메뉴 건너뛰기




Volumn 133, Issue 6, 1996, Pages 1217-1236

Annexin II in exocytosis: Catecholamine secretion requires the translocation of p36 to the subplasmalemmal region in chromaffin cells

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN; LIPOCORTIN 2; NORADRENALIN;

EID: 0030013509     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.133.6.1217     Document Type: Article
Times cited : (104)

References (79)
  • 1
    • 0025291478 scopus 로고
    • The stimulatory effect of calpactin (annexin II) on calcium-dependent exocytosis in adrenal chromaffin cells: Requirement for both the N-terminal and core domains of p36 and ATP
    • Ali, S., and R.D. Burgoyne. 1990. The stimulatory effect of calpactin (annexin II) on calcium-dependent exocytosis in adrenal chromaffin cells: requirement for both the N-terminal and core domains of p36 and ATP. Cell Signal. 2:265-276.
    • (1990) Cell Signal. , vol.2 , pp. 265-276
    • Ali, S.1    Burgoyne, R.D.2
  • 2
    • 0024390672 scopus 로고
    • A role for calpactin in calcium dependent exocytosis in adrenal chromaffin cells
    • Ali, S., M.J. Geisow, and R.D. Burgoyne. 1989. A role for calpactin in calcium dependent exocytosis in adrenal chromaffin cells. Nature (Lond.). 340:313-315.
    • (1989) Nature (Lond.). , vol.340 , pp. 313-315
    • Ali, S.1    Geisow, M.J.2    Burgoyne, R.D.3
  • 3
    • 0019847651 scopus 로고
    • Immunochemical study of microtubules in chromaffin cells in culture and evidence that tubulin is not an integral protein of the chromaffin granule membrane
    • Bader, M.F., J. Ciesielski-Treska, D. Thiersé, J. Hesketh, and D. Aunis. 1981. Immunochemical study of microtubules in chromaffin cells in culture and evidence that tubulin is not an integral protein of the chromaffin granule membrane. J. Neurochem. 37:917-933.
    • (1981) J. Neurochem. , vol.37 , pp. 917-933
    • Bader, M.F.1    Ciesielski-Treska, J.2    Thiersé, D.3    Hesketh, J.4    Aunis, D.5
  • 4
    • 0022979266 scopus 로고
    • Characterization of hormone and protein release from α-toxin-permeabilized chromaffin cells in primary culture
    • Bader, M.F., D. Thiersé, D. Aunis, G. Ahnert-Hilger, and M. Gratzl. 1986. Characterization of hormone and protein release from α-toxin-permeabilized chromaffin cells in primary culture. J. Biol.Chem. 261:5777-5783.
    • (1986) J. Biol.Chem. , vol.261 , pp. 5777-5783
    • Bader, M.F.1    Thiersé, D.2    Aunis, D.3    Ahnert-Hilger, G.4    Gratzl, M.5
  • 5
    • 0026778460 scopus 로고
    • Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett, M.K., N. Calakos, and R.H. Scheller. 1992. Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science (Wash. DC). 257:255-259.
    • (1992) Science (Wash. DC). , vol.257 , pp. 255-259
    • Bennett, M.K.1    Calakos, N.2    Scheller, R.H.3
  • 6
    • 0026450902 scopus 로고
    • S-100 protein hinds to annexin II and p11, the heavy and light chains of calpactin I
    • Bianchi, R., G. Pula, P. Ceccarelli, I. Giambanco, and R. Donato. 1992. S-100 protein hinds to annexin II and p11, the heavy and light chains of calpactin I. Biochem. Biophys. Acta. 1160:67-75.
    • (1992) Biochem. Biophys. Acta. , vol.1160 , pp. 67-75
    • Bianchi, R.1    Pula, G.2    Ceccarelli, P.3    Giambanco, I.4    Donato, R.5
  • 7
    • 0026631563 scopus 로고
    • Synaptotagmin: A calcium sensor on the synaptic vesicle surface
    • Brose, N., A.G. Petrenko, T.C. Südhof, and R. Jahn. 1992. Synaptotagmin: a calcium sensor on the synaptic vesicle surface. Science (Wash. DC). 256: 1021-1025.
