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Volumn 287, Issue 20, 2012, Pages 16510-16520

Cellular prion protein regulates its ownα-cleavage through ADAM8 in skeletal muscle

Author keywords

[No Author keywords available]

Indexed keywords

CELL CULTURE; MAMMALS; PRASEODYMIUM COMPOUNDS; PROTEINS;

EID: 84860864336     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.360891     Document Type: Article
Times cited : (39)

References (81)
  • 1
    • 0037242707 scopus 로고    scopus 로고
    • Embryonic activation and developmental expression of the murine prion protein gene
    • Miele, G., Alejo Blanco A. R., Baybutt, H., Horvat, S., Manson, J., and Clinton, M. (2003) Embryonic activation and developmental expression of the murine prion protein gene. Gene Expr. 11, 1-12 (Pubitemid 36395880)
    • (2003) Gene Expression , vol.11 , Issue.1 , pp. 1-12
    • Miele, G.1    Alejo, B.A.R.2    Baybutt, H.3    Horvat, S.4    Manson, J.5    Clinton, M.6
  • 3
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
    • Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., and Strittmatter, S. M. (2009) Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers. Nature 457, 1128-1132
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Laurén, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 5
    • 77955617917 scopus 로고    scopus 로고
    • The prion protein as a receptor for amyloid-β
    • Kessels, H. W., Nguyen, L. N., Nabavi, S., and Malinow, R. (2010) The prion protein as a receptor for amyloid-β. Nature 466, E3-4
    • (2010) Nature , vol.466
    • Kessels, H.W.1    Nguyen, L.N.2    Nabavi, S.3    Malinow, R.4
  • 6
    • 77549087970 scopus 로고    scopus 로고
    • Prion protein: From physiology to cancer biology
    • Mehrpour, M., and Codogno, P. (2010) Prion protein: From physiology to cancer biology. Cancer. Lett. 290, 1-23
    • (2010) Cancer. Lett. , vol.290 , pp. 1-23
    • Mehrpour, M.1    Codogno, P.2
  • 10
    • 74249118091 scopus 로고    scopus 로고
    • Is, indeed, the prion protein a Harlequin servant of "many" masters?
    • Sorgato, M. C., Peggion, C., and Bertoli, A. (2009) Is, indeed, the prion protein a Harlequin servant of "many" masters? Prion 3, 202-205
    • (2009) Prion , vol.3 , pp. 202-205
    • Sorgato, M.C.1    Peggion, C.2    Bertoli, A.3
  • 12
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • DOI 10.1074/jbc.273.50.33107
    • Pauly, P. C., and Harris, D. A. (1998) Copper stimulates endocytosis of the prion protein. J. Biol. Chem. 273, 33107-33110 (Pubitemid 29005676)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.50 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 13
    • 67749133712 scopus 로고    scopus 로고
    • Prion protein (PrP) knock-out mice show altered iron metabolism: A functional role for PrP in iron uptake and transport
    • Singh, A., Kong, Q., Luo, X., Petersen, R. B., Meyerson, H., and Singh, N. (2009) Prion protein (PrP) knock-out mice show altered iron metabolism: a functional role for PrP in iron uptake and transport. PLoS One 4, e6115
    • (2009) PLoS One , vol.4
    • Singh, A.1    Kong, Q.2    Luo, X.3    Petersen, R.B.4    Meyerson, H.5    Singh, N.6
  • 17
    • 77951217018 scopus 로고    scopus 로고
    • Endogenous proteolytic cleavage of disease-associated prion protein to produce C2 fragments is strongly celland tissue-dependent
    • Dron, M., Moudjou, M., Chapuis, J., Salamat, M. K., Bernard, J., Cronier, S., Langevin, C., and Laude, H. (2010) Endogenous proteolytic cleavage of disease-associated prion protein to produce C2 fragments is strongly celland tissue-dependent. J. Biol. Chem. 285, 10252-10264
