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Volumn 291, Issue 20, 2016, Pages 10528-10540

Trehalose alters subcellular trafficking and the metabolism of the Alzheimer-associated amyloid precursor protein

Author keywords

[No Author keywords available]

Indexed keywords

BIODEGRADATION; GLYCOPROTEINS; METABOLISM; NEURODEGENERATIVE DISEASES; PHYSIOLOGY;

EID: 84969165518     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M116.719286     Document Type: Article
Times cited : (56)

References (54)
  • 1
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe, D. J. (2001) Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81, 741-766
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 2
    • 79959886270 scopus 로고    scopus 로고
    • Amyloid precursor protein processing and Alzheimer's disease
    • O'Brien, R. J., and Wong, P. C. (2011) Amyloid precursor protein processing and Alzheimer's disease. Annu. Rev. Neurosci. 34, 185-204
    • (2011) Annu. Rev. Neurosci. , vol.34 , pp. 185-204
    • O'Brien, R.J.1    Wong, P.C.2
  • 3
    • 0037698096 scopus 로고    scopus 로고
    • Presenilin-1, nicastrin, amyloid precursor protein, and γ-secretase activity are co-localized in the lysosomal membrane
    • Pasternak, S. H., Bagshaw, R. D., Guiral, M., Zhang, S., Ackerley, C. A., Pak, B. J., Callahan, J. W., and Mahuran, D. J. (2003) Presenilin-1, nicastrin, amyloid precursor protein, and γ-secretase activity are co-localized in the lysosomal membrane. J. Biol. Chem. 278, 26687-26694
    • (2003) J. Biol. Chem. , vol.278 , pp. 26687-26694
    • Pasternak, S.H.1    Bagshaw, R.D.2    Guiral, M.3    Zhang, S.4    Ackerley, C.A.5    Pak, B.J.6    Callahan, J.W.7    Mahuran, D.J.8
  • 4
    • 33646461282 scopus 로고    scopus 로고
    • β-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system
    • Almeida, C. G., Takahashi, R. H., and Gouras, G. K. (2006) β-Amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system. J. Neurosci. 26, 4277-4288
    • (2006) J. Neurosci. , vol.26 , pp. 4277-4288
    • Almeida, C.G.1    Takahashi, R.H.2    Gouras, G.K.3
  • 6
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima, N., Levine, B., Cuervo, A. M., and Klionsky, D. J. (2008) Autophagy fights disease through cellular self-digestion. Nature 451, 1069-1075
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 7
    • 35448981935 scopus 로고    scopus 로고
    • Autophagy: From phenomenology to molecular understanding in less than a decade
    • Klionsky, D. J. (2007) Autophagy: from phenomenology to molecular understanding in less than a decade. Nat. Rev. Mol. Cell Biol. 8, 931-937
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 931-937
    • Klionsky, D.J.1
  • 8
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine, B., and Kroemer, G. (2008) Autophagy in the pathogenesis of disease. Cell 132, 27-42
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 9
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • Kroemer, G., Mariño, G., and Levine, B. (2010) Autophagy and the integrated stress response. Mol. Cell 40, 280-293
    • (2010) Mol. Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Mariño, G.2    Levine, B.3
  • 10
    • 84875892111 scopus 로고    scopus 로고
    • Autophagy as a stress-response and quality-control mechanism: Implications for cell injury and human disease
    • Murrow, L., and Debnath, J. (2013) Autophagy as a stress-response and quality-control mechanism: implications for cell injury and human disease. Annu. Rev. Pathol. 8, 105-137
    • (2013) Annu. Rev. Pathol. , vol.8 , pp. 105-137
    • Murrow, L.1    Debnath, J.2
  • 15
    • 41749114288 scopus 로고    scopus 로고
    • Autophagy: Basic principles and relevance to disease
