메뉴 건너뛰기




Volumn 35, Issue 8, 2014, Pages 1792-1800

Exosome reduction invivo is associated with lower amyloid plaque load in the 5XFAD mouse model of Alzheimer's disease

Author keywords

Alzheimer's disease; Amyloid beta; Astrocytes; Exosomes; GW4869; Neutral sphingomyelinase; Primary culture

Indexed keywords

3,3' (1,4 PHENYLENE)BIS[N [4 (4,5 DIHYDRO 1H IMIDAZOL 2 YL)PHENYL]ACRYLAMIDE]; CERAMIDE; SPHINGOMYELIN; SPHINGOMYELIN PHOSPHODIESTERASE; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); ANILINE DERIVATIVE; BENZYLIDENE DERIVATIVE; PEPTIDE FRAGMENT; SMPD3 PROTEIN, MOUSE;

EID: 84899968840     PISSN: 01974580     EISSN: 15581497     Source Type: Journal    
DOI: 10.1016/j.neurobiolaging.2014.02.012     Document Type: Article
Times cited : (370)

References (58)
  • 1
    • 0031905956 scopus 로고    scopus 로고
    • Role of sphingolipid-mediated cell death in neurodegenerative diseases
    • Ariga T., Jarvis W.D., Yu R.K. Role of sphingolipid-mediated cell death in neurodegenerative diseases. J.Lipid Res. 1998, 39:1-16.
    • (1998) J.Lipid Res. , vol.39 , pp. 1-16
    • Ariga, T.1    Jarvis, W.D.2    Yu, R.K.3
  • 2
    • 84868211262 scopus 로고    scopus 로고
    • Circulating microRNAs in exosomes indicate hepatocyte injury and inflammation in alcoholic, drug-induced, and inflammatory liver diseases
    • Bala S., Petrasek J., Mundkur S., Catalano D., Levin I., Ward J., Alao H., Kodys K., Szabo G. Circulating microRNAs in exosomes indicate hepatocyte injury and inflammation in alcoholic, drug-induced, and inflammatory liver diseases. Hepatology 2012, 56:1946-1957.
    • (2012) Hepatology , vol.56 , pp. 1946-1957
    • Bala, S.1    Petrasek, J.2    Mundkur, S.3    Catalano, D.4    Levin, I.5    Ward, J.6    Alao, H.7    Kodys, K.8    Szabo, G.9
  • 3
    • 84866426167 scopus 로고    scopus 로고
    • Exosomes: vehicles for the transfer of toxic proteins associated with neurodegenerative diseases?
    • Bellingham S.A., Guo B.B., Coleman B.M., Hill A.F. Exosomes: vehicles for the transfer of toxic proteins associated with neurodegenerative diseases?. Front Physiol. 2012, 3:124.
    • (2012) Front Physiol. , vol.3 , pp. 124
    • Bellingham, S.A.1    Guo, B.B.2    Coleman, B.M.3    Hill, A.F.4
  • 4
    • 52449089987 scopus 로고    scopus 로고
    • Thirty years of Alzheimer's disease genetics: the implications of systematic meta-analyses
    • Bertram L., Tanzi R.E. Thirty years of Alzheimer's disease genetics: the implications of systematic meta-analyses. Nat. Rev. Neurosci. 2008, 9:768-778.
    • (2008) Nat. Rev. Neurosci. , vol.9 , pp. 768-778
    • Bertram, L.1    Tanzi, R.E.2
  • 5
    • 42149107502 scopus 로고    scopus 로고
    • Genetic aspects of Alzheimer disease
    • Bird T.D. Genetic aspects of Alzheimer disease. Genet. Med. 2008, 10:231-239.
    • (2008) Genet. Med. , vol.10 , pp. 231-239
    • Bird, T.D.1
  • 7
    • 75149166216 scopus 로고    scopus 로고
    • Insulin-degrading enzyme sorting in exosomes: a secretory pathway for a key brain amyloid-beta degrading protease
    • Bulloj A., Leal M.C., Xu H., Castano E.M., Morelli L. Insulin-degrading enzyme sorting in exosomes: a secretory pathway for a key brain amyloid-beta degrading protease. J.Alzheimers Dis. 2010, 19:79-95.
    • (2010) J.Alzheimers Dis. , vol.19 , pp. 79-95
    • Bulloj, A.1    Leal, M.C.2    Xu, H.3    Castano, E.M.4    Morelli, L.5
  • 9
    • 26844507790 scopus 로고    scopus 로고
    • ATrkA-to-p75NTR molecular switch activates amyloid beta-peptide generation during aging
    • Costantini C., Weindruch R., Della Valle G., Puglielli L. ATrkA-to-p75NTR molecular switch activates amyloid beta-peptide generation during aging. Biochem. J. 2005, 391:59-67.