    • (2010) J. Biol. Chem. , vol.285 , pp. 10252-10264
    • Dron, M.1    Moudjou, M.2    Chapuis, J.3    Salamat, M.K.4    Bernard, J.5    Cronier, S.6    Langevin, C.7    Laude, H.8
  • 19
    • 0027074458 scopus 로고
    • Purification and properties of the cellular prion protein from Syrian hamster brain
    • Pan, K. M., Stahl, N., and Prusiner, S. B. (1992) Purification and properties of the cellular prion protein from Syrian hamster brain. Protein Sci. 1, 1343-1352 (Pubitemid 23009228)
    • (1992) Protein Science , vol.1 , Issue.10 , pp. 1343-1352
    • Pan, K.-M.1    Stahl, N.2    Prusiner, S.B.3
  • 21
    • 1642410070 scopus 로고    scopus 로고
    • α- and β-cleavages of the amino-terminus of the cellular prion protein
    • Mangé, A., Béranger, F., Peoc'h, K., Onodera, T., Frobert, Y., and Lehmann, S. (2004) α- and β-cleavages of the amino-terminus of the cellular prion protein. Biol. Cell 96, 125-132
    • (2004) Biol. Cell , vol.96 , pp. 125-132
    • Mangé, A.1    Béranger, F.2    Peoc'H, K.3    Onodera, T.4    Frobert, Y.5    Lehmann, S.6
  • 25
    • 22844451837 scopus 로고    scopus 로고
    • C complex that leads to prion propagation
    • DOI 10.1074/jbc.M413441200
    • Norstrom, E. M., and Mastrianni, J. A. (2005) The AGAAAAGA palindrome in PrP is required to generate a productive PrPSc-PrPC complex that leads to prion propagation. J. Biol. Chem. 280, 27236-27243 (Pubitemid 41040763)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.29 , pp. 27236-27243
    • Norstrom, E.M.1    Mastrianni, J.A.2
  • 27
    • 27744547982 scopus 로고    scopus 로고
    • Reactive oxygen species-mediated β-clevage of the prion protein in the cellular response to oxidative stress
    • DOI 10.1074/jbc.M507327200
    • Watt, N. T., Taylor, D. R., Gillott, A., Thomas, D. A., Perera, W. S., and Hooper, N. M. (2005) Reactive oxygen species-mediated β-cleavage of the prion protein in the cellular response to oxidative stress. J. Biol. Chem. 280, 35914-35921 (Pubitemid 41633859)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.43 , pp. 35914-35921
    • Watt, N.T.1    Taylor, D.R.2    Gillott, A.3    Thomas, D.A.4    Perera, W.S.S.5    Hooper, N.M.6
  • 28
    • 0034001444 scopus 로고    scopus 로고
    • Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie- associated prion protein accumulation
    • DOI 10.1128/JVI.74.10.4894-4897.2000
    • Doh-Ura, K., Iwaki, T., and Caughey, B. (2000) Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation. J. Virol. 74, 4894-4897 (Pubitemid 30237920)
    • (2000) Journal of Virology , vol.74 , Issue.10 , pp. 4894-4897
    • Doh-Ura, K.1    Iwaki, T.2    Caughey, B.3
  • 29
    • 3242744362 scopus 로고    scopus 로고
    • Cathepsin B and L are involved in degradation of prions in GT1-1 neuronal cells
    • DOI 10.1097/01.wnr.0000134931.81690.34
    • Luhr, K. M., Nordström, E. K., Löw, P., and Kristensson, K. (2004) Cathepsin B and L are involved in degradation of prions in GT1-1 neuronal cells. Neuroreport 15, 1663-1667 (Pubitemid 38971190)
    • (2004) NeuroReport , vol.15 , Issue.10 , pp. 1663-1667
    • Luhr, K.M.1    Nordstrom, E.K.2    Low, P.3    Kristensson, K.4
  • 30
    • 60549094701 scopus 로고    scopus 로고
    • Specific biarsenical labeling of cell surface proteins allows fluorescent- And biotin-tagging of amyloid precursor protein and prion proteins