    • (1992) Science (Wash. DC) , vol.256 , pp. 1021-1025
    • Brose, N.1    Petrenko, A.G.2    Südhof, T.C.3    Jahn, R.4
  • 9
    • 0024442407 scopus 로고
    • Simultaneous measurements of cytosolic calcium and secretion in single bovine adrenal chromaffin cells by fluorescent imaging of fura-2 in co-cultured cells
    • Cheek, T.R., T.R. Jackson, A.J. O'Sullivan, R.B. Moreton, M.J. Berridge, and R.D. Burgoyne. 1989. Simultaneous measurements of cytosolic calcium and secretion in single bovine adrenal chromaffin cells by fluorescent imaging of fura-2 in co-cultured cells. J. Cell Biol. 109:1219-1227.
    • (1989) J. Cell Biol. , vol.109 , pp. 1219-1227
    • Cheek, T.R.1    Jackson, T.R.2    O'Sullivan, A.J.3    Moreton, R.B.4    Berridge, M.J.5    Burgoyne, R.D.6
  • 10
    • 0026550828 scopus 로고
    • Delay in vesicle fusion revealed by electrochemical monitoring of single secretory events in adrenal chromaffin cells
    • Chow, R.H., L.V. Ruden, and E. Neher. 1992. Delay in vesicle fusion revealed by electrochemical monitoring of single secretory events in adrenal chromaffin cells. Nature (Lond.). 356:60-63.
    • (1992) Nature (Lond.). , vol.356 , pp. 60-63
    • Chow, R.H.1    Ruden, L.V.2    Neher, E.3
  • 11
    • 0026452240 scopus 로고
    • The annexins and exocytosis
    • Creutz, C.E. 1992. The annexins and exocytosis. Science (Wash. DC). 258:924-931.
    • (1992) Science (Wash. DC) , vol.258 , pp. 924-931
    • Creutz, C.E.1
  • 12
    • 0027934987 scopus 로고
    • Secretory and synaptic vesicle membrane proteins and their possible roles in regulated exocytosis
    • Damer, C.K., and C.E. Creutz. 1994. Secretory and synaptic vesicle membrane proteins and their possible roles in regulated exocytosis. Neuroscience. 43: 511-536.
    • (1994) Neuroscience , vol.43 , pp. 511-536
    • Damer, C.K.1    Creutz, C.E.2
  • 13
    • 0023818448 scopus 로고
    • Aggregation of chromaffin granules by calpactin at micromolar levels of calcium
    • Drust, D.S., and C.E. Creutz. 1988. Aggregation of chromaffin granules by calpactin at micromolar levels of calcium. Nature (Land.). 331:88-91.
    • (1988) Nature (Land.). , vol.331 , pp. 88-91
    • Drust, D.S.1    Creutz, C.E.2
  • 14
    • 0029087203 scopus 로고
    • In vivo and in vitro phosphorylation of annexin II in T cells: Potential regulation by annexin V
    • Dubois, T., J.P. Oudinet, F. Russo-Marie, and B. Rothhut. 1995. In vivo and in vitro phosphorylation of annexin II in T cells: potential regulation by annexin V. Biochem. J. 310:243-248.
    • (1995) Biochem. J. , vol.310 , pp. 243-248
    • Dubois, T.1    Oudinet, J.P.2    Russo-Marie, F.3    Rothhut, B.4
  • 17
    • 0028029717 scopus 로고
    • Calcium and membrane-binding properties of monomeric and multimeric Annexin II
    • Evans, T.C., Jr., and G.L. Nelsestuen. 1994. Calcium and membrane-binding properties of monomeric and multimeric Annexin II. Biochemistry. 33: 13231-13238.
    • (1994) Biochemistry , vol.33 , pp. 13231-13238
    • Evans Jr., T.C.1    Nelsestuen, G.L.2
  • 18
    • 0028921025 scopus 로고
    • Annexin XIIIb: A novel epithelial specific annexin is implicated in vesicular traffic to the apical plasma membrane
    • Fiedler, K., F. Lafont, R.G. Parton, and K. Simons. 1995. Annexin XIIIb: a novel epithelial specific annexin is implicated in vesicular traffic to the apical plasma membrane. J. Cell Biol. 128:1043-1053.
