메뉴 건너뛰기




Volumn 2, Issue 5, 1999, Pages 440-446

Regulation of dense core release from neuroendocrine cells revealed by imaging single exocytic events

Author keywords

[No Author keywords available]

Indexed keywords

BROMOCRIPTINE; CYCLIC AMP; POTASSIUM; PROLACTIN;

EID: 0033363497     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/8107     Document Type: Article
Times cited : (140)

References (45)
  • 1
    • 0030044498 scopus 로고    scopus 로고
    • Rapid fluctuations in transmitter release from single vesicles in bovine adrenal chromaffin cells
    • Zhou, Z., Misler, S. & Chow, R. H. Rapid fluctuations in transmitter release from single vesicles in bovine adrenal chromaffin cells. Biophys. J. 70, 1543-1552 (1996).
    • (1996) Biophys. J. , vol.70 , pp. 1543-1552
    • Zhou, Z.1    Misler, S.2    Chow, R.H.3
  • 2
    • 0031035397 scopus 로고    scopus 로고
    • Pre- and postfusion regulation of transmitter release
    • Rahamimoff R. & Fernandez, J. M. Pre- and postfusion regulation of transmitter release. Neuron 18, 17-27 (1997).
    • (1997) Neuron , vol.18 , pp. 17-27
    • Rahamimoff, R.1    Fernandez, J.M.2
  • 3
    • 0026032663 scopus 로고
    • Increased cytosolic calcium stimulates exocytosis in bovine lactotrophs
    • Zorec, R., Sikdar, S. K. & Mason, W. T. Increased cytosolic calcium stimulates exocytosis in bovine lactotrophs. J. Gen. Physiol. 97, 473-497 (1991).
    • (1991) J. Gen. Physiol. , vol.97 , pp. 473-497
    • Zorec, R.1    Sikdar, S.K.2    Mason, W.T.3
  • 4
    • 0021063085 scopus 로고
    • Thyrotropin-releasing hormone rapidly activates the phosphodiester hydrolysis of polyphosphoinositides in GH3 pituitary cells. Evidence for the role of a polyphosphoinositide-specific phospholipase C in hormone action
    • Martin, T. F. Thyrotropin-releasing hormone rapidly activates the phosphodiester hydrolysis of polyphosphoinositides in GH3 pituitary cells. Evidence for the role of a polyphosphoinositide-specific phospholipase C in hormone action. J. Biol. Chem. 258, 14816-14822 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 14816-14822
    • Martin, T.F.1
  • 5
    • 0029016670 scopus 로고
    • Three phases of TRH-induced facilitation of exocytosis by single lactotrophs
    • Fomina, A. F. & Levitan, E. S. Three phases of TRH-induced facilitation of exocytosis by single lactotrophs. J. Neurosci. 15, 4982-4991 (1995).
    • (1995) J. Neurosci. , vol.15 , pp. 4982-4991
    • Fomina, A.F.1    Levitan, E.S.2
  • 6
    • 0025319664 scopus 로고
    • Regulation of prolactin secretion at the level of the lactotroph
    • Lamberts, S. W. & Macleod, R. M. Regulation of prolactin secretion at the level of the lactotroph. Physiol. Rev. 70, 279-318 (1990).
    • (1990) Physiol. Rev. , vol.70 , pp. 279-318
    • Lamberts, S.W.1    Macleod, R.M.2
  • 7
    • 7144259743 scopus 로고    scopus 로고
    • A prolactin-releasing peptide in the brain
    • Hinuma S. et al. A prolactin-releasing peptide in the brain. Nature 393, 272-276 (1998).
    • (1998) Nature , vol.393 , pp. 272-276
    • Hinuma, S.1
  • 8
    • 0018376707 scopus 로고
    • Dopamine inhibits adenylate cyclase in human prolactin-secreting pituitary adenomas
    • De Camilli, P., Macconi, D. & Spada, A. Dopamine inhibits adenylate cyclase in human prolactin-secreting pituitary adenomas. Nature 278, 252-254 (1979).
