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Volumn 95, Issue 3, 2000, Pages 921-929

Molecular mechanisms of platelet exocytosis: Role of SNAP-23 and syntaxin 2 in dense core granule release

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; PROTEIN DERIVATIVE; SNARE PROTEIN; SYNTAXIN;

EID: 0034142239     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v95.3.921.003k17_921_929     Document Type: Article
Times cited : (143)

References (63)
  • 2
    • 0014096144 scopus 로고
    • Electron microscopic observations on the membrane systems of the rat blood platelet
    • Behnke O. Electron microscopic observations on the membrane systems of the rat blood platelet. Anat Rec. 1984;158:121.
    • (1984) Anat Rec , vol.158 , pp. 121
    • Behnke, O.1
  • 3
    • 0019887749 scopus 로고
    • Isolation, purification, and partial characterization of platelet membrane glycoproteins IIb and IIIa
    • Leung LL, Kinoshita T, Nachman RL. Isolation, purification, and partial characterization of platelet membrane glycoproteins IIb and IIIa. J Biol Chem. 1981;265:1994.
    • (1981) J Biol Chem , vol.265 , pp. 1994
    • Leung, L.L.1    Kinoshita, T.2    Nachman, R.L.3
  • 4
    • 0014704013 scopus 로고
    • A search for the platelet secretory pathway using electron dense tracers
    • White JG. A search for the platelet secretory pathway using electron dense tracers. Am J Pathol. 1970;58:31.
    • (1970) Am J Pathol , vol.58 , pp. 31
    • White, J.G.1
  • 5
    • 0028385277 scopus 로고
    • Implications of the SNARE hypothesis for intracellular membrane topology and dynamics
    • Rothman JE, Warren G. Implications of the SNARE hypothesis for intracellular membrane topology and dynamics. Curr Biol. 1994;4:220-233.
    • (1994) Curr Biol , vol.4 , pp. 220-233
    • Rothman, J.E.1    Warren, G.2
  • 6
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof TC. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature. 1995;375: 645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 7
    • 0030857288 scopus 로고    scopus 로고
    • Stages of regulated exocytosis
    • Martin TFJ. Stages of regulated exocytosis. Trends Cell Biol. 1997;7:271-276.
    • (1997) Trends Cell Biol , vol.7 , pp. 271-276
    • Martin, T.F.J.1
  • 8
    • 0027413655 scopus 로고
    • SNAP receptors implicated in vesicle targeting and fusion
    • Sšllner T, Whiteheart SW, Brunner M, et al. SNAP receptors implicated in vesicle targeting and fusion. Nature. 1993;362:318-324.
    • (1993) Nature , vol.362 , pp. 318-324
    • Sšllner, T.1    Whiteheart, S.W.2    Brunner, M.3
  • 9
    • 0032549708 scopus 로고    scopus 로고
    • SNAREpins: Minimal machinery for membrane fusion
    • Weber T, Zemelman BV, McNew JA, et al. SNAREpins: minimal machinery for membrane fusion. Cell. 1998;92:759-772.
    • (1998) Cell , vol.92 , pp. 759-772
    • Weber, T.1    Zemelman, B.V.2    McNew, J.A.3
  • 11
    • 0031794650 scopus 로고    scopus 로고
    • NSF - Fusion and beyond
    • Haas A. NSF - fusion and beyond. Trends Cell Biol. 1998;8:471-473.
    • (1998) Trends Cell Biol , vol.8 , pp. 471-473
    • Haas, A.1
  • 12
    • 0032506543 scopus 로고    scopus 로고
    • Defining the functions of trans-SNARE pairs
    • Ungermann C, Sato K, Wickner W. Defining the functions of trans-SNARE pairs. Nature. 1999; 396:543-548.
    • (1999) Nature , vol.396 , pp. 543-548
    • Ungermann, C.1    Sato, K.2    Wickner, W.3
  • 13
    • 0031040763 scopus 로고    scopus 로고
    • Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF)
    • Mayer A, Wickner W. Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF). J Cell Biol. 1997;136:307-317.
    • (1997) J Cell Biol , vol.136 , pp. 307-317
    • Mayer, A.1    Wickner, W.2
  • 14
    • 0029980441 scopus 로고    scopus 로고
    • Sec18p (NSF)-driven release of Sed17p (a-SNAP) can precede docking and fusion of yeast vacuoles
    • Mayer A, Wickner W, Haas A. Sec18p (NSF)-driven release of Sed17p (a-SNAP) can precede docking and fusion of yeast vacuoles. Cell. 1996; 85:83-94.