    • (1995) J. Cell Biol. , vol.128 , pp. 1043-1053
    • Fiedler, K.1    Lafont, F.2    Parton, R.G.3    Simons, K.4
  • 20
    • 0016192094 scopus 로고
    • -] and ionic strength determined from equilibrium studies of the reaction
    • -] and ionic strength determined from equilibrium studies of the reaction. J. Biol. Chem. 249:3465-3474.
    • (1974) J. Biol. Chem. , vol.249 , pp. 3465-3474
    • Flodgaard, H.1    Fleron, P.2
  • 22
    • 0023321841 scopus 로고
    • Annexins: New family of calcium-regulated phospholipid binding protein
    • Geisow, M.J., J.H. Walker, C. Boustead, and W. Taylor. 1991. Annexins: new family of calcium-regulated phospholipid binding protein. Biosci. Rep. 7: 289-298.
    • (1991) Biosci. Rep. , vol.7 , pp. 289-298
    • Geisow, M.J.1    Walker, J.H.2    Boustead, C.3    Taylor, W.4
  • 23
    • 0021299594 scopus 로고
    • Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush border; calcium dependent binding to non-erythroid spectrin and F-actin
    • Gerke, V., and K. Weber. 1984. Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush border; calcium dependent binding to non-erythroid spectrin and F-actin. EMBO (Eur. Mol. Biol. Organ.) J. 3:227-233.
    • (1984) EMBO (Eur. Mol. Biol. Organ.) J , vol.3 , pp. 227-233
    • Gerke, V.1    Weber, K.2
  • 24
    • 85034621179 scopus 로고
    • Amino-terminal sequence of p36 and associated p10: Identification of the site of tyrosine phosphorylation and homology with S-100
    • Glenney, J.R., and B.T. Tack. 1985. Amino-terminal sequence of p36 and associated p10: identification of the site of tyrosine phosphorylation and homology with S-100. Proc. Natl. Acad. Sci. USA. 83:4258-4262.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4258-4262
    • Glenney, J.R.1    Tack, B.T.2
  • 25
    • 0022996716 scopus 로고
    • Association of the S-100-related calpaclin I light chain with the aminoterminal tail of the 36 kDa heavy chain
    • Glenney, J.R., M. Boudreau, R. Galyean, T. Hunter, and B. Tack. 1986. Association of the S-100-related calpaclin I light chain with the aminoterminal tail of the 36 kDa heavy chain. J. Biol. Chem. 261:10485-10488.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10485-10488
    • Glenney, J.R.1    Boudreau, M.2    Galyean, R.3    Hunter, T.4    Tack, B.5
  • 27
    • 0022755882 scopus 로고
    • The proteintyrosine kinase substrate (p36) is a substrate for protein kinase C in vitro and in viva
    • Gould, K.L., J.R. Woodgett, C.M. Isack, and T. Hunter. 1986. The proteintyrosine kinase substrate (p36) is a substrate for protein kinase C in vitro and in viva. Mol. Cell Biol. 6:2738-2744.
    • (1986) Mol. Cell Biol. , vol.6 , pp. 2738-2744
    • Gould, K.L.1    Woodgett, J.R.2    Isack, C.M.3    Hunter, T.4
  • 28
    • 0020645068 scopus 로고
    • Microinjection of tissue culture cells
    • Graessmann, M., and A. Graessmann. 1983. Microinjection of tissue culture cells. Methods Enzymol. 101:482-492.
    • (1983) Methods Enzymol. , vol.101 , pp. 482-492
    • Graessmann, M.1    Graessmann, A.2
  • 29
    • 0023756854 scopus 로고
    • Induction of neurofilament phosphorylation in cultured chromaffin cells
    • Grant, N., B. Demeneix, D. Aunis, and O.K. Langley. 1988. Induction of neurofilament phosphorylation in cultured chromaffin cells. Neuroscienee. 27: 717-726.