    • Kundu, M., and Thompson, C. B. (2008) Autophagy: basic principles and relevance to disease. Annu. Rev. Pathol. 3, 427-455
    • (2008) Annu. Rev. Pathol. , vol.3 , pp. 427-455
    • Kundu, M.1    Thompson, C.B.2
  • 16
    • 65549099222 scopus 로고    scopus 로고
    • All-you-can-eat: Autophagy in neurodegeneration and neuroprotection
    • Jaeger, P. A., and Wyss-Coray, T. (2009) All-you-can-eat: autophagy in neurodegeneration and neuroprotection. Mol. Neurodegener. 4, 16
    • (2009) Mol. Neurodegener. , vol.4 , pp. 16
    • Jaeger, P.A.1    Wyss-Coray, T.2
  • 17
    • 84885736277 scopus 로고    scopus 로고
    • Adaptor complex AP2/PICALM, through interaction with LC3, targets Alzheimer's APP-CTF for terminal degradation via autophagy
    • Tian, Y., Chang, J. C., Fan, E. Y., Flajolet, M., and Greengard, P. (2013) Adaptor complex AP2/PICALM, through interaction with LC3, targets Alzheimer's APP-CTF for terminal degradation via autophagy. Proc. Natl. Acad. Sci. U.S.A. 110, 17071-17076
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 17071-17076
    • Tian, Y.1    Chang, J.C.2    Fan, E.Y.3    Flajolet, M.4    Greengard, P.5
  • 21
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and α-synuclein
    • Sarkar, S., Davies, J. E., Huang, Z., Tunnacliffe, A., and Rubinsztein, D. C. (2007) Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and α-synuclein. J. Biol. Chem. 282, 5641-5652
    • (2007) J. Biol. Chem. , vol.282 , pp. 5641-5652
    • Sarkar, S.1    Davies, J.E.2    Huang, Z.3    Tunnacliffe, A.4    Rubinsztein, D.C.5
  • 22
    • 79952104480 scopus 로고    scopus 로고
    • The accumulation of neurotoxic proteins, induced by proteasome inhibition, is reverted by trehalose, an enhancer of autophagy, in human neuroblastoma cells
    • Casarejos, M. J., Solano, R. M., Gómez, A., Perucho, J., de Yébenes, J. G., and Mena, M. A. (2011) The accumulation of neurotoxic proteins, induced by proteasome inhibition, is reverted by trehalose, an enhancer of autophagy, in human neuroblastoma cells. Neurochem. Int. 58, 512-520
    • (2011) Neurochem. Int. , vol.58 , pp. 512-520
    • Casarejos, M.J.1    Solano, R.M.2    Gómez, A.3    Perucho, J.4    De Yébenes, J.G.5    Mena, M.A.6
  • 23
    • 84862285881 scopus 로고    scopus 로고
    • Autophagic degradation of tau in primary neurons and its enhancement by trehalose
    • Krüger, U., Wang, Y., Kumar, S., and Mandelkow, E. M. (2012) Autophagic degradation of tau in primary neurons and its enhancement by trehalose. Neurobiol. Aging 33, 2291-2305
    • (2012) Neurobiol. Aging , vol.33 , pp. 2291-2305
    • Krüger, U.1    Wang, Y.2    Kumar, S.3    Mandelkow, E.M.4
  • 24
    • 84863210676 scopus 로고    scopus 로고
    • Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy
    • Schaeffer, V., Lavenir, I., Ozcelik, S., Tolnay, M., Winkler, D. T., and Goedert, M. (2012) Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy. Brain 135, 2169-2177
    • (2012) Brain , vol.135 , pp. 2169-2177
    • Schaeffer, V.1    Lavenir, I.2    Ozcelik, S.3    Tolnay, M.4    Winkler, D.T.5    Goedert, M.6
  • 29
    • 84887853222 scopus 로고    scopus 로고
    • Sequential proteolytic processing of the triggering receptor expressed on myeloid cells-2 (TREM2) protein by ectodomain shedding and γ-secretase-dependent intramembranous cleavage
    • Wunderlich, P., Glebov, K., Kemmerling, N., Tien, N. T., Neumann, H., and Walter, J. (2013) Sequential proteolytic processing of the triggering receptor expressed on myeloid cells-2 (TREM2) protein by ectodomain shedding and γ-secretase-dependent intramembranous cleavage. J. Biol. Chem. 288, 33027-33036
    • (2013) J. Biol. Chem. , vol.288 , pp. 33027-33036
    • Wunderlich, P.1    Glebov, K.2    Kemmerling, N.3    Tien, N.T.4    Neumann, H.5    Walter, J.6
