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Volumn 84, Issue 8, 2003, Pages 2279-2283

Up-regulation of cathepsin B and cathepsin L activities in scrapie-infected mouse Neuro2a cells

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN B; CATHEPSIN L; CELL SURFACE PROTEIN; CYSTEINE PROTEINASE; ISOPROTEIN; PRION PROTEIN; PROTEINASE K;

EID: 0043169474     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/vir.0.19153-0     Document Type: Short Survey
Times cited : (30)

References (34)
  • 3
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H and cathepsin L
    • Edited by S. P. Colowick & N. O. Kaplan. New York: Academic Press
    • Barrett, A. J. & Kirschke, H. (1981). Cathepsin B, cathepsin H and cathepsin L. In Methods in Enzymology, pp. 535-561. Edited by S. P. Colowick & N. O. Kaplan. New York: Academic Press.
    • (1981) Methods in Enzymology , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 4
    • 0033999635 scopus 로고    scopus 로고
    • Cultured cell sublines highly susceptible to prion infection
    • Bosque, P. J. & Prusiner, S. B. (2000). Cultured cell sublines highly susceptible to prion infection. J Virol 74, 4377-4386.
    • (2000) J. Virol. , vol.74 , pp. 4377-4386
    • Bosque, P.J.1    Prusiner, S.B.2
  • 5
    • 0028782007 scopus 로고
    • Scrapie-associated PrP accumulation and agent replication: Effects of sulphated glycosaminoglycan analogues
    • Caughey, B. (1994). Scrapie-associated PrP accumulation and agent replication: effects of sulphated glycosaminoglycan analogues. Philos Trans R Soc Lond Ser B 343, 399-404.
    • (1994) Philos. Trans. R. Soc. Lond. Ser. B , vol.343 , pp. 399-404
    • Caughey, B.1
  • 6
    • 0035223716 scopus 로고    scopus 로고
    • Transmissible spongiform encephalopathies and prion protein interconversions
    • Caughey, B. & Chesebro, B. (2001). Transmissible spongiform encephalopathies and prion protein interconversions. Adv Virus Res 56, 277-311.
    • (2001) Adv. Virus Res. , vol.56 , pp. 277-311
    • Caughey, B.1    Chesebro, B.2
  • 7
    • 0027535855 scopus 로고
    • Sulfated polyanion inhibition of scrapie-associated PrP accumulation in cultured cells
    • Caughey, B. & Raymond, G. J. (1993). Sulfated polyanion inhibition of scrapie-associated PrP accumulation in cultured cells. J Virol 67, 643-650.
    • (1993) J. Virol. , vol.67 , pp. 643-650
    • Caughey, B.1    Raymond, G.J.2
  • 8
    • 0025876226 scopus 로고
    • N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): Implications regarding the site of conversion of PrP to the protease-resistant state
    • Caughey, B., Raymond, G. J., Ernst, D. & Race, R. E. (1991). N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state. J Virol 65, 6597-6603.
    • (1991) J. Virol. , vol.65 , pp. 6597-6603
    • Caughey, B.1    Raymond, G.J.2    Ernst, D.3    Race, R.E.4
  • 9
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: Their causes and molecular basis
    • Collinge, J. (2001). Prion diseases of humans and animals: their causes and molecular basis. Annu Rev Neurosci 24, 519-550.
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 519-550
    • Collinge, J.1
  • 10
    • 0032571330 scopus 로고    scopus 로고
    • Gene expression in scrapie: Cloning of a new scrapie-responsive gene and the identification of increased levels of seven other mRNA transcripts
    • Dandoy-Dron, F., Guillo, F., Benboudjema, L., Deslys, J. P., Lasmezas, C., Dormont, D., Tovey, M. G. & Dron, M. (1998). Gene expression in scrapie: cloning of a new scrapie-responsive gene and the identification of increased levels of seven other mRNA transcripts. J Biol Chem 273, 7691-7697.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7691-7697
    • Dandoy-Dron, F.1    Guillo, F.2    Benboudjema, L.3    Deslys, J.P.4    Lasmezas, C.5    Dormont, D.6    Tovey, M.G.7    Dron, M.8