    • (1988) Neuroscienee , vol.27 , pp. 717-726
    • Grant, N.1    Demeneix, B.2    Aunis, D.3    Langley, O.K.4
  • 30
    • 0026523298 scopus 로고
    • Cloning and characterization of the human gene encoding p11: Structural similarity to other members of the S-100 gene family
    • Harder, T., E. Kube, and V. Gerke. 1992. Cloning and characterization of the human gene encoding p11: structural similarity to other members of the S-100 gene family. Gene (Amst.). 113:269-274.
    • (1992) Gene (Amst.). , vol.113 , pp. 269-274
    • Harder, T.1    Kube, E.2    Gerke, V.3
  • 32
    • 0026664632 scopus 로고
    • Resolution of regulated secretion into sequential MgATP-dependent and calcium-dependent stages mediated by distinct cytosolic proteins
    • Hay, J.C., and T.J.F. Martin. 1992. Resolution of regulated secretion into sequential MgATP-dependent and calcium-dependent stages mediated by distinct cytosolic proteins. J. Cell Biol. 119:139-151.
    • (1992) J. Cell Biol. , vol.119 , pp. 139-151
    • Hay, J.C.1    Martin, T.J.F.2
  • 33
    • 0028023444 scopus 로고
    • Calcium dependence of the rate of exocytosis in a synaptic terminal
    • Heidelberger, R., C. Heinemann, E. Neher, and G. Matthews. 1994. Calcium dependence of the rate of exocytosis in a synaptic terminal. Nature (Lond.). 371:513-515.
    • (1994) Nature (Lond.). , vol.371 , pp. 513-515
    • Heidelberger, R.1    Heinemann, C.2    Neher, E.3    Matthews, G.4
  • 34
    • 0024603065 scopus 로고
    • MgATP-independent and MgATP-dependent exocytosis. Evidence that MgATP primes adrenal chromaffin cells to undergo exocytosis
    • Holz, R.W., M.A. Bittner, S.C. Peppers, R.A. Senter, and D.A. Eberhard. 1989. MgATP-independent and MgATP-dependent exocytosis. Evidence that MgATP primes adrenal chromaffin cells to undergo exocytosis. J. Biol. Chem. 264:5412-5419.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5412-5419
    • Holz, R.W.1    Bittner, M.A.2    Peppers, S.C.3    Senter, R.A.4    Eberhard, D.A.5
  • 35
    • 0026575572 scopus 로고
    • Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins
    • Huber, R., R. Berendes, A. Burger, M. Schneider, A. Karshikov, H. Luecke, J. Romish, and E.P. Paques. 1992. Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins. J. Mol. Biol. 223:683-704.
    • (1992) J. Mol. Biol. , vol.223 , pp. 683-704
    • Huber, R.1    Berendes, R.2    Burger, A.3    Schneider, M.4    Karshikov, A.5    Luecke, H.6    Romish, J.7    Paques, E.P.8
  • 36
    • 0029062772 scopus 로고
    • Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells
    • Ikonen, E., M. Tagaya, O. Ullrich, C. Montecucco, and K. Simmons. 1995. Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells. Cell. 81:571-580.
    • (1995) Cell , vol.81 , pp. 571-580
    • Ikonen, E.1    Tagaya, M.2    Ullrich, O.3    Montecucco, C.4    Simmons, K.5
  • 37
    • 0022491787 scopus 로고
    • Binding sites for calcium, lipid and p11 on p36. the substrate of retroviral tyrosine-specific protein kinases
    • Johnsson, N., J. Vanderkerkhove, J. VanDamme, and K. Weber. 1986. Binding sites for calcium, lipid and p11 on p36. the substrate of retroviral tyrosine-specific protein kinases. FEBS Lett. 198:361-364.
    • (1986) FEBS Lett. , vol.198 , pp. 361-364
    • Johnsson, N.1    Vanderkerkhove, J.2    Vandamme, J.3    Weber, K.4
  • 38
    • 0024062670 scopus 로고
    • p36, the major cytoplasmic substrate of src tyrosine protein kinase. binds to its p11 regulatory subunit via a short amino-terminal amphiphatic helix
    • Johnsson, N., G. Marriott, and K. Weber. 1988. p36, the major cytoplasmic substrate of src tyrosine protein kinase. binds to its p11 regulatory subunit via a short amino-terminal amphiphatic helix. EMBO (Eur. Mol. Biol. Organ.) J. 7:2435-2442.