  • 31
    • 84872036691 scopus 로고    scopus 로고
    • Structure of the human ATG12∼ATG5 conjugate required for LC3 lipidation in autophagy
    • Otomo, C., Metlagel, Z., Takaesu, G., and Otomo, T. (2013) Structure of the human ATG12∼ATG5 conjugate required for LC3 lipidation in autophagy. Nat. Struct. Mol. Biol. 20, 59-66
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 59-66
    • Otomo, C.1    Metlagel, Z.2    Takaesu, G.3    Otomo, T.4
  • 32
    • 27944504351 scopus 로고    scopus 로고
    • P62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtininduced cell death
    • Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Overvatn, A., Stenmark, H., and Johansen, T. (2005) p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtininduced cell death. J. Cell Biol. 171, 603-614
    • (2005) J. Cell Biol. , vol.171 , pp. 603-614
    • Bjørkøy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 33
    • 70350418625 scopus 로고    scopus 로고
    • MTORsignaling at a glance
    • Laplante, M., and Sabatini, D. M. (2009)mTORsignaling at a glance. J. Cell Sci. 122, 3589-3594
    • (2009) J. Cell Sci. , vol.122 , pp. 3589-3594
    • Laplante, M.1    Sabatini, D.M.2
  • 35
    • 66149110750 scopus 로고    scopus 로고
    • Oxidation of maltose and trehalose during prolonged moderate-intensity exercise
    • Venables, M. C., Brouns, F., and Jeukendrup, A. E. (2008) Oxidation of maltose and trehalose during prolonged moderate-intensity exercise. Med. Sci. Sports Exerc. 40, 1653-1659
    • (2008) Med. Sci. Sports Exerc. , vol.40 , pp. 1653-1659
    • Venables, M.C.1    Brouns, F.2    Jeukendrup, A.E.3
  • 38
    • 50649106648 scopus 로고    scopus 로고
    • Cathepsin D - Many functions of one aspartic protease
    • Benes, P., Vetvicka, V., and Fusek, M. (2008) Cathepsin D - many functions of one aspartic protease. Crit. Rev. Oncol. Hematol. 68, 12-28
    • (2008) Crit. Rev. Oncol. Hematol. , vol.68 , pp. 12-28
    • Benes, P.1    Vetvicka, V.2    Fusek, M.3
  • 39
    • 0027414640 scopus 로고
    • Two crystal structures for cathepsin D: The lysosomal targeting signal and active site
    • Metcalf, P., and Fusek, M. (1993) Two crystal structures for cathepsin D: the lysosomal targeting signal and active site. EMBO J. 12, 1293-1302
    • (1993) EMBO J. , vol.12 , pp. 1293-1302
    • Metcalf, P.1    Fusek, M.2
  • 40
    • 0021978631 scopus 로고
    • Processing of human cathepsin D in lysosomes in vitro
    • Gieselmann, V., Hasilik, A., and von Figura, K. (1985) Processing of human cathepsin D in lysosomes in vitro. J. Biol. Chem. 260, 3215-3220
    • (1985) J. Biol. Chem. , vol.260 , pp. 3215-3220
    • Gieselmann, V.1    Hasilik, A.2    Von Figura, K.3
  • 41
    • 0028238397 scopus 로고
    • Structural requirements of procathepsin D activation and maturation
    • Richo, G. R., and Conner, G. E. (1994) Structural requirements of procathepsin D activation and maturation. J. Biol. Chem. 269, 14806-14812
    • (1994) J. Biol. Chem. , vol.269 , pp. 14806-14812
    • Richo, G.R.1    Conner, G.E.2
  • 42
    • 0035477333 scopus 로고    scopus 로고
    • The cell biology of Alzheimer's disease: Uncovering the secrets of secretases
    • Walter, J., Kaether, C., Steiner, H., and Haass, C. (2001) The cell biology of Alzheimer's disease: uncovering the secrets of secretases. Curr. Opin. Neurobiol. 11, 585-590
    • (2001) Curr. Opin. Neurobiol. , vol.11 , pp. 585-590
    • Walter, J.1    Kaether, C.2    Steiner, H.3    Haass, C.4
  • 43
    • 84886874221 scopus 로고    scopus 로고
    • Cross-talk of membrane lipids and Alzheimer-related proteins
    • Walter, J., and van Echten-Deckert, G. (2013) Cross-talk of membrane lipids and Alzheimer-related proteins. Mol. Neurodegener. 8, 34