    • (2005) Biochem. J. , vol.391 , pp. 59-67
    • Costantini, C.1    Weindruch, R.2    Della Valle, G.3    Puglielli, L.4
  • 11
    • 26444530166 scopus 로고    scopus 로고
    • Age-related changes in neutral sphingomyelin-specific phospholipase C activity in striatum, hippocampus, and frontal cortex: implication for sensitivity to stress and inflammation
    • Crivello N.A., Rosenberg I.H., Dallal G.E., Bielinski D., Joseph J.A. Age-related changes in neutral sphingomyelin-specific phospholipase C activity in striatum, hippocampus, and frontal cortex: implication for sensitivity to stress and inflammation. Neurochem. Int. 2005, 47:573-579.
    • (2005) Neurochem. Int. , vol.47 , pp. 573-579
    • Crivello, N.A.1    Rosenberg, I.H.2    Dallal, G.E.3    Bielinski, D.4    Joseph, J.A.5
  • 12
    • 0035091921 scopus 로고    scopus 로고
    • Chromatographic resolution and quantitative assay of CNS tissue sphingoids and sphingolipids
    • Dasgupta S., Hogan E.L. Chromatographic resolution and quantitative assay of CNS tissue sphingoids and sphingolipids. J.Lipid Res. 2001, 42:301-308.
    • (2001) J.Lipid Res. , vol.42 , pp. 301-308
    • Dasgupta, S.1    Hogan, E.L.2
  • 13
    • 33745151966 scopus 로고    scopus 로고
    • Effects of sphingomyelin, cholesterol and zinc ions on the binding, insertion and aggregation of the amyloid Abeta(1-40) peptide in solid-supported lipid bilayers
    • Devanathan S., Salamon Z., Lindblom G., Gröbner G., Tollin G. Effects of sphingomyelin, cholesterol and zinc ions on the binding, insertion and aggregation of the amyloid Abeta(1-40) peptide in solid-supported lipid bilayers. FEBS J. 2006, 273:1389-1402.
    • (2006) FEBS J. , vol.273 , pp. 1389-1402
    • Devanathan, S.1    Salamon, Z.2    Lindblom, G.3    Gröbner, G.4    Tollin, G.5
  • 18
    • 51249193286 scopus 로고
    • Methods for methanolysis of sphingolipids and direct determination of long-chain bases by gas chromatography
    • Gaver R.C., Sweeley C.C. Methods for methanolysis of sphingolipids and direct determination of long-chain bases by gas chromatography. J.Am. Oil Chem. Soc. 1965, 42:294-298.
    • (1965) J.Am. Oil Chem. Soc. , vol.42 , pp. 294-298
    • Gaver, R.C.1    Sweeley, C.C.2
  • 19
    • 84877633354 scopus 로고    scopus 로고
    • Inhibition of serine palmitoyltransferase reduces Aβ and tau hyperphosphorylation in a murine model: a safe therapeutic strategy for Alzheimer's disease
    • Geekiyanage H., Upadhye A., Chan C. Inhibition of serine palmitoyltransferase reduces Aβ and tau hyperphosphorylation in a murine model: a safe therapeutic strategy for Alzheimer's disease. Neurobiol. Aging 2013, 34:2037-2051.
    • (2013) Neurobiol. Aging , vol.34 , pp. 2037-2051
    • Geekiyanage, H.1    Upadhye, A.2    Chan, C.3
  • 20
    • 0028866435 scopus 로고
    • The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway
    • Haass C., Lemere C.A., Capell A., Citron M., Seubert P., Schenk D., Lannfelt L., Selkoe D.J. The Swedish mutation causes early-onset Alzheimer's disease by beta-secretase cleavage within the secretory pathway. Nat. Med. 1995, 1:1291-1296.
    • (1995) Nat. Med. , vol.1 , pp. 1291-1296
    • Haass, C.1    Lemere, C.A.2    Capell, A.3    Citron, M.4    Seubert, P.5    Schenk, D.6    Lannfelt, L.7    Selkoe, D.J.8
  • 21
    • 80053551906 scopus 로고    scopus 로고
    • Amyloid-b aggregation on model lipid membranes: an atomic force microscopy study
    • Hane F., Drolle E., Gaikwad R., Faught E., Leonenko Z. Amyloid-b aggregation on model lipid membranes: an atomic force microscopy study. J.Alzheimers Dis. 2011, 26:485-494.
