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Volumn 291, Issue 1, 2003, Pages 150-166

Regulation of membrane trafficking and subcellular organization of endocytic compartments revealed with FM1-43 in resting and activated human T cells

Author keywords

Calcium; Cytoskeleton; Endocytosis; Endosomes; Exosomes; Photoconversion

Indexed keywords

CALCIUM; CALYCULIN A; CD3 ANTIGEN; CYTOCHALASIN D; FLUORESCENT DYE; IONOMYCIN; PHOSPHATIDYLSERINE; SPHINGOLIPID ACTIVATOR PROTEIN 1; THAPSIGARGIN;

EID: 0242333900     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-4827(03)00372-0     Document Type: Article
Times cited : (77)

References (75)
  • 1
    • 0023256274 scopus 로고
    • Endocytosis and recycling of the T3-T cell receptor complex, the role of T3 phosphorylation
    • Krangel M.S. Endocytosis and recycling of the T3-T cell receptor complex, The role of T3 phosphorylation. J. Exp. Med. 165:1987;1141-1159.
    • (1987) J. Exp. Med. , vol.165 , pp. 1141-1159
    • Krangel, M.S.1
  • 2
    • 0033638003 scopus 로고    scopus 로고
    • On the dynamics of TCR:CD3 complex cell surface expression and downmodulation
    • Liu H., Rhodes M., Wiest D.L., Vignali D.A. On the dynamics of TCR:CD3 complex cell surface expression and downmodulation. Immunity. 13:2000;665-675.
    • (2000) Immunity , vol.13 , pp. 665-675
    • Liu, H.1    Rhodes, M.2    Wiest, D.L.3    Vignali, D.A.4
  • 3
    • 0023665090 scopus 로고
    • Internalization and cycling of the T cell antigen receptor, Role of protein kinase C
    • Minami Y., Samelson L.E., Klausner R.D. Internalization and cycling of the T cell antigen receptor, Role of protein kinase C. J. Biol. Chem. 262:1987;13342-13347.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13342-13347
    • Minami, Y.1    Samelson, L.E.2    Klausner, R.D.3
  • 4
    • 0032526345 scopus 로고    scopus 로고
    • Relationships among TCR ligand potency, thresholds for effector function elicitation, and the quality of early signaling events in human T cells
    • Hemmer B., Stefanova I., Vergelli M., Germain R.N., Martin R. Relationships among TCR ligand potency, thresholds for effector function elicitation, and the quality of early signaling events in human T cells. J. Immunol. 160:1998;5807-5814.
    • (1998) J. Immunol. , vol.160 , pp. 5807-5814
    • Hemmer, B.1    Stefanova, I.2    Vergelli, M.3    Germain, R.N.4    Martin, R.5
  • 5
    • 0033558278 scopus 로고    scopus 로고
    • Serial TCR engagement and down-modulation by peptide: MHC molecule ligands: Relationship to the quality of individual TCR signaling events
    • Itoh Y., Hemmer B., Martin R., Germain R.N. Serial TCR engagement and down-modulation by peptide MHC molecule ligands: relationship to the quality of individual TCR signaling events . J. Immunol. 162:1999;2073-2080.
    • (1999) J. Immunol. , vol.162 , pp. 2073-2080
    • Itoh, Y.1    Hemmer, B.2    Martin, R.3    Germain, R.N.4
  • 6
    • 0029037210 scopus 로고
    • Serial triggering of many T-cell receptors by a few peptide-MHC complexes
    • Valitutti S., Muller S., Cella M., Padovan E., Lanzavecchia A. Serial triggering of many T-cell receptors by a few peptide-MHC complexes. Nature. 375:1995;148-151.
    • (1995) Nature , vol.375 , pp. 148-151
    • Valitutti, S.1    Muller, S.2    Cella, M.3    Padovan, E.4    Lanzavecchia, A.5
  • 7
    • 1842331510 scopus 로고    scopus 로고
    • Degradation of T cell receptor (TCR)-CD3-zeta complexes after antigenic stimulation
    • Valitutti S., Muller S., Salio M., Lanzavecchia A. Degradation of T cell receptor (TCR)-CD3-zeta complexes after antigenic stimulation. J. Exp. Med. 185:1997;1859-1864.
