메뉴 건너뛰기




Volumn 3, Issue 1, 2014, Pages

Routes and mechanisms of extracellular vesicle uptake

Author keywords

Cell communication; Cell EV interaction; Endocytosis; EV internalization; EV uptake; Exosomes; Extracellular vesicles

Indexed keywords

ALPHA3 INTEGRIN; ALPHA4 INTEGRIN; ALPHA5 INTEGRIN; BETA3 INTEGRIN; CAVEOLIN; CAVEOLIN 1; CD11B ANTIGEN; CD28 ANTIGEN; CD51 ANTIGEN; CD63 ANTIGEN; CD81 ANTIGEN; CD9 ANTIGEN; CLATHRIN; CYTOCHALASIN D; DYNAMIN II; FLUORESCENT DYE; GLYCOPROTEIN P 15095; GREEN FLUORESCENT PROTEIN; HERMES ANTIGEN; INTERCELLULAR ADHESION MOLECULE 1; L SELECTIN; LECTIN; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; MAJOR HISTOCOMPATIBILITY ANTIGEN; PROTEOGLYCAN; T LYMPHOCYTE RECEPTOR; TETRASPANIN; UNINDEXED DRUG; VASCULAR CELL ADHESION MOLECULE 1;

EID: 85013654823     PISSN: None     EISSN: 20013078     Source Type: Journal    
DOI: 10.3402/jev.v3.24641     Document Type: Review
Times cited : (2022)

References (155)
  • 1
    • 84874377202 scopus 로고    scopus 로고
    • Extracellular vesicles: exosomes, microvesicles, and friends
    • Raposo G, Stoorvogel W. Extracellular vesicles: exosomes, microvesicles, and friends. J Cell Biol. 2013;200:373-83.
    • (2013) J Cell Biol. , vol.200 , pp. 373-383
    • Raposo, G.1    Stoorvogel, W.2
  • 2
    • 0040089526 scopus 로고    scopus 로고
    • Molecular characterization of dendritic cell-derived exosomes. Selective accumulation of the heat shock protein hsc73
    • Théry C, Regnault A, Garin J, Wolfers J, Zitvogel L, Ricciardi-Castagnoli P, et al. Molecular characterization of dendritic cell-derived exosomes. Selective accumulation of the heat shock protein hsc73. J Cell Biol. 1999;147:599-610.
    • (1999) J Cell Biol. , vol.147 , pp. 599-610
    • Théry, C.1    Regnault, A.2    Garin, J.3    Wolfers, J.4    Zitvogel, L.5    Ricciardi-Castagnoli, P.6
  • 3
    • 34249302620 scopus 로고    scopus 로고
    • Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells
    • Valadi H, Ekström K, Bossios A, Sjöstrand M, Lee JJ, Lötvall JO. Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells. Nat Cell Biol. 2007;9:654-9.
    • (2007) Nat Cell Biol. , vol.9 , pp. 654-659
    • Valadi, H.1    Ekström, K.2    Bossios, A.3    Sjöstrand, M.4    Lee, J.J.5    Lötvall, J.O.6
  • 5
    • 70350747789 scopus 로고    scopus 로고
    • Gastric cancer exosomes promote tumour cell proliferation through PI3K/Akt and MAPK/ERK activation
    • Qu JL, Qu XJ, Zhao MF, Teng YE, Zhang Y, Hou KZ, et al. Gastric cancer exosomes promote tumour cell proliferation through PI3K/Akt and MAPK/ERK activation. Dig Liver Dis. 2009;41:875-80.
    • (2009) Dig Liver Dis. , vol.41 , pp. 875-880
    • Qu, J.L.1    Qu, X.J.2    Zhao, M.F.3    Teng, Y.E.4    Zhang, Y.5    Hou, K.Z.6
  • 7
    • 84861367071 scopus 로고    scopus 로고
    • Possible role of exosomes containing RNA in mediating nontargeted effect of ionizing radiation
    • Al-Mayah AH, Irons SL, Pink RC, Carter DR, Kadhim MA. Possible role of exosomes containing RNA in mediating nontargeted effect of ionizing radiation. Radiat Res. 2012; 177:539-45.
    • (2012) Radiat Res. , vol.177 , pp. 539-545
    • Al-Mayah, A.H.1    Irons, S.L.2    Pink, R.C.3    Carter, D.R.4    Kadhim, M.A.5
  • 8
    • 0345701525 scopus 로고    scopus 로고
    • Antigen-presenting cell exosomes are protected from complement-mediated lysis by expression of CD55 and CD59
    • Clayton A, Harris CL, Court J, Mason MD, Morgan BP. Antigen-presenting cell exosomes are protected from complement-mediated lysis by expression of CD55 and CD59. Eur J Immunol. 2003;33:522-31.
    • (2003) Eur J Immunol. , vol.33 , pp. 522-531
    • Clayton, A.1    Harris, C.L.2    Court, J.3    Mason, M.D.4    Morgan, B.P.5
  • 11
    • 77951152406 scopus 로고    scopus 로고
    • An exosome-based secretion pathway is responsible for protein export from Leishmania and communication with macrophages
    • Silverman JM, Clos J, de'Oliveira CC, Shirvani O, Fang Y, Wang C, et al. An exosome-based secretion pathway is responsible for protein export from Leishmania and communication with macrophages. J Cell Sci. 2010;123:842-52.
    • (2010) J Cell Sci. , vol.123 , pp. 842-852
    • Silverman, J.M.1    Clos, J.2    de'Oliveira, C.C.3    Shirvani, O.4    Fang, Y.5    Wang, C.6
  • 12
    • 61849139471 scopus 로고    scopus 로고
    • Blood diffusion and Th1-suppressive effects of galectin-9-containing exosomes released by Epstein-Barr virus-infected nasopharyngeal carcinoma cells
    • Klibi J, Niki T, Riedel A, Pioche-Durieu C, Souquere S, Rubinstein E, et al. Blood diffusion and Th1-suppressive effects of galectin-9-containing exosomes released by Epstein-Barr virus-infected nasopharyngeal carcinoma cells. Blood. 2009;113:1957-66.
    • (2009) Blood. , vol.113 , pp. 1957-1966
    • Klibi, J.1    Niki, T.2    Riedel, A.3    Pioche-Durieu, C.4    Souquere, S.5    Rubinstein, E.6
  • 14
    • 84893550430 scopus 로고    scopus 로고
    • Meta-analysis using a novel database, miRStress, reveals miRNAs that are frequently associated with the radiation and hypoxia stress-responses
    • Jacobs LA, Bewicke-Copley F, Poolman MG, Pink RC, Mulcahy LA, Baker I, et al. Meta-analysis using a novel database, miRStress, reveals miRNAs that are frequently associated with the radiation and hypoxia stress-responses. PLoS One. 2013;8:e80844.
    • (2013) PLoS One. , vol.8
    • Jacobs, L.A.1    Bewicke-Copley, F.2    Poolman, M.G.3    Pink, R.C.4    Mulcahy, L.A.5    Baker, I.6
  • 15
    • 77956404647 scopus 로고    scopus 로고
    • Exosomes: extracellular organelles important in intercellular communication
    • Mathivanan S, Ji H, Simpson RJ. Exosomes: extracellular organelles important in intercellular communication. J Proteomics. 2010;73:1907-20.
    • (2010) J Proteomics. , vol.73 , pp. 1907-1920
    • Mathivanan, S.1    Ji, H.2    Simpson, R.J.3
  • 17
    • 77049115799 scopus 로고    scopus 로고
    • Microvesicle entry into marrow cells mediates tissue-specific changes in mRNA by direct delivery of mRNA and induction of transcription
    • Aliotta JM, Pereira M, Johnson KW, de Paz N, Dooner MS, Puente N, et al. Microvesicle entry into marrow cells mediates tissue-specific changes in mRNA by direct delivery of mRNA and induction of transcription. Exp Hematol. 2010;38: 233-45.