    • (2011) J.Alzheimers Dis. , vol.26 , pp. 485-494
    • Hane, F.1    Drolle, E.2    Gaikwad, R.3    Faught, E.4    Leonenko, Z.5
  • 22
    • 77957191723 scopus 로고    scopus 로고
    • Fibrillar amyloid-beta-activated human astroglia kill primary human neurons via neutral sphingomyelinase: implications for Alzheimer's disease
    • Jana A., Pahan K. Fibrillar amyloid-beta-activated human astroglia kill primary human neurons via neutral sphingomyelinase: implications for Alzheimer's disease. J.Neurosci. 2010, 30:12676-12689.
    • (2010) J.Neurosci. , vol.30 , pp. 12676-12689
    • Jana, A.1    Pahan, K.2
  • 24
    • 34147175939 scopus 로고    scopus 로고
    • Development and characterization of a novel anti-ceramide antibody
    • Krishnamurthy K., Dasgupta S., Bieberich E. Development and characterization of a novel anti-ceramide antibody. J.Lipid Res. 2007, 48:968-975.
    • (2007) J.Lipid Res. , vol.48 , pp. 968-975
    • Krishnamurthy, K.1    Dasgupta, S.2    Bieberich, E.3
  • 25
    • 0016029344 scopus 로고
    • Identification of 2-hydroxy fatty acids in complex mixtures of fatty acid methyl esters by mass chromatography
    • Laine R.A., Young N.D., Gerber J.N., Sweeley C.C. Identification of 2-hydroxy fatty acids in complex mixtures of fatty acid methyl esters by mass chromatography. Biomed. Mass Spectrom. 1974, 1:10-14.
    • (1974) Biomed. Mass Spectrom. , vol.1 , pp. 10-14
    • Laine, R.A.1    Young, N.D.2    Gerber, J.N.3    Sweeley, C.C.4
  • 26
    • 84876251551 scopus 로고    scopus 로고
    • MER5101, a novel Abeta1-15:DT conjugate vaccine, generates a robust anti-Aβ antibody response and attenuates Aβ pathology and cognitive deficits in APPswe/PS1δE9 transgenic mice
    • Liu B., Frost J.L., Sun J., Fu H., Grimes S., Blackburn P., Lemere C.A. MER5101, a novel Abeta1-15:DT conjugate vaccine, generates a robust anti-Aβ antibody response and attenuates Aβ pathology and cognitive deficits in APPswe/PS1δE9 transgenic mice. J.Neurosci. 2013, 33:7027-7037.
    • (2013) J.Neurosci. , vol.33 , pp. 7027-7037
    • Liu, B.1    Frost, J.L.2    Sun, J.3    Fu, H.4    Grimes, S.5    Blackburn, P.6    Lemere, C.A.7
  • 30
    • 0030892291 scopus 로고    scopus 로고
    • Characterization of the interactions of Alzheimer beta- amyloid peptides with phospholipid membranes
    • McLaurin J., Chakrabartty A. Characterization of the interactions of Alzheimer beta- amyloid peptides with phospholipid membranes. Eur. J. Biochem. 1997, 245:355-363.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 355-363
    • McLaurin, J.1    Chakrabartty, A.2
  • 32
    • 77954375412 scopus 로고    scopus 로고
    • Astrocytic A beta 1-42 uptake is determined by A beta-aggregation state and the presence of amyloid-associated proteins
    • Nielsen H.M., Mulder S.D., Belien J.A., Musters R.J., Eikelenboom P., Veerhuis R. Astrocytic A beta 1-42 uptake is determined by A beta-aggregation state and the presence of amyloid-associated proteins. Glia 2010, 58:1235-1246.
    • (2010) Glia , vol.58 , pp. 1235-1246
    • Nielsen, H.M.1    Mulder, S.D.2    Belien, J.A.3    Musters, R.J.4    Eikelenboom, P.5    Veerhuis, R.6
  • 33
    • 33749521100 scopus 로고    scopus 로고
    • Intraneuronal beta-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: potential factors in amyloid plaque formation
    • Oakley H., Cole S.L., Logan S., Maus E., Shao P., Craft J., Guillozet-Bongaarts A., Ohno M., Disterhoft J., Van Eldik L., Berry R., Vassar R. Intraneuronal beta-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: potential factors in amyloid plaque formation. J.Neurosci. 2006, 26:10129-10140.