    • (1997) J. Exp. Med. , vol.185 , pp. 1859-1864
    • Valitutti, S.1    Muller, S.2    Salio, M.3    Lanzavecchia, A.4
  • 8
    • 0031448209 scopus 로고    scopus 로고
    • Activation of the Lck tyrosine kinase targets cell surface T cell antigen receptors for lysosomal degradation
    • D'Oro U., Vacchio M.S., Weissman A.M., Ashwell J.D. Activation of the Lck tyrosine kinase targets cell surface T cell antigen receptors for lysosomal degradation. Immunity. 7:1997;619-628.
    • (1997) Immunity , vol.7 , pp. 619-628
    • D'Oro, U.1    Vacchio, M.S.2    Weissman, A.M.3    Ashwell, J.D.4
  • 11
    • 0033213195 scopus 로고    scopus 로고
    • Intracellular protein traffic in lymphocytes: "How do I get THERE from HERE"?
    • Roche P.A. Intracellular protein traffic in lymphocytes "How do I get THERE from HERE"? Immunity. 11:1999;391-398.
    • (1999) Immunity , vol.11 , pp. 391-398
    • Roche, P.A.1
  • 12
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • Mellman I. Endocytosis and molecular sorting. Annu. Rev. Cell Dev. Biol. 12:1996;575-625.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 575-625
    • Mellman, I.1
  • 14
    • 0033767690 scopus 로고    scopus 로고
    • Exosome: From internal vesicle of the multivesicular body to intercellular signaling device
    • Denzer K., Kleijmeer M.J., Heijnen H.F., Stoorvogel W., Geuze H.J. Exosome from internal vesicle of the multivesicular body to intercellular signaling device . J. Cell Sci. 113:2000;3365-3374.
    • (2000) J. Cell Sci. , vol.113 , pp. 3365-3374
    • Denzer, K.1    Kleijmeer, M.J.2    Heijnen, H.F.3    Stoorvogel, W.4    Geuze, H.J.5
  • 16
  • 18
    • 0036533633 scopus 로고    scopus 로고
    • TCR activation of human T cells induces the production of exosomes bearing the TCR/CD3/zeta complex
    • Blanchard N., Lankar D., Faure F., Regnault A., Dumont C., Raposo G., Hivroz C. TCR activation of human T cells induces the production of exosomes bearing the TCR/CD3/zeta complex. J. Immunol. 168:2002;3235-3241.
    • (2002) J. Immunol. , vol.168 , pp. 3235-3241
    • Blanchard, N.1    Lankar, D.2    Faure, F.3    Regnault, A.4    Dumont, C.5    Raposo, G.6    Hivroz, C.7
  • 22
    • 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. 16:1996;3960-3967.
    • (1996) J. Neurosci. , vol.16 , pp. 3960-3967
    • Henkel, A.W.1    Simpson, L.L.2    Ridge, R.M.3    Betz, W.J.4
  • 23
    • 0035511278 scopus 로고    scopus 로고
    • Limited numbers of recycling vesicles in small CNS nerve terminals: Implications for neural signaling and vesicular cycling
    • Harata N., Pyle J.L., Aravanis A.M., Mozhayeva M., Kavalali E.T., Tsien R.W. Limited numbers of recycling vesicles in small CNS nerve terminals implications for neural signaling and vesicular cycling . Trends Neurosci. 24:2001;637-643.
    • (2001) Trends Neurosci. , vol.24 , pp. 637-643
    • Harata, N.1    Pyle, J.L.2    Aravanis, A.M.3    Mozhayeva, M.4    Kavalali, E.T.5    Tsien, R.W.6
  • 25
    • 0018279136 scopus 로고
    • Regulation of membrane enzymes by lipids
    • Sandermann H. Regulation of membrane enzymes by lipids. Biochim. Biophys. Acta. 515:1978;209-237.
    • (1978) Biochim. Biophys. Acta , vol.515 , pp. 209-237
    • Sandermann, H.1
  • 26
    • 0033525748 scopus 로고    scopus 로고
    • 2+, calcineurin, and NF-AT
    • 2+, calcineurin, and NF-AT . Cell. 96:1999;611-614.
    • (1999) Cell , vol.96 , pp. 611-614
    • Crabtree, G.R.1
  • 27
    • 0023159083 scopus 로고
    • Gradual and stepwise changes in the membrane capacitance of rat peritoneal mast cells
    • Almers W., Neher E. Gradual and stepwise changes in the membrane capacitance of rat peritoneal mast cells. J. Physiol. (London). 386:1987;205-217.
