메뉴 건너뛰기




Volumn 128, Issue 6, 2014, Pages 950-961

Over-expression of an inactive mutant cathepsin D increases endogenous alpha-synuclein and cathepsin B activity in SH-SY5Y cells

Author keywords

autophagy; cathepsin D; lysosome; synuclein

Indexed keywords

ALPHA SYNUCLEIN; CASPASE; CATHEPSIN B; CATHEPSIN D; CHYMOTRYPSIN; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2; PEPSTATIN;

EID: 84895920556     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/jnc.12497     Document Type: Article
Times cited : (38)

References (33)
  • 3
    • 0019948262 scopus 로고
    • L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L
    • Barrett A. J., Kembhavi A. A., Brown M. A., Kirschke H., Knight C. G., Tamai M., and, Hanada K., (1982) L-trans-Epoxysuccinyl-leucylamido(4-guanidino) butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem. J. 201, 189-198.
    • (1982) Biochem. J. , vol.201 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3    Kirschke, H.4    Knight, C.G.5    Tamai, M.6    Hanada, K.7
  • 4
    • 4644290985 scopus 로고    scopus 로고
    • Alpha-synuclein locus duplication as a cause of familial Parkinson's disease
    • Chartier-Harlin M. C., Kachergus J., Roumier C., et al,. (2004) Alpha-synuclein locus duplication as a cause of familial Parkinson's disease. Lancet 364, 1167-1169.
    • (2004) Lancet , vol.364 , pp. 1167-1169
    • Chartier-Harlin, M.C.1    Kachergus, J.2    Roumier, C.3
  • 6
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo A. M., Stefanis L., Fredenburg R., Lansbury P. T., and, Sulzer D., (2004) Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 305, 1292-1295.
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 7
    • 64949185378 scopus 로고    scopus 로고
    • Cathepsin D expression level affects alpha-synuclein processing, aggregation, and toxicity in vivo
    • Cullen V., Lindfors M., Ng J., et al,. (2009) Cathepsin D expression level affects alpha-synuclein processing, aggregation, and toxicity in vivo. Mol. Brain 2, 5.
    • (2009) Mol. Brain , vol.2 , pp. 5
    • Cullen, V.1    Lindfors, M.2    Ng, J.3
  • 9
    • 84879047011 scopus 로고    scopus 로고
    • Cellular Metabolic and Autophagic Pathways: Traffic Control by Redox Signaling
    • Dodson M., Darley-Usmar V., and, Zhang J., (2013) Cellular Metabolic and Autophagic Pathways: Traffic Control by Redox Signaling. Free Radic. Biol. Med. 63, 207-221.
    • (2013) Free Radic. Biol. Med. , vol.63 , pp. 207-221
    • Dodson, M.1    Darley-Usmar, V.2    Zhang, J.3
  • 10
    • 33749041268 scopus 로고    scopus 로고
    • Roles of LAMP-1 and LAMP-2 in lysosome biogenesis and autophagy
    • Eskelinen E. L., (2006) Roles of LAMP-1 and LAMP-2 in lysosome biogenesis and autophagy. Mol. Aspects Med. 27, 495-502.
    • (2006) Mol. Aspects Med. , vol.27 , pp. 495-502
    • Eskelinen, E.L.1
  • 12
    • 0035909530 scopus 로고    scopus 로고
    • A mutated cathepsin-D devoid of its catalytic activity stimulates the growth of cancer cells
    • Glondu M., Coopman P., Laurent-Matha V., Garcia M., Rochefort H., and, Liaudet-Coopman E., (2001) A mutated cathepsin-D devoid of its catalytic activity stimulates the growth of cancer cells. Oncogene 20, 6920-6929.
    • (2001) Oncogene , vol.20 , pp. 6920-6929
    • Glondu, M.1    Coopman, P.2    Laurent-Matha, V.3    Garcia, M.4    Rochefort, H.5    Liaudet-Coopman, E.6
  • 14