    • Taguchi, Y., Shi, Z. D., Ruddy, B., Dorward, D. W., Greene, L., and Baron, G. S. (2009) Specific biarsenical labeling of cell surface proteins allows fluorescent- and biotin-tagging of amyloid precursor protein and prion proteins. Mol. Biol. Cell 20, 233-244
    • (2009) Mol. Biol. Cell , vol.20 , pp. 233-244
    • Taguchi, Y.1    Shi, Z.D.2    Ruddy, B.3    Dorward, D.W.4    Greene, L.5    Baron, G.S.6
  • 31
    • 72149127389 scopus 로고    scopus 로고
    • The alpha-secretase-derived N-terminal product of cellular prion, N1, displays neuroprotective function in vitro and in vivo
    • Guillot-Sestier, M. V., Sunyach, C., Druon, C., Scarzello, S., and Checler, F. (2009) The alpha-secretase-derived N-terminal product of cellular prion, N1, displays neuroprotective function in vitro and in vivo. J. Biol. Chem. 284, 35973-35986
    • (2009) J. Biol. Chem. , vol.284 , pp. 35973-35986
    • Guillot-Sestier, M.V.1    Sunyach, C.2    Druon, C.3    Scarzello, S.4    Checler, F.5
  • 32
    • 33847299070 scopus 로고    scopus 로고
    • The C-terminal products of cellular prion protein processing, C1 and C2, exert distinct influence on p53-dependent staurosporine-induced caspase-3 activation
    • DOI 10.1074/jbc.M609663200
    • Sunyach, C., Cisse, M. A., da Costa, C. A., Vincent, B., and Checler, F. (2007) The C-terminal products of cellular prion protein processing, C1 and C2, exert distinct influence on p53-dependent staurosporine-induced caspase-3 activation. J. Biol. Chem. 282, 1956-1963 (Pubitemid 47076732)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.3 , pp. 1956-1963
    • Sunyach, C.1    Cisse, M.A.2    Da, C.C.A.3    Vincent, B.4    Checler, F.5
  • 35
    • 0027204276 scopus 로고
    • A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells
    • Shyng, S. L., Huber, M. T., and Harris, D. A. (1993) A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells. J. Biol. Chem. 268, 15922-15928 (Pubitemid 23222097)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.21 , pp. 15922-15928
    • Shyng, S.-L.1    Huber, M.T.2    Harris, D.A.3
  • 36
    • 0027405573 scopus 로고
    • Processing of a cellular prion protein: Identification of N- and C- terminal cleavage sites
    • DOI 10.1021/bi00055a003
    • Harris, D. A., Huber, M. T., van Dijken, P., Shyng, S. L., Chait, B. T., and Wang, R. (1993) Processing of a cellular prion protein: identification of Nand C-terminal cleavage sites. Biochemistry 32, 1009-1016 (Pubitemid 23057673)
    • (1993) Biochemistry , vol.32 , Issue.4 , pp. 1009-1016
    • Harris, D.A.1    Huber, M.T.2    Van Dijken, P.3    Shyng, S.-L.4    Chait, B.T.5    Wang, R.6
  • 37
    • 0034634655 scopus 로고    scopus 로고
    • Phorbol ester-regulated cleavage of normal prion protein in HEK293 human cells and murine neurons
    • Vincent, B., Paitel, E., Frobert, Y., Lehmann, S., Grassi, J., and Checler, F. (2000) Phorbol ester-regulated cleavage of normal prion protein in HEK293 human cells and murine neurons. J. Biol. Chem. 275, 35612-35616
    • (2000) J. Biol. Chem. , vol.275 , pp. 35612-35616
    • Vincent, B.1    Paitel, E.2    Frobert, Y.3    Lehmann, S.4    Grassi, J.5    Checler, F.6
  • 38
    • 0035851151 scopus 로고    scopus 로고
    • The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein
    • Vincent, B., Paitel, E., Saftig, P., Frobert, Y., Hartmann, D., De Strooper, B., Grassi, J., Lopez-Perez, E., and Checler, F. (2001) The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. J. Biol. Chem. 276, 37743-37746
    • (2001) J. Biol. Chem. , vol.276 , pp. 37743-37746
    • Vincent, B.1    Paitel, E.2    Saftig, P.3    Frobert, Y.4    Hartmann, D.5    De Strooper, B.6    Grassi, J.7    Lopez-Perez, E.8    Checler, F.9