  • 11
    • 0025951302 scopus 로고
    • Neuropathological changes in scrapie and Alzheimer's disease are associated with increased expression of apolipoprotein E and cathepsin D in astrocytes
    • Diedrich, J. F., Minnigan, H., Carp, R. I., Whitaker, J. N., Race, R., Frey, W. & Haase, A. T. (1991). Neuropathological changes in scrapie and Alzheimer's disease are associated with increased expression of apolipoprotein E and cathepsin D in astrocytes. J Virol 65, 4759-4768.
    • (1991) J. Virol. , vol.65 , pp. 4759-4768
    • Diedrich, J.F.1    Minnigan, H.2    Carp, R.I.3    Whitaker, J.N.4    Race, R.5    Frey, W.6    Haase, A.T.7
  • 12
    • 0034001444 scopus 로고    scopus 로고
    • Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation
    • Doh-ura, K., Iwaki, T. & Caughey, B. (2000). Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation. J Virol 74, 4894-4897.
    • (2000) J. Virol. , vol.74 , pp. 4894-4897
    • Doh-ura, K.1    Iwaki, T.2    Caughey, B.3
  • 13
    • 0017702291 scopus 로고
    • Flow cytometric measurement of peptidases with use of 5-nitrosalicylaldehyde and 4-methoxy-beta-naphthylamine derivatives
    • Dolbeare, F. A. & Smith, R. E. (1977). Flow cytometric measurement of peptidases with use of 5-nitrosalicylaldehyde and 4-methoxy-beta-naphthylamine derivatives. Clin Chem 23, 1485-1491.
    • (1977) Clin. Chem. , vol.23 , pp. 1485-1491
    • Dolbeare, F.A.1    Smith, R.E.2
  • 16
    • 0029085515 scopus 로고
    • Neuronal cell death in scrapie-infected mice is due to apoptosis
    • Giese, A., Groschup, M. H., Hess, B. & Kretzschmar, H. A. (1995). Neuronal cell death in scrapie-infected mice is due to apoptosis. Brain Pathol 5, 213-221.
    • (1995) Brain Pathol. , vol.5 , pp. 213-221
    • Giese, A.1    Groschup, M.H.2    Hess, B.3    Kretzschmar, H.A.4
  • 19
    • 0029590746 scopus 로고
    • Procathepsin L degrades extracellular matrix proteins in the presence of glycosaminoglycans in vitro
    • Ishidoh, K. & Kominami, E. (1995). Procathepsin L degrades extracellular matrix proteins in the presence of glycosaminoglycans in vitro. Biochem Biophys Res Commun 217, 624-631.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 624-631
    • Ishidoh, K.1    Kominami, E.2
  • 21
    • 0034307476 scopus 로고    scopus 로고
    • Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy
    • Kegel, K. B., Kim, M., Sapp, E., McIntyre, C., Castano, J. G., Aronin, N. & DiFiglia, M. (2000). Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy. J Neurosci 20, 7268-7278.
    • (2000) J. Neurosci. , vol.20 , pp. 7268-7278
    • Kegel, K.B.1    Kim, M.2    Sapp, E.3    McIntyre, C.4    Castano, J.G.5    Aronin, N.6    DiFiglia, M.7
  • 22
    • 0035096992 scopus 로고    scopus 로고
    • Microglial secreted cathepsin B induces neuronal apoptosis
    • Kingham, P. J. & Pocock, J. M. (2001). Microglial secreted cathepsin B induces neuronal apoptosis. J Neurochem 76, 1475-1484.
    • (2001) J. Neurochem. , vol.76 , pp. 1475-1484
    • Kingham, P.J.1    Pocock, J.M.2
  • 23
    • 0033987067 scopus 로고    scopus 로고
    • Upregulation of the genes encoding lysosomal hydrolases, a perforin-like protein, and peroxidases in the brains of mice affected with an experimental prion disease
    • Kopacek, J., Sakaguchi, S., Shigematsu, K., Nishida, N., Atarashi, R., Nakaoke, R., Moriuchi, R., Niwa, M. & Katamine, S. (2000). Upregulation of the genes encoding lysosomal hydrolases, a perforin-like protein, and peroxidases in the brains of mice affected with an experimental prion disease. J Virol 74, 411-417.
    • (2000) J. Virol. , vol.74 , pp. 411-417
    • Kopacek, J.1    Sakaguchi, S.2    Shigematsu, K.3    Nishida, N.4    Atarashi, R.5    Nakaoke, R.6    Moriuchi, R.7    Niwa, M.8    Katamine, S.9
  • 24
    • 0029959819 scopus 로고    scopus 로고