    • (1996) Cell , vol.85 , pp. 83-94
    • Mayer, A.1    Wickner, W.2    Haas, A.3
  • 15
    • 0030846534 scopus 로고    scopus 로고
    • Regulated secretion in platelets: Identification of elements of the platelet exocytosis machinery
    • Lemons PP, Chen D, Bernstein AM, Bennett MK, Whiteheart SW. Regulated secretion in platelets: identification of elements of the platelet exocytosis machinery. Blood. 1997;90:1490-1500.
    • (1997) Blood , vol.90 , pp. 1490-1500
    • Lemons, P.P.1    Chen, D.2    Bernstein, A.M.3    Bennett, M.K.4    Whiteheart, S.W.5
  • 16
    • 0033593207 scopus 로고    scopus 로고
    • Proteins of the exocytotic core complex mediate platelet alpha-granule secretion: Roles of vesicle-associated membrane protein, SNAP-23, and syntaxin 4
    • Flaumenhaft R, Croce K, Chen E, Furie B, Furie BC. Proteins of the exocytotic core complex mediate platelet alpha-granule secretion: roles of vesicle-associated membrane protein, SNAP-23, and syntaxin 4. J Biol Chem. 1999;274:2492-2501.
    • (1999) J Biol Chem , vol.274 , pp. 2492-2501
    • Flaumenhaft, R.1    Croce, K.2    Chen, E.3    Furie, B.4    Furie, B.C.5
  • 17
    • 0029929223 scopus 로고    scopus 로고
    • Identification of a novel syntaxin- and synaptobrevin/ VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues
    • Ravichandran V, Chawla A, Roche PA. Identification of a novel syntaxin- and synaptobrevin/ VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues. J Biol Chem. 1996;271: 13,300-13,303.
    • (1996) J Biol Chem , vol.271
    • Ravichandran, V.1    Chawla, A.2    Roche, P.A.3
  • 18
    • 0032584609 scopus 로고    scopus 로고
    • Inhibition of insulin-induced GLUT4 translocation by Munc18c through interaction with syntaxin4 in 3T3-L1 adipocytes
    • Tamori Y, Kawanishi M, Niki T, et al. Inhibition of insulin-induced GLUT4 translocation by Munc18c through interaction with syntaxin4 in 3T3-L1 adipocytes. J Biol Chem. 1998;273(31):19,740-19,746.
    • (1998) J Biol Chem , vol.273 , Issue.31
    • Tamori, Y.1    Kawanishi, M.2    Niki, T.3
  • 19
    • 17144463802 scopus 로고    scopus 로고
    • Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc1Bc
    • Araki S, Tamori Y, Kawanishi M, et al. Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc1Bc. Biochem Biophys Res Commun. 1997; 234:257-262.
    • (1997) Biochem Biophys Res Commun , vol.234 , pp. 257-262
    • Araki, S.1    Tamori, Y.2    Kawanishi, M.3
  • 20
    • 0031814298 scopus 로고    scopus 로고
    • A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells
    • Galli T, Zahraoui A, Vaidyanathan VV, et al. A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells. Mol Biol Cell. 1998;9(6):1437-1448.
    • (1998) Mol Biol Cell , vol.9 , Issue.6 , pp. 1437-1448
    • Galli, T.1    Zahraoui, A.2    Vaidyanathan, V.V.3
  • 21
    • 0031550236 scopus 로고    scopus 로고
    • Tissue distribution of SNAP-23 and its subcellular localization in 3T3-L1 cells
    • Wong PP, Daneman N, Volchuk A, et al. Tissue distribution of SNAP-23 and its subcellular localization in 3T3-L1 cells. Biochem Biophys Res Commun. 1997;230:64-68.
    • (1997) Biochem Biophys Res Commun , vol.230 , pp. 64-68
    • Wong, P.P.1    Daneman, N.2    Volchuk, A.3
  • 22
    • 0031559931 scopus 로고    scopus 로고
    • SNAP-23 is located in the basolateral plasma membrane of rat pancreatic acinar
    • Gaisano HY, Sheu L, Wong PP, Klip A, Trimble WS. SNAP-23 is located in the basolateral plasma membrane of rat pancreatic acinar. FEBS Lett 1997;414(2):298-302.
