메뉴 건너뛰기




Volumn 25, Issue 1, 2011, Pages 326-336

Heat-shock protein 70 modulates toxic extracellular α-synuclein oligomers and rescues trans-synaptic toxicity

Author keywords

Aggregation; Microfluidic culture system; Parkinson's disease; Protein complementation

Indexed keywords

ALPHA SYNUCLEIN; HEAT SHOCK PROTEIN 70; PARVOVIRUS VECTOR;

EID: 79251565507     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.10-164624     Document Type: Article
Times cited : (247)

References (56)
  • 1
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of α-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck, P. K., Chan, H. Y. E., Trojanowski, J. Q., Lee, V. M.-Y., and Bonini, N. M. (2002) Chaperone suppression of α-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 295, 865-868
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.E.2    Trojanowski, J.Q.3    Lee, V.M.-Y.4    Bonini, N.M.5
  • 4
    • 0037426346 scopus 로고    scopus 로고
    • Beta-synuclein inhibits formation of alpha-synuclein protofibrils: A possible therapeutic strategy against Parkinson's disease
    • Park, J. Y., and Lansbury, P. T., Jr. (2003) Beta-synuclein inhibits formation of alpha-synuclein protofibrils: a possible therapeutic strategy against Parkinson's disease. Biochemistry 42, 3696-3700
    • (2003) Biochemistry , vol.42 , pp. 3696-3700
    • Park, J.Y.1    Lansbury Jr., P.T.2
  • 5
    • 0031944830 scopus 로고    scopus 로고
    • Nigral and cortical Lewy bodies and dystrophic nigral neurites in Parkinson's disease and cortical Lewy body disease contain alpha-synuclein immunoreactivity
    • Irizarry, M. C., Growdon, W., Gomez-Isla, T., Newell, K., George, J. M., Clayton, D. F., and Hyman, B. T. (1998) Nigral and cortical Lewy bodies and dystrophic nigral neurites in Parkinson's disease and cortical Lewy body disease contain alpha-synuclein immunoreactivity. J. Neuropathol. Exp. Neurol. 57, 334-337
    • (1998) J. Neuropathol. Exp. Neurol. , vol.57 , pp. 334-337
    • Irizarry, M.C.1    Growdon, W.2    Gomez-Isla, T.3    Newell, K.4    George, J.M.5    Clayton, D.F.6    Hyman, B.T.7
  • 7
    • 43249114934 scopus 로고    scopus 로고
    • Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease
    • Kordower, J. H., Chu, Y., Hauser, R. A., Freeman, T. B., and Olanow, C. W. (2008) Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease. Nat. Med. 14, 504-506
    • (2008) Nat. Med. , vol.14 , pp. 504-506
    • Kordower, J.H.1    Chu, Y.2    Hauser, R.A.3    Freeman, T.B.4    Olanow, C.W.5
  • 10
    • 70349223775 scopus 로고    scopus 로고
    • Seeding induced by alpha-synuclein oligomers provides evidence for spreading of alpha-synuclein pathology
    • Danzer, K. M., Krebs, S. K., Wolff, M., Birk, G., and Hengerer, B. (2009) Seeding induced by alpha-synuclein oligomers provides evidence for spreading of alpha-synuclein pathology. J. Neurochem. 111, 192-203
    • (2009) J. Neurochem. , vol.111 , pp. 192-203
    • Danzer, K.M.1    Krebs, S.K.2    Wolff, M.3    Birk, G.4    Hengerer, B.5
  • 12
    • 52449117926 scopus 로고    scopus 로고
    • Research in motion: The enigma of Parkinson's disease pathology spread
    • Brundin, P., Li, J. Y., Holton, J. L., Lindvall, O., and Revesz, T. (2008) Research in motion: the enigma of Parkinson's disease pathology spread. Nat. Rev. Neurosci. 9, 741-745
    • (2008) Nat. Rev. Neurosci. , vol.9 , pp. 741-745
    • Brundin, P.1    Li, J.Y.2    Holton, J.L.3    Lindvall, O.4    Revesz, T.5
  • 14
    • 33645833848 scopus 로고    scopus 로고
    • Detection of oligomeric forms of alpha-synuclein protein in human plasma as a potential biomarker for Parkinson's disease