    • (1979) Nature , vol.278 , pp. 252-254
    • De Camilli, P.1    Macconi, D.2    Spada, A.3
  • 9
    • 0023615353 scopus 로고
    • An islet-activating protein-sensitive g protein is involved in dopamine inhibition of angiotensin and thyrotropin-releasing hormone-stimulated inositol phosphate production in anterior pituitary cells
    • Journot, L. et al. An islet-activating protein-sensitive G protein is involved in dopamine inhibition of angiotensin and thyrotropin-releasing hormone-stimulated inositol phosphate production in anterior pituitary cells. J. Biol. Chem. 262, 1506-15110 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 1506-15110
    • Journot, L.1
  • 10
    • 0027477778 scopus 로고
    • Guanine nucleotide binding proteins mediate D2 dopamine receptor activation of a potassium channel in rat lactotrophs
    • Einhorn, L. C. & Oxford, G. S. Guanine nucleotide binding proteins mediate D2 dopamine receptor activation of a potassium channel in rat lactotrophs. J. Physiol (Lond) 462, 563-578 (1993).
    • (1993) J. Physiol (Lond) , vol.462 , pp. 563-578
    • Einhorn, L.C.1    Oxford, G.S.2
  • 12
    • 0029035666 scopus 로고
    • Structural variants of prolactin: Occurrence and physiological significance
    • Sinha, Y. N. Structural variants of prolactin: occurrence and physiological significance. Endocr. Rev. 16, 354-369 (1995).
    • (1995) Endocr. Rev. , vol.16 , pp. 354-369
    • Sinha, Y.N.1
  • 13
    • 0014107427 scopus 로고
    • Secretion of a chromaffin granule protein, chromogranin, from the adrenal gland after splanchnic stimulation
    • Blaschko, H., Comiline, R. S., Schneider, R. H., Silver, M. & Smith, A. D. Secretion of a chromaffin granule protein, chromogranin, from the adrenal gland after splanchnic stimulation. Nature 215, 58-59 (1967).
    • (1967) Nature , vol.215 , pp. 58-59
    • Blaschko, H.1    Comiline, R.S.2    Schneider, R.H.3    Silver, M.4    Smith, A.D.5
  • 14
    • 0029925501 scopus 로고    scopus 로고
    • A morphometric analysis of exocytosis in KC1-stimulated bovine chromaffin cells
    • Fox, G. Q. A morphometric analysis of exocytosis in KC1-stimulated bovine chromaffin cells. Cell Tissue Res. 284, 303-316 (1996).
    • (1996) Cell Tissue Res. , vol.284 , pp. 303-316
    • Fox, G.Q.1
  • 15
    • 0031425428 scopus 로고    scopus 로고
    • Ultrastructural organization of bovine chromaffin cell cortex - Analysis by cryofixation and morphometry of aspects pertinent to exocytosis
    • Plattner, H., Artalejo, A. R. & Neher, E. Ultrastructural organization of bovine chromaffin cell cortex - analysis by cryofixation and morphometry of aspects pertinent to exocytosis. J. Cell Biol. 139, 1709-1717 (1997).
    • (1997) J. Cell Biol. , vol.139 , pp. 1709-1717
    • Plattner, H.1    Artalejo, A.R.2    Neher, E.3
  • 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
    • 0026536634 scopus 로고
    • Activity-dependent fluorescent staining and destaining of living vertebrate motor nerve terminals
    • Betz, W. J., Mao, F. & Bewick, G. S. Activity-dependent fluorescent staining and destaining of living vertebrate motor nerve terminals. J. Neurosci. 12, 363-375 (1992).
    • (1992) J. Neurosci. , vol.12 , pp. 363-375
    • Betz, W.J.1    Mao, F.2    Bewick, G.S.3
  • 18
    • 0032937384 scopus 로고    scopus 로고
    • Monitoring secretory membrane with FM1-43 fluorescence
    • Cochilla, A. J., Angleson, J. K. & Betz, W. J. Monitoring secretory membrane with FM1-43 fluorescence. Annu. Rev. Neurosci. 22, 1-10 (1999).