    • (2010) Exp Hematol. , vol.38 , pp. 233-245
    • Aliotta, J.M.1    Pereira, M.2    Johnson, K.W.3    de Paz, N.4    Dooner, M.S.5    Puente, N.6
  • 18
    • 74049102373 scopus 로고    scopus 로고
    • Human villous trophoblasts express and secrete placenta-specific microRNAs into maternal circulation via exosomes
    • Luo SS, Ishibashi O, Ishikawa G, Ishikawa T, Katayama A, Mishima T, et al. Human villous trophoblasts express and secrete placenta-specific microRNAs into maternal circulation via exosomes. Biol Reprod. 2009;81:717-29.
    • (2009) Biol Reprod. , vol.81 , pp. 717-729
    • Luo, S.S.1    Ishibashi, O.2    Ishikawa, G.3    Ishikawa, T.4    Katayama, A.5    Mishima, T.6
  • 19
    • 84893734492 scopus 로고    scopus 로고
    • The role of extracellular vesicles in phenotypic cancer transformation
    • Ogorevc E, Kralj-Iglic V, Veranic P. The role of extracellular vesicles in phenotypic cancer transformation. Radiol Oncol. 2013;47:197-205.
    • (2013) Radiol Oncol. , vol.47 , pp. 197-205
    • Ogorevc, E.1    Kralj-Iglic, V.2    Veranic, P.3
  • 21
    • 84871780796 scopus 로고    scopus 로고
    • Delivery of chemotherapeutic drugs in tumour cell-derived microparticles
    • Tang K, Zhang Y, Zhang H, Xu P, Liu J, Ma J, et al. Delivery of chemotherapeutic drugs in tumour cell-derived microparticles. Nat Commun. 2012;3:1282.
    • (2012) Nat Commun. , vol.3 , pp. 1282
    • Tang, K.1    Zhang, Y.2    Zhang, H.3    Xu, P.4    Liu, J.5    Ma, J.6
  • 23
    • 80052577736 scopus 로고    scopus 로고
    • Human trophoblastderived exosomal fibronectin induces pro-inflammatory IL-1b production by macrophages
    • Atay S, Gercel-Taylor C, Taylor DD. Human trophoblastderived exosomal fibronectin induces pro-inflammatory IL-1b production by macrophages. Am J Reprod Immunol. 2011; 66:259-69.
    • (2011) Am J Reprod Immunol. , vol.66 , pp. 259-269
    • Atay, S.1    Gercel-Taylor, C.2    Taylor, D.D.3
  • 24
    • 77449102731 scopus 로고    scopus 로고
    • Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages
    • Barrés C, Blanc L, Bette-Bobillo P, AndréS, Mamoun R, Gabius HJ, et al. Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages. Blood. 2010;115:696-705.
    • (2010) Blood. , vol.115 , pp. 696-705
    • Barrés, C.1    Blanc, L.2    Bette-Bobillo, P.3    André, S.4    Mamoun, R.5    Gabius, H.J.6
  • 25
    • 84886387008 scopus 로고    scopus 로고
    • Cancer cell exosomes depend on cell-surface heparan sulfate proteoglycans for their internalization and functional activity
    • Christianson HC, Svensson KJ, van Kuppevelt TH, Li JP, Belting M. Cancer cell exosomes depend on cell-surface heparan sulfate proteoglycans for their internalization and functional activity. Proc Natl Acad Sci U S A. 2013;110: 17380-5.
    • (2013) Proc Natl Acad Sci U S A. , vol.110 , pp. 17380-17385
    • Christianson, H.C.1    Svensson, K.J.2    van Kuppevelt, T.H.3    Li, J.P.4    Belting, M.5
  • 26
    • 84879046970 scopus 로고    scopus 로고
    • Exosome uptake depends on ERK1/2-heat shock protein 27 signalling and lipid raft-mediated endocytosis negatively regulated by caveolin-1
    • Svensson KJ, Christianson HC, Wittrup A, Bourseau-Guilmain E, Lindqvist E, Svensson LM, et al. Exosome uptake depends on ERK1/2-heat shock protein 27 signalling and lipid raft-mediated endocytosis negatively regulated by caveolin-1. J Biol Chem. 2013;288:17713-24.
    • (2013) J Biol Chem. , vol.288 , pp. 17713-17724
    • Svensson, K.J.1    Christianson, H.C.2    Wittrup, A.3    Bourseau-Guilmain, E.4    Lindqvist, E.5    Svensson, L.M.6
  • 27
    • 77953154769 scopus 로고    scopus 로고
    • Cellular internalization of exosomes occurs through phagocytosis
    • Feng D, Zhao WL, Ye YY, Bai XC, Liu RQ, Chang LF, et al. Cellular internalization of exosomes occurs through phagocytosis. Traffic. 2010;11:675-87.
    • (2010) Traffic. , vol.11 , pp. 675-687
    • Feng, D.1    Zhao, W.L.2    Ye, Y.Y.3    Bai, X.C.4    Liu, R.Q.5    Chang, L.F.6
  • 29
    • 84892175747 scopus 로고    scopus 로고
    • Exosomes from breast milk inhibit HIV-1 infection of dendritic cells and subsequent viral transfer to CD4-T cells
    • Näslund TI, Paquin-Proulx D, Paredes PT, Vallhov H, Sandberg JK, Gabrielsson S. Exosomes from breast milk inhibit HIV-1 infection of dendritic cells and subsequent viral transfer to CD4-T cells. AIDS. 2014;28:171-80.
    • (2014) AIDS. , vol.28 , pp. 171-180
    • Näslund, T.I.1    Paquin-Proulx, D.2    Paredes, P.T.3    Vallhov, H.4    Sandberg, J.K.5    Gabrielsson, S.6
  • 31
    • 84859499570 scopus 로고    scopus 로고
    • Sphingolipidmodulated exosome secretion promotes clearance of amyloidb by microglia
    • Yuyama K, Sun H, Mitsutake S, Igarashi Y. Sphingolipidmodulated exosome secretion promotes clearance of amyloidb by microglia. J Biol Chem. 2012;287:10977-89.
    • (2012) J Biol Chem. , vol.287 , pp. 10977-10989
    • Yuyama, K.1    Sun, H.2    Mitsutake, S.3    Igarashi, Y.4
  • 35
    • 76749106591 scopus 로고    scopus 로고
    • Cell surface tetraspanin Tspan8 contributes to molecular pathways of exosome-induced endothelial cell activation
    • Nazarenko I, Rana S, Baumann A, McAlear J, Hellwig A, Trendelenburg M, et al. Cell surface tetraspanin Tspan8 contributes to molecular pathways of exosome-induced endothelial cell activation. Cancer Res. 2010;70:1668-78.
    • (2010) Cancer Res. , vol.70 , pp. 1668-1678
    • Nazarenko, I.1    Rana, S.2    Baumann, A.3    McAlear, J.4    Hellwig, A.5    Trendelenburg, M.6
  • 36
    • 85028102817 scopus 로고    scopus 로고
    • Hepatic cell-to-cell transmission of small silencing RNA can extend the therapeutic reach of RNA interference (RNAi)
    • Pan Q, Ramakrishnaiah V, Henry S, Fouraschen S, de Ruiter PE, Kwekkeboom J, et al. Hepatic cell-to-cell transmission of small silencing RNA can extend the therapeutic reach of RNA interference (RNAi). Gut. 2012;61:1330-9.
    • (2012) Gut. , vol.61 , pp. 1330-1339
    • Pan, Q.1    Ramakrishnaiah, V.2    Henry, S.3    Fouraschen, S.4    de Ruiter, P.E.5    Kwekkeboom, J.6
  • 37
    • 84863439963 scopus 로고    scopus 로고
    • Toward tailored exosomes: the exosomal tetraspanin web contributes to target cell selection
    • Rana S, Yue S, Stadel D, Zöller M. Toward tailored exosomes: the exosomal tetraspanin web contributes to target cell selection. Int J Biochem Cell Biol. 2012;44:1574-84.
    • (2012) Int J Biochem Cell Biol. , vol.44 , pp. 1574-1584
    • Rana, S.1    Yue, S.2    Stadel, D.3    Zöller, M.4
  • 38
    • 84870861230 scopus 로고    scopus 로고
    • Tumor-exosomes and leukocyte activation: an ambivalent crosstalk
    • Zech D, Rana S, Büchler MW, Zöller M. Tumor-exosomes and leukocyte activation: an ambivalent crosstalk. Cell Commun Signal. 2012;10:37.