    • Differential suppression by protease inhibitors and cytokines of apoptosis induced by wild-type p53 and cytotoxic agents
    • Lotem, J. & Sachs, L. (1996). Differential suppression by protease inhibitors and cytokines of apoptosis induced by wild-type p53 and cytotoxic agents. Proc Natl Acad Sci U S A 93, 12507-12512.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 12507-12512
    • Lotem, J.1    Sachs, L.2
  • 26
    • 0035902194 scopus 로고    scopus 로고
    • Shattuck lecture - Neurodegenerative diseases and prions
    • Prusiner, S. B. (2001). Shattuck lecture - neurodegenerative diseases and prions. N Engl J Med 344, 1548-1551.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1548-1551
    • Prusiner, S.B.1
  • 27
    • 0032859935 scopus 로고    scopus 로고
    • Autocatalytic processing of recombinant human procathepsin B is a bimolecular process
    • Rozman, J., Stojan, J., Kuhelj, R., Turk, V. & Turk, B. (1999). Autocatalytic processing of recombinant human procathepsin B is a bimolecular process. FEBS Lett 459, 358-362.
    • (1999) FEBS Lett. , vol.459 , pp. 358-362
    • Rozman, J.1    Stojan, J.2    Kuhelj, R.3    Turk, V.4    Turk, B.5
  • 28
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • Saborio, G. P., Permanne, B. & Soto, C. (2001). Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411, 810-813.
    • (2001) Nature , vol.411 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 29
    • 0025243737 scopus 로고
    • Immunolocalization of heparan sulfate proteoglycans to the prion protein amyloid plaques of Gerstmann-Sträussler syndrome, Creutzfeldt-Jakob disease and scrapie
    • Snow, A. D., Wight, T. N., Nochlin, D., Koike, Y., Kimata, K., DeArmond, S. J. & Prusiner, S. B. (1990). Immunolocalization of heparan sulfate proteoglycans to the prion protein amyloid plaques of Gerstmann-Sträussler syndrome, Creutzfeldt-Jakob disease and scrapie. Lab Invest 63, 601-611.
    • (1990) Lab. Invest. , vol.63 , pp. 601-611
    • Snow, A.D.1    Wight, T.N.2    Nochlin, D.3    Koike, Y.4    Kimata, K.5    DeArmond, S.J.6    Prusiner, S.B.7
  • 30
    • 0029328568 scopus 로고
    • Quantification of intracellular cathepsin activities in human lung tumor cell lines by flow cytometry
    • Ulbricht, B., Spiess, E., Schwartz-Albiez, R. & Ebert, W. (1995). Quantification of intracellular cathepsin activities in human lung tumor cell lines by flow cytometry. Biol Chem Hoppe Seyler 376, 407-414.
    • (1995) Biol. Chem. Hoppe. Seyler , vol.376 , pp. 407-414
    • Ulbricht, B.1    Spiess, E.2    Schwartz-Albiez, R.3    Ebert, W.4
  • 31
    • 0031793017 scopus 로고    scopus 로고
    • Atractyloside-induced release of cathepsin B, a protease with caspase-processing activity
    • 7 other authors
    • Vancompernolle, K., Van Herreweghe, F, Pynaert, G. & 7 other authors (1998). Atractyloside-induced release of cathepsin B, a protease with caspase-processing activity. FEBS Lett 438, 150-158.
    • (1998) FEBS Lett. , vol.438 , pp. 150-158
    • Vancompernolle, K.1    Van Herreweghe, F.2    Pynaert, G.3
  • 33
    • 0034739734 scopus 로고    scopus 로고
    • Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates
    • Yamashima, T. (2000). Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates. Prog Neurobiol 62, 273-295.
    • (2000) Prog. Neurobiol. , vol.62 , pp. 273-295
    • Yamashima, T.1
  • 34
    • 0037740712 scopus 로고    scopus 로고
    • In situ analysis of cellular poly(ADP-ribose) production in scrapie-infected mouse neuroblastoma cells
    • Zhang, Y., Poirier, G. G. & Bürkle, A. (2002). In situ analysis of cellular poly(ADP-ribose) production in scrapie-infected mouse neuroblastoma cells. Histochem J 34, 357-363.
    • (2002) Histochem. J. , vol.34 , pp. 357-363
    • Zhang, Y.1    Poirier, G.G.2    Bürkle, A.3


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