    • (1999) Annu. Rev. Neurosci. , vol.22 , pp. 1-10
    • Cochilla, A.J.1    Angleson, J.K.2    Betz, W.J.3
  • 19
    • 0029972449 scopus 로고    scopus 로고
    • Simultaneous independent measurement of endocytosis and exocytosis
    • Smith, C. B. & Betz, W. J. Simultaneous independent measurement of endocytosis and exocytosis. Nature 380, 531-534 (1996).
    • (1996) Nature , vol.380 , pp. 531-534
    • Smith, C.B.1    Betz, W.J.2
  • 21
    • 0027286691 scopus 로고
    • Focal exocytosis by eosinophils - Compound exocytosis and cumulative fusion
    • Scepek, S. & Lindau, M. Focal exocytosis by eosinophils - compound exocytosis and cumulative fusion. EMBO J. 12, 1811-1817 (1993).
    • (1993) EMBO J. , vol.12 , pp. 1811-1817
    • Scepek, S.1    Lindau, M.2
  • 22
    • 0023656592 scopus 로고
    • 2+ increases in rat lactotroph cells
    • 2+ increases in rat lactotroph cells. J. Biol. Chem. 262, 13920-13927 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 13920-13927
    • Malgaroli, A.1
  • 23
    • 0028310392 scopus 로고
    • Different G proteins are involved in the biphasic response of clonal rat pituitary cells to thyrotropin-releasing hormone
    • Bauer, C. K., Davison, I., Kubasov, I., Schwarz, J. R. & Mason, W. T. Different G proteins are involved in the biphasic response of clonal rat pituitary cells to thyrotropin-releasing hormone. Pflugers Arch. 428, 17-25 (1994).
    • (1994) Pflugers Arch. , vol.428 , pp. 17-25
    • Bauer, C.K.1    Davison, I.2    Kubasov, I.3    Schwarz, J.R.4    Mason, W.T.5
  • 24
    • 0023879644 scopus 로고
    • Morphological characterisation of lactotrophs separated from the bovine pituitary by a rapid enrichment technique
    • Ingram, D., Keefe, P. D., Wooding, F. B. & Bicknell, R. J. Morphological characterisation of lactotrophs separated from the bovine pituitary by a rapid enrichment technique. Cell Tissue Res. 252, 655-659 (1988).
    • (1988) Cell Tissue Res. , vol.252 , pp. 655-659
    • Ingram, D.1    Keefe, P.D.2    Wooding, F.B.3    Bicknell, R.J.4
  • 25
    • 0030010317 scopus 로고    scopus 로고
    • FM1-43 dye ultrastructural localization in and release from frog motor nerve terminals
    • Henkel, A. W., Lubke, J. & Betz, W. J. FM1-43 dye ultrastructural localization in and release from frog motor nerve terminals. Proc. Natl. Acad. Sci. USA 93, 1918-1923 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1918-1923
    • Henkel, A.W.1    Lubke, J.2    Betz, W.J.3
  • 26
    • 0016374051 scopus 로고
    • Misplaced exocytosis
    • Horvath, E. & Kovacs, K. Misplaced exocytosis. Arch. Pathol. 97, 221-224 (1974).
    • (1974) Arch. Pathol. , vol.97 , pp. 221-224
    • Horvath, E.1    Kovacs, K.2
  • 27
    • 0020674554 scopus 로고
    • Ultrastructural aspects of the effect of calcium ionophore A23187 on incubated anterior pituitary cells of rats
    • Fujita, H., Kuromi, H. & Miyagawa J. Ultrastructural aspects of the effect of calcium ionophore A23187 on incubated anterior pituitary cells of rats. Cell Tissue Res. 129-136 (1983).
    • (1983) Cell Tissue Res. , pp. 129-136
    • Fujita, H.1    Kuromi, H.2    Miyagawa, J.3
  • 28
    • 0026346320 scopus 로고
    • Decreased prolactin level in secretory granules and their increased exocytosis in estrogen-induced pituitary hyperplasia in rats treated with a dopamine agonist
    • Maeda, T., Sawada, K., Itoh, Y., Moriwaki, K. & Mori, H. Decreased prolactin level in secretory granules and their increased exocytosis in estrogen-induced pituitary hyperplasia in rats treated with a dopamine agonist. Lab. Invest. 65, 679-687 (1991).