  • 39
    • 28844433559 scopus 로고    scopus 로고
    • The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity
    • DOI 10.1074/jbc.M506069200
    • Cissé, M. A., Sunyach, C., Lefranc-Jullien, S., Postina, R., Vincent, B., and Checler, F. (2005) The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity. J. Biol. Chem. 280, 40624-40631 (Pubitemid 41780553)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.49 , pp. 40624-40631
    • Cisse, M.A.1    Sunyach, C.2    Lefranc-Jullien, S.3    Postina, R.4    Vincent, B.5    Checler, F.6
  • 40
    • 59349099006 scopus 로고    scopus 로고
    • α-cleavage of the prion protein occurs in a late compartment of the secretory pathway and is independent of lipid rafts
    • Walmsley, A. R., Watt, N. T., Taylor, D. R., Perera, W. S., and Hooper, N. M. (2009)α-cleavage of the prion protein occurs in a late compartment of the secretory pathway and is independent of lipid rafts. Mol. Cell. Neurosci. 40, 242-248
    • (2009) Mol. Cell. Neurosci. , vol.40 , pp. 242-248
    • Walmsley, A.R.1    Watt, N.T.2    Taylor, D.R.3    Perera, W.S.4    Hooper, N.M.5
  • 41
    • 0141533033 scopus 로고    scopus 로고
    • ADAMs: Modulators of cell-cell and cell-matrix interactions
    • White, J. M. (2003) ADAMs: modulators of cell-cell and cell-matrix interactions. Curr. Opin. Cell Biol. 15, 598-606
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 598-606
    • White, J.M.1
  • 43
    • 0038056151 scopus 로고    scopus 로고
    • Shedding of membrane proteins by ADAM family proteases
    • Moss, M. L., and Lambert, M. H. (2002) Shedding of membrane proteins by ADAM family proteases. Essays Biochem. 38, 141-153 (Pubitemid 36589200)
    • (2002) Essays in Biochemistry , vol.38 , pp. 141-153
    • Moss, M.L.1    Lambert, M.H.2
  • 44
    • 34247115682 scopus 로고    scopus 로고
    • 3 muscarinic receptors control physiological processing of cellular prion by modulating ADAM17 phosphorylation and activity
    • DOI 10.1523/JNEUROSCI.5293-06.2007
    • Alfa Cissé, M., Sunyach, C., Slack B. E., Fisher, A., Vincent, B., and Checler, F. (2007) M1 and M3 muscarinic receptors control physiological processing of cellular prion by modulating ADAM17 phosphorylation and activity. J. Neurosci. 27, 4083-4092 (Pubitemid 46597172)
    • (2007) Journal of Neuroscience , vol.27 , Issue.15 , pp. 4083-4092
    • Cisse, M.A.1    Sunyach, C.2    Slack, B.E.3    Fisher, A.4    Vincent, B.5    Checler, F.6
  • 46
    • 70349783752 scopus 로고    scopus 로고
    • Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo
    • Endres, K., Mitteregger, G., Kojro, E., Kretzschmar, H., and Fahrenholz, F. (2009) Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo. Neurobiol. Dis. 36, 233-241
    • (2009) Neurobiol. Dis. , vol.36 , pp. 233-241
    • Endres, K.1    Mitteregger, G.2    Kojro, E.3    Kretzschmar, H.4    Fahrenholz, F.5
  • 49
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling, G. C., Scott, M., Mastrianni, J., Gabizon, R., Torchia, M., Cohen, F. E., DeArmond, S. J., and Prusiner, S. B. (1995) Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83, 79-90
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1    Scott, M.2    Mastrianni, J.3    Gabizon, R.4    Torchia, M.5    Cohen, F.E.6    DeArmond, S.J.7    Prusiner, S.B.8
  • 52
    • 31444435798 scopus 로고    scopus 로고
    • C metabolism in skeletal muscle cells
    • DOI 10.1016/j.febslet.2006.01.008, PII S001457930600041X
