axonal transport. Biochemistry 28, 9006-9012 (1989).
    • (1989) Biochemistry , vol.28 , pp. 9006-9012
    • Pfister, K.K.1    Wagner, M.C.2    Bloom, G.S.3    Brady, S.T.4
  • 33
    • 0033578419 scopus 로고    scopus 로고
    • N-ethylmaleimide inhibits Ncd motor function by modification of a cysteine in the stalk domain
    • Phelps, K.K. & Walker, R.A. N-ethylmaleimide inhibits Ncd motor function by modification of a cysteine in the stalk domain. Biochemistry 38, 10750-10757 (1999).
    • (1999) Biochemistry , vol.38 , pp. 10750-10757
    • Phelps, K.K.1    Walker, R.A.2
  • 34
    • 13244281307 scopus 로고
    • The action of thiol reagents on the adenosine-triphosphatase activities of heavy meromyosin and L-myosin
    • Perry, S.V. & Cotterill, J. The action of thiol reagents on the adenosine-triphosphatase activities of heavy meromyosin and L-myosin. Biochem. J. 96, 224-230 (1965).
    • (1965) Biochem. J. , vol.96 , pp. 224-230
    • Perry, S.V.1    Cotterill, J.2
  • 35
    • 0034517694 scopus 로고    scopus 로고
    • Size of vesicle pools, rates of mobilization, and recycling at neuromuscular synapses of a Drosophila mutant, shibire
    • Delgado, R., Maureira, C., Oliva, C., Kidokoro, Y. & Labarca, P. Size of vesicle pools, rates of mobilization, and recycling at neuromuscular synapses of a Drosophila mutant, shibire. Neuron 28, 941-953 (2000).
    • (2000) Neuron , vol.28 , pp. 941-953
    • Delgado, R.1    Maureira, C.2    Oliva, C.3    Kidokoro, Y.4    Labarca, P.5
  • 36
    • 1642296166 scopus 로고    scopus 로고
    • The structural organization of the readily releasable pool of synaptic vesicles
    • Rizzoli, S.O. & Betz, W.J. The structural organization of the readily releasable pool of synaptic vesicles. Science 303, 2037-2039 (2004).
    • (2004) Science , vol.303 , pp. 2037-2039
    • Rizzoli, S.O.1    Betz, W.J.2
  • 37
    • 0034459678 scopus 로고    scopus 로고
    • Functional interaction between the coactivator Drosophila CREB-binding protein and ASH1, a member of the trithorax group of chromatin modifiers
    • Bantignies, F., Goodman, R.H. & Smolik, S.M. Functional interaction between the coactivator Drosophila CREB-binding protein and ASH1, a member of the trithorax group of chromatin modifiers. Mol. Cell Biol. 20, 9317-9330 (2000).
    • (2000) Mol. Cell Biol. , vol.20 , pp. 9317-9330
    • Bantignies, F.1    Goodman, R.H.2    Smolik, S.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.