    • (1991) Lab. Invest. , vol.65 , pp. 679-687
    • Maeda, T.1    Sawada, K.2    Itoh, Y.3    Moriwaki, K.4    Mori, H.5
  • 29
    • 0026643657 scopus 로고
    • Dissociation of dopamine from its receptor as a signal in the pleitropic hypothalamic regulation of prolactin secretion
    • Martinez de la Escalera, G. M. & Weiner, R. I. Dissociation of dopamine from its receptor as a signal in the pleitropic hypothalamic regulation of prolactin secretion. Endocr. Rev. 13, 241-254 (1992).
    • (1992) Endocr. Rev. , vol.13 , pp. 241-254
    • Martinez De La Escalera, G.M.1    Weiner, R.I.2
  • 30
    • 0030670913 scopus 로고    scopus 로고
    • The cortical actin cytoskeleton of lactotropes as an intracellular target for the control of prolactin secretion
    • Carbajal, M. E. & Vitale, J. L. The cortical actin cytoskeleton of lactotropes as an intracellular target for the control of prolactin secretion. Endocrinology 138, 5374-5384 (1997).
    • (1997) Endocrinology , vol.138 , pp. 5374-5384
    • Carbajal, M.E.1    Vitale, J.L.2
  • 31
    • 0021222929 scopus 로고
    • Competitive cAMP antagonists for cAMP-receptor proteins
    • Van Hasstert, P. J. Competitive cAMP antagonists for cAMP-receptor proteins. J. Biol. Chem. 259, 10020-10024 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 10020-10024
    • Van Hasstert, P.J.1
  • 32
    • 0001477595 scopus 로고
    • cAMP analogs promote survival and neurite outgrowth in cultures of rat sympathetic and sensory neurons independently of nerve growth factor
    • Rydel, R. E. & Greene, L. A. cAMP analogs promote survival and neurite outgrowth in cultures of rat sympathetic and sensory neurons independently of nerve growth factor. Proc. Natl. Acad. Sci. USA 85, 1257-1261 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1257-1261
    • Rydel, R.E.1    Greene, L.A.2
  • 33
    • 0028800961 scopus 로고
    • Direct membrane retrieval into large vesicles after exocytosis in sea urchin eggs
    • Whalley, T., Terasaki, M., Cho, M.-S. & Vogel, S. S. Direct membrane retrieval into large vesicles after exocytosis in sea urchin eggs. J. Cell Biol. 131, 1183-1192 (1995).
    • (1995) J. Cell Biol. , vol.131 , pp. 1183-1192
    • Whalley, T.1    Terasaki, M.2    Cho, M.-S.3    Vogel, S.S.4
  • 34
    • 0022981170 scopus 로고
    • Anti-prolactin cell-surface immunoreactivity identifies a subpopulation of lactotrophs from the rat anterior pituitary
    • St. John, P. A., Dufy-Barbe, L. & Barker, J. L. Anti-prolactin cell-surface immunoreactivity identifies a subpopulation of lactotrophs from the rat anterior pituitary. Endocrinology 119, 2783-2795 (1986).
    • (1986) Endocrinology , vol.119 , pp. 2783-2795
    • St John, P.A.1    Dufy-Barbe, L.2    Barker, J.L.3
  • 35
    • 0028167819 scopus 로고
    • 2 dopamine receptors and calcium channels in lactotrophs from cycling female rats
    • 2 dopamine receptors and calcium channels in lactotrophs from cycling female rats. Endocrinology 135, 501-508 (1994).
    • (1994) Endocrinology , vol.135 , pp. 501-508
    • Rendt, J.1    Oxford, G.S.2
  • 36
    • 0019163936 scopus 로고
    • Molecular size variants of prolactin and growth hormone in mouse serum: Strain differences and alterations of concentration by physiological and pharmacological stimuli
    • Sinha, Y. N. Molecular size variants of prolactin and growth hormone in mouse serum: strain differences and alterations of concentration by physiological and pharmacological stimuli. Endocrinology 107, 1959-1969 (1980).