    • (1997) FEBS Lett , vol.414 , Issue.2 , pp. 298-302
    • Gaisano, H.Y.1    Sheu, L.2    Wong, P.P.3    Klip, A.4    Trimble, W.S.5
  • 23
    • 0001203866 scopus 로고    scopus 로고
    • Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells
    • Low SH, Roche PA, Anderson HA, et al. Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells. J Biol Chem. 1998;273(6):3422-3430.
    • (1998) J Biol Chem , vol.273 , Issue.6 , pp. 3422-3430
    • Low, S.H.1    Roche, P.A.2    Anderson, H.A.3
  • 24
    • 0032504156 scopus 로고    scopus 로고
    • SNAP-23 requirement for transferrin recycling in streptolysin-O-permeabilized Madin-Darby canine kidney cells
    • Leung SM, Chen D, DasGupta BR, Whiteheart SW, Apodaca G. SNAP-23 requirement for transferrin recycling in streptolysin-O-permeabilized Madin-Darby canine kidney cells. J Biol Chem. 1998;273:17,732-17,741.
    • (1998) J Biol Chem , vol.273
    • Leung, S.M.1    Chen, D.2    DasGupta, B.R.3    Whiteheart, S.W.4    Apodaca, G.5
  • 25
    • 0032555722 scopus 로고    scopus 로고
    • Relocation of the t-SNARE SNAP-23 from lamellipodia-like cell surface projections regulates compound exocytosis in mast cells
    • Guo Z, Turner C, Castle D. Relocation of the t-SNARE SNAP-23 from lamellipodia-like cell surface projections regulates compound exocytosis in mast cells. Cell. 1998;94(4):537-548.
    • (1998) Cell , vol.94 , Issue.4 , pp. 537-548
    • Guo, Z.1    Turner, C.2    Castle, D.3
  • 27
    • 0033556147 scopus 로고    scopus 로고
    • Identification of a cellubrevin/vesicle associated membrane protein 3 homologue in human platelets
    • Bernstein AM, Whiteheart SW. Identification of a cellubrevin/vesicle associated membrane protein 3 homologue in human platelets. Blood. 1999;93: 571-579.
    • (1999) Blood , vol.93 , pp. 571-579
    • Bernstein, A.M.1    Whiteheart, S.W.2
  • 28
    • 0033549253 scopus 로고    scopus 로고
    • Organization of the secretory machinery in the rodent brain: Distribution of the t-SNAREs, SNAP-25 and SNAP-23
    • Chen D, Minger SL, Honer WG, Whiteheart SW. Organization of the secretory machinery in the rodent brain: distribution of the t-SNAREs, SNAP-25 and SNAP-23. Brain Res. 1999;831: 11-24.
    • (1999) Brain Res , vol.831 , pp. 11-24
    • Chen, D.1    Minger, S.L.2    Honer, W.G.3    Whiteheart, S.W.4
  • 29
    • 0028132782 scopus 로고
    • N-ethylmaleimide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion
    • Whiteheart SW, Rossnagel K, Buhrow SA, Brunner M, Jaenicke R, Rothman JE. N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J Cell Biol. 1994;126:945-954.
    • (1994) J Cell Biol , vol.126 , pp. 945-954
    • Whiteheart, S.W.1    Rossnagel, K.2    Buhrow, S.A.3    Brunner, M.4    Jaenicke, R.5    Rothman, J.E.6
  • 30
    • 0028096570 scopus 로고
    • Role of two nucleotide-binding regions in an N-ethylmaleimide-sensitive factor involved in vesicle-mediated protein transport
    • Sumida M, Hong RM, Tagaya M. Role of two nucleotide-binding regions in an N-ethylmaleimide-sensitive factor involved in vesicle-mediated protein transport. J Biol Chem. 1994;269:20,636-20,641.
    • (1994) J Biol Chem , vol.269
    • Sumida, M.1    Hong, R.M.2    Tagaya, M.3
  • 31
    • 0027402091 scopus 로고
    • SNAP family of NSF attachment proteins includes a brain-specific isoform
    • Whiteheart SW, Griff IC, Brunner M, et al. SNAP family of NSF attachment proteins includes a brain-specific isoform. Nature. 1993;362:353-356.
    • (1993) Nature , vol.362 , pp. 353-356
    • Whiteheart, S.W.1    Griff, I.C.2    Brunner, M.3
  • 32
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier C. Phase separation of integral membrane proteins in Triton X-114 solution. J Biol Chem. 1981;256(4):1604-1607.