    • (1988) EMBO (Eur. Mol. Biol. Organ.) J , vol.7 , pp. 2435-2442
    • Johnsson, N.1    Marriott, G.2    Weber, K.3
  • 39
    • 0027052218 scopus 로고
    • Phosphorylation of annexin II tetramer by protein kinase C inhibits aggregation of lipid vesicles by the protein
    • Johnstone, S.A., I. Hubaishy, and D.M. Waisman. 1992. Phosphorylation of annexin II tetramer by protein kinase C inhibits aggregation of lipid vesicles by the protein. J. Biol. Chem. 267:25976-25981.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25976-25981
    • Johnstone, S.A.1    Hubaishy, I.2    Waisman, D.M.3
  • 41
    • 0028072888 scopus 로고
    • Annexin 3 is associated with cytoplasmic granules in neutrophils and monocytes and translocates to the plasma membrane in activated cells
    • LeCabec, V., and I. Maridonneau-Parini. 1994. Annexin 3 is associated with cytoplasmic granules in neutrophils and monocytes and translocates to the plasma membrane in activated cells. Biochem. J. 303:481-487.
    • (1994) Biochem. J. , vol.303 , pp. 481-487
    • LeCabec, V.1    Maridonneau-Parini, I.2
  • 42
    • 0025111205 scopus 로고
    • Nicotinic-receptor mediated catecholamine secretion from individual chromaffin cells : Chemical evidence for exocytosis
    • Leszczyszyn, D.J., J.A. Jankowsky, O.H. Viveros, E.J. Diliberto, J.A. Near, and R.M. Wightman. 1991. Nicotinic-receptor mediated catecholamine secretion from individual chromaffin cells : chemical evidence for exocytosis. J. Biol. Chem. 265:14736-14737.
    • (1991) J. Biol. Chem. , vol.265 , pp. 14736-14737
    • Leszczyszyn, D.J.1    Jankowsky, J.A.2    Viveros, O.H.3    Diliberto, E.J.4    Near, J.A.5    Wightman, R.M.6
  • 43
    • 0022502259 scopus 로고
    • Quantitative analysis of the cytosolic free calcium dependency of exocytosis from three subcellular compartments in intact human neutrophils
    • Lew, P.D., A. Monod, F.A. Waldvogel, B. Dewald, M. Baggiolini, and T. Pozzan. 1986. Quantitative analysis of the cytosolic free calcium dependency of exocytosis from three subcellular compartments in intact human neutrophils. J. Cell Biol. 102:2197-21204.
    • (1986) J. Cell Biol. , vol.102 , pp. 2197-21204
    • Lew, P.D.1    Monod, A.2    Waldvogel, F.A.3    Dewald, B.4    Baggiolini, M.5    Pozzan, T.6
  • 44
    • 0026514824 scopus 로고
    • Microdomains of high calcium concentration in presynaptic terminal
    • Llinas, R., M. Sugimori, and R.B. Silver. 1992. Microdomains of high calcium concentration in presynaptic terminal. Science (Wash. DC). 256:677-679.
    • (1992) Science (Wash. DC). , vol.256 , pp. 677-679
    • Llinas, R.1    Sugimori, M.2    Silver, R.B.3
  • 45
    • 0025286727 scopus 로고
    • Cell surface complexes isolated from Paramecium tetraurelia cells as a model system for analysing exocytosis in vitro in conjunction with microinjection studies
    • Lumpert, C.J., H. Kersken, and H. Plattner. 1990. Cell surface complexes isolated from Paramecium tetraurelia cells as a model system for analysing exocytosis in vitro in conjunction with microinjection studies. Biochem. J. 269: 639-645.
    • (1990) Biochem. J. , vol.269 , pp. 639-645
    • Lumpert, C.J.1    Kersken, H.2    Plattner, H.3
  • 46
    • 0025971079 scopus 로고
    • Modulation of hexokinase association with mitochondria analyzed with quantitative 3D confocal microscopy
    • Lynch, R.M., K.E. Fogarty, and F.S. Fay. 1991. Modulation of hexokinase association with mitochondria analyzed with quantitative 3D confocal microscopy. J. Cell Biol. 112:385-395.