    • (1987) J. Physiol. (London) , vol.386 , pp. 205-217
    • Almers, W.1    Neher, E.2
  • 28
    • 0029985418 scopus 로고    scopus 로고
    • Molecular mechanisms in synaptic vesicle endocytosis and recycling
    • De Camilli P., Takei K. Molecular mechanisms in synaptic vesicle endocytosis and recycling. Neuron. 16:1996;481-486.
    • (1996) Neuron , vol.16 , pp. 481-486
    • De Camilli, P.1    Takei, K.2
  • 29
    • 0034235408 scopus 로고    scopus 로고
    • FM1-43 reports plasma membrane phospholipid scrambling in T-lymphocytes
    • Zweifach A. FM1-43 reports plasma membrane phospholipid scrambling in T-lymphocytes. Biochem. J. 349:2000;255-260.
    • (2000) Biochem. J. , vol.349 , pp. 255-260
    • Zweifach, A.1
  • 30
    • 0034046180 scopus 로고    scopus 로고
    • T cell activation and the cytoskeleton
    • Acuto O., Cantrell D. T cell activation and the cytoskeleton. Annu. Rev. Immunol. 18:2000;165-184.
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 165-184
    • Acuto, O.1    Cantrell, D.2
  • 31
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • Cooper J.A. Effects of cytochalasin and phalloidin on actin. J. Cell Biol. 105:1987;1473-1478.
    • (1987) J. Cell Biol. , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 33
    • 0026493689 scopus 로고
    • Protein phosphatase inhibitors okadaic acid and calyculin A alter cell shape and F-actin distribution and inhibit stimulus-dependent increases in cytoskeletal actin of human neutrophils
    • Kreienbuhl P., Keller H., Niggli V. Protein phosphatase inhibitors okadaic acid and calyculin A alter cell shape and F-actin distribution and inhibit stimulus-dependent increases in cytoskeletal actin of human neutrophils. Blood. 80:1992;2911-2919.
    • (1992) Blood , vol.80 , pp. 2911-2919
    • Kreienbuhl, P.1    Keller, H.2    Niggli, V.3
  • 34
    • 0027336045 scopus 로고
    • Okadaic acid-induced actin assembly in neutrophils: Role of protein phosphatases
    • Downey G.P., Takai A., Zamel R., Grinstein S., Chan C.K. Okadaic acid-induced actin assembly in neutrophils role of protein phosphatases . J. Cell Physiol. 155:1993;505-519.
    • (1993) J. Cell Physiol. , vol.155 , pp. 505-519
    • Downey, G.P.1    Takai, A.2    Zamel, R.3    Grinstein, S.4    Chan, C.K.5
  • 37
    • 0030053909 scopus 로고    scopus 로고
    • Membrane dynamics in endocytosis
    • Robinson M.S., Watts C., Zerial M. Membrane dynamics in endocytosis. Cell. 84:1996;13-21.
    • (1996) Cell , vol.84 , pp. 13-21
    • Robinson, M.S.1    Watts, C.2    Zerial, M.3
  • 40
    • 0036418964 scopus 로고    scopus 로고
    • The plasticity of multivesicular bodies and the regulation of antigen presentation
    • Murk J., Stoorvogel W., Kleijmeer M., Geuze H. The plasticity of multivesicular bodies and the regulation of antigen presentation. Semin. Cell Dev. Biol. 13:2002;303-311.
    • (2002) Semin. Cell Dev. Biol. , vol.13 , pp. 303-311
    • Murk, J.1    Stoorvogel, W.2    Kleijmeer, M.3    Geuze, H.4
  • 41
    • 0027970448 scopus 로고
    • Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae
    • Fra A.M., Williamson E., Simons K., Parton R.G. Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae. J. Biol. Chem. 269:1994;30745-30748.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30745-30748
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 42
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder T., Scheiffele P., Verkade P., Simons K. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell Biol. 141:1998;929-942.
    • (1998) J. Cell Biol. , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 45
    • 0027159139 scopus 로고
    • Calcium oscillations in human T and natural killer cells depend upon membrane potential and calcium influx
    • Hess S.D., Oortgiesen M., Cahalan M.D. Calcium oscillations in human T and natural killer cells depend upon membrane potential and calcium influx. J. Immunol. 150:1993;2620-2633.