    • (1981) J Biol Chem , vol.256 , Issue.4 , pp. 1604-1607
    • Bordier, C.1
  • 34
    • 0024510475 scopus 로고
    • Measurement of secretion of lysosomal acid glycosidases
    • Holmsen H, Dangelmaier CA. Measurement of secretion of lysosomal acid glycosidases. Methods Enzymol. 1989;169:336-342.
    • (1989) Methods Enzymol , vol.169 , pp. 336-342
    • Holmsen, H.1    Dangelmaier, C.A.2
  • 35
    • 0031952838 scopus 로고    scopus 로고
    • SNAP-25 palmitoylation and plasma membrane targeting require a functional secretory pathway
    • Gonzalo S, Linder ME. SNAP-25 palmitoylation and plasma membrane targeting require a functional secretory pathway. Mol Biol Cell. 1998;9: 585-597.
    • (1998) Mol Biol Cell , vol.9 , pp. 585-597
    • Gonzalo, S.1    Linder, M.E.2
  • 36
    • 0026471991 scopus 로고
    • The 25 KDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS
    • Hess DT, Slater TM, Wilson MC, Skene JH. The 25 KDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS. J Neurosci. 1992;12:4634-4641.
    • (1992) J Neurosci , vol.12 , pp. 4634-4641
    • Hess, D.T.1    Slater, T.M.2    Wilson, M.C.3    Skene, J.H.4
  • 37
    • 18244432240 scopus 로고    scopus 로고
    • Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25
    • Veit M, Sollner TH, Rothman JE. Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25. FEBS Lett. 1996;385:119-123.
    • (1996) FEBS Lett , vol.385 , pp. 119-123
    • Veit, M.1    Sollner, T.H.2    Rothman, J.E.3
  • 38
    • 0033605664 scopus 로고    scopus 로고
    • Role of the cysteine-rich domain of the t-SNARE component, SYNDET, in membrane binding and subcellular localization
    • Koticha DK, Huddleston SJ, Witkin JW, Baldini G. Role of the cysteine-rich domain of the t-SNARE component, SYNDET, in membrane binding and subcellular localization. J BiolChem. 1999;274: 9053-9060.
    • (1999) J BiolChem , vol.274 , pp. 9053-9060
    • Koticha, D.K.1    Huddleston, S.J.2    Witkin, J.W.3    Baldini, G.4
  • 39
    • 0033542139 scopus 로고    scopus 로고
    • SNAP-23 and SNAP-25 are palmitoylated in vivo
    • Vogel K, Roche PA. SNAP-23 and SNAP-25 are palmitoylated in vivo. Biochem Biophys Res Commun. 1999;258:407-410.
    • (1999) Biochem Biophys Res Commun , vol.258 , pp. 407-410
    • Vogel, K.1    Roche, P.A.2
  • 40
    • 0024368011 scopus 로고
    • Poration by α-toxin and streptolysin O: An approach to analyze intracellular process
    • Ahnert-Hilger G, Mach W, Fahr KJ, Gratzl M. Poration by α-toxin and streptolysin O: an approach to analyze intracellular process. Methods Cell Biol. 1989;31:63-90.
    • (1989) Methods Cell Biol , vol.31 , pp. 63-90
    • Ahnert-Hilger, G.1    Mach, W.2    Fahr, K.J.3    Gratzl, M.4
  • 42
    • 0030699914 scopus 로고    scopus 로고
    • 2+-dependent mechanisms of secretion from streptolysin O-permeabilized platelets: Effects of leakage of cytosolic proteins
    • 2+-dependent mechanisms of secretion from streptolysin O-permeabilized platelets: effects of leakage of cytosolic proteins. Biochem J. 1997;328:13-21.
    • (1997) Biochem J , vol.328 , pp. 13-21
    • Sloan, D.C.1    Haslam, R.J.2
  • 43
    • 0030044758 scopus 로고    scopus 로고
    • Differential effects of G-protein activators on 5-hydroxytryptamine and platelet-derived growth factor release from streptolysin-O-permeabilized human platelets
    • Padfield PJ, Panesar N, Henderson P, Baldassare JJ. Differential effects of G-protein activators on 5-hydroxytryptamine and platelet-derived growth factor release from streptolysin-O-permeabilized human platelets. Biochem J. 1996;314: 123-128.