    • (1991) J. Cell Biol. , vol.112 , pp. 385-395
    • Lynch, R.M.1    Fogarty, K.E.2    Fay, F.S.3
  • 47
    • 0025687548 scopus 로고
    • Changes in PC12 cell morphology induced by transfection with 42C cDNA, coding for a member of the S-100 protein family
    • Masiakowski, P., and E.M. Shooter. 1990. Changes in PC12 cell morphology induced by transfection with 42C cDNA, coding for a member of the S-100 protein family. J. Neurosc. Res. 27:264-269.
    • (1990) J. Neurosc. Res. , vol.27 , pp. 264-269
    • Masiakowski, P.1    Shooter, E.M.2
  • 49
    • 0028870106 scopus 로고
    • A role for soluble NSF attachment proteins (SNAPs) in regulated exocytosis in adrenal chromaffin cells
    • Morgan, A., and R.D. Burgoyne. 1995. A role for soluble NSF attachment proteins (SNAPs) in regulated exocytosis in adrenal chromaffin cells. EMBO (Eur. Mol. Biol. Organ.) J. 14:232-239.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 232-239
    • Morgan, A.1    Burgoyne, R.D.2
  • 50
    • 0001906480 scopus 로고
    • S.E. Moss, editor. Portland Press, London, UK
    • Moss, S.E. 1992. The Annexins, S.E. Moss, editor. Portland Press, London, UK. pp. 1-9.
    • (1992) The Annexins , pp. 1-9
    • Moss, S.E.1
  • 51
    • 0025117429 scopus 로고
    • Conformational change and localization of calpactin I complex involved in exocytosis as revealed by quickfreeze, deep-etch electron microscopy and immunocytochemistry
    • Nakata, T., K. Sobue, and N. Hirokawa. 1990. Conformational change and localization of calpactin I complex involved in exocytosis as revealed by quickfreeze, deep-etch electron microscopy and immunocytochemistry. J. Cell Biol. 110:13-24.
    • (1990) J. Cell Biol. , vol.110 , pp. 13-24
    • Nakata, T.1    Sobue, K.2    Hirokawa, N.3
  • 52
    • 0027409301 scopus 로고
    • Multiple calcium-dependent processes related to secretion in bovine chromaffin cells
    • Neher, E., and R.S. Zucker. 1993. Multiple calcium-dependent processes related to secretion in bovine chromaffin cells. Neuron. 10:21-30.
    • (1993) Neuron. , vol.10 , pp. 21-30
    • Neher, E.1    Zucker, R.S.2
  • 55
    • 0021847682 scopus 로고
    • Reorganization of α-fodrin induced by stimulation in secretory cells
    • Perrin, D., and D. Aunis. 1985. Reorganization of α-fodrin induced by stimulation in secretory cells. Nature (Lond.). 315:589-592.
    • (1985) Nature (Lond.). , vol.315 , pp. 589-592
    • Perrin, D.1    Aunis, D.2
  • 57
    • 0028324464 scopus 로고
    • Annexins: The problem of assessing the biological role for a gene family of multifunctional calcium- And phospholipid-binding proteins
    • Raynal, P., and H.B. Pollard. 1994. Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. Biochem. Biophys. Acid. 1197:63-93.
    • (1994) Biochem. Biophys. Acid. , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 58
    • 0028972270 scopus 로고
    • "In vitro" phosphorylation of annexin II helerotetramer by protein kinase C. Comparative properties of the unphosphorylated and phosphorylated annexin II on the aggregation and fusion of chromaffin granule membranes
    • Regnouf, F., I. Sagot, B. Delouche, G. Devilliers, J. Cartaud, J.P. Henry, and L.A. Pradel. 1995. "In vitro" phosphorylation of annexin II helerotetramer by protein kinase C. Comparative properties of the unphosphorylated and phosphorylated annexin II on the aggregation and fusion of chromaffin granule membranes. J. Biol. Chem. 270:2714.3-27150.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27143-27150
    • Regnouf, F.1    Sagot, I.2    Delouche, B.3    Devilliers, G.4    Cartaud, J.5    Henry, J.P.6    Pradel, L.A.7
  • 59
    • 0026555196 scopus 로고
    • Molecular dissection of the secretory pathway
    • Rothman, J.E., and L. Orci. 1992. Molecular dissection of the secretory pathway. Nature (Lond.). 355:409-415.