    • Massimino, M. L., Ferrari, J., Sorgato, M. C., and Bertoli, A. (2006) Heterogeneous PrPC metabolism in skeletal muscle cells. FEBS Lett. 580, 878-884 (Pubitemid 43152308)
    • (2006) FEBS Letters , vol.580 , Issue.3 , pp. 878-884
    • Massimino, M.L.1    Ferrari, J.2    Sorgato, M.C.3    Bertoli, A.4
  • 53
  • 55
    • 0027433773 scopus 로고
    • Prion protein is abnormally accumulated in inclusion-body myositis
    • Askanas, V., Bilak, M., Engel, W. K., Alvarez, R. B., Tomé, F., and Leclerc, A. (1993) Prion protein is abnormally accumulated in inclusion-body myositis. Neuroreport 5, 25-28 (Pubitemid 23330812)
    • (1993) NeuroReport , vol.5 , Issue.1 , pp. 25-28
    • Askanas, V.1    Bilak, M.2    Engel, W.K.3    Alvarez, R.B.4    Tome, F.5    Leclerc, A.6
  • 56
    • 0028075620 scopus 로고
    • Abnormal accumulation of prion protein mRNA in muscle fibers of patients with sporadic inclusion-body myositis and hereditary inclusion-body myopathy
    • Sarkozi, E., Askanas, V., and Engel, W. K. (1994) Abnormal accumulation of prion protein mRNA in muscle fibers of patients with sporadic inclusion- body myositis and hereditary inclusion-body myopathy. Am. J. Pathol. 145, 1280-1284 (Pubitemid 24378481)
    • (1994) American Journal of Pathology , vol.145 , Issue.6 , pp. 1280-1284
    • Sarkozi, E.1    Askanas, V.2    Engel, W.K.3
  • 58
    • 0028052363 scopus 로고
    • Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins
    • DOI 10.1016/0092-8674(94)90177-5
    • Westaway, D., DeArmond, S. J., Cayetano-Canlas, J., Groth, D., Foster, D., Yang, S. L., Torchia, M., Carlson, G. A., and Prusiner, S. B. (1994) Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins. Cell 76, 117-129 (Pubitemid 24035286)
    • (1994) Cell , vol.76 , Issue.1 , pp. 117-129
    • Westaway, D.1    DeArmond, S.J.2    Cayetano-Canlas, J.3    Groth, D.4    Foster, D.5    Yang, S.-L.6    Torchia, M.7    Carlson, G.A.8    Prusiner, S.B.9
  • 63
    • 4444356433 scopus 로고    scopus 로고
    • Epitope scanning reveals gain and loss of strain specific antibody binding epitopes associated with the conversion of normal cellular prion to scrapie prion
    • DOI 10.1111/j.1471-4159.2004.02582.x
    • Pan, T., Li, R., Kang, S. C., Wong, B. S., Wisniewski, T., and Sy, M. S. (2004) Epitope scanning reveals gain and loss of strain specific antibody binding epitopes associated with the conversion of normal cellular prion to scrapie prion. J. Neurochem. 90, 1205-1217 (Pubitemid 39167353)
    • (2004) Journal of Neurochemistry , vol.90 , Issue.5 , pp. 1205-1217
    • Pan, T.1    Li, R.2    Kang, S.-C.3    Wong, B.-S.4    Wisniewski, T.5    Sy, M.-S.6
  • 64
    • 0033601248 scopus 로고    scopus 로고
    • Membrane environment alters the conformational structure of the recombinant human prion protein
    • Morillas, M., Swietnicki, W., Gambetti, P., and Surewicz, W. K. (1999) Membrane environment alters the conformational structure of the recombinant human prion protein. J. Biol. Chem. 274, 36859-36865
    • (1999) J. Biol. Chem. , vol.274 , pp. 36859-36865
    • Morillas, M.1    Swietnicki, W.2    Gambetti, P.3    Surewicz, W.K.4
  • 65
    • 34547702317 scopus 로고    scopus 로고
    • Characterization of the prion protein 3F4 epitope and its use as a molecular tag
    • DOI 10.1016/j.jneumeth.2007.06.005, PII S0165027007002737
    • Lund, C., Olsen, C. M., Tveit, H., and Tranulis, M. A. (2007) Characterization of the prion protein 3F4 epitope and its use as a molecular tag. J. Neurosci. Methods 165, 183-190 (Pubitemid 47212461)
    • (2007) Journal of Neuroscience Methods , vol.165 , Issue.2 , pp. 183-190