    • (2006) J.Neurosci. , vol.26 , pp. 10129-10140
    • Oakley, H.1    Cole, S.L.2    Logan, S.3    Maus, E.4    Shao, P.5    Craft, J.6    Guillozet-Bongaarts, A.7    Ohno, M.8    Disterhoft, J.9    Van Eldik, L.10    Berry, R.11    Vassar, R.12
  • 35
    • 84871118236 scopus 로고    scopus 로고
    • The exosome secretory pathway transports amyloid precursor protein carboxyl-terminal fragments from the cell into the brain extracellular space
    • Perez-Gonzalez R., Gauthier S.A., Kumar A., Levy E. The exosome secretory pathway transports amyloid precursor protein carboxyl-terminal fragments from the cell into the brain extracellular space. J.Biol. Chem. 2012, 287:43108-43115.
    • (2012) J.Biol. Chem. , vol.287 , pp. 43108-43115
    • Perez-Gonzalez, R.1    Gauthier, S.A.2    Kumar, A.3    Levy, E.4
  • 36
    • 0017772265 scopus 로고
    • Gas chromatography of methyl glycosides as their tri-methylsilyl ethers. The methanolysis and re-N-acetylation steps
    • Pritchard D.G., Todd C.W. Gas chromatography of methyl glycosides as their tri-methylsilyl ethers. The methanolysis and re-N-acetylation steps. J.Chromatogr. 1977, 133:133-139.
    • (1977) J.Chromatogr. , vol.133 , pp. 133-139
    • Pritchard, D.G.1    Todd, C.W.2
  • 37
    • 0037490159 scopus 로고    scopus 로고
    • Ceramide stabilizes beta-site amyloid precursor protein-cleaving enzyme 1 and promotes amyloid beta-peptide biogenesis
    • Puglielli L., Ellis B.C., Saunders A.J., Kovacs D.M. Ceramide stabilizes beta-site amyloid precursor protein-cleaving enzyme 1 and promotes amyloid beta-peptide biogenesis. J.Biol. Chem. 2003, 278:19777-19783.
    • (2003) J.Biol. Chem. , vol.278 , pp. 19777-19783
    • Puglielli, L.1    Ellis, B.C.2    Saunders, A.J.3    Kovacs, D.M.4
  • 40
    • 35848937327 scopus 로고    scopus 로고
    • Regulation of neutral sphingomyelinase-2 by GSH: a new insight to the role of oxidative stress in aging-associated inflammation
    • Rutkute K., Asmis R.H., Nikolova-Karakashian M.N. Regulation of neutral sphingomyelinase-2 by GSH: a new insight to the role of oxidative stress in aging-associated inflammation. J.Lipid Res. 2007, 48:2443-2452.
    • (2007) J.Lipid Res. , vol.48 , pp. 2443-2452
    • Rutkute, K.1    Asmis, R.H.2    Nikolova-Karakashian, M.N.3
  • 42
    • 80052501210 scopus 로고    scopus 로고
    • Resolving controversies on the path to Alzheimer's therapeutics
    • Selkoe D.J. Resolving controversies on the path to Alzheimer's therapeutics. Nat. Med. 2011, 17:1060-1065.
    • (2011) Nat. Med. , vol.17 , pp. 1060-1065
    • Selkoe, D.J.1
  • 43
    • 43249087541 scopus 로고    scopus 로고
    • Inhibition of gamma-secretase causes increased secretion of amyloid precursor protein C-terminal fragments in association with exosomes
    • Sharples R.A., Vella L.J., Nisbet R.M., Naylor R., Perez K., Barnham K.J., Masters C.L., Hill A.F. Inhibition of gamma-secretase causes increased secretion of amyloid precursor protein C-terminal fragments in association with exosomes. FASEB J. 2008, 22:1469-1478.
    • (2008) FASEB J. , vol.22 , 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    Masters, C.L.7    Hill, A.F.8
  • 44
    • 0007692414 scopus 로고    scopus 로고
    • Invivo and invitro evidence supporting a role for the inflammatory cytokine interleukin-1 as a driving force in Alzheimer pathogenesis
    • Sheng J.G., Ito K., Skinner R.D., Mrak R.E., Rovnaghi C.R., Van Eldik L.J., Griffin W.S. Invivo and invitro evidence supporting a role for the inflammatory cytokine interleukin-1 as a driving force in Alzheimer pathogenesis. Neurobiol. Aging 1996, 17:761-766.
    • (1996) Neurobiol. Aging , vol.17 , pp. 761-766
    • Sheng, J.G.1    Ito, K.2    Skinner, R.D.3    Mrak, R.E.4    Rovnaghi, C.R.5    Van Eldik, L.J.6    Griffin, W.S.7
  • 47
    • 77957220100 scopus 로고    scopus 로고
    • Inhibition of neutral sphingomyelinase-2 perturbs brain sphingolipid balance and spatial memory in mice
    • Tabatadze N., Savonenko A., Song H., Bandaru V.V., Chu M., Haughey N.J. Inhibition of neutral sphingomyelinase-2 perturbs brain sphingolipid balance and spatial memory in mice. J.Neurosci. Res. 2010, 88:2940-2951.