    • (2012) Cell Commun Signal. , vol.10 , pp. 37
    • Zech, D.1    Rana, S.2    Büchler, M.W.3    Zöller, M.4
  • 39
    • 38749126175 scopus 로고    scopus 로고
    • Exovesicles from human activated dendritic cells fuse with resting dendritic cells, allowing them to present alloantigens
    • Obregon C, Rothen-Rutishauser B, Gitahi SK, Gehr P, Nicod LP. Exovesicles from human activated dendritic cells fuse with resting dendritic cells, allowing them to present alloantigens. Am J Pathol. 2006;169:2127-36.
    • (2006) Am J Pathol. , vol.169 , pp. 2127-2136
    • Obregon, C.1    Rothen-Rutishauser, B.2    Gitahi, S.K.3    Gehr, P.4    Nicod, L.P.5
  • 40
    • 77957269172 scopus 로고    scopus 로고
    • Visualizing of the cellular uptake and intracellular trafficking of exosomes by live-cell microscopy
    • Tian T, Wang Y, Wang H, Zhu Z, Xiao Z. Visualizing of the cellular uptake and intracellular trafficking of exosomes by live-cell microscopy. J Cell Biochem. 2010;111:488-96.
    • (2010) J Cell Biochem. , vol.111 , pp. 488-496
    • Tian, T.1    Wang, Y.2    Wang, H.3    Zhu, Z.4    Xiao, Z.5
  • 41
    • 79953081976 scopus 로고    scopus 로고
    • Interaction and uptake of exosomes by ovarian cancer cells
    • Escrevente C, Keller S, Altevogt P, Costa J. Interaction and uptake of exosomes by ovarian cancer cells. BMC Cancer. 2011;11:108.
    • (2011) BMC Cancer. , vol.11 , pp. 108
    • Escrevente, C.1    Keller, S.2    Altevogt, P.3    Costa, J.4
  • 42
    • 63649092087 scopus 로고    scopus 로고
    • Systemic presence and tumor-growth promoting effect of ovarian carcinoma released exosomes
    • Keller S, König AK, MarméF, Runz S, Wolterink S, Koensgen D, et al. Systemic presence and tumor-growth promoting effect of ovarian carcinoma released exosomes. Cancer Lett. 2009;278:73-81.
    • (2009) Cancer Lett. , vol.278 , pp. 73-81
    • Keller, S.1    König, A.K.2    Marmé, F.3    Runz, S.4    Wolterink, S.5    Koensgen, D.6
  • 43
    • 78149476304 scopus 로고    scopus 로고
    • Dendritic cells recruit T cell exosomes via exosomal LFA-1 leading to inhibition of CD8-CTL responses through downregulation of peptide/MHC class I and Fas ligandmediated cytotoxicity
    • Xie Y, Zhang H, LiW, Deng Y, Munegowda MA, Chibbar R, et al. Dendritic cells recruit T cell exosomes via exosomal LFA-1 leading to inhibition of CD8-CTL responses through downregulation of peptide/MHC class I and Fas ligandmediated cytotoxicity. J Immunol. 2010;185:5268-78.
    • (2010) J Immunol. , vol.185 , pp. 5268-5278
    • Xie, Y.1    Zhang, H.2    Li, W.3    Deng, Y.4    Munegowda, M.A.5    Chibbar, R.6
  • 44
    • 33845677330 scopus 로고    scopus 로고
    • Mature dendritic cells pulsed with exosomes stimulate efficient cytotoxic T-lymphocyte responses and antitumour immunity
    • Hao S, Bai O, Li F, Yuan J, Laferte S, Xiang J. Mature dendritic cells pulsed with exosomes stimulate efficient cytotoxic T-lymphocyte responses and antitumour immunity. Immunology. 2007;120:90-102.
    • (2007) Immunology. , vol.120 , pp. 90-102
    • Hao, S.1    Bai, O.2    Li, F.3    Yuan, J.4    Laferte, S.5    Xiang, J.6
  • 45
    • 79955010722 scopus 로고    scopus 로고
    • GP120-specific exosome-targeted T cellbased vaccine capable of stimulating DC-and CD4(-) Tindependent CTL responses
    • Nanjundappa RH, Wang R, Xie Y, Umeshappa CS, Chibbar R, Wei Y, et al. GP120-specific exosome-targeted T cellbased vaccine capable of stimulating DC-and CD4(-) Tindependent CTL responses. Vaccine. 2011;29:3538-47.
    • (2011) Vaccine. , vol.29 , pp. 3538-3547
    • Nanjundappa, R.H.1    Wang, R.2    Xie, Y.3    Umeshappa, C.S.4    Chibbar, R.5    Wei, Y.6
  • 46
    • 45049087024 scopus 로고    scopus 로고
    • Enhancement of immunostimulatory properties of exosomal vaccines by incorporation of fusioncompetent G protein of vesicular stomatitis virus
    • Temchura VV, Tenbusch M, Nchinda G, Nabi G, Tippler B, Zelenyuk M, et al. Enhancement of immunostimulatory properties of exosomal vaccines by incorporation of fusioncompetent G protein of vesicular stomatitis virus. Vaccine. 2008;26:3662-72.
    • (2008) Vaccine. , vol.26 , pp. 3662-3672
    • Temchura, V.V.1    Tenbusch, M.2    Nchinda, G.3    Nabi, G.4    Tippler, B.5    Zelenyuk, M.6
  • 47
    • 80052446161 scopus 로고    scopus 로고
    • Detachment of breast tumor cells induces rapid secretion of exosomes which subsequently mediate cellular adhesion and spreading
    • Koumangoye RB, Sakwe AM, Goodwin JS, Patel T, Ochieng J. Detachment of breast tumor cells induces rapid secretion of exosomes which subsequently mediate cellular adhesion and spreading. PLoS One. 2011;6:e24234.
    • (2011) PLoS One. , vol.6
    • Koumangoye, R.B.1    Sakwe, A.M.2    Goodwin, J.S.3    Patel, T.4    Ochieng, J.5
  • 49
    • 66149115524 scopus 로고    scopus 로고
    • Noncytotoxic suppression of human immunodeficiency virus type 1 transcription by exosomes secreted from CD8-T cells
    • Tumne A, Prasad VS, Chen Y, Stolz DB, Saha K, Ratner DM, et al. Noncytotoxic suppression of human immunodeficiency virus type 1 transcription by exosomes secreted from CD8-T cells. J Virol. 2009;83:4354-64.
    • (2009) J Virol. , vol.83 , pp. 4354-4364
    • Tumne, A.1    Prasad, V.S.2    Chen, Y.3    Stolz, D.B.4    Saha, K.5    Ratner, D.M.6
  • 50
    • 79953202918 scopus 로고    scopus 로고
    • Exosome target cell selection and the importance of exosomal tetraspanins: a hypothesis
    • Rana S, Zöller M. Exosome target cell selection and the importance of exosomal tetraspanins: a hypothesis. Biochem Soc Trans. 2011;39:559-62.
    • (2011) Biochem Soc Trans. , vol.39 , pp. 559-562
    • Rana, S.1    Zöller, M.2
  • 51
    • 84886738545 scopus 로고    scopus 로고
    • Exosomes as new vesicular lipid transporters involved in cell-cell communication and various pathophysiologies
    • Record M, Carayon K, Poirot M, Silvente-Poirot S. Exosomes as new vesicular lipid transporters involved in cell-cell communication and various pathophysiologies. Biochim Biophys Acta. 2014;1841:108-20.
    • (2014) Biochim Biophys Acta. , vol.1841 , pp. 108-120
    • Record, M.1    Carayon, K.2    Poirot, M.3    Silvente-Poirot, S.4
  • 52
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • Hemler ME. Tetraspanin functions and associated microdomains. Nat Rev Mol Cell Biol. 2005;6:801-11.
    • (2005) Nat Rev Mol Cell Biol. , vol.6 , pp. 801-811
    • Hemler, M.E.1
  • 53
    • 57749169272 scopus 로고    scopus 로고
    • Tetraspanins: push and pull in suppressing and promoting metastasis
    • Zöller M. Tetraspanins: push and pull in suppressing and promoting metastasis. Nat Rev Cancer. 2009;9:40-55.
    • (2009) Nat Rev Cancer. , vol.9 , pp. 40-55
    • Zöller, M.1
  • 54
    • 0032493658 scopus 로고    scopus 로고
    • Selective enrichment of tetraspan proteins on the internal vesicles of multivesicular endosomes and on exosomes secreted by human B-lymphocytes
    • Escola JM, Kleijmeer MJ, Stoorvogel W, Griffith JM, Yoshie O, Geuze HJ. Selective enrichment of tetraspan proteins on the internal vesicles of multivesicular endosomes and on exosomes secreted by human B-lymphocytes. J Biol Chem. 1998;273:20121-7.
    • (1998) J Biol Chem. , vol.273 , pp. 20121-20127
    • Escola, J.M.1    Kleijmeer, M.J.2    Stoorvogel, W.3    Griffith, J.M.4    Yoshie, O.5    Geuze, H.J.6
  • 55
    • 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 HF, Schiel AE, Fijnheer R, Geuze HJ, Sixma JJ. Activated platelets release two types of membrane vesicles: microvesicles by surface shedding and exosomes derived from exocytosis of multivesicular bodies and alpha-granules. Blood. 1999;94:3791-9.
    • (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
  • 57
    • 0036333987 scopus 로고    scopus 로고
    • Residues SFQ (173-175) in the large extracellular loop of CD9 are required for gamete fusion
    • Zhu GZ, Miller BJ, Boucheix C, Rubinstein E, Liu CC, Hynes RO, et al. Residues SFQ (173-175) in the large extracellular loop of CD9 are required for gamete fusion. Development. 2002;129:1995-2002.
    • (2002) Development. , vol.129 , pp. 1995-2002
    • Zhu, G.Z.1    Miller, B.J.2    Boucheix, C.3    Rubinstein, E.4    Liu, C.C.5    Hynes, R.O.6
  • 58
    • 37049025380 scopus 로고    scopus 로고
    • The molecular basis of macrophage fusion
    • Helming L, Gordon S. The molecular basis of macrophage fusion. Immunobiology. 2007;212:785-93.
    • (2007) Immunobiology. , vol.212 , pp. 785-793
    • Helming, L.1    Gordon, S.2
  • 61
    • 77950501337 scopus 로고    scopus 로고
    • The roles of tetraspanins in HIV-1 replication
    • Thali M. The roles of tetraspanins in HIV-1 replication. Curr Top Microbiol Immunol. 2009;339:85-102.
    • (2009) Curr Top Microbiol Immunol. , vol.339 , pp. 85-102
    • Thali, M.1
  • 62
    • 13444259476 scopus 로고    scopus 로고
    • The tetraspanin web modulates immunesignalling complexes
    • Levy S, Shoham T. The tetraspanin web modulates immunesignalling complexes. Nat Rev Immunol. 2005;5:136-48.
    • (2005) Nat Rev Immunol. , vol.5 , pp. 136-148
    • Levy, S.1    Shoham, T.2
  • 63
    • 38449103840 scopus 로고    scopus 로고
    • New insights into the molecular basis of mammalian sperm-egg membrane interactions
    • Vjugina U, Evans JP. New insights into the molecular basis of mammalian sperm-egg membrane interactions. Front Biosci. 2008;13:462-76.
    • (2008) Front Biosci. , vol.13 , pp. 462-476
    • Vjugina, U.1    Evans, J.P.2
  • 64
    • 33645314949 scopus 로고    scopus 로고
    • Exosomes biological significance: a concise review
    • Johnstone RM. Exosomes biological significance: a concise review. Blood Cells Mol Dis. 2006;36:315-21.
    • (2006) Blood Cells Mol Dis. , vol.36 , pp. 315-321
    • Johnstone, R.M.1
  • 65
    • 42749092828 scopus 로고    scopus 로고
    • Itinerant exosomes: emerging roles in cell and tissue polarity
    • Lakkaraju A, Rodriguez-Boulan E. Itinerant exosomes: emerging roles in cell and tissue polarity. Trends Cell Biol. 2008;18:199-209.
    • (2008) Trends Cell Biol. , vol.18 , pp. 199-209
    • Lakkaraju, A.1    Rodriguez-Boulan, E.2
  • 66
    • 43149120419 scopus 로고    scopus 로고
    • Exosome function: from tumor immunology to pathogen biology
    • Schorey JS, Bhatnagar S. Exosome function: from tumor immunology to pathogen biology. Traffic. 2008;9:871-81.
    • (2008) Traffic. , vol.9 , pp. 871-881
    • Schorey, J.S.1    Bhatnagar, S.2
  • 67
    • 50849118813 scopus 로고    scopus 로고
    • Exosome-mediated quality control: substrate recruitment and molecular activity
    • Lebreton A, Séraphin B. Exosome-mediated quality control: substrate recruitment and molecular activity. Biochim Biophys Acta. 2008;1779:558-65.
    • (2008) Biochim Biophys Acta. , vol.1779 , pp. 558-565
    • Lebreton, A.1    Séraphin, B.2
  • 68
    • 0031745571 scopus 로고    scopus 로고
    • Signal transduction and signal modulation by cell adhesion receptors: the role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins
    • Aplin AE, Howe A, Alahari SK, Juliano RL. Signal transduction and signal modulation by cell adhesion receptors: the role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins. Pharmacol Rev. 1998;50: 197-263.
    • (1998) Pharmacol Rev. , vol.50 , pp. 197-263
    • Aplin, A.E.1    Howe, A.2    Alahari, S.K.3    Juliano, R.L.4
  • 69
    • 0023644247 scopus 로고
    • Purified intercellular adhesion molecule-1 (ICAM-1) is a ligand for lymphocyte functionassociated antigen 1 (LFA-1)
    • Marlin SD, Springer TA. Purified intercellular adhesion molecule-1 (ICAM-1) is a ligand for lymphocyte functionassociated antigen 1 (LFA-1). Cell. 1987;51:813-9.
    • (1987) Cell. , vol.51 , pp. 813-819
    • Marlin, S.D.1    Springer, T.A.2
  • 71
    • 0038312168 scopus 로고    scopus 로고
    • Direct stimulation of naive T cells by membrane vesicles from antigen-presenting cells: distinct roles for CD54 and B7 molecules
    • Hwang I, Shen X, Sprent J. Direct stimulation of naive T cells by membrane vesicles from antigen-presenting cells: distinct roles for CD54 and B7 molecules. Proc Natl Acad Sci U S A. 2003;100:6670-5.
    • (2003) Proc Natl Acad Sci U S A. , vol.100 , pp. 6670-6675
    • Hwang, I.1    Shen, X.2    Sprent, J.3
  • 73
    • 0033215527 scopus 로고    scopus 로고
    • A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry
    • Shukla D, Liu J, Blaiklock P, Shworak NW, Bai X, Esko JD, et al. A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry. Cell. 1999;99:13-22.
    • (1999) Cell. , vol.99 , pp. 13-22
    • Shukla, D.1    Liu, J.2    Blaiklock, P.3    Shworak, N.W.4    Bai, X.5    Esko, J.D.6
  • 74
    • 84884812281 scopus 로고    scopus 로고
    • The physiological role of DC-SIGN: a tale of mice and men
    • Garcia-Vallejo JJ, van Kooyk Y. The physiological role of DC-SIGN: a tale of mice and men. Trends Immunol. 2013; 34:482-6.
    • (2013) Trends Immunol. , vol.34 , pp. 482-486
    • Garcia-Vallejo, J.J.1    van Kooyk, Y.2
  • 75
    • 0019320646 scopus 로고
    • Cytochalasins block actin filament elongation by binding to high affinity sites associated with F-actin
    • Flanagan MD, Lin S. Cytochalasins block actin filament elongation by binding to high affinity sites associated with F-actin. J Biol Chem. 1980;255:835-8.
    • (1980) J Biol Chem. , vol.255 , pp. 835-838
    • Flanagan, M.D.1    Lin, S.2
  • 76
    • 0030860515 scopus 로고    scopus 로고
    • The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells
    • Lamaze C, Fujimoto LM, Yin HL, Schmid SL. The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells. J Biol Chem. 1997;272:20332-5.
    • (1997) J Biol Chem. , vol.272 , pp. 20332-20335
    • Lamaze, C.1    Fujimoto, L.M.2    Yin, H.L.3    Schmid, S.L.4
  • 77
    • 68449100791 scopus 로고    scopus 로고
    • Active uptake of dendritic cell-derived exovesicles by epithelial cells induces the release of inflammatory mediators through a TNF-alpha-mediated pathway
    • Obregon C, Rothen-Rutishauser B, Gerber P, Gehr P, Nicod LP. Active uptake of dendritic cell-derived exovesicles by epithelial cells induces the release of inflammatory mediators through a TNF-alpha-mediated pathway. Am J Pathol. 2009; 175:696-705.
    • (2009) Am J Pathol. , vol.175 , pp. 696-705
    • Obregon, C.1    Rothen-Rutishauser, B.2    Gerber, P.3    Gehr, P.4    Nicod, L.P.5
  • 79
    • 0037443410 scopus 로고    scopus 로고
    • Mast cell-derived exosomes induce phenotypic and functional maturation of dendritic cells and elicit specific immune responses in vivo
    • Skokos D, Botros HG, Demeure C, Morin J, Peronet R, Birkenmeier G, et al. Mast cell-derived exosomes induce phenotypic and functional maturation of dendritic cells and elicit specific immune responses in vivo. J Immunol. 2003; 170:3037-45.
    • (2003) J Immunol. , vol.170 , pp. 3037-3045
    • Skokos, D.1    Botros, H.G.2    Demeure, C.3    Morin, J.4    Peronet, R.5    Birkenmeier, G.6
  • 80
    • 63849314148 scopus 로고    scopus 로고
    • Capture and transfer of HIV-1 particles by mature dendritic cells converges with the exosome-dissemination pathway
    • Izquierdo-Useros N, Naranjo-Gómez M, Archer J, Hatch SC, Erkizia I, Blanco J, et al. Capture and transfer of HIV-1 particles by mature dendritic cells converges with the exosome-dissemination pathway. Blood. 2009;113:2732-41.
    • (2009) Blood. , vol.113 , pp. 2732-2741
    • Izquierdo-Useros, N.1    Naranjo-Gómez, M.2    Archer, J.3    Hatch, S.C.4    Erkizia, I.5    Blanco, J.6
  • 82
    • 80055002179 scopus 로고    scopus 로고
    • Targeted drug delivery using immunoconjugates: principles and applications
    • Pasquetto MV, Vecchia L, Covini D, Digilio R, Scotti C. Targeted drug delivery using immunoconjugates: principles and applications. J Immunother. 2011;34:611-28.
    • (2011) J Immunother. , vol.34 , pp. 611-628
    • Pasquetto, M.V.1    Vecchia, L.2    Covini, D.3    Digilio, R.4    Scotti, C.5
  • 84
    • 0027520440 scopus 로고
    • Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation
    • Wang LH, Rothberg KG, Anderson RG. Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation. J Cell Biol. 1993;123:1107-17.
    • (1993) J Cell Biol. , vol.123 , pp. 1107-1117
    • Wang, L.H.1    Rothberg, K.G.2    Anderson, R.G.3
  • 87
    • 4444224966 scopus 로고    scopus 로고
    • Endocytosis by random initiation and stabilization of clathrin-coated pits
    • Ehrlich M, Boll W, Van Oijen A, Hariharan R, Chandran K, Nibert ML, et al. Endocytosis by random initiation and stabilization of clathrin-coated pits. Cell. 2004;118:591-605.
    • (2004) Cell. , vol.118 , pp. 591-605
    • Ehrlich, M.1    Boll, W.2    Van Oijen, A.3    Hariharan, R.4    Chandran, K.5    Nibert, M.L.6
  • 88
    • 0036714223 scopus 로고    scopus 로고
    • Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits
    • Merrifield CJ, Feldman ME,Wan L, Almers W. Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits. Nat Cell Biol. 2002;4:691-8.
    • (2002) Nat Cell Biol. , vol.4 , pp. 691-698
    • Merrifield, C.J.1    Feldman, M.E.2    Wan, L.3    Almers, W.4
  • 89
    • 84859986511 scopus 로고    scopus 로고
    • A feedback loop between dynamin and actin recruitment during clathrinmediated endocytosis
    • Taylor MJ, Lampe M, Merrifield CJ. A feedback loop between dynamin and actin recruitment during clathrinmediated endocytosis. PLoS Biol. 2012;10:e1001302.
    • (2012) PLoS Biol. , vol.10
    • Taylor, M.J.1    Lampe, M.2    Merrifield, C.J.3
  • 90
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
    • Damke H, Baba T, Warnock DE, Schmid SL. Induction of mutant dynamin specifically blocks endocytic coated vesicle formation. J Cell Biol. 1994;127:915-34.
    • (1994) J Cell Biol. , vol.127 , pp. 915-934
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Schmid, S.L.4
  • 91
    • 0035826257 scopus 로고    scopus 로고
    • GTPase activity of dynamin and resulting conformation change are essential for endocytosis
    • Marks B, Stowell MH, Vallis Y, Mills IG, Gibson A, Hopkins CR, et al. GTPase activity of dynamin and resulting conformation change are essential for endocytosis. Nature. 2001;410:231-5.
    • (2001) Nature. , vol.410 , pp. 231-235
    • Marks, B.1    Stowell, M.H.2    Vallis, Y.3    Mills, I.G.4    Gibson, A.5    Hopkins, C.R.6
  • 92
    • 77953023419 scopus 로고    scopus 로고
    • G domain dimerization controls dynamin's assembly-stimulated GTPase activity
    • Chappie JS, Acharya S, Leonard M, Schmid SL, Dyda F. G domain dimerization controls dynamin's assembly-stimulated GTPase activity. Nature. 2010;465:435-40.
    • (2010) Nature. , vol.465 , pp. 435-440
    • Chappie, J.S.1    Acharya, S.2    Leonard, M.3    Schmid, S.L.4    Dyda, F.5
  • 93
    • 0032937051 scopus 로고    scopus 로고
    • Essential role of the dynamin pleckstrin homology domain in receptor-mediated endocytosis
    • Achiriloaie M, Barylko B, Albanesi JP. Essential role of the dynamin pleckstrin homology domain in receptor-mediated endocytosis. Mol Cell Biol. 1999;19:1410-5.
    • (1999) Mol Cell Biol. , vol.19 , pp. 1410-1415
    • Achiriloaie, M.1    Barylko, B.2    Albanesi, J.P.3
  • 94
    • 0033545702 scopus 로고    scopus 로고
    • Dominantnegative inhibition of receptor-mediated endocytosis by a dynamin-1 mutant with a defective pleckstrin homology domain
    • Lee A, Frank DW, Marks MS, Lemmon MA. Dominantnegative inhibition of receptor-mediated endocytosis by a dynamin-1 mutant with a defective pleckstrin homology domain. Curr Biol. 1999;9:261-4.
    • (1999) Curr Biol. , vol.9 , pp. 261-264
    • Lee, A.1    Frank, D.W.2    Marks, M.S.3    Lemmon, M.A.4
  • 95
    • 0033545698 scopus 로고    scopus 로고
    • Importance of the pleckstrin homology domain of dynamin in clathrin-mediated endocytosis
    • Vallis Y, Wigge P, Marks B, Evans PR, McMahon HT. Importance of the pleckstrin homology domain of dynamin in clathrin-mediated endocytosis. Curr Biol. 1999;9:257-60.
    • (1999) Curr Biol. , vol.9 , pp. 257-260
    • Vallis, Y.1    Wigge, P.2    Marks, B.3    Evans, P.R.4    McMahon, H.T.5
  • 96
    • 73949099250 scopus 로고    scopus 로고
    • Membrane insertion of the pleckstrin homology domain variable loop 1 is critical for dynamin-catalyzed vesicle scission
    • Ramachandran R, Pucadyil TJ, Liu YW, Acharya S, Leonard M, Lukiyanchuk V, et al. Membrane insertion of the pleckstrin homology domain variable loop 1 is critical for dynamin-catalyzed vesicle scission. Mol Biol Cell. 2009; 20:4630-9.
    • (2009) Mol Biol Cell. , vol.20 , pp. 4630-4639
    • Ramachandran, R.1    Pucadyil, T.J.2    Liu, Y.W.3    Acharya, S.4    Leonard, M.5    Lukiyanchuk, V.6
  • 98
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • Anderson RG. The caveolae membrane system. Annu Rev Biochem. 1998;67:199-225.
    • (1998) Annu Rev Biochem. , vol.67 , pp. 199-225
    • Anderson, R.G.1
  • 100
    • 0037684840 scopus 로고    scopus 로고
    • Caveolae/raft-dependent endocytosis
    • Nabi IR, Le PU. Caveolae/raft-dependent endocytosis. J Cell Biol. 2003;161:673-7.
    • (2003) J Cell Biol. , vol.161 , pp. 673-677
    • Nabi, I.R.1    Le, P.U.2
  • 102
    • 33845188467 scopus 로고    scopus 로고
    • Inhibition of dynamin completely blocks compensatory synaptic vesicle endocytosis
    • Newton AJ, Kirchhausen T, Murthy VN. Inhibition of dynamin completely blocks compensatory synaptic vesicle endocytosis. Proc Natl Acad Sci U S A. 2006;103:17955-60.
    • (2006) Proc Natl Acad Sci U S A. , vol.103 , pp. 17955-17960
    • Newton, A.J.1    Kirchhausen, T.2    Murthy, V.N.3
  • 103
    • 84883301160 scopus 로고    scopus 로고
    • Exosomes derived from Epstein-Barr virus-infected cells are internalized via caveola-dependent endocytosis and promote phenotypic modulation in target cells
    • Nanbo A, Kawanishi E, Yoshida R, Yoshiyama H. Exosomes derived from Epstein-Barr virus-infected cells are internalized via caveola-dependent endocytosis and promote phenotypic modulation in target cells. J Virol. 2013;87:10334-47.
    • (2013) J Virol. , vol.87 , pp. 10334-10347
    • Nanbo, A.1    Kawanishi, E.2    Yoshida, R.3    Yoshiyama, H.4
  • 104
    • 84890149349 scopus 로고    scopus 로고
    • Induction and transport of Wnt 5a during macrophageinduced malignant invasion is mediated by two types of extracellular vesicles
    • Menck K, Klemm F, Gross JC, Pukrop T, Wenzel D, Binder C. Induction and transport of Wnt 5a during macrophageinduced malignant invasion is mediated by two types of extracellular vesicles. Oncotarget. 2013;4:2057-66.
    • (2013) Oncotarget. , vol.4 , pp. 2057-2066
    • Menck, K.1    Klemm, F.2    Gross, J.C.3    Pukrop, T.4    Wenzel, D.5    Binder, C.6
  • 105
    • 0037039414 scopus 로고    scopus 로고
    • The large GTPase dynamin regulates actin comet formation and movement in living cells
    • Orth JD, Krueger EW, Cao H, McNiven MA. The large GTPase dynamin regulates actin comet formation and movement in living cells. Proc Natl Acad Sci U S A. 2002; 99:167-72.
    • (2002) Proc Natl Acad Sci U S A. , vol.99 , pp. 167-172
    • Orth, J.D.1    Krueger, E.W.2    Cao, H.3    McNiven, M.A.4
  • 106
    • 0035851197 scopus 로고    scopus 로고
    • Caveolin-1 null mice are viable but show evidence of hyperproliferative and vascular abnormalities
    • Razani B, Engelman JA, Wang XB, Schubert W, Zhang XL, Marks CB, et al. Caveolin-1 null mice are viable but show evidence of hyperproliferative and vascular abnormalities. J Biol Chem. 2001;276:38121-38.
    • (2001) J Biol Chem. , vol.276 , pp. 38121-38138
    • Razani, B.1    Engelman, J.A.2    Wang, X.B.3    Schubert, W.4    Zhang, X.L.5    Marks, C.B.6
  • 107
    • 47749107873 scopus 로고    scopus 로고
    • Shaping cups into phagosomes and macropinosomes
    • Swanson JA. Shaping cups into phagosomes and macropinosomes. Nat Rev Mol Cell Biol. 2008;9:639-49.
    • (2008) Nat Rev Mol Cell Biol. , vol.9 , pp. 639-649
    • Swanson, J.A.1
  • 108
    • 63049113263 scopus 로고    scopus 로고
    • Defining macropinocytosis
    • Kerr MC, Teasdale RD. Defining macropinocytosis. Traffic. 2009;10:364-71.
    • (2009) Traffic. , vol.10 , pp. 364-371
    • Kerr, M.C.1    Teasdale, R.D.2
  • 109
    • 0037099047 scopus 로고    scopus 로고
    • Membrane ruffling and macropinocytosis in A431 cells require cholesterol
    • Grimmer S, van Deurs B, Sandvig K. Membrane ruffling and macropinocytosis in A431 cells require cholesterol. J Cell Sci. 2002;115:2953-62.
    • (2002) J Cell Sci. , vol.115 , pp. 2953-2962
    • Grimmer, S.1    van Deurs, B.2    Sandvig, K.3
  • 110
    • 0034329464 scopus 로고    scopus 로고
    • Rac1-induced endocytosis is associated with intracellular proteolysis during migration through a three-dimensional matrix
    • Ahram M, Sameni M, Qiu RG, Linebaugh B, Kirn D, Sloane BF. Rac1-induced endocytosis is associated with intracellular proteolysis during migration through a three-dimensional matrix. Exp Cell Res. 2000;260:292-303.
    • (2000) Exp Cell Res. , vol.260 , pp. 292-303
    • Ahram, M.1    Sameni, M.2    Qiu, R.G.3    Linebaugh, B.4    Kirn, D.5    Sloane, B.F.6
  • 111
    • 33748994545 scopus 로고    scopus 로고
    • Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking
    • Ridley AJ. Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking. Trends Cell Biol. 2006;16: 522-9.
    • (2006) Trends Cell Biol. , vol.16 , pp. 522-529
    • Ridley, A.J.1
  • 112
    • 54549088877 scopus 로고    scopus 로고
    • Rac activation and inactivation control plasticity of tumor cell movement
    • Sanz-Moreno V, Gadea G, Ahn J, Paterson H, Marra P, Pinner S, et al. Rac activation and inactivation control plasticity of tumor cell movement. Cell. 2008;135:510-23.
    • (2008) Cell. , vol.135 , pp. 510-523
    • Sanz-Moreno, V.1    Gadea, G.2    Ahn, J.3    Paterson, H.4    Marra, P.5    Pinner, S.6
  • 113
    • 0027728934 scopus 로고
    • In vitro phagocytosis assay of nano-and microparticles by chemiluminescence. III. Uptake of differently sized surface-modified particles, and its correlation to particle properties and in vivo distribution
    • Rudt S, Müller RH. In vitro phagocytosis assay of nano-and microparticles by chemiluminescence. III. Uptake of differently sized surface-modified particles, and its correlation to particle properties and in vivo distribution. Eur J Pharm Sci. 1993;1:31-9.
    • (1993) Eur J Pharm Sci. , vol.1 , pp. 31-39
    • Rudt, S.1    Müller, R.H.2
  • 114
    • 0036532121 scopus 로고    scopus 로고
    • Roles of PI3Ks in leukocyte chemotaxis and phagocytosis
    • Stephens L, Ellson C, Hawkins P. Roles of PI3Ks in leukocyte chemotaxis and phagocytosis. Curr Opin Cell Biol. 2002;14: 203-13.
    • (2002) Curr Opin Cell Biol. , vol.14 , pp. 203-213
    • Stephens, L.1    Ellson, C.2    Hawkins, P.3
  • 115
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
    • Fadok VA, Voelker DR, Campbell PA, Cohen JJ, Bratton DL, Henson PM. Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J Immunol. 1992;148:2207-16.
    • (1992) J Immunol. , vol.148 , pp. 2207-2216
    • Fadok, V.A.1    Voelker, D.R.2    Campbell, P.A.3    Cohen, J.J.4    Bratton, D.L.5    Henson, P.M.6
  • 116
    • 0033807545 scopus 로고    scopus 로고
    • Phosphatidylserine-mediated phagocytosis of influenza A virus-infected cells by mouse peritoneal macrophages
    • Shiratsuchi A, Kaido M, Takizawa T, Nakanishi Y. Phosphatidylserine-mediated phagocytosis of influenza A virus-infected cells by mouse peritoneal macrophages. J Virol. 2000;74:9240-4.
    • (2000) J Virol. , vol.74 , pp. 9240-9244
    • Shiratsuchi, A.1    Kaido, M.2    Takizawa, T.3    Nakanishi, Y.4
  • 117
    • 0242333900 scopus 로고    scopus 로고
    • Regulation of membrane trafficking and subcellular organization of endocytic compartments revealed with FM1-43 in resting and activated human T cells
    • Fomina AF, Deerinck TJ, Ellisman MH, Cahalan MD. Regulation of membrane trafficking and subcellular organization of endocytic compartments revealed with FM1-43 in resting and activated human T cells. Exp Cell Res. 2003;291: 150-66.
    • (2003) Exp Cell Res. , vol.291 , pp. 150-166
    • Fomina, A.F.1    Deerinck, T.J.2    Ellisman, M.H.3    Cahalan, M.D.4
  • 118
    • 0036733578 scopus 로고    scopus 로고
    • Cholesterol, lipid rafts, and disease
    • Simons K, Ehehalt R. Cholesterol, lipid rafts, and disease. J Clin Invest. 2002;110:597-603.
    • (2002) J Clin Invest. , vol.110 , pp. 597-603
    • Simons, K.1    Ehehalt, R.2
  • 119
    • 35748931458 scopus 로고    scopus 로고
    • Lipids as modulators of membrane fusion mediated by viral fusion proteins
    • Teissier E, Pécheur EI. Lipids as modulators of membrane fusion mediated by viral fusion proteins. Eur Biophys J. 2007;36:887-99.
    • (2007) Eur Biophys J. , vol.36 , pp. 887-899
    • Teissier, E.1    Pécheur, E.I.2
  • 121
    • 30344486984 scopus 로고    scopus 로고
    • Flotillin-1 defines a clathrin-independent endocytic pathway in mammalian cells
    • Glebov OO, Bright NA, Nichols BJ. Flotillin-1 defines a clathrin-independent endocytic pathway in mammalian cells. Nat Cell Biol. 2006;8:46-54.
    • (2006) Nat Cell Biol. , vol.8 , pp. 46-54
    • Glebov, O.O.1    Bright, N.A.2    Nichols, B.J.3
  • 122
    • 34250851923 scopus 로고    scopus 로고
    • Coassembly of flotillins induces formation of membrane microdomains, membrane curvature, and vesicle budding
    • Frick M, Bright NA, Riento K, Bray A, Merrified C, Nichols BJ. Coassembly of flotillins induces formation of membrane microdomains, membrane curvature, and vesicle budding. Curr Biol. 2007;17:1151-6.
    • (2007) Curr Biol. , vol.17 , pp. 1151-1156
    • Frick, M.1    Bright, N.A.2    Riento, K.3    Bray, A.4    Merrified, C.5    Nichols, B.J.6
  • 123
    • 0033617415 scopus 로고    scopus 로고
    • Flotillins/cavatellins are differentially expressed in cells and tissues and form a hetero-oligomeric complex with caveolins in vivo. Characterization and epitope-mapping of a novel flotillin-1 monoclonal antibody probe
    • Volonte D, Galbiati F, Li S, Nishiyama K, Okamoto T, Lisanti MP. Flotillins/cavatellins are differentially expressed in cells and tissues and form a hetero-oligomeric complex with caveolins in vivo. Characterization and epitope-mapping of a novel flotillin-1 monoclonal antibody probe. J Biol Chem. 1999;274:12702-9.
    • (1999) J Biol Chem. , vol.274 , pp. 12702-12709
    • Volonte, D.1    Galbiati, F.2    Li, S.3    Nishiyama, K.4    Okamoto, T.5    Lisanti, M.P.6
  • 124
    • 0031010267 scopus 로고    scopus 로고
    • Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins
    • Bickel PE, Scherer PE, Schnitzer JE, Oh P, Lisanti MP, Lodish HF. Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins. J Biol Chem. 1997;272:13793-802.
    • (1997) J Biol Chem. , vol.272 , pp. 13793-13802
    • Bickel, P.E.1    Scherer, P.E.2    Schnitzer, J.E.3    Oh, P.4    Lisanti, M.P.5    Lodish, H.F.6
  • 125
    • 84856866968 scopus 로고    scopus 로고
    • The roles of flotillin microdomains-endocytosis and beyond
    • Otto GP, Nichols BJ. The roles of flotillin microdomains-endocytosis and beyond. J Cell Sci. 2011;124:3933-40.
    • (2011) J Cell Sci. , vol.124 , pp. 3933-3940
    • Otto, G.P.1    Nichols, B.J.2
  • 126
    • 0026317132 scopus 로고
    • Inhibition of sphingolipid biosynthesis by fumonisins. Implications for diseases associated with Fusarium moniliforme
    • Wang E, Norred WP, Bacon CW, Riley RT, Merrill AH. Inhibition of sphingolipid biosynthesis by fumonisins. Implications for diseases associated with Fusarium moniliforme. J Biol Chem. 1991;266:14486-90.
    • (1991) J Biol Chem. , vol.266 , pp. 14486-14490
    • Wang, E.1    Norred, W.P.2    Bacon, C.W.3    Riley, R.T.4    Merrill, A.H.5
  • 127
    • 0028176432 scopus 로고
    • Nbutyldeoxynojirimycin is a novel inhibitor of glycolipid biosynthesis
    • Platt FM, Neises GR, Dwek RA, Butters TD. Nbutyldeoxynojirimycin is a novel inhibitor of glycolipid biosynthesis. J Biol Chem. 1994;269:8362-5.
    • (1994) J Biol Chem. , vol.269 , pp. 8362-8365
    • Platt, F.M.1    Neises, G.R.2    Dwek, R.A.3    Butters, T.D.4
  • 129
    • 0023636677 scopus 로고
    • Biomembrane fusion: a new concept derived from model studies using two interacting planar lipid bilayers
    • Chernomordik LV, Melikyan GB, Chizmadzhev YA. Biomembrane fusion: a new concept derived from model studies using two interacting planar lipid bilayers. Biochim Biophys Acta. 1987;906:309-52.
    • (1987) Biochim Biophys Acta. , vol.906 , pp. 309-352
    • Chernomordik, L.V.1    Melikyan, G.B.2    Chizmadzhev, Y.A.3
  • 131
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn R, Südhof TC. Membrane fusion and exocytosis. Annu Rev Biochem. 1999;68:863-911.
    • (1999) Annu Rev Biochem. , vol.68 , pp. 863-911
    • Jahn, R.1    Südhof, T.C.2
  • 132
    • 80052187639 scopus 로고    scopus 로고
    • Lipid raft endocytosis and exosomal transport facilitate extracellular trafficking of annexin A2
    • Valapala M, Vishwanatha JK. Lipid raft endocytosis and exosomal transport facilitate extracellular trafficking of annexin A2. J Biol Chem. 2011;286:30911-25.
    • (2011) J Biol Chem. , vol.286 , pp. 30911-30925
    • Valapala, M.1    Vishwanatha, J.K.2
  • 133
    • 84872149261 scopus 로고    scopus 로고
    • Extracellular vesicles in physiological and pathological conditions
    • Yuana Y, Sturk A, Nieuwland R. Extracellular vesicles in physiological and pathological conditions. Blood Rev. 2013; 27:31-9.
    • (2013) Blood Rev. , vol.27 , pp. 31-39
    • Yuana, Y.1    Sturk, A.2    Nieuwland, R.3
  • 134
    • 65449117971 scopus 로고    scopus 로고
    • High levels of exosomes expressing CD63 and caveolin-1 in plasma of melanoma patients
    • Logozzi M, De Milito A, Lugini L, Borghi M, Calabrò L, Spada M, et al. High levels of exosomes expressing CD63 and caveolin-1 in plasma of melanoma patients. PLoS One. 2009;4:e5219.