    • (1993) J. Immunol. , vol.150 , pp. 2620-2633
    • Hess, S.D.1    Oortgiesen, M.2    Cahalan, M.D.3
  • 47
    • 0027487057 scopus 로고
    • The kinetics of synaptic vesicle recycling measured at single presynaptic boutons
    • Ryan T.A., Reuter H., Wendland B., Schweizer F.E., Tsien R.W., Smith S.J. The kinetics of synaptic vesicle recycling measured at single presynaptic boutons. Neuron. 11:1993;713-724.
    • (1993) Neuron , vol.11 , pp. 713-724
    • Ryan, T.A.1    Reuter, H.2    Wendland, B.3    Schweizer, F.E.4    Tsien, R.W.5    Smith, S.J.6
  • 49
    • 0034605038 scopus 로고    scopus 로고
    • Molecular links between endocytosis and the actin cytoskeleton
    • Qualmann B., Kessels M.M., Kelly R.B. Molecular links between endocytosis and the actin cytoskeleton. J. Cell Biol. 150:2000;F111-F116.
    • (2000) J. Cell Biol. , vol.150
    • Qualmann, B.1    Kessels, M.M.2    Kelly, R.B.3
  • 50
    • 0035890047 scopus 로고    scopus 로고
    • Pathways linking endocytosis and actin cytoskeleton in mammalian cells
    • Lanzetti L., Di Fiore P.P., Scita G. Pathways linking endocytosis and actin cytoskeleton in mammalian cells. Exp. Cell Res. 271:2001;45-56.
    • (2001) Exp. Cell Res. , vol.271 , pp. 45-56
    • Lanzetti, L.1    Di Fiore, P.P.2    Scita, G.3
  • 51
    • 0027469161 scopus 로고
    • Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells
    • Gottlieb T.A., Ivanov I.E., Adesnik M., Sabatini D.D. Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells. J. Cell Biol. 120:1993;695-710.
    • (1993) J. Cell Biol. , vol.120 , pp. 695-710
    • Gottlieb, T.A.1    Ivanov, I.E.2    Adesnik, M.3    Sabatini, D.D.4
  • 52
    • 0034139820 scopus 로고    scopus 로고
    • Actin assembly plays a variable, but not obligatory role in receptor-mediated endocytosis in mammalian cells
    • Fujimoto L.M., Roth R., Heuser J.E., Schmid S.L. Actin assembly plays a variable, but not obligatory role in receptor-mediated endocytosis in mammalian cells. Traffic. 1:2000;161-171.
    • (2000) Traffic , vol.1 , pp. 161-171
    • Fujimoto, L.M.1    Roth, R.2    Heuser, J.E.3    Schmid, S.L.4
  • 53
    • 0028085551 scopus 로고
    • Inhibition of apical but not basolateral endocytosis of ricin and folate in Caco-2 cells by cytochalasin D
    • Jackman M.R., Shurety W., Ellis J.A., Luzio J.P. Inhibition of apical but not basolateral endocytosis of ricin and folate in Caco-2 cells by cytochalasin D. J. Cell Sci. 107:1994;2547-2556.
    • (1994) J. Cell Sci. , vol.107 , pp. 2547-2556
    • Jackman, M.R.1    Shurety, W.2    Ellis, J.A.3    Luzio, J.P.4
  • 55
    • 0026356880 scopus 로고
    • Fluid phase endocytosis investigated by fluorescence with trimethylamino-diphenylhexatriene in L929 cells; the influence of temperature and of cytoskeleton depolymerizing drugs
    • Illinger D., Poindron P., Kuhry J.G. Fluid phase endocytosis investigated by fluorescence with trimethylamino-diphenylhexatriene in L929 cells; the influence of temperature and of cytoskeleton depolymerizing drugs. Biol. Cell. 73:1991;131-138.
    • (1991) Biol. Cell. , vol.73 , pp. 131-138
    • Illinger, D.1    Poindron, P.2    Kuhry, J.G.3
  • 56
  • 57
    • 0024442942 scopus 로고
    • Temperature effect on endocytosis and exocytosis by rabbit alveolar macrophages
    • Tomoda H., Kishimoto Y., Lee Y.C. Temperature effect on endocytosis and exocytosis by rabbit alveolar macrophages. J. Biol. Chem. 264:1989;15445-15450.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15445-15450
    • Tomoda, H.1    Kishimoto, Y.2    Lee, Y.C.3
  • 58
    • 0019475760 scopus 로고
    • Temperature dependence of endocytosis mediated by the asialoglycoprotein receptor in isolated rat hepatocytes. Evidence for two potentially rate-limiting steps
    • Weigel P.H., Oka J.A. Temperature dependence of endocytosis mediated by the asialoglycoprotein receptor in isolated rat hepatocytes. Evidence for two potentially rate-limiting steps. J. Biol. Chem. 256:1981;2615-2617.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2615-2617
    • Weigel, P.H.1    Oka, J.A.2
  • 59
    • 0037192130 scopus 로고    scopus 로고
    • PI-specific phospholipase C cleavage of a reconstituted GPI-anchored protein: Modulation by the lipid bilayer
    • Lehto M.T., Sharom F.J. PI-specific phospholipase C cleavage of a reconstituted GPI-anchored protein modulation by the lipid bilayer . Biochemistry. 41:2002;1398-1408.