    • Lund, C.1    Olsen, C.M.2    Tveit, H.3    Tranulis, M.A.4
  • 67
    • 78650114658 scopus 로고    scopus 로고
    • Prion and TNFα: TAC(E)it agreement between the prion protein and cell signaling
    • Stella, R., Massimino, M. L., Sorgato, M. C., and Bertoli, A. (2010) Prion and TNFα: TAC(E)it agreement between the prion protein and cell signaling. Cell Cycle 9, 4616-4621
    • (2010) Cell Cycle , vol.9 , pp. 4616-4621
    • Stella, R.1    Massimino, M.L.2    Sorgato, M.C.3    Bertoli, A.4
  • 69
    • 34250669605 scopus 로고    scopus 로고
    • TNF-α regulates myogenesis and muscle regeneration by activating p38 MAPK
    • DOI 10.1152/ajpcell.00486.2006
    • Chen, S. E., Jin, B., and Li, Y. P. (2007) TNF-α regulates myogenesis and muscle regeneration by activating p38 MAPK. Am. J. Physiol. Cell. Physiol. 292, C1660-C1671 (Pubitemid 47080547)
    • (2007) American Journal of Physiology - Cell Physiology , vol.292 , Issue.5
    • Chen, S.-E.1    Jin, B.2    Li, Y.-P.3
  • 70
    • 33947315778 scopus 로고    scopus 로고
    • TACE release of TNF-α mediates mechanotransduction-induced activation of p38 MAPK and myogenesis
    • DOI 10.1242/jcs.03372
    • Zhan, M., Jin, B., Chen, S. E., Reecy, J. M., and Li, Y. P. (2007) TACE release of TNF-alpha mediates mechanotransduction-induced activation of p38 MAPK and myogenesis. J. Cell Sci. 120, 692-701 (Pubitemid 46437903)
    • (2007) Journal of Cell Science , vol.120 , Issue.4 , pp. 692-701
    • Zhan, M.1    Jin, B.2    Chen, S.-E.3    Reecy, J.M.4    Li, Y.-P.5
  • 71
    • 33745183356 scopus 로고    scopus 로고
    • The p38 MAPK signaling pathway: A major regulator of skeletal muscle development
    • Keren, A., Tamir, Y., and Bengal, E. (2006) The p38 MAPK signaling pathway: a major regulator of skeletal muscle development. Mol. Cell. Endocrinol. 252, 224-230
    • (2006) Mol. Cell. Endocrinol. , vol.252 , pp. 224-230
    • Keren, A.1    Tamir, Y.2    Bengal, E.3
  • 72
    • 0033582459 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase pathway promotes skeletal muscle differentiation. Participation of the Mef2c transcription factor
    • Zetser, A., Gredinger, E., and Bengal, E. (1999) p38 mitogen-activated protein kinase pathway promotes skeletal muscle differentiation. Participation of the Mef2c transcription factor. J. Biol. Chem. 274, 5193-5200
    • (1999) J. Biol. Chem. , vol.274 , pp. 5193-5200
    • Zetser, A.1    Gredinger, E.2    Bengal, E.3
  • 73
    • 0034332481 scopus 로고    scopus 로고
    • Tumor necrosis factor α induces a metalloproteasedisintegrin, ADAM8 (CD 156): Implications for neuron-glia interactions during neurodegeneration
    • Schlomann, U., Rathke-Hartlieb, S., Yamamoto, S., Jockusch, H., and Bartsch, J. W. (2000) Tumor necrosis factor α induces a metalloproteasedisintegrin, ADAM8 (CD 156): implications for neuron-glia interactions during neurodegeneration. J. Neurosci. 20, 7964-7971
    • (2000) J. Neurosci. , vol.20 , pp. 7964-7971
    • Schlomann, U.1    Rathke-Hartlieb, S.2    Yamamoto, S.3    Jockusch, H.4    Bartsch, J.W.5
  • 74
    • 77956602522 scopus 로고    scopus 로고
    • Tumor necrosis factor-α (TNF-α) regulates shedding of TNF-α receptor 1 by the metalloprotease-disintegrin ADAM8: Evidence for a protease-regulated feedback loop in neuroprotection
    • Bartsch, J. W., Wildeboer, D., Koller, G., Naus, S., Rittger, A., Moss, M. L., Minai, Y., and Jockusch, H. (2010) Tumor necrosis factor-α (TNF-α) regulates shedding of TNF-α receptor 1 by the metalloprotease-disintegrin ADAM8: evidence for a protease-regulated feedