메뉴 건너뛰기




Volumn 6, Issue 1, 2017, Pages

The role of exosomes in the pathogenesis of Alzheimer' disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; TAU PROTEIN;

EID: 85011343408     PISSN: None     EISSN: 20479158     Source Type: Journal    
DOI: 10.1186/s40035-017-0072-x     Document Type: Review
Times cited : (103)

References (76)
  • 1
    • 84861882207 scopus 로고    scopus 로고
    • Analysis of PLA2G6 gene mutation in sporadic early-onset parkinsonism patients from Chinese population
    • Tian JY, Tang BS, Shi CH, Lv ZY, Li K, Yu RL, et al. Analysis of PLA2G6 gene mutation in sporadic early-onset parkinsonism patients from Chinese population. Neurosci Lett. 2012;514(2):156-8. doi: 10.1016/j.neulet.2012.02.078.
    • (2012) Neurosci Lett , vol.514 , Issue.2 , pp. 156-158
    • Tian, J.Y.1    Tang, B.S.2    Shi, C.H.3    Lv, Z.Y.4    Li, K.5    Yu, R.L.6
  • 2
    • 84925880097 scopus 로고    scopus 로고
    • Alzheimer's disease facts and figures
    • Alzheimer's A. Alzheimer's disease facts and figures. Alzheimers Dement. 2015;11(3):332-84.
    • (2015) Alzheimers Dement , vol.11 , Issue.3 , pp. 332-384
    • Alzheimer's, A.1
  • 3
    • 79956098248 scopus 로고    scopus 로고
    • Toward defining the preclinical stages of Alzheimer's disease: recommendations from the National Institute on Aging-Alzheimer's Association workgroups on diagnostic guidelines for Alzheimer's disease
    • Sperling RA, Aisen PS, Beckett LA, Bennett DA, Craft S, Fagan AM, et al. Toward defining the preclinical stages of Alzheimer's disease: recommendations from the National Institute on Aging-Alzheimer's Association workgroups on diagnostic guidelines for Alzheimer's disease. Alzheimers Dement. 2011;7(3):280-92. doi: 10.1016/j.jalz.2011.03.003.
    • (2011) Alzheimers Dement , vol.7 , Issue.3 , pp. 280-292
    • Sperling, R.A.1    Aisen, P.S.2    Beckett, L.A.3    Bennett, D.A.4    Craft, S.5    Fagan, A.M.6
  • 5
    • 84866555624 scopus 로고    scopus 로고
    • Potential contribution of exosomes to the prion-like propagation of lesions in Alzheimer's disease
    • Vingtdeux V, Sergeant N, Buee L. Potential contribution of exosomes to the prion-like propagation of lesions in Alzheimer's disease. Front Physiol. 2012;3:229. doi: 10.3389/fphys.2012.00229.
    • (2012) Front Physiol , vol.3 , pp. 229
    • Vingtdeux, V.1    Sergeant, N.2    Buee, L.3
  • 6
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak H, Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol. 1991;82(4):239-59.
    • (1991) Acta Neuropathol , vol.82 , Issue.4 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 7
    • 84947460163 scopus 로고    scopus 로고
    • Extracellular membrane vesicles as vehicles for brain cell-to-cell interactions in physiological as well as pathological conditions
    • Schiera G, Di Liegro CM, Di Liegro I. Extracellular membrane vesicles as vehicles for brain cell-to-cell interactions in physiological as well as pathological conditions. Biomed Res Int. 2015;2015:152926. doi: 10.1155/2015/152926.
    • (2015) Biomed Res Int , vol.2015 , pp. 152926
    • Schiera, G.1    Liegro, C.M.2    Liegro, I.3
  • 8
    • 33746593662 scopus 로고    scopus 로고
    • Alzheimer's disease beta-amyloid peptides are released in association with exosomes
    • Rajendran L, Honsho M, Zahn TR, Keller P, Geiger KD, Verkade P, et al. Alzheimer's disease beta-amyloid peptides are released in association with exosomes. Proc Natl Acad Sci U S A. 2006;103(30):11172-7. doi: 10.1073/pnas.0603838103.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.30 , pp. 11172-11177
    • Rajendran, L.1    Honsho, M.2    Zahn, T.R.3    Keller, P.4    Geiger, K.D.5    Verkade, P.6
  • 9
    • 84973570803 scopus 로고    scopus 로고
    • Impact of lysosome status on extracellular vesicle content and release
    • Eitan E, Suire C, Zhang S, Mattson MP. Impact of lysosome status on extracellular vesicle content and release. Ageing Res Rev. 2016. doi: 10.1016/j.arr.2016.05.001.
    • (2016) Ageing Res Rev
    • Eitan, E.1    Suire, C.2    Zhang, S.3    Mattson, M.P.4
  • 10
    • 0020804037 scopus 로고
    • Receptor-mediated endocytosis of transferrin and recycling of the transferrin receptor in rat reticulocytes
    • Harding C, Heuser J, Stahl P. Receptor-mediated endocytosis of transferrin and recycling of the transferrin receptor in rat reticulocytes. J Cell Biol. 1983;97(2):329-39.
    • (1983) J Cell Biol , vol.97 , Issue.2 , pp. 329-339
    • Harding, C.1    Heuser, J.2    Stahl, P.3
  • 11
    • 0020956787 scopus 로고
    • Fate of the transferrin receptor during maturation of sheep reticulocytes in vitro: selective externalization of the receptor
    • Pan BT, Johnstone RM. Fate of the transferrin receptor during maturation of sheep reticulocytes in vitro: selective externalization of the receptor. Cell. 1983;33(3):967-78.
    • (1983) Cell , vol.33 , Issue.3 , pp. 967-978
    • Pan, B.T.1    Johnstone, R.M.2
  • 12
    • 0022201056 scopus 로고
    • Electron microscopic evidence for externalization of the transferrin receptor in vesicular form in sheep reticulocytes
    • Pan BT, Teng K, Wu C, Adam M, Johnstone RM. Electron microscopic evidence for externalization of the transferrin receptor in vesicular form in sheep reticulocytes. J Cell Biol. 1985;101(3):942-8.
    • (1985) J Cell Biol , vol.101 , Issue.3 , pp. 942-948
    • Pan, B.T.1    Teng, K.2    Wu, C.3    Adam, M.4    Johnstone, R.M.5
  • 13
    • 0036827031 scopus 로고    scopus 로고
    • Intraneuronal Alzheimer abeta42 accumulates in multivesicular bodies and is associated with synaptic pathology
    • Takahashi RH, Milner TA, Li F, Nam EE, Edgar MA, Yamaguchi H, et al. Intraneuronal Alzheimer abeta42 accumulates in multivesicular bodies and is associated with synaptic pathology. Am J Pathol. 2002;161(5):1869-79.
    • (2002) Am J Pathol , vol.161 , Issue.5 , pp. 1869-1879
    • Takahashi, R.H.1    Milner, T.A.2    Li, F.3    Nam, E.E.4    Edgar, M.A.5    Yamaguchi, H.6
  • 14
    • 84962733931 scopus 로고    scopus 로고
    • Introduction to extracellular vesicles: biogenesis, RNA cargo selection, content, release, and uptake
    • Abels ER, Breakefield XO. Introduction to extracellular vesicles: biogenesis, RNA cargo selection, content, release, and uptake. Cell Mol Neurobiol. 2016;36(3):301-12. doi: 10.1007/s10571-016-0366-z.
    • (2016) Cell Mol Neurobiol , vol.36 , Issue.3 , pp. 301-312
    • Abels, E.R.1    Breakefield, X.O.2
  • 15
    • 84904704297 scopus 로고    scopus 로고
    • Biogenesis, secretion, and intercellular interactions of exosomes and other extracellular vesicles
    • Colombo M, Raposo G, Thery C. Biogenesis, secretion, and intercellular interactions of exosomes and other extracellular vesicles. Annu Rev Cell Dev Biol. 2014;30:255-89. doi: 10.1146/annurev-cellbio-101512-122326.
    • (2014) Annu Rev Cell Dev Biol , vol.30 , pp. 255-289
    • Colombo, M.1    Raposo, G.2    Thery, C.3
  • 16
    • 84960969593 scopus 로고    scopus 로고
    • Exosomes and other extracellular vesicles in neural cells and neurodegenerative diseases
    • Janas AM, Sapon K, Janas T, Stowell MH, Janas T. Exosomes and other extracellular vesicles in neural cells and neurodegenerative diseases. Biochim Biophys Acta. 2016;1858(6):1139-51. doi: 10.1016/j.bbamem.2016.02.011.
    • (2016) Biochim Biophys Acta , vol.1858 , Issue.6 , pp. 1139-1151
    • Janas, A.M.1    Sapon, K.2    Janas, T.3    Stowell, M.H.4    Janas, T.5
  • 17
    • 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(1):108-20. doi: 10.1016/j.bbalip.2013.10.004.
    • (2014) Biochim Biophys Acta , vol.1841 , Issue.1 , pp. 108-120
    • Record, M.1    Carayon, K.2    Poirot, M.3    Silvente-Poirot, S.4
  • 18
    • 84929292388 scopus 로고    scopus 로고
    • Extracellular vesicles in cancer: exosomes, microvesicles and the emerging role of large oncosomes
    • Minciacchi VR, Freeman MR, Di Vizio D. Extracellular vesicles in cancer: exosomes, microvesicles and the emerging role of large oncosomes. Semin Cell Dev Biol. 2015;40:41-51. doi: 10.1016/j.semcdb.2015.02.010.
    • (2015) Semin Cell Dev Biol , vol.40 , pp. 41-51
    • Minciacchi, V.R.1    Freeman, M.R.2    Vizio, D.3
  • 19
    • 69949117622 scopus 로고    scopus 로고
    • Multivesicular bodies associate with components of miRNA effector complexes and modulate miRNA activity
    • Gibbings DJ, Ciaudo C, Erhardt M, Voinnet O. Multivesicular bodies associate with components of miRNA effector complexes and modulate miRNA activity. Nat Cell Biol. 2009;11(9):1143-9. doi: 10.1038/ncb1929.
    • (2009) Nat Cell Biol , vol.11 , Issue.9 , pp. 1143-1149
    • Gibbings, D.J.1    Ciaudo, C.2    Erhardt, M.3    Voinnet, O.4
  • 20
    • 77952920881 scopus 로고    scopus 로고
    • Secretory mechanisms and intercellular transfer of microRNAs in living cells
    • Kosaka N, Iguchi H, Yoshioka Y, Takeshita F, Matsuki Y, Ochiya T. Secretory mechanisms and intercellular transfer of microRNAs in living cells. J Biol Chem. 2010;285(23):17442-52. doi: 10.1074/jbc.M110.107821.
    • (2010) J Biol Chem , vol.285 , Issue.23 , pp. 17442-17452
    • Kosaka, N.1    Iguchi, H.2    Yoshioka, Y.3    Takeshita, F.4    Matsuki, Y.5    Ochiya, T.6
  • 21
    • 67249110996 scopus 로고    scopus 로고
    • Multivesicular endosome biogenesis in the absence of ESCRTs
    • Stuffers S, Sem Wegner C, Stenmark H, Brech A. Multivesicular endosome biogenesis in the absence of ESCRTs. Traffic. 2009;10(7):925-37. doi: 10.1111/j.1600-0854.2009.00920.x.
    • (2009) Traffic , vol.10 , Issue.7 , pp. 925-937
    • Stuffers, S.1    Sem Wegner, C.2    Stenmark, H.3    Brech, A.4
  • 22
    • 84929330896 scopus 로고    scopus 로고
    • The 5XFAD mouse model of alzheimer's disease exhibits an age-dependent increase in anti-ceramide igg and exogenous administration of ceramide further increases anti-ceramide titers and amyloid plaque burden
    • Dinkins MB, Dasgupta S, Wang G, Zhu G, He Q, Kong JN, et al. The 5XFAD mouse model of alzheimer's disease exhibits an age-dependent increase in anti-ceramide igg and exogenous administration of ceramide further increases anti-ceramide titers and amyloid plaque burden. J Alzheimer's Dis. 2015;46(1):55-61. doi: 10.3233/JAD-150088.
    • (2015) J Alzheimer's Dis , vol.46 , Issue.1 , pp. 55-61
    • Dinkins, M.B.1    Dasgupta, S.2    Wang, G.3    Zhu, G.4    He, Q.5    Kong, J.N.6
  • 23
    • 84922340030 scopus 로고    scopus 로고
    • The neutral sphingomyelinase pathway regulates packaging of the prion protein into exosomes
    • Guo BB, Bellingham SA, Hill AF. The neutral sphingomyelinase pathway regulates packaging of the prion protein into exosomes. J Biol Chem. 2015;290(6):3455-67. doi: 10.1074/jbc.M114.605253.
    • (2015) J Biol Chem , vol.290 , Issue.6 , pp. 3455-3467
    • Guo, B.B.1    Bellingham, S.A.2    Hill, A.F.3
  • 24
    • 77957325731 scopus 로고    scopus 로고
    • Multivesicular body formation requires OSBP-related proteins and cholesterol
    • Kobuna H, Inoue T, Shibata M, Gengyo-Ando K, Yamamoto A, Mitani S et al. Multivesicular body formation requires OSBP-related proteins and cholesterol. PLoS genetics. 2010;6(8). doi: 10.1371/journal.pgen.1001055.
    • (2010) PLoS genetics , vol.6 , Issue.8
    • Kobuna, H.1    Inoue, T.2    Shibata, M.3    Gengyo-Ando, K.4    Yamamoto, A.5    Mitani, S.6
  • 25
    • 0035008062 scopus 로고    scopus 로고
    • Cholesterol requirement for cation-independent mannose 6-phosphate receptor exit from multivesicular late endosomes to the Golgi
    • Miwako I, Yamamoto A, Kitamura T, Nagayama K, Ohashi M. Cholesterol requirement for cation-independent mannose 6-phosphate receptor exit from multivesicular late endosomes to the Golgi. J Cell Sci. 2001;114(Pt 9):1765-76.
    • (2001) J Cell Sci , vol.114 , pp. 1765-1776
    • Miwako, I.1    Yamamoto, A.2    Kitamura, T.3    Nagayama, K.4    Ohashi, M.5
  • 26
    • 84890458696 scopus 로고    scopus 로고
    • Analysis of ESCRT functions in exosome biogenesis, composition and secretion highlights the heterogeneity of extracellular vesicles
    • Colombo M, Moita C, van Niel G, Kowal J, Vigneron J, Benaroch P, et al. Analysis of ESCRT functions in exosome biogenesis, composition and secretion highlights the heterogeneity of extracellular vesicles. J Cell Sci. 2013;126(Pt 24):5553-65. doi: 10.1242/jcs.128868.
    • (2013) J Cell Sci , vol.126 , pp. 5553-5565
    • Colombo, M.1    Moita, C.2    Niel, G.3    Kowal, J.4    Vigneron, J.5    Benaroch, P.6
  • 27
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic
    • Stenmark H. Rab GTPases as coordinators of vesicle traffic. Nat Rev Mol Cell Biol. 2009;10(8):513-25. doi: 10.1038/nrm2728.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , Issue.8 , pp. 513-525
    • Stenmark, H.1
  • 28
    • 77951183654 scopus 로고    scopus 로고
    • Regulation of exosome secretion by Rab35 and its GTPase-activating proteins TBC1D10A-C
    • Hsu C, Morohashi Y, Yoshimura S, Manrique-Hoyos N, Jung S, Lauterbach MA, et al. Regulation of exosome secretion by Rab35 and its GTPase-activating proteins TBC1D10A-C. J Cell Biol. 2010;189(2):223-32. doi: 10.1083/jcb.200911018.
    • (2010) J Cell Biol , vol.189 , Issue.2 , pp. 223-232
    • Hsu, C.1    Morohashi, Y.2    Yoshimura, S.3    Manrique-Hoyos, N.4    Jung, S.5    Lauterbach, M.A.6
  • 29
    • 84964507658 scopus 로고    scopus 로고
    • Axonal maintenance, glia, exosomes, and heat shock proteins
    • Tytell M, Lasek RJ, Gainer H. Axonal maintenance, glia, exosomes, and heat shock proteins. F1000Research. 2016;5. doi: 10.12688/f1000research.7247.1.
    • (2016) F1000Research , pp. 5
    • Tytell, M.1    Lasek, R.J.2    Gainer, H.3
  • 30
    • 84934270711 scopus 로고    scopus 로고
    • Emerging roles of exosomes in normal and pathological conditions: new insights for diagnosis and therapeutic applications
    • De Toro J, Herschlik L, Waldner C, Mongini C. Emerging roles of exosomes in normal and pathological conditions: new insights for diagnosis and therapeutic applications. Front Immunol. 2015;6:203. doi: 10.3389/fimmu.2015.00203.
    • (2015) Front Immunol , vol.6 , pp. 203
    • Toro, J.1    Herschlik, L.2    Waldner, C.3    Mongini, C.4
  • 32
    • 84974530686 scopus 로고    scopus 로고
    • Extracellular vesicles isolated from the brains of rTg4510 mice seed Tau protein aggregation in a threshold-dependent manner
    • Polanco JC, Scicluna BJ, Hill AF, Gotz J. Extracellular vesicles isolated from the brains of rTg4510 mice seed Tau protein aggregation in a threshold-dependent manner. J Biol Chem. 2016;291(24):12445-66. doi: 10.1074/jbc.M115.709485.
    • (2016) J Biol Chem , vol.291 , Issue.24 , pp. 12445-12466
    • Polanco, J.C.1    Scicluna, B.J.2    Hill, A.F.3    Gotz, J.4
  • 33
    • 84961231281 scopus 로고    scopus 로고
    • alpha-Synuclein in extracellular vesicles: functional implications and diagnostic opportunities
    • Loov C, Scherzer CR, Hyman BT, Breakefield XO, Ingelsson M. alpha-Synuclein in extracellular vesicles: functional implications and diagnostic opportunities. Cell Mol Neurobiol. 2016;36(3):437-48. doi: 10.1007/s10571-015-0317-0.
    • (2016) Cell Mol Neurobiol , vol.36 , Issue.3 , pp. 437-448
    • Loov, C.1    Scherzer, C.R.2    Hyman, B.T.3    Breakefield, X.O.4    Ingelsson, M.5
  • 34
    • 84943414298 scopus 로고    scopus 로고
    • Exposure to ALS-FTD-CSF generates TDP-43 aggregates in glioblastoma cells through exosomes and TNTs-like structure
    • Ding X, Ma M, Teng J, Teng RK, Zhou S, Yin J, et al. Exposure to ALS-FTD-CSF generates TDP-43 aggregates in glioblastoma cells through exosomes and TNTs-like structure. Oncotarget. 2015;6(27):24178-91. doi: 10.18632/oncotarget.4680.
    • (2015) Oncotarget , vol.6 , Issue.27 , pp. 24178-24191
    • Ding, X.1    Ma, M.2    Teng, J.3    Teng, R.K.4    Zhou, S.5    Yin, J.6
  • 36
    • 84957952693 scopus 로고    scopus 로고
    • Physiological and pathological roles of exosomes in the nervous system
    • Yuyama K, Igarashi Y. Physiological and pathological roles of exosomes in the nervous system. Biomol Concepts. 2016;7(1):53-68. doi: 10.1515/bmc-2015-0033.
    • (2016) Biomol Concepts , vol.7 , Issue.1 , pp. 53-68
    • Yuyama, K.1    Igarashi, Y.2
  • 37
    • 84960907941 scopus 로고    scopus 로고
    • Exogenous DNA loading into extracellular vesicles via electroporation is size-dependent and enables limited gene delivery
    • Lamichhane TN, Raiker RS, Jay SM. Exogenous DNA loading into extracellular vesicles via electroporation is size-dependent and enables limited gene delivery. Mol Pharm. 2015;12(10):3650-7. doi: 10.1021/acs.molpharmaceut.5b00364.
    • (2015) Mol Pharm , vol.12 , Issue.10 , pp. 3650-3657
    • Lamichhane, T.N.1    Raiker, R.S.2    Jay, S.M.3
  • 38
    • 84877298502 scopus 로고    scopus 로고
    • Characterization of human plasma-derived exosomal RNAs by deep sequencing
    • Huang X, Yuan T, Tschannen M, Sun Z, Jacob H, Du M, et al. Characterization of human plasma-derived exosomal RNAs by deep sequencing. BMC Genomics. 2013;14:319. doi: 10.1186/1471-2164-14-319.
    • (2013) BMC Genomics , vol.14 , pp. 319
    • Huang, X.1    Yuan, T.2    Tschannen, M.3    Sun, Z.4    Jacob, H.5    Du, M.6
  • 39
    • 84888329506 scopus 로고    scopus 로고
    • Characterization of RNA in exosomes secreted by human breast cancer cell lines using next-generation sequencing
    • Jenjaroenpun P, Kremenska Y, Nair VM, Kremenskoy M, Joseph B, Kurochkin IV. Characterization of RNA in exosomes secreted by human breast cancer cell lines using next-generation sequencing. PeerJ. 2013;1:e201. doi: 10.7717/peerj.201.
    • (2013) PeerJ , vol.1
    • Jenjaroenpun, P.1    Kremenska, Y.2    Nair, V.M.3    Kremenskoy, M.4    Joseph, B.5    Kurochkin, I.V.6
  • 40
    • 85026337731 scopus 로고    scopus 로고
    • Distinct RNA profiles in subpopulations of extracellular vesicles: apoptotic bodies, microvesicles and exosomes
    • Crescitelli R, Lasser C, Szabo TG, Kittel A, Eldh M, Dianzani I et al. Distinct RNA profiles in subpopulations of extracellular vesicles: apoptotic bodies, microvesicles and exosomes. J Extracell Vesicles. 2013;2. doi: 10.3402/jev.v2i0.20677.
    • (2013) J Extracell Vesicles , pp. 2
    • Crescitelli, R.1    Lasser, C.2    Szabo, T.G.3    Kittel, A.4    Eldh, M.5    Dianzani, I.6
  • 41
    • 84938747588 scopus 로고    scopus 로고
    • Circular RNA is enriched and stable in exosomes: a promising biomarker for cancer diagnosis
    • Li Y, Zheng Q, Bao C, Li S, Guo W, Zhao J, et al. Circular RNA is enriched and stable in exosomes: a promising biomarker for cancer diagnosis. Cell Res. 2015;25(8):981-4. doi: 10.1038/cr.2015.82.
    • (2015) Cell Res , vol.25 , Issue.8 , pp. 981-984
    • Li, Y.1    Zheng, Q.2    Bao, C.3    Li, S.4    Guo, W.5    Zhao, J.6
  • 42
    • 84977103339 scopus 로고    scopus 로고
    • Circulating long RNAs in serum extracellular vesicles: their characterization and potential application as biomarkers for diagnosis of colorectal cancer
    • Dong L, Lin W, Qi P, Xu MD, Wu X, Ni S, et al. Circulating long RNAs in serum extracellular vesicles: their characterization and potential application as biomarkers for diagnosis of colorectal cancer. Cancer Epidemiol Biomarkers Prev. 2016;25(7):1158-66. doi: 10.1158/1055-9965.EPI-16-0006.
    • (2016) Cancer Epidemiol Biomarkers Prev , vol.25 , Issue.7 , pp. 1158-1166
    • Dong, L.1    Lin, W.2    Qi, P.3    Xu, M.D.4    Wu, X.5    Ni, S.6
  • 43
    • 34249302620 scopus 로고    scopus 로고
    • Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells
    • Valadi H, Ekstrom K, Bossios A, Sjostrand M, Lee JJ, Lotvall JO. Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells. Nat Cell Biol. 2007;9(6):654-9. doi: 10.1038/ncb1596.
    • (2007) Nat Cell Biol , vol.9 , Issue.6 , pp. 654-659
    • Valadi, H.1    Ekstrom, K.2    Bossios, A.3    Sjostrand, M.4    Lee, J.J.5    Lotvall, J.O.6
  • 44
    • 84977567322 scopus 로고    scopus 로고
    • Exosome-mediated transfer of miR-222 is sufficient to increase tumor malignancy in melanoma
    • Felicetti F, De Feo A, Coscia C, Puglisi R, Pedini F, Pasquini L, et al. Exosome-mediated transfer of miR-222 is sufficient to increase tumor malignancy in melanoma. J Transl Med. 2016;14:56. doi: 10.1186/s12967-016-0811-2.
    • (2016) J Transl Med , vol.14 , pp. 56
    • Felicetti, F.1    Feo, A.2    Coscia, C.3    Puglisi, R.4    Pedini, F.5    Pasquini, L.6
  • 45
    • 84962610919 scopus 로고    scopus 로고
    • Improvement of neuronal cell survival by astrocyte-derived exosomes under hypoxic and ischemic conditions depends on prion protein
    • Guitart K, Loers G, Buck F, Bork U, Schachner M, Kleene R. Improvement of neuronal cell survival by astrocyte-derived exosomes under hypoxic and ischemic conditions depends on prion protein. Glia. 2016;64(6):896-910. doi: 10.1002/glia.22963.
    • (2016) Glia , vol.64 , Issue.6 , pp. 896-910
    • Guitart, K.1    Loers, G.2    Buck, F.3    Bork, U.4    Schachner, M.5    Kleene, R.6
  • 46
    • 84906097556 scopus 로고    scopus 로고
    • Multifaceted effects of oligodendroglial exosomes on neurons: impact on neuronal firing rate, signal transduction and gene regulation
    • Frohlich D, Kuo WP, Fruhbeis C, Sun JJ, Zehendner CM, Luhmann HJ et al. Multifaceted effects of oligodendroglial exosomes on neurons: impact on neuronal firing rate, signal transduction and gene regulation. Philos Trans R Soc Lond B Biol Sci. 2014;369(1652). doi: 10.1098/rstb.2013.0510.
    • (2014) Philos Trans R Soc Lond B Biol Sci , vol.369 , Issue.1652
    • Frohlich, D.1    Kuo, W.P.2    Fruhbeis, C.3    Sun, J.J.4    Zehendner, C.M.5    Luhmann, H.J.6
  • 47
    • 84945474523 scopus 로고    scopus 로고
    • Depletion of microglia and inhibition of exosome synthesis halt tau propagation
    • Asai H, Ikezu S, Tsunoda S, Medalla M, Luebke J, Haydar T, et al. Depletion of microglia and inhibition of exosome synthesis halt tau propagation. Nat Neurosci. 2015;18(11):1584-93. doi: 10.1038/nn.4132.
    • (2015) Nat Neurosci , vol.18 , Issue.11 , pp. 1584-1593
    • Asai, H.1    Ikezu, S.2    Tsunoda, S.3    Medalla, M.4    Luebke, J.5    Haydar, T.6
  • 48
    • 43249087541 scopus 로고    scopus 로고
    • Inhibition of gamma-secretase causes increased secretion of amyloid precursor protein C-terminal fragments in association with exosomes
    • Sharples RA, Vella LJ, Nisbet RM, Naylor R, Perez K, Barnham KJ, et al. Inhibition of gamma-secretase causes increased secretion of amyloid precursor protein C-terminal fragments in association with exosomes. FASEB J. 2008;22(5):1469-78. doi: 10.1096/fj.07-9357com.
    • (2008) FASEB J , vol.22 , Issue.5 , pp. 1469-1478
    • Sharples, R.A.1    Vella, L.J.2    Nisbet, R.M.3    Naylor, R.4    Perez, K.5    Barnham, K.J.6
  • 49
    • 84899488150 scopus 로고    scopus 로고
    • Exosomes as mediators of neuroinflammation
    • Gupta A, Pulliam L. Exosomes as mediators of neuroinflammation. J Neuroinflammation. 2014;11:68. doi: 10.1186/1742-2094-11-68.
    • (2014) J Neuroinflammation , vol.11 , pp. 68
    • Gupta, A.1    Pulliam, L.2
  • 50
    • 84979201265 scopus 로고    scopus 로고
    • Biogenesis and functions of exosomes and extracellular vesicles
    • Dreyer F, Baur A. Biogenesis and functions of exosomes and extracellular vesicles. Methods Mol Biol. 2016;1448:201-16. doi: 10.1007/978-1-4939-3753-0_15.
    • (2016) Methods Mol Biol , vol.1448 , pp. 201-216
    • Dreyer, F.1    Baur, A.2
  • 51
    • 84960337763 scopus 로고    scopus 로고
    • Communication by extracellular vesicles: where we are and where we need to go
    • Tkach M, Thery C. Communication by extracellular vesicles: where we are and where we need to go. Cell. 2016;164(6):1226-32. doi: 10.1016/j.cell.2016.01.043.
    • (2016) Cell , vol.164 , Issue.6 , pp. 1226-1232
    • Tkach, M.1    Thery, C.2
  • 52
    • 84938713652 scopus 로고    scopus 로고
    • Exosomes secreted by cortical neurons upon glutamatergic synapse activation specifically interact with neurons
    • Chivet M, Javalet C, Laulagnier K, Blot B, Hemming FJ, Sadoul R. Exosomes secreted by cortical neurons upon glutamatergic synapse activation specifically interact with neurons. J Extracell Vesicles. 2014;3:24722.
    • (2014) J Extracell Vesicles , vol.3 , pp. 24722
    • Chivet, M.1    Javalet, C.2    Laulagnier, K.3    Blot, B.4    Hemming, F.J.5    Sadoul, R.6
  • 53
    • 84887392802 scopus 로고    scopus 로고
    • Exosomes neutralize synaptic-plasticity-disrupting activity of Abeta assemblies in vivo
    • An K, Klyubin I, Kim Y, Jung JH, Mably AJ, O'Dowd ST, et al. Exosomes neutralize synaptic-plasticity-disrupting activity of Abeta assemblies in vivo. Mol Brain. 2013;6:47. doi: 10.1186/1756-6606-6-47.
    • (2013) Mol Brain , vol.6 , pp. 47
    • An, K.1    Klyubin, I.2    Kim, Y.3    Jung, J.H.4    Mably, A.J.5    O'Dowd, S.T.6
  • 54
    • 84868244886 scopus 로고    scopus 로고
    • Neurochemical biomarkers in Alzheimer's disease and related disorders
    • Bibl M, Esselmann H, Wiltfang J. Neurochemical biomarkers in Alzheimer's disease and related disorders. Ther Adv Neurol Disord. 2012;5(6):335-48. doi: 10.1177/1756285612455367.
    • (2012) Ther Adv Neurol Disord , vol.5 , Issue.6 , pp. 335-348
    • Bibl, M.1    Esselmann, H.2    Wiltfang, J.3
  • 55
    • 0842297602 scopus 로고
    • The beta-amyloid protein precursor of Alzheimer disease has soluble derivatives found in human brain and cerebrospinal fluid
    • Palmert MR, Podlisny MB, Witker DS, Oltersdorf T, Younkin LH, Selkoe DJ, et al. The beta-amyloid protein precursor of Alzheimer disease has soluble derivatives found in human brain and cerebrospinal fluid. Proc Natl Acad Sci U S A. 1989;86(16):6338-42.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , Issue.16 , pp. 6338-6342
    • Palmert, M.R.1    Podlisny, M.B.2    Witker, D.S.3    Oltersdorf, T.4    Younkin, L.H.5    Selkoe, D.J.6
  • 56
    • 84865145017 scopus 로고    scopus 로고
    • New highly sensitive rodent and human tests for soluble amyloid precursor protein alpha quantification: preclinical and clinical applications in Alzheimer's disease
    • Rose C, Peoc'h K, Chasseigneaux S, Paquet C, Dumurgier J, Bourasset F, et al. New highly sensitive rodent and human tests for soluble amyloid precursor protein alpha quantification: preclinical and clinical applications in Alzheimer's disease. BMC Neurosci. 2012;13:84. doi: 10.1186/1471-2202-13-84.
    • (2012) BMC Neurosci , vol.13 , pp. 84
    • Rose, C.1    Peoc'h, K.2    Chasseigneaux, S.3    Paquet, C.4    Dumurgier, J.5    Bourasset, F.6
  • 58
    • 34547093203 scopus 로고    scopus 로고
    • Alkalizing drugs induce accumulation of amyloid precursor protein by-products in luminal vesicles of multivesicular bodies
    • Vingtdeux V, Hamdane M, Loyens A, Gele P, Drobeck H, Begard S, et al. Alkalizing drugs induce accumulation of amyloid precursor protein by-products in luminal vesicles of multivesicular bodies. J Biol Chem. 2007;282(25):18197-205. doi: 10.1074/jbc.M609475200.
    • (2007) J Biol Chem , vol.282 , Issue.25 , pp. 18197-18205
    • Vingtdeux, V.1    Hamdane, M.2    Loyens, A.3    Gele, P.4    Drobeck, H.5    Begard, S.6
  • 59
    • 84929269782 scopus 로고    scopus 로고
    • Extracellular vesicles--Their role in the packaging and spread of misfolded proteins associated with neurodegenerative diseases
    • Coleman BM, Hill AF. Extracellular vesicles--Their role in the packaging and spread of misfolded proteins associated with neurodegenerative diseases. Semin Cell Dev Biol. 2015;40:89-96. doi: 10.1016/j.semcdb.2015.02.007.
    • (2015) Semin Cell Dev Biol , vol.40 , pp. 89-96
    • Coleman, B.M.1    Hill, A.F.2
  • 60
    • 35148816608 scopus 로고    scopus 로고
    • Endosomal accumulation of GM1 ganglioside-bound amyloid beta-protein in neurons of aged monkey brains
    • Kimura N, Yanagisawa K. Endosomal accumulation of GM1 ganglioside-bound amyloid beta-protein in neurons of aged monkey brains. Neuroreport. 2007;18(16):1669-73. doi: 10.1097/WNR.0b013e3282f0d2ab.
    • (2007) Neuroreport , vol.18 , Issue.16 , pp. 1669-1673
    • Kimura, N.1    Yanagisawa, K.2
  • 61
    • 41149088714 scopus 로고    scopus 로고
    • Accelerated release of exosome-associated GM1 ganglioside (GM1) by endocytic pathway abnormality: another putative pathway for GM1-induced amyloid fibril formation
    • Yuyama K, Yamamoto N, Yanagisawa K. Accelerated release of exosome-associated GM1 ganglioside (GM1) by endocytic pathway abnormality: another putative pathway for GM1-induced amyloid fibril formation. J Neurochem. 2008;105(1):217-24. doi: 10.1111/j.1471-4159.2007.05128.x.
    • (2008) J Neurochem , vol.105 , Issue.1 , pp. 217-224
    • Yuyama, K.1    Yamamoto, N.2    Yanagisawa, K.3
  • 62
    • 84862274671 scopus 로고    scopus 로고
    • Astrocytes secrete exosomes enriched with proapoptotic ceramide and prostate apoptosis response 4 (PAR-4): potential mechanism of apoptosis induction in Alzheimer disease (AD)
    • Wang G, Dinkins M, He Q, Zhu G, Poirier C, Campbell A, et al. Astrocytes secrete exosomes enriched with proapoptotic ceramide and prostate apoptosis response 4 (PAR-4): potential mechanism of apoptosis induction in Alzheimer disease (AD). J Biol Chem. 2012;287(25):21384-95. doi: 10.1074/jbc.M112.340513.
    • (2012) J Biol Chem , vol.287 , Issue.25 , pp. 21384-21395
    • Wang, G.1    Dinkins, M.2    He, Q.3    Zhu, G.4    Poirier, C.5    Campbell, A.6
  • 63
    • 84899968840 scopus 로고    scopus 로고
    • Exosome reduction in vivo is associated with lower amyloid plaque load in the 5XFAD mouse model of Alzheimer's disease
    • Dinkins MB, Dasgupta S, Wang G, Zhu G, Bieberich E. Exosome reduction in vivo is associated with lower amyloid plaque load in the 5XFAD mouse model of Alzheimer's disease. Neurobiol Aging. 2014;35(8):1792-800. doi: 10.1016/j.neurobiolaging.2014.02.012.
    • (2014) Neurobiol Aging , vol.35 , Issue.8 , pp. 1792-1800
    • Dinkins, M.B.1    Dasgupta, S.2    Wang, G.3    Zhu, G.4    Bieberich, E.5
  • 64
    • 84906871864 scopus 로고    scopus 로고
    • Decreased amyloid-beta pathologies by intracerebral loading of glycosphingolipid-enriched exosomes in Alzheimer model mice
    • Yuyama K, Sun H, Sakai S, Mitsutake S, Okada M, Tahara H, et al. Decreased amyloid-beta pathologies by intracerebral loading of glycosphingolipid-enriched exosomes in Alzheimer model mice. J Biol Chem. 2014;289(35):24488-98. doi: 10.1074/jbc.M114.577213.
    • (2014) J Biol Chem , vol.289 , Issue.35 , pp. 24488-24498
    • Yuyama, K.1    Sun, H.2    Sakai, S.3    Mitsutake, S.4    Okada, M.5    Tahara, H.6
  • 65
    • 84918776208 scopus 로고    scopus 로고
    • A potential function for neuronal exosomes: sequestering intracerebral amyloid-beta peptide
    • Yuyama K, Sun H, Usuki S, Sakai S, Hanamatsu H, Mioka T, et al. A potential function for neuronal exosomes: sequestering intracerebral amyloid-beta peptide. FEBS Lett. 2015;589(1):84-8. doi: 10.1016/j.febslet.2014.11.027.
    • (2015) FEBS Lett , vol.589 , Issue.1 , pp. 84-88
    • Yuyama, K.1    Sun, H.2    Usuki, S.3    Sakai, S.4    Hanamatsu, H.5    Mioka, T.6
  • 66
    • 84859499570 scopus 로고    scopus 로고
    • Sphingolipid-modulated exosome secretion promotes clearance of amyloid-beta by microglia
    • Yuyama K, Sun H, Mitsutake S, Igarashi Y. Sphingolipid-modulated exosome secretion promotes clearance of amyloid-beta by microglia. J Biol Chem. 2012;287(14):10977-89. doi: 10.1074/jbc.M111.324616.
    • (2012) J Biol Chem , vol.287 , Issue.14 , pp. 10977-10989
    • Yuyama, K.1    Sun, H.2    Mitsutake, S.3    Igarashi, Y.4
  • 67
    • 84959300206 scopus 로고    scopus 로고
    • Exosomal cellular prion protein drives fibrillization of amyloid beta and counteracts amyloid beta-mediated neurotoxicity
    • Falker C, Hartmann A, Guett I, Dohler F, Altmeppen H, Betzel C, et al. Exosomal cellular prion protein drives fibrillization of amyloid beta and counteracts amyloid beta-mediated neurotoxicity. J Neurochem. 2016;137(1):88-100. doi: 10.1111/jnc.13514.
    • (2016) J Neurochem , vol.137 , Issue.1 , pp. 88-100
    • Falker, C.1    Hartmann, A.2    Guett, I.3    Dohler, F.4    Altmeppen, H.5    Betzel, C.6
  • 68
    • 80053289984 scopus 로고    scopus 로고
    • Tau accumulation causes mitochondrial distribution deficits in neurons in a mouse model of tauopathy and in human Alzheimer's disease brain
    • Kopeikina KJ, Carlson GA, Pitstick R, Ludvigson AE, Peters A, Luebke JI, et al. Tau accumulation causes mitochondrial distribution deficits in neurons in a mouse model of tauopathy and in human Alzheimer's disease brain. Am J Pathol. 2011;179(4):2071-82. doi: 10.1016/j.ajpath.2011.07.004.
    • (2011) Am J Pathol , vol.179 , Issue.4 , pp. 2071-2082
    • Kopeikina, K.J.1    Carlson, G.A.2    Pitstick, R.3    Ludvigson, A.E.4    Peters, A.5    Luebke, J.I.6
  • 69
    • 84863641754 scopus 로고    scopus 로고
    • Protein tau: prime cause of synaptic and neuronal degeneration in Alzheimer's disease
    • Crespo-Biel N, Theunis C, Van Leuven F. Protein tau: prime cause of synaptic and neuronal degeneration in Alzheimer's disease. Int J Alzheimers Dis. 2012;2012:251426. doi: 10.1155/2012/251426.
    • (2012) Int J Alzheimers Dis , vol.2012 , pp. 251426
    • Crespo-Biel, N.1    Theunis, C.2    Leuven, F.3
  • 70
    • 0025600995 scopus 로고
    • Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization
    • Goedert M, Jakes R. Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization. EMBO J. 1990;9(13):4225-30.
    • (1990) EMBO J , vol.9 , Issue.13 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 71
    • 80855138704 scopus 로고    scopus 로고
    • Neuropathology of frontotemporal lobar degeneration-tau (FTLD-tau)
    • Dickson DW, Kouri N, Murray ME, Josephs KA. Neuropathology of frontotemporal lobar degeneration-tau (FTLD-tau). J Mol Neurosci. 2011;45(3):384-9. doi: 10.1007/s12031-011-9589-0.
    • (2011) J Mol Neurosci , vol.45 , Issue.3 , pp. 384-389
    • Dickson, D.W.1    Kouri, N.2    Murray, M.E.3    Josephs, K.A.4
  • 72
    • 10744231654 scopus 로고    scopus 로고
    • 4-repeat tauopathy sharing pathological and biochemical features of corticobasal degeneration and progressive supranuclear palsy
    • Katsuse O, Iseki E, Arai T, Akiyama H, Togo T, Uchikado H, et al. 4-repeat tauopathy sharing pathological and biochemical features of corticobasal degeneration and progressive supranuclear palsy. Acta Neuropathol. 2003;106(3):251-60. doi: 10.1007/s00401-003-0728-8.
    • (2003) Acta Neuropathol , vol.106 , Issue.3 , pp. 251-260
    • Katsuse, O.1    Iseki, E.2    Arai, T.3    Akiyama, H.4    Togo, T.5    Uchikado, H.6
  • 73
    • 78549275132 scopus 로고    scopus 로고
    • Three- and four-repeat Tau coassemble into heterogeneous filaments: an implication for Alzheimer disease
    • Siddiqua A, Margittai M. Three- and four-repeat Tau coassemble into heterogeneous filaments: an implication for Alzheimer disease. J Biol Chem. 2010;285(48):37920-6. doi: 10.1074/jbc.M110.185728.
    • (2010) J Biol Chem , vol.285 , Issue.48 , pp. 37920-37926
    • Siddiqua, A.1    Margittai, M.2
  • 74
    • 79955441814 scopus 로고    scopus 로고
    • Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles
    • Guo JL, Lee VM. Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles. J Biol Chem. 2011;286(17):15317-31. doi: 10.1074/jbc.M110.209296.
    • (2011) J Biol Chem , vol.286 , Issue.17 , pp. 15317-15331
    • Guo, J.L.1    Lee, V.M.2
  • 75
    • 84929707383 scopus 로고    scopus 로고
    • Templated misfolding of Tau by prion-like seeding along neuronal connections impairs neuronal network function and associated behavioral outcomes in Tau transgenic mice
    • Stancu IC, Vasconcelos B, Ris L, Wang P, Villers A, Peeraer E, et al. Templated misfolding of Tau by prion-like seeding along neuronal connections impairs neuronal network function and associated behavioral outcomes in Tau transgenic mice. Acta Neuropathol. 2015;129(6):875-94. doi: 10.1007/s00401-015-1413-4.
    • (2015) Acta Neuropathol , vol.129 , Issue.6 , pp. 875-894
    • Stancu, I.C.1    Vasconcelos, B.2    Ris, L.3    Wang, P.4    Villers, A.5    Peeraer, E.6
  • 76
    • 84856707794 scopus 로고    scopus 로고
    • Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease
    • Saman S, Kim W, Raya M, Visnick Y, Miro S, Saman S, et al. Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease. J Biol Chem. 2012;287(6):3842-9. doi: 10.1074/jbc.M111.277061.
    • (2012) J Biol Chem , vol.287 , Issue.6 , pp. 3842-3849
    • Saman, S.1    Kim, W.2    Raya, M.3    Visnick, Y.4    Miro, S.5    Saman, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.