    • (2010) J.Neurosci. Res. , vol.88 , pp. 2940-2951
    • Tabatadze, N.1    Savonenko, A.2    Song, H.3    Bandaru, V.V.4    Chu, M.5    Haughey, N.J.6
  • 48
  • 49
    • 2342442848 scopus 로고    scopus 로고
    • The effect of cholesterol and monosialoganglioside (GM1) on the release and aggregation of amyloid beta-peptide from liposomes prepared from brain membrane-like lipids
    • Tashima Y., Oe R., Lee S., Sugihara G., Chambers E.J., Takahashi M., Yamada T. The effect of cholesterol and monosialoganglioside (GM1) on the release and aggregation of amyloid beta-peptide from liposomes prepared from brain membrane-like lipids. J.Biol. Chem. 2004, 279:17587-17595.
    • (2004) J.Biol. Chem. , vol.279 , pp. 17587-17595
    • Tashima, Y.1    Oe, R.2    Lee, S.3    Sugihara, G.4    Chambers, E.J.5    Takahashi, M.6    Yamada, T.7
  • 50
    • 0028982292 scopus 로고
    • Self-association of beta-amyloid peptide (1-40) in solution and binding to lipid membranes
    • Terzi E., Hölzemann G., Seelig J. Self-association of beta-amyloid peptide (1-40) in solution and binding to lipid membranes. J.Mol. Biol. 1995, 252:633-642.
    • (1995) J.Mol. Biol. , vol.252 , pp. 633-642
    • Terzi, E.1    Hölzemann, G.2    Seelig, J.3
  • 51
    • 79960096964 scopus 로고    scopus 로고
    • Exosomes: secreted vesicles and intercellular communications
    • Thery C. Exosomes: secreted vesicles and intercellular communications. F1000 Biol. Rep. 2011, 3:15.
    • (2011) F1000 Biol. Rep. , vol.3 , pp. 15
    • Thery, C.1
  • 54
    • 84862274671 scopus 로고    scopus 로고
    • Astrocytes secrete exosomes enriched with proapoptotic ceramide and prostate apoptosis response 4 (PAR-4): potential mechanism ofapoptosis induction in Alzheimer disease (AD)
    • Wang G., Dinkins M., He Q., Zhu G., Poirier C., Campbell A., Mayer-Proschel M., Bieberich E. Astrocytes secrete exosomes enriched with proapoptotic ceramide and prostate apoptosis response 4 (PAR-4): potential mechanism ofapoptosis induction in Alzheimer disease (AD). J.Biol. Chem. 2012, 287:21384-21395.
    • (2012) J.Biol. Chem. , vol.287 , pp. 21384-21395
    • Wang, G.1    Dinkins, M.2    He, Q.3    Zhu, G.4    Poirier, C.5    Campbell, A.6    Mayer-Proschel, M.7    Bieberich, E.8
  • 55
    • 0036451728 scopus 로고    scopus 로고
    • Cholesterol-dependent aggregation of amyloid beta-protein
    • Yanagisawa K., Matsuzaki K. Cholesterol-dependent aggregation of amyloid beta-protein. Ann. N.Y Acad. Sci. 2002, 977:384-386.
    • (2002) Ann. N.Y Acad. Sci. , vol.977 , pp. 384-386
    • Yanagisawa, K.1    Matsuzaki, K.2
  • 56
    • 0028885854 scopus 로고
    • GM1 ganglioside-bound amyloid beta-protein (A beta): a possible form of preamyloid in Alzheimer's disease
    • Yanagisawa K., Odaka A., Suzuki N., Ihara Y. GM1 ganglioside-bound amyloid beta-protein (A beta): a possible form of preamyloid in Alzheimer's disease. Nat. Med. 1995, 1:1062-1066.
    • (1995) Nat. Med. , vol.1 , pp. 1062-1066
    • Yanagisawa, K.1    Odaka, A.2    Suzuki, N.3    Ihara, Y.4
  • 57
    • 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, 105:217-224.
    • (2008) J.Neurochem. , vol.105 , pp. 217-224
    • Yuyama, K.1    Yamamoto, N.2    Yanagisawa, K.3
  • 58
    • 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, 287:10977-10989.
    • (2012) J.Biol. Chem. , vol.287 , pp. 10977-10989
    • Yuyama, K.1    Sun, H.2    Mitsutake, S.3    Igarashi, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.