    • 0142154275 scopus 로고    scopus 로고
    • Alpha-synuclein degradation by serine protease neurosin: Implication for pathogenesis of synucleinopathies
    • Iwata A., Maruyama M., Akagi T., Hashikawa T., Kanazawa I., Tsuji S., and, Nukina N., (2003) Alpha-synuclein degradation by serine protease neurosin: implication for pathogenesis of synucleinopathies. Hum. Mol. Genet. 12, 2625-2635.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2625-2635
    • Iwata, A.1    Maruyama, M.2    Akagi, T.3    Hashikawa, T.4    Kanazawa, I.5    Tsuji, S.6    Nukina, N.7
  • 15
    • 0034666116 scopus 로고    scopus 로고
    • Cathepsin D deficiency induces lysosomal storage with ceroid lipofuscin in mouse CNS neurons
    • Koike M., Nakanishi H., Saftig P., et al,. (2000) Cathepsin D deficiency induces lysosomal storage with ceroid lipofuscin in mouse CNS neurons. J. Neurosci. 20, 6898-6906.
    • (2000) J. Neurosci. , vol.20 , pp. 6898-6906
    • Koike, M.1    Nakanishi, H.2    Saftig, P.3
  • 16
    • 77951248828 scopus 로고    scopus 로고
    • Autophagy: Links with the proteasome
    • Lamark T., and, Johansen T., (2010) Autophagy: links with the proteasome. Curr. Opin. Cell Biol. 22, 192-198.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 192-198
    • Lamark, T.1    Johansen, T.2
  • 17
    • 84555195856 scopus 로고    scopus 로고
    • Autophagy, mitochondria and oxidative stress: Cross-talk and redox signalling
    • Lee J., Giordano S., and, Zhang J., (2012) Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling. Biochem. J. 441, 523-540.
    • (2012) Biochem. J. , vol.441 , pp. 523-540
    • Lee, J.1    Giordano, S.2    Zhang, J.3
  • 21
    • 0037266549 scopus 로고    scopus 로고
    • A replacement of the active-site aspartic acid residue 293 in mouse cathepsin D affects its intracellular stability, processing and transport in HEK-293 cells
    • Partanen S., Storch S., Loffler H. G., Hasilik A., Tyynela J., and, Braulke T., (2003) A replacement of the active-site aspartic acid residue 293 in mouse cathepsin D affects its intracellular stability, processing and transport in HEK-293 cells. Biochem. J. 369, 55-62.
    • (2003) Biochem. J. , vol.369 , pp. 55-62
    • Partanen, S.1    Storch, S.2    Loffler, H.G.3    Hasilik, A.4    Tyynela, J.5    Braulke, T.6
  • 22
    • 64749103447 scopus 로고    scopus 로고
    • Inhibition of lysosomal functions reduces proteasomal activity
    • Qiao L., and, Zhang J., (2009) Inhibition of lysosomal functions reduces proteasomal activity. Neurosci. Lett. 456, 15-19.
    • (2009) Neurosci. Lett. , vol.456 , pp. 15-19
    • Qiao, L.1    Zhang, J.2
  • 23
    • 79955694568 scopus 로고    scopus 로고
    • Lysosomal enzyme cathepsin D protects against alpha-synuclein aggregation and toxicity
    • Qiao L., Hamamichi S., Caldwell K. A., et al,. (2008) Lysosomal enzyme cathepsin D protects against alpha-synuclein aggregation and toxicity. Mol. Brain 1, 17.
    • (2008) Mol. Brain , vol.1 , pp. 17
    • Qiao, L.1    Hamamichi, S.2    Caldwell, K.A.3
  • 24
    • 77950672979 scopus 로고    scopus 로고
    • Lysosomal function in macromolecular homeostasis and bioenergetics in Parkinson's disease
    • Schneider L., and, Zhang J., (2010) Lysosomal function in macromolecular homeostasis and bioenergetics in Parkinson's disease. Mol. Neurodegener. 5, 14.
    • (2010) Mol. Neurodegener. , vol.5 , pp. 14