    • (2002) Biochemistry , vol.41 , pp. 1398-1408
    • Lehto, M.T.1    Sharom, F.J.2
  • 60
    • 0015040195 scopus 로고
    • Temperature "breaks" in Arrhenius plots: A thermodynamic consequence of a phase change
    • Kumamoto J., Raison J.K., Lyons J.M. Temperature "breaks" in Arrhenius plots a thermodynamic consequence of a phase change . J. Theor. Biol. 31:1971;47-51.
    • (1971) J. Theor. Biol. , vol.31 , pp. 47-51
    • Kumamoto, J.1    Raison, J.K.2    Lyons, J.M.3
  • 61
    • 0028179026 scopus 로고
    • CD3 gamma contains a phosphoserine-dependent di-leucine motif involved in down-regulation of the T cell receptor
    • Dietrich J., Hou X., Wegener A.M., Geisler C. CD3 gamma contains a phosphoserine-dependent di-leucine motif involved in down-regulation of the T cell receptor. EMBO J. 13:1994;2156-2166.
    • (1994) EMBO J. , vol.13 , pp. 2156-2166
    • Dietrich, J.1    Hou, X.2    Wegener, A.M.3    Geisler, C.4
  • 62
    • 0031114123 scopus 로고    scopus 로고
    • Tyrosine and serine protein kinase activities associated with ligand-induced internalized TCR/CD3 complexes
    • Luton F., Legendre V., Gorvel J.P., Schmitt-Verhulst A.M., Boyer C. Tyrosine and serine protein kinase activities associated with ligand-induced internalized TCR/CD3 complexes. J. Immunol. 158:1997;3140-3147.
    • (1997) J. Immunol. , vol.158 , pp. 3140-3147
    • Luton, F.1    Legendre, V.2    Gorvel, J.P.3    Schmitt-Verhulst, A.M.4    Boyer, C.5
  • 63
    • 0035265834 scopus 로고    scopus 로고
    • Interleukin 2 receptors and detergent-resistant membrane domains define a clathrin-independent endocytic pathway
    • Lamaze C., Dujeancourt A., Baba T., Lo C.G., Benmerah A., Dautry-Varsat A. Interleukin 2 receptors and detergent-resistant membrane domains define a clathrin-independent endocytic pathway. Mol. Cell. 7:2001;661-671.
    • (2001) Mol. Cell. , vol.7 , pp. 661-671
    • Lamaze, C.1    Dujeancourt, A.2    Baba, T.3    Lo, C.G.4    Benmerah, A.5    Dautry-Varsat, A.6
  • 64
    • 0036166314 scopus 로고    scopus 로고
    • Immunoelectron microscopic investigations of patching, capping, endocytotic and shedding processes in T and B lymphocytes
    • Burkhardt O., Merker H.J. Immunoelectron microscopic investigations of patching, capping, endocytotic and shedding processes in T and B lymphocytes. Ann. Anat. 184:2002;45-53.
    • (2002) Ann. Anat. , vol.184 , pp. 45-53
    • Burkhardt, O.1    Merker, H.J.2
  • 65
    • 0033485648 scopus 로고    scopus 로고
    • Activated platelets release two types of membrane vesicles: Microvesicles by surface shedding and exosomes derived from exocytosis of multivesicular bodies and alpha-granules
    • Heijnen H.F., Schiel A.E., Fijnheer R., Geuze H.J., Sixma J.J. Activated platelets release two types of membrane vesicles microvesicles by surface shedding and exosomes derived from exocytosis of multivesicular bodies and alpha-granules . Blood. 94:1999;3791-3799.