    • (1992) Nature (Lond.). , vol.355 , pp. 409-415
    • Rothman, J.E.1    Orci, L.2
  • 60
    • 0026063254 scopus 로고
    • The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kmase C
    • Sarafian, T., L.A. Pradel, J.P. Henry, D. Aunis, and M.F. Bader. 1991. The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kmase C. J. Cell Biol. 114:1135-1147.
    • (1991) J. Cell Biol. , vol.114 , pp. 1135-1147
    • Sarafian, T.1    Pradel, L.A.2    Henry, J.P.3    Aunis, D.4    Bader, M.F.5
  • 62
    • 0028321701 scopus 로고
    • Calcium-induced translocation of annexins to subcellular organelles of human neulrophils
    • Sjölin, C., O. Stendahl, and C. Dahlgren. 1994. Calcium-induced translocation of annexins to subcellular organelles of human neulrophils. Biochem. J. 300: 325-330.
    • (1994) Biochem. J. , vol.300 , pp. 325-330
    • Sjölin, C.1    Stendahl, O.2    Dahlgren, C.3
  • 64
    • 0023931882 scopus 로고
    • Peripheral actin filaments control calcium-mediated catecholamine release from streptolysin-O-permeabilized chromaffin cells
    • Sontag, J.M., D. Aunis, and M.F. Bader. 1988. Peripheral actin filaments control calcium-mediated catecholamine release from streptolysin-O-permeabilized chromaffin cells. Eur. J. Cell Biol. 46:316-326.
    • (1988) Eur. J. Cell Biol. , vol.46 , pp. 316-326
    • Sontag, J.M.1    Aunis, D.2    Bader, M.F.3
  • 65
    • 0020338386 scopus 로고
    • Calelectrin self-aggregates and promotes membrane aggregation in the presence of calcium
    • Südhof, T.C., J.H. Walker, and T. Obrocki. 1982. Calelectrin self-aggregates and promotes membrane aggregation in the presence of calcium. EMBO (Eur. Mol. Biol. Organ.) J. 1:1167-1170.
    • (1982) EMBO (Eur. Mol. Biol. Organ.) J , vol.1 , pp. 1167-1170
    • Südhof, T.C.1    Walker, J.H.2    Obrocki, T.3
  • 67
    • 0027338262 scopus 로고
    • 2+ receptor controls the final steps in peptide secretion from pituitary melanotrophs
    • 2+ receptor controls the final steps in peptide secretion from pituitary melanotrophs. Neuron. 11:90-104.
    • (1993) Neuron , vol.11 , pp. 90-104
    • Thomas, P.1    Wong, J.G.2    Lee, A.K.3    Almers, W.4
  • 68
    • 0027471403 scopus 로고
    • The gene encoding the calcium binding protein calcyclin is expressed at sites of exocytosis in the mouse
    • Timmons, P.M., C.T. Chan, P.W. Rigby, and F. Poirier. 1993. The gene encoding the calcium binding protein calcyclin is expressed at sites of exocytosis in the mouse. J. Cell Sci. 104:187-196.
    • (1993) J. Cell Sci. , vol.104 , pp. 187-196
    • Timmons, P.M.1    Chan, C.T.2    Rigby, P.W.3    Poirier, F.4
  • 69
    • 0022243842 scopus 로고
    • Immuno-histochemical and biochemical study on the development of the noradrenaline- And adrenaline-storing cells of the adrenal medulla of the rat
    • Verhofstad, A.A.J., R.E. Coupland, T.R. Parker, and M. Goldstein. 1985. Immuno-histochemical and biochemical study on the development of the noradrenaline- and adrenaline-storing cells of the adrenal medulla of the rat. Cell Tissue Res. 242:233-243.