    • Schneider, L.1    Zhang, J.2
  • 25
    • 0242300619 scopus 로고    scopus 로고
    • Alpha-Synuclein locus triplication causes Parkinson's disease
    • Singleton A. B., Farrer M., Johnson J., et al,. (2003) alpha-Synuclein locus triplication causes Parkinson's disease. Science 302, 841.
    • (2003) Science , vol.302 , pp. 841
    • Singleton, A.B.1    Farrer, M.2    Johnson, J.3
  • 26
    • 0034659833 scopus 로고    scopus 로고
    • A mutation in the ovine cathepsin D gene causes a congenital lysosomal storage disease with profound neurodegeneration
    • Tyynela J., Sohar I., Sleat D. E., Gin R. M., Donnelly R. J., Baumann M., Haltia M., and, Lobel P., (2000) A mutation in the ovine cathepsin D gene causes a congenital lysosomal storage disease with profound neurodegeneration. EMBO J. 19, 2786-2792.
    • (2000) EMBO J. , vol.19 , pp. 2786-2792
    • Tyynela, J.1    Sohar, I.2    Sleat, D.E.3    Gin, R.M.4    Donnelly, R.J.5    Baumann, M.6    Haltia, M.7    Lobel, P.8
  • 27
    • 84859600567 scopus 로고    scopus 로고
    • Targeting intracellular and extracellular alpha-synuclein as a therapeutic strategy in Parkinson's disease and other synucleinopathies
    • Vekrellis K., and, Stefanis L., (2012) Targeting intracellular and extracellular alpha-synuclein as a therapeutic strategy in Parkinson's disease and other synucleinopathies. Expert. Opin. Ther. Targets. 16, 421-432.
    • (2012) Expert. Opin. Ther. Targets. , vol.16 , pp. 421-432
    • Vekrellis, K.1    Stefanis, L.2
  • 28
    • 53049098471 scopus 로고    scopus 로고
    • Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells
    • Vogiatzi T., Xilouri M., Vekrellis K., and, Stefanis L., (2008) Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells. J. Biol. Chem. 283, 23542-23556.
    • (2008) J. Biol. Chem. , vol.283 , pp. 23542-23556
    • Vogiatzi, T.1    Xilouri, M.2    Vekrellis, K.3    Stefanis, L.4
  • 30
    • 77957189194 scopus 로고    scopus 로고
    • Alpha-Synuclein impairs macroautophagy: Implications for Parkinson's disease
    • Winslow A. R., Chen C. W., Corrochano S., et al,. (2010) alpha-Synuclein impairs macroautophagy: implications for Parkinson's disease. J. Cell Biol. 190, 1023-1037.
    • (2010) J. Cell Biol. , vol.190 , pp. 1023-1037
    • Winslow, A.R.1    Chen, C.W.2    Corrochano, S.3
  • 31
    • 0031593675 scopus 로고    scopus 로고
    • Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells
    • Yamamoto A., Tagawa Y., Yoshimori T., Moriyama Y., Masaki R., and, Tashiro Y., (1998) Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells. Cell Struct. Funct. 23, 33-42.
    • (1998) Cell Struct. Funct. , vol.23 , pp. 33-42
    • Yamamoto, A.1    Tagawa, Y.2    Yoshimori, T.3    Moriyama, Y.4    Masaki, R.5    Tashiro, Y.6
  • 32
    • 77956404377 scopus 로고    scopus 로고
    • Eaten alive: A history of macroautophagy
    • Yang Z., and, Klionsky D. J., (2010) Eaten alive: a history of macroautophagy. Nat. Cell Biol. 12, 814-822.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 814-822
    • Yang, Z.1    Klionsky, D.J.2
  • 33
    • 84879475204 scopus 로고    scopus 로고
    • Autophagy and mitophagy in cellular damage control
    • Zhang J., (2013) Autophagy and mitophagy in cellular damage control. Redox Biol. 1, 19-23.
    • (2013) Redox Biol. , vol.1 , pp. 19-23
    • Zhang, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.