    • (1996) Biochem J , vol.314 , pp. 123-128
    • Padfield, P.J.1    Panesar, N.2    Henderson, P.3    Baldassare, J.J.4
  • 44
    • 0030682481 scopus 로고    scopus 로고
    • Stimulation of NSF ATPase activity by α-SNAP is required for SNARE complex disassembly and exocytosis
    • Barnard RJO, Morgan A, Burgoyne RD. Stimulation of NSF ATPase activity by α-SNAP is required for SNARE complex disassembly and exocytosis. J Cell Biol. 1997;139:875-883.
    • (1997) J Cell Biol , vol.139 , pp. 875-883
    • Barnard, R.J.O.1    Morgan, A.2    Burgoyne, R.D.3
  • 45
    • 0025359065 scopus 로고
    • SNAPS, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast
    • Clary DO, Griff IC, Rothman JE. SNAPS, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast. Cell. 1990;61:709-721.
    • (1990) Cell , vol.61 , pp. 709-721
    • Clary, D.O.1    Griff, I.C.2    Rothman, J.E.3
  • 46
    • 0028985213 scopus 로고
    • SNAP-mediated protein-protein interactions essential for neurotransmitter release
    • DeBello WM, O'Connor V, Dresbach T, et al. SNAP-mediated protein-protein interactions essential for neurotransmitter release. Nature. 1995;373:626-630.
    • (1995) Nature , vol.373 , pp. 626-630
    • DeBello, W.M.1    O'Connor, V.2    Dresbach, T.3
  • 47
    • 0032563194 scopus 로고    scopus 로고
    • Syndet, an adipocyte target SNARE involved in the insulin-induced translocation of GLUT4 to the cell surface
    • Rea S, Martin LB, McIntosh S, et al. Syndet, an adipocyte target SNARE involved in the insulin-induced translocation of GLUT4 to the cell surface. J Biol Chem. 1998;273:18,784-18,792.
    • (1998) J Biol Chem , vol.273
    • Rea, S.1    Martin, L.B.2    McIntosh, S.3
  • 48
    • 0032508645 scopus 로고    scopus 로고
    • The 26-mer peptide released from SNAP-25 cleavage by botulinum neurotoxin e inhibits vesicle docking
    • Ferrer-Montiel AV, Gutierrez LM, Apland JP, et al. The 26-mer peptide released from SNAP-25 cleavage by botulinum neurotoxin E inhibits vesicle docking. FEBS Lett. 1998;435(1):84-88.
    • (1998) FEBS Lett , vol.435 , Issue.1 , pp. 84-88
    • Ferrer-Montiel, A.V.1    Gutierrez, L.M.2    Apland, J.P.3
  • 50
    • 0033021577 scopus 로고    scopus 로고
    • SNAP23 promotes insulin-dependent glucose uptake in 3T3-L1 adipocytes: Possible interaction with cytoskeleton
    • Foster U, Yaworsky K, Trimble WS, Klip A. SNAP23 promotes insulin-dependent glucose uptake in 3T3-L1 adipocytes: possible interaction with cytoskeleton. Am J Physiol. 1999;276: C1108-C1114.
    • (1999) Am J Physiol , vol.276
    • Foster, U.1    Yaworsky, K.2    Trimble, W.S.3    Klip, A.4
  • 51
    • 0023764453 scopus 로고
    • Platelet cytoskeletal protein distributions in two triton-insoluble fractions and how they are affected by stimulants and reagents that modify cytoskeletal protein interactions
    • Jung SM, Moroi M. Platelet cytoskeletal protein distributions in two triton-insoluble fractions and how they are affected by stimulants and reagents that modify cytoskeletal protein interactions. Thromb Res. 1988;50(6):775-787.
    • (1988) Thromb Res , vol.50 , Issue.6 , pp. 775-787
    • Jung, S.M.1    Moroi, M.2
  • 52
    • 0000113350 scopus 로고
    • Reversible alterations in platelet morphology produced by anticoagulants and by cold
    • Zucker MB, Borelli BA. Reversible alterations in platelet morphology produced by anticoagulants and by cold. Blood. 1954;9:602-608.
    • (1954) Blood , vol.9 , pp. 602-608
    • Zucker, M.B.1    Borelli, B.A.2
  • 53
    • 0014155999 scopus 로고
    • An ultrastructural basis for the shape changes induced in platelets by chilling
    • White JG, Krivit W. An ultrastructural basis for the shape changes induced in platelets by chilling. Blood. 1967;30:625-635.
    • (1967) Blood , vol.30 , pp. 625-635
    • White, J.G.1    Krivit, W.2
  • 54
    • 0029737003 scopus 로고    scopus 로고
    • Membrane phase transition of intact human platelets: Correlation with cold-induced activation
    • Tablin F, Oliver AE, Walker NJ, Crowe LM, Crowe JH. Membrane phase transition of intact human platelets: correlation with cold-induced activation. J Cell Physiol. 1996;168:305-313.
    • (1996) J Cell Physiol , vol.168 , pp. 305-313
    • Tablin, F.1    Oliver, A.E.2    Walker, N.J.3    Crowe, L.M.4    Crowe, J.H.5
  • 55
    • 0028936855 scopus 로고
    • Mechanism of shape change in chilled human platelets
    • Winokur R, Hartwig JH. Mechanism of shape change in chilled human platelets. Blood. 1995; 85:1796-1804.
    • (1995) Blood , vol.85 , pp. 1796-1804
    • Winokur, R.1    Hartwig, J.H.2
  • 56
    • 0032921716 scopus 로고    scopus 로고
    • The internal calcium concentration of human platelets increases during chilling
    • Oliver AE, Tablin F, Walker NJ, Crowe JH. The internal calcium concentration of human platelets increases during chilling. Biochim Biophys Acta. 1999;1416:349-360.
    • (1999) Biochim Biophys Acta , vol.1416 , pp. 349-360
    • Oliver, A.E.1    Tablin, F.2    Walker, N.J.3    Crowe, J.H.4
  • 57
    • 0021916613 scopus 로고
    • Measurement of ionized calcium in blood platelets with the photoprotein aequorin comparison with Quin 2
    • Johnson PC, Ware JA, Cliveden PB, Smith M, Dvorak AM, Salzman EW. Measurement of ionized calcium in blood platelets with the photoprotein aequorin comparison with Quin 2. J Biol Chem. 1985;260:2069-2076.
    • (1985) J Biol Chem , vol.260 , pp. 2069-2076
    • Johnson, P.C.1    Ware, J.A.2    Cliveden, P.B.3    Smith, M.4    Dvorak, A.M.5    Salzman, E.W.6
  • 58
    • 0020469346 scopus 로고
    • Thrombin-induced secretion of serotonin from platelets can occur in seconds
    • Gear AR, Burke D. Thrombin-induced secretion of serotonin from platelets can occur in seconds. Blood. 1982;60(5):1231-1234.
    • (1982) Blood , vol.60 , Issue.5 , pp. 1231-1234
    • Gear, A.R.1    Burke, D.2
  • 59
    • 0029741443 scopus 로고    scopus 로고
    • Pantophysin is a ubiquitously expressed synaptophysin homologue and defines constitutive transport vesicles
    • Haass NK, Kartenbeck J, Leube R. Pantophysin is a ubiquitously expressed synaptophysin homologue and defines constitutive transport vesicles. J Cell Biol. 1996;134(3):731-746.
    • (1996) J Cell Biol , vol.134 , Issue.3 , pp. 731-746
    • Haass, N.K.1    Kartenbeck, J.2    Leube, R.3
  • 60
    • 0028300004 scopus 로고
    • Expression of the synaptophysin gene family is not restricted to neuronal and neuroendocrine differentiation in rat and human
    • Leube RE. Expression of the synaptophysin gene family is not restricted to neuronal and neuroendocrine differentiation in rat and human. Differentiation. 1994;56:163-171.
    • (1994) Differentiation , vol.56 , pp. 163-171
    • Leube, R.E.1
  • 61
    • 0027202087 scopus 로고
    • Identification of small GTP-binding rab proteins in human platelets: Thrombin-induced phosphorylation of rab3B, rab6, and rab8 proteins
    • Karniguian A, Zahraoui A, Tavitian A. Identification of small GTP-binding rab proteins in human platelets: thrombin-induced phosphorylation of rab3B, rab6, and rab8 proteins. Proc Natl Acad Sci U S A. 1993;90:7647-7651.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 7647-7651
    • Karniguian, A.1    Zahraoui, A.2    Tavitian, A.3
  • 63
    • 0033566920 scopus 로고    scopus 로고
    • A critical role for N-ethylmaleimide-sensitive fusion protein (NSF) in platelet granule secretion
    • Poiger J, Reed GL. A critical role for N-ethylmaleimide-sensitive fusion protein (NSF) in platelet granule secretion. Blood. 1999;94:1313-1318.
    • (1999) Blood , vol.94 , pp. 1313-1318
    • Poiger, J.1    Reed, G.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.