    • (1980) Endocrinology , vol.107 , pp. 1959-1969
    • Sinha, Y.N.1
  • 37
    • 0026475392 scopus 로고
    • Immunoradiometric analysis of circulating human glycosylated and nonglycosylated prolactin forms: Spontaneous and stimulated secretions
    • Brue, T. Immunoradiometric analysis of circulating human glycosylated and nonglycosylated prolactin forms: spontaneous and stimulated secretions. J. Clin. Endocrinol. Metab. 75, 1338-1344 (1992).
    • (1992) J. Clin. Endocrinol. Metab. , vol.75 , pp. 1338-1344
    • Brue, T.1
  • 38
    • 0019520090 scopus 로고
    • Identification of a less immunoreactive form of prolactin in the rat pituitary
    • Sinha, Y. N. & Gilligan, T. A. Identification of a less immunoreactive form of prolactin in the rat pituitary. Endocrinology 108, 1091-1094 (1981).
    • (1981) Endocrinology , vol.108 , pp. 1091-1094
    • Sinha, Y.N.1    Gilligan, T.A.2
  • 39
    • 0028180154 scopus 로고
    • G(i)alpha2- and G(o) alpha-mediated signaling in the Pit-1 dependent inhibition of the prolactin gene promoter. Control of transcription by dopamine D2 receptors
    • Lew, A. M., Yao, H. & Elsholtz, H. P. G(i)alpha2- and G(o) alpha-mediated signaling in the Pit-1 dependent inhibition of the prolactin gene promoter. Control of transcription by dopamine D2 receptors. J. Biol. Chem. 269, 12007-12013 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 12007-12013
    • Lew, A.M.1    Yao, H.2    Elsholtz, H.P.3
  • 41
    • 0030043593 scopus 로고    scopus 로고
    • Secretory granule content proteins and the luminal domains of granule membrane proteins aggregate in vitro at mildly acidic pH
    • Colomer, V., Kicska, G. A. & Rindler, M. J. Secretory granule content proteins and the luminal domains of granule membrane proteins aggregate in vitro at mildly acidic pH. J. Biol. Chem. 271, 48-55 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 48-55
    • Colomer, V.1    Kicska, G.A.2    Rindler, M.J.3
  • 42
    • 0033068183 scopus 로고    scopus 로고
    • 2+-induced deprotonation of peptide hormones inside secretory vesicles in preparation for release
    • 2+-induced deprotonation of peptide hormones inside secretory vesicles in preparation for release. J. Neurosci. 19, 900-905 (1999).
    • (1999) J. Neurosci. , vol.19 , pp. 900-905
    • Han, W.1    Li, D.2    Stout, A.K.3    Takimoto, K.4    Levitan, E.S.5
  • 43
    • 84979376595 scopus 로고
    • Mechanosensitivity of voltagegated calcium currents in rat anterior pituitary cells
    • Ben-Tabou, S., Keller, E. & Nussinovitch, I. Mechanosensitivity of voltagegated calcium currents in rat anterior pituitary cells. J. Physiol. (Lond) 476, 29-39 (1994).
    • (1994) J. Physiol. (Lond) , vol.476 , pp. 29-39
    • Ben-Tabou, S.1    Keller, E.2    Nussinovitch, I.3
  • 44
    • 0023858306 scopus 로고
    • Patch-clamp techniques for time resolved capacitance measurements in single cells
    • Lindau, M. & Neher, E. Patch-clamp techniques for time resolved capacitance measurements in single cells. Pflugers Arch. 411, 137-146 (1988).
    • (1988) Pflugers Arch. , vol.411 , pp. 137-146
    • Lindau, M.1    Neher, E.2
  • 45
    • 0031761396 scopus 로고    scopus 로고
    • Effects of cellular interactions on calcium dynamics in prolactin-secreting cells
    • Abraham, E. J., Villalobos, C. & Frawley, L. S. Effects of cellular interactions on calcium dynamics in prolactin-secreting cells. Endocrinology 139, 2988-2993 (1998).
    • (1998) Endocrinology , vol.139 , pp. 2988-2993
    • Abraham, E.J.1    Villalobos, C.2    Frawley, L.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.