    • El-Agnaf, O. M., Salem, S. A., Paleologou, K. E., Curran, M. D., Gibson, M. J., Court, J. A., Schlossmacher, M. G., and Allsop, D. (2006) Detection of oligomeric forms of alpha-synuclein protein in human plasma as a potential biomarker for Parkinson's disease. FASEB J. 20, 419-425
    • (2006) FASEB J , vol.20 , pp. 419-425
    • El-Agnaf, O.M.1    Salem, S.A.2    Paleologou, K.E.3    Curran, M.D.4    Gibson, M.J.5    Court, J.A.6    Schlossmacher, M.G.7    Allsop, D.8
  • 16
    • 33751208345 scopus 로고    scopus 로고
    • A highly sensitive protein-protein interaction assay based on Gaussia luciferase
    • Remy, I., and Michnick, S. W. (2006) A highly sensitive protein-protein interaction assay based on Gaussia luciferase. Nat Methods 3, 977-979
    • (2006) Nat Methods , vol.3 , pp. 977-979
    • Remy, I.1    Michnick, S.W.2
  • 17
  • 20
    • 0035800097 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar alpha-synuclein: Implications for the pathogenesis and treatment of Parkinson's disease
    • Volles, M. J., Lee, S. J., Rochet, J. C., Shtilerman, M. D., Ding, T. T., Kessler, J. C., and Lansbury, P. T., Jr. (2001) Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease. Biochemistry 40, 7812-7819
    • (2001) Biochemistry , vol.40 , pp. 7812-7819
    • Volles, M.J.1    Lee, S.J.2    Rochet, J.C.3    Shtilerman, M.D.4    Ding, T.T.5    Kessler, J.C.6    Lansbury Jr., P.T.7
  • 21
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 22
    • 0037418472 scopus 로고    scopus 로고
    • Microfluidic multicompartment device for neuroscience research
    • Taylor, A. (2003) Microfluidic multicompartment device for neuroscience research. Langmuir 19, 1551-1556
    • (2003) Langmuir , vol.19 , pp. 1551-1556
    • Taylor, A.1
  • 23
    • 21344456506 scopus 로고    scopus 로고
    • Intravesicular localization and exocytosis of alpha-synuclein and its aggregates
    • DOI 10.1523/JNEUROSCI.0692-05.2005
    • Lee, H. J., Patel, S., and Lee, S. J. (2005) Intravesicular localization and exocytosis of alpha-synuclein and its aggregates. J. Neurosci. 25, 6016-6024 (Pubitemid 40911433)
    • (2005) Journal of Neuroscience , vol.25 , Issue.25 , pp. 6016-6024
    • Lee, H.-J.1    Patel, S.2    Lee, S.-J.3
  • 26
    • 1542375250 scopus 로고    scopus 로고
    • A cDNA library functional screening strategy based on fluorescent protein complementation assays to identify novel components of signaling pathways
    • Remy, I., and Michnick, S. W. (2004) A cDNA library functional screening strategy based on fluorescent protein complementation assays to identify novel components of signaling pathways. Methods 32, 381-388
    • (2004) Methods , vol.32 , pp. 381-388
    • Remy, I.1    Michnick, S.W.2
  • 32
    • 0036852712 scopus 로고    scopus 로고
    • Pharmacological prevention of Parkinson disease in Drosophila
    • Auluck, P. K., and Bonini, N. M. (2002) Pharmacological prevention of Parkinson disease in Drosophila. Nat. Med. 8, 1185-1186
    • (2002) Nat. Med. , vol.8 , pp. 1185-1186
    • Auluck, P.K.1    Bonini, N.M.2
  • 33
    • 4344569643 scopus 로고    scopus 로고
    • Geldanamycin induces Hsp70 and prevents alpha-synuclein aggregation and toxicity in vitro
    • McLean, P. J., Klucken, J., Shin, Y., and Hyman, B. T. (2004) Geldanamycin induces Hsp70 and prevents alpha-synuclein aggregation and toxicity in vitro. Biochem. Biophys. Res. Commun. 321, 665-669
    • (2004) Biochem. Biophys. Res. Commun. , vol.321 , pp. 665-669
    • McLean, P.J.1    Klucken, J.2    Shin, Y.3    Hyman, B.T.4
  • 34
    • 0037484291 scopus 로고    scopus 로고
    • Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlates with its membrane delivery and release
    • Broquet, A. H., Thomas, G., Masliah, J., Trugnan, G., and Bachelet, M. (2003) Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlates with its membrane delivery and release. J. Biol. Chem. 278, 21601-21606
    • (2003) J. Biol. Chem. , vol.278 , pp. 21601-21606
    • Broquet, A.H.1    Thomas, G.2    Masliah, J.3    Trugnan, G.4    Bachelet, M.5
  • 36
    • 3042636977 scopus 로고    scopus 로고
    • Cat exposure induces both intra- and extracellular Hsp72: The role of adrenal hormones
    • Fleshner, M., Campisi, J., Amiri, L., and Diamond, D. M. (2004) Cat exposure induces both intra- and extracellular Hsp72: the role of adrenal hormones. Psychoneuroendocrinology 29, 1142-1152
    • (2004) Psychoneuroendocrinology , vol.29 , pp. 1142-1152
    • Fleshner, M.1    Campisi, J.2    Amiri, L.3    Diamond, D.M.4
  • 37
    • 0035964907 scopus 로고    scopus 로고
    • In vitro studies show that Hsp70 can be released by glia and that exogenous Hsp70 can enhance neuronal stress tolerance
    • Guzhova, I., Kislyakova, K., Moskaliova, O., Fridlanskaya, I., Tytell, M., Cheetham, M., and Margulis, B. (2001) In vitro studies show that Hsp70 can be released by glia and that exogenous Hsp70 can enhance neuronal stress tolerance. Brain Res. 914, 66-73
    • (2001) Brain Res , vol.914 , pp. 66-73
    • Guzhova, I.1    Kislyakova, K.2    Moskaliova, O.3    Fridlanskaya, I.4    Tytell, M.5    Cheetham, M.6    Margulis, B.7
  • 39
    • 34848889680 scopus 로고    scopus 로고
    • Mechanisms for Hsp70 secretion: Crossing membranes without a leader
    • Mambula, S. S., Stevenson, M. A., Ogawa, K., and Calderwood, S. K. (2007) Mechanisms for Hsp70 secretion: crossing membranes without a leader. Methods 43, 168-175
    • (2007) Methods , vol.43 , pp. 168-175
    • Mambula, S.S.1    Stevenson, M.A.2    Ogawa, K.3    Calderwood, S.K.4
  • 40
    • 44849084963 scopus 로고    scopus 로고
    • Hsp70 translocates into the plasma membrane after stress and is released into the extracellular environment in a membrane-associated form that activates macrophages
    • Vega, V. L., Rodriguez-Silva, M., Frey, T., Gehrmann, M., Diaz, J. C., Steinem, C., Multhoff, G., Arispe, N., and De Maio, A. (2008) Hsp70 translocates into the plasma membrane after stress and is released into the extracellular environment in a membrane-associated form that activates macrophages. J. Immunol. 180, 4299-4307
    • (2008) J. Immunol. , vol.180 , pp. 4299-4307
    • Vega, V.L.1    Rodriguez-Silva, M.2    Frey, T.3    Gehrmann, M.4    Diaz, J.C.5    Steinem, C.6    Multhoff, G.7    Arispe, N.8    De Maio, A.9
  • 41
    • 20744436655 scopus 로고    scopus 로고
    • Exosome-dependent trafficking of HSP70: A novel secretory pathway for cellular stress proteins
    • Lancaster, G. I., and Febbraio, M. A. (2005) Exosome-dependent trafficking of HSP70: a novel secretory pathway for cellular stress proteins. J. Biol. Chem. 280, 23349-23355
    • (2005) J. Biol. Chem. , vol.280 , pp. 23349-23355
    • Lancaster, G.I.1    Febbraio, M.A.2
  • 43
    • 33750570923 scopus 로고    scopus 로고
    • Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes
    • Mambula, S. S., and Calderwood, S. K. (2006) Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosomes. J. Immunol. 177, 7849-7857
    • (2006) J. Immunol. , vol.177 , pp. 7849-7857
    • Mambula, S.S.1    Calderwood, S.K.2
  • 44
    • 0024541931 scopus 로고
    • Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins
    • Hightower, L. E., and Guidon, P. T., Jr. (1989) Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins. J. Cell. Physiol. 138, 257-266
    • (1989) J. Cell. Physiol. , vol.138 , pp. 257-266
    • Hightower, L.E.1    Guidon Jr., P.T.2
  • 45
    • 0022637881 scopus 로고
    • Heat shock-like protein is transferred from glia to axon
    • Tytell, M., Greenberg, S. G., and Lasek, R. J. (1986) Heat shock-like protein is transferred from glia to axon. Brain Res. 363, 161-164
    • (1986) Brain Res , vol.363 , pp. 161-164
    • Tytell, M.1    Greenberg, S.G.2    Lasek, R.J.3
  • 46
    • 26044433779 scopus 로고    scopus 로고
    • Message in a bottle: Role of the 70-kDa heat shock protein family in anti-tumor immunity
    • Calderwood, S. K., Theriault, J. R., and Gong, J. (2005) Message in a bottle: role of the 70-kDa heat shock protein family in anti-tumor immunity. Eur. J. Immunol. 35, 2518-2527
    • (2005) Eur. J. Immunol. , vol.35 , pp. 2518-2527
    • Calderwood, S.K.1    Theriault, J.R.2    Gong, J.3
  • 48
    • 13244267202 scopus 로고    scopus 로고
    • Mechanisms of suppression of α-synuclein neurotoxicity by geldanamycin in Drosophila
    • Auluck, P. K., Meulener, M. C., and Bonini, N. M. (2005) Mechanisms of suppression of α-synuclein neurotoxicity by geldanamycin in Drosophila. J. Biol. Chem. 280, 2873-2878
    • (2005) J. Biol. Chem. , vol.280 , pp. 2873-2878
    • Auluck, P.K.1    Meulener, M.C.2    Bonini, N.M.3
  • 49
    • 77957564570 scopus 로고    scopus 로고
    • Extracellular adenosine triphosphate and adenosine in cancer
    • E-pub ahead of print doi: 10.1038/onc.2010.292
    • Stagg, J., and Smyth, M. J. (2010) Extracellular adenosine triphosphate and adenosine in cancer. [E-pub ahead of print] Oncogene doi: 10.1038/onc.2010.292
    • (2010) Oncogene
    • Stagg, J.1    Smyth, M.J.2
  • 50
    • 17644383748 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species
    • Dedmon, M. M., Christodoulou, J., Wilson, M. R., and Dobson, C. M. (2005) Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species. J. Biol. Chem. 280, 14733-14740
    • (2005) J. Biol. Chem. , vol.280 , pp. 14733-14740
    • Dedmon, M.M.1    Christodoulou, J.2    Wilson, M.R.3    Dobson, C.M.4
  • 51
    • 0033913783 scopus 로고    scopus 로고
    • Transmissible spongiform encephalopathies, amyloidoses and yeast prions: Common threads?
    • Caughey, B. (2000) Transmissible spongiform encephalopathies, amyloidoses and yeast prions: common threads? Nat. Med. 6, 751-754
    • (2000) Nat. Med. , vol.6 , pp. 751-754
    • Caughey, B.1
  • 53
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost, B., Jacks, R. L., and Diamond, M. I. (2009) Propagation of tau misfolding from the outside to the inside of a cell. J. Biol. Chem. 284, 12845-12852
    • (2009) J. Biol. Chem. , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 54
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • Ren, P. H., Lauckner, J. E., Kachirskaia, I., Heuser, J. E., Melki, R., and Kopito, R. R. (2009) Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat. Cell Biol. 11, 219-225
    • (2009) Nat. Cell Biol. , vol.11 , pp. 219-225
    • Ren, P.H.1    Lauckner, J.E.2    Kachirskaia, I.3    Heuser, J.E.4    Melki, R.5    Kopito, R.R.6
  • 56
    • 33745785300 scopus 로고    scopus 로고
    • Visualization of molecular interactions by fluorescence complementation
    • Kerppola, T. K. (2006) Visualization of molecular interactions by fluorescence complementation. Nat. Rev. Mol. Cell. Biol. 7, 449-456
    • (2006) Nat. Rev. Mol. Cell. Biol. , vol.7 , pp. 449-456
    • Kerppola, T.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.