    • (1999) Blood , vol.94 , pp. 3791-3799
    • Heijnen, H.F.1    Schiel, A.E.2    Fijnheer, R.3    Geuze, H.J.4    Sixma, J.J.5
  • 66
    • 0032466618 scopus 로고    scopus 로고
    • Interaction of the neuronal marker dye FM1-43 with lipid membranes. Thermodynamics and lipid ordering
    • Schote U., Seelig J. Interaction of the neuronal marker dye FM1-43 with lipid membranes. Thermodynamics and lipid ordering. Biochim. Biophys. Acta. 1415:1998;135-146.
    • (1998) Biochim. Biophys. Acta , vol.1415 , pp. 135-146
    • Schote, U.1    Seelig, J.2
  • 67
    • 0029994378 scopus 로고    scopus 로고
    • Endocytosis of GPI-anchored proteins in human lymphocytes: Role of glycolipid-based domains, actin cytoskeleton, and protein kinases
    • Deckert M., Ticchioni M., Bernard A. Endocytosis of GPI-anchored proteins in human lymphocytes role of glycolipid-based domains, actin cytoskeleton, and protein kinases . J. Cell Biol. 133:1996;791-799.
    • (1996) J. Cell Biol. , vol.133 , pp. 791-799
    • Deckert, M.1    Ticchioni, M.2    Bernard, A.3
  • 68
    • 0032727709 scopus 로고    scopus 로고
    • Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor
    • Janes P.W., Ley S.C., Magee A.I. Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor. J. Cell Biol. 147:1999;447-461.
    • (1999) J. Cell Biol. , vol.147 , pp. 447-461
    • Janes, P.W.1    Ley, S.C.2    Magee, A.I.3
  • 70
    • 0036900081 scopus 로고    scopus 로고
    • Membrane rafts in immunoreceptor signaling: New doubts, new proofs?
    • Horejsi V. Membrane rafts in immunoreceptor signaling new doubts, new proofs? Trends Immunol. 23:2002;562-564.
    • (2002) Trends Immunol. , vol.23 , pp. 562-564
    • Horejsi, V.1
  • 72
    • 0034515432 scopus 로고    scopus 로고
    • The central role of phosphatidylserine in the phagocytosis of apoptotic thymocytes
    • Schlegel R.A., Callahan M.K., Williamson P. The central role of phosphatidylserine in the phagocytosis of apoptotic thymocytes. Ann. NY Acad. Sci. 926:2000;217-225.
    • (2000) Ann. NY Acad. Sci. , vol.926 , pp. 217-225
    • Schlegel, R.A.1    Callahan, M.K.2    Williamson, P.3
  • 73
    • 3543053363 scopus 로고    scopus 로고
    • Immature dendritic cells phagocytose apoptotic cells via alphavbeta5 and CD36, and cross-present antigens to cytotoxic T lymphocytes
    • Albert M.L., Pearce S.F., Francisco L.M., Sauter B., Roy P., Silverstein R.L., Bhardwaj N. Immature dendritic cells phagocytose apoptotic cells via alphavbeta5 and CD36, and cross-present antigens to cytotoxic T lymphocytes. J. Exp. Med. 188:1998;1359-1368.
    • (1998) J. Exp. Med. , vol.188 , pp. 1359-1368
    • Albert, M.L.1    Pearce, S.F.2    Francisco, L.M.3    Sauter, B.4    Roy, P.5    Silverstein, R.L.6    Bhardwaj, N.7
  • 74
    • 0023645106 scopus 로고
    • Vesicle formation during reticulocyte maturation. Association of plasma membrane activities with released vesicles (exosomes)
    • Johnstone R.M., Adam M., Hammond J.R., Orr L., Turbide C. Vesicle formation during reticulocyte maturation. Association of plasma membrane activities with released vesicles (exosomes). J. Biol. Chem. 262:1987;9412-9420.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9412-9420
    • Johnstone, R.M.1    Adam, M.2    Hammond, J.R.3    Orr, L.4    Turbide, C.5
  • 75
    • 0025890156 scopus 로고
    • Exosome formation during maturation of mammalian and avian reticulocytes: Evidence that exosome release is a major route for externalization of obsolete membrane proteins
    • Johnstone R.M., Mathew A., Mason A.B., Teng K. Exosome formation during maturation of mammalian and avian reticulocytes evidence that exosome release is a major route for externalization of obsolete membrane proteins . J. Cell Physiol. 147:1991;27-36.
    • (1991) J. Cell Physiol. , vol.147 , pp. 27-36
    • Johnstone, R.M.1    Mathew, A.2    Mason, A.B.3    Teng, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.