    • (2009) PLoS One. , vol.4
    • Logozzi, M.1    De Milito, A.2    Lugini, L.3    Borghi, M.4    Calabrò, L.5    Spada, M.6
  • 136
    • 84876980723 scopus 로고    scopus 로고
    • FedExosomes: engineering therapeutic biological nanoparticles that truly deliver
    • Marcus ME, Leonard JN. FedExosomes: engineering therapeutic biological nanoparticles that truly deliver. Pharmaceuticals (Basel). 2013;6:659-80.
    • (2013) Pharmaceuticals (Basel). , vol.6 , pp. 659-680
    • Marcus, M.E.1    Leonard, J.N.2
  • 138
    • 0031863853 scopus 로고    scopus 로고
    • Eradication of established murine tumors using a novel cell-free vaccine: dendritic cell-derived exosomes
    • Zitvogel L, Regnault A, Lozier A, Wolfers J, Flament C, Tenza D, et al. Eradication of established murine tumors using a novel cell-free vaccine: dendritic cell-derived exosomes. Nat Med. 1998;4:594-600.
    • (1998) Nat Med. , vol.4 , pp. 594-600
    • Zitvogel, L.1    Regnault, A.2    Lozier, A.3    Wolfers, J.4    Flament, C.5    Tenza, D.6
  • 139
    • 0019829488 scopus 로고
    • Cytochalasin D inhibits actin polymerization and induces depolymerization of actin filaments formed during platelet shape change
    • Casella JF, Flanagan MD, Lin S. Cytochalasin D inhibits actin polymerization and induces depolymerization of actin filaments formed during platelet shape change. Nature. 1981;293:302-5.
    • (1981) Nature. , vol.293 , pp. 302-305
    • Casella, J.F.1    Flanagan, M.D.2    Lin, S.3
  • 140
    • 0022002296 scopus 로고
    • Cytochalasin treatment disrupts the endogenous currents associated with cell polarization in fucoid zygotes: studies of the role of F-actin in embryogenesis
    • Brawley SH, Robinson KR. Cytochalasin treatment disrupts the endogenous currents associated with cell polarization in fucoid zygotes: studies of the role of F-actin in embryogenesis. J Cell Biol. 1985;100:1173-84.
    • (1985) J Cell Biol. , vol.100 , pp. 1173-1184
    • Brawley, S.H.1    Robinson, K.R.2
  • 141
    • 0019518333 scopus 로고
    • Effects of cytoskeletal disrupting agents on replication of bovine endothelium
    • Selden SC, Rabinovitch PS, Schwartz SM. Effects of cytoskeletal disrupting agents on replication of bovine endothelium. J Cell Physiol. 1981;108:195-211.
    • (1981) J Cell Physiol. , vol.108 , pp. 195-211
    • Selden, S.C.1    Rabinovitch, P.S.2    Schwartz, S.M.3
  • 142
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley LC. The phosphoinositide 3-kinase pathway. Science. 2002;296:1655-7.
    • (2002) Science. , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 143
    • 0028925751 scopus 로고
    • Signal transduction of phagocytosis
    • Greenberg S. Signal transduction of phagocytosis. Trends Cell Biol. 1995;5:93-9.
    • (1995) Trends Cell Biol. , vol.5 , pp. 93-99
    • Greenberg, S.1
  • 144
    • 0030250021 scopus 로고    scopus 로고
    • Inhibitory effect of wortmannin on phosphatidylinositol 3-kinase-mediated cellular events
    • Hazeki O, Hazeki K, Katada T, Ui M. Inhibitory effect of wortmannin on phosphatidylinositol 3-kinase-mediated cellular events. J Lipid Mediat Cell Signal. 1996;14:259-61.
    • (1996) J Lipid Mediat Cell Signal. , vol.14 , pp. 259-261
    • Hazeki, O.1    Hazeki, K.2    Katada, T.3    Ui, M.4
  • 145
    • 79952109804 scopus 로고    scopus 로고
    • Small molecule inhibitors of the PI3-kinase family
    • Knight ZA. Small molecule inhibitors of the PI3-kinase family. Curr Top Microbiol Immunol. 2010;347:263-78.
    • (2010) Curr Top Microbiol Immunol. , vol.347 , pp. 263-278
    • Knight, Z.A.1
  • 146
    • 0030459125 scopus 로고    scopus 로고
    • A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages
    • Araki N, Johnson MT, Swanson JA. A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages. J Cell Biol. 1996;135:1249-60.
    • (1996) J Cell Biol. , vol.135 , pp. 1249-1260
    • Araki, N.1    Johnson, M.T.2    Swanson, J.A.3
  • 147
    • 33646891942 scopus 로고    scopus 로고
    • Involvement of the Rho/Rac family member RhoG in caveolar endocytosis
    • Prieto-Sánchez RM, Berenjeno IM, Bustelo XR. Involvement of the Rho/Rac family member RhoG in caveolar endocytosis. Oncogene. 2006;25:2961-73.
    • (2006) Oncogene. , vol.25 , pp. 2961-2973
    • Prieto-Sánchez, R.M.1    Berenjeno, I.M.2    Bustelo, X.R.3
  • 148
    • 48749130913 scopus 로고    scopus 로고
    • Dynamics of dynamin during clathrin mediated endocytosis in PC12 cells
    • Rappoport JZ, Heyman KP, Kemal S, Simon SM. Dynamics of dynamin during clathrin mediated endocytosis in PC12 cells. PLoS One. 2008;3:e2416.
    • (2008) PLoS One. , vol.3
    • Rappoport, J.Z.1    Heyman, K.P.2    Kemal, S.3    Simon, S.M.4
  • 149
  • 151
    • 0030985763 scopus 로고    scopus 로고
    • Loss, restoration, and maintenance of plasma membrane integrity
    • McNeil PL, Steinhardt RA. Loss, restoration, and maintenance of plasma membrane integrity. J Cell Biol. 1997;137: 1-4.
    • (1997) J Cell Biol. , vol.137 , pp. 1-4
    • McNeil, P.L.1    Steinhardt, R.A.2
  • 153
    • 31544437691 scopus 로고    scopus 로고
    • A role for exosomes in the constitutive and stimulus-induced ectodomain cleavage of L1 and CD44
    • Stoeck A, Keller S, Riedle S, Sanderson MP, Runz S, Le Naour F, et al. A role for exosomes in the constitutive and stimulus-induced ectodomain cleavage of L1 and CD44. Biochem J. 2006;393:609-18.
    • (2006) Biochem J. , vol.393 , pp. 609-618
    • Stoeck, A.1    Keller, S.2    Riedle, S.3    Sanderson, M.P.4    Runz, S.5    Le Naour, F.6
  • 154
    • 4644366103 scopus 로고    scopus 로고
    • Complement inhibitor membrane cofactor protein (MCP; CD46) is constitutively shed from cancer cell membranes in vesicles and converted by a metalloproteinase to a functionally active soluble form
    • Hakulinen J, Junnikkala S, Sorsa T, Meri S. Complement inhibitor membrane cofactor protein (MCP; CD46) is constitutively shed from cancer cell membranes in vesicles and converted by a metalloproteinase to a functionally active soluble form. Eur J Immunol. 2004;34:2620-9.
    • (2004) Eur J Immunol. , vol.34 , pp. 2620-2629
    • Hakulinen, J.1    Junnikkala, S.2    Sorsa, T.3    Meri, S.4
  • 155
    • 0842277810 scopus 로고    scopus 로고
    • Release of full-length 55-kDa TNF receptor 1 in exosome-like vesicles: a mechanism for generation of soluble cytokine receptors
    • Hawari FI, Rouhani FN, Cui X, Yu ZX, Buckley C, Kaler M, et al. Release of full-length 55-kDa TNF receptor 1 in exosome-like vesicles: a mechanism for generation of soluble cytokine receptors. Proc Natl Acad Sci U S A. 2004;101: 1297-302.
    • (2004) Proc Natl Acad Sci U S A. , vol.101 , pp. 1297-1302
    • Hawari, F.I.1    Rouhani, F.N.2    Cui, X.3    Yu, Z.X.4    Buckley, C.5    Kaler, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.