    • (1985) Cell Tissue Res. , vol.242 , pp. 233-243
    • Verhofstad, A.A.J.1    Coupland, R.E.2    Parker, T.R.3    Goldstein, M.4
  • 70
    • 0028339479 scopus 로고
    • Localization and quantification of the insulin-like growth factor-1 receptor in mouse articular cartilage by confocal laser scanning microscopy
    • Verschure, P.J., J. Van Marie, L.A.B. Jooslen, and W.B. Van Den Berg. 1994. Localization and quantification of the insulin-like growth factor-1 receptor in mouse articular cartilage by confocal laser scanning microscopy, J. Histochem. Cytochem. 42:765-773.
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 765-773
    • Verschure, P.J.1    Van Marie, J.2    Jooslen, L.A.B.3    Van Den Berg, W.B.4
  • 71
    • 0028302133 scopus 로고
    • Exocytosis in chromaffin cells: Evidence for a MgATP-independent step that requires a pertussis loxin-scnsilive GTP-binding protein
    • Vitale, N., D. Thiersé, D. Aunis, and M.F. Bader. 1994. Exocytosis in chromaffin cells: evidence for a MgATP-independent step that requires a pertussis loxin-scnsilive GTP-binding protein. Biochem. J. 300:217-227.
    • (1994) Biochem. J. , vol.300 , pp. 217-227
    • Vitale, N.1    Thiersé, D.2    Aunis, D.3    Bader, M.F.4
  • 73
    • 0026808777 scopus 로고
    • Regulation of the chromaffin granule aggregating activity of annexin I by phosphorylation
    • Wang, W., and C.E. Creutz. 1992. Regulation of the chromaffin granule aggregating activity of annexin I by phosphorylation. Biochemistry. 31:9934-9939.
    • (1992) Biochemistry. , vol.31 , pp. 9934-9939
    • Wang, W.1    Creutz, C.E.2
  • 74
    • 0027923827 scopus 로고
    • Cell biology. Bridging the gap
    • Warren, G. 1993. Cell biology. Bridging the gap. Nature (Lond.). 362:297-298.
    • (1993) Nature (Lond.). , vol.362 , pp. 297-298
    • Warren, G.1
  • 76
    • 0028997457 scopus 로고
    • NSF-independent fusion mechanisms
    • Wilson, K.L. 1995. NSF-independent fusion mechanisms. Cell. 81:475-477.
    • (1995) Cell , vol.81 , pp. 475-477
    • Wilson, K.L.1
  • 77
    • 0028019458 scopus 로고
    • Fluorescent choleric and cholestatic bile salts take different paths across the hepatocyte: Transcytosis of glycolithocholate leads to an extensive redistribution of annexin II
    • Wilton, J.C., G.M. Matthews, R.D. Burgoyne, C.O. Mills, J.K. Chipman, and R. Coleman. 1994. Fluorescent choleric and cholestatic bile salts take different paths across the hepatocyte: transcytosis of glycolithocholate leads to an extensive redistribution of annexin II. J. Cell Biol. 127:401-410.
    • (1994) J. Cell Biol. , vol.127 , pp. 401-410
    • Wilton, J.C.1    Matthews, G.M.2    Burgoyne, R.D.3    Mills, C.O.4    Chipman, J.K.5    Coleman, R.6
  • 78
    • 0025907574 scopus 로고
    • 2+-dependent secretion to digitonin-permeabilized bovine chromaffin cells
    • 2+-dependent secretion to digitonin-permeabilized bovine chromaffin cells. FEBS Lett. 282:197-199.
    • (1991) FEBS Lett. , vol.282 , pp. 197-199
    • Wu, Y.N.1    Wagner, P.D.2
  • 79
    • 0023600206 scopus 로고
    • The calpaetin light chain is tightly linked to the cytoskeletal form of ealpaetin I: Studies using monoclonal antibodies to calpactin subunits
    • Zokas, L., and J.R. Glenney. 1987. The calpaetin light chain is tightly linked to the cytoskeletal form of ealpaetin I: studies using monoclonal antibodies to calpactin subunits. J. Cell Biol. 105:2111-2121.
    • (1987) J. Cell Biol. , vol.105 , pp. 2111-2121
    • Zokas, L.1    Glenney, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.