    • (2013) Mol. Neurodegener. , vol.8 , pp. 34
    • Walter, J.1    Van Echten-Deckert, G.2
  • 44
    • 0026735070 scopus 로고
    • Targeting of cell-surface β-amyloid precursor protein to lysosomes: Alternative processing into amyloid-bearing fragments
    • Haass, C., Koo, E. H., Mellon, A., Hung, A. Y., and Selkoe, D. J. (1992) Targeting of cell-surface β-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. Nature 357, 500-503
    • (1992) Nature , vol.357 , pp. 500-503
    • Haass, C.1    Koo, E.H.2    Mellon, A.3    Hung, A.Y.4    Selkoe, D.J.5
  • 45
    • 76849086405 scopus 로고    scopus 로고
    • The secretases: Enzymes with therapeutic potential in Alzheimer disease
    • De Strooper, B., Vassar, R., and Golde, T. (2010) The secretases: enzymes with therapeutic potential in Alzheimer disease. Nat. Rev. Neurol. 6, 99-107
    • (2010) Nat. Rev. Neurol. , vol.6 , pp. 99-107
    • De Strooper, B.1    Vassar, R.2    Golde, T.3
  • 47
    • 84879052241 scopus 로고    scopus 로고
    • Tubulin polymerization-promoting protein (TPPP/p25α) promotes unconventional secretion of α-synuclein through exophagy by impairing autophagosome-lysosome fusion
    • Ejlerskov, P., Rasmussen, I., Nielsen, T. T., Bergström, A. L., Tohyama, Y., Jensen, P. H., and Vilhardt, F. (2013) Tubulin polymerization-promoting protein (TPPP/p25α) promotes unconventional secretion of α-synuclein through exophagy by impairing autophagosome-lysosome fusion. J. Biol. Chem. 288, 17313-17335
    • (2013) J. Biol. Chem. , vol.288 , pp. 17313-17335
    • Ejlerskov, P.1    Rasmussen, I.2    Nielsen, T.T.3    Bergström, A.L.4    Tohyama, Y.5    Jensen, P.H.6    Vilhardt, F.7
  • 48
    • 84904607788 scopus 로고    scopus 로고
    • Starvation and inhibition of lysosomal function increased tau secretion by primary cortical neurons
    • Mohamed, N. V., Plouffe, V., Rémillard-Labrosse, G., Planel, E., and Leclerc, N. (2014) Starvation and inhibition of lysosomal function increased tau secretion by primary cortical neurons. Sci. Rep. 4, 5715
    • (2014) Sci. Rep. , vol.4 , pp. 5715
    • Mohamed, N.V.1    Plouffe, V.2    Rémillard-Labrosse, G.3    Planel, E.4    Leclerc, N.5
  • 51
    • 4344689871 scopus 로고    scopus 로고
    • Autophagic vacuoles are enriched in amyloid precursor protein-secretase activities: Implications for β-amyloid peptide over-production and localization in Alzheimer's disease
    • Yu, W. H., Kumar, A., Peterhoff, C., Shapiro Kulnane, L., Uchiyama, Y., Lamb, B. T., Cuervo, A. M., and Nixon, R. A. (2004) Autophagic vacuoles are enriched in amyloid precursor protein-secretase activities: implications for β-amyloid peptide over-production and localization in Alzheimer's disease. Int. J. Biochem. Cell Biol. 36, 2531-2540
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2531-2540
    • Yu, W.H.1    Kumar, A.2    Peterhoff, C.3    Shapiro Kulnane, L.4    Uchiyama, Y.5    Lamb, B.T.6    Cuervo, A.M.7    Nixon, R.A.8
  • 53
    • 0032039542 scopus 로고    scopus 로고
    • Multiple effects of trehalose on protein folding in vitro and in vivo
    • Singer, M. A., and Lindquist, S. (1998) Multiple effects of trehalose on protein folding in vitro and in vivo. Mol. Cell 1, 639-648
    • (1998) Mol. Cell , vol.1 , pp. 639-648
    • Singer, M.A.1    Lindquist, S.2
  • 54
    • 33846640013 scopus 로고    scopus 로고
    • Study of the dynamical properties of water in disaccharide solutions
    • Magazù, S., Migliardo, F., and Telling, M. T. (2007) Study of the dynamical properties of water in disaccharide solutions. Eur. Biophys. J. 36, 163-171
    • (2007) Eur. Biophys. J. , vol.36 , pp. 163-171
    • Magazù, S.1    Migliardo, F.2    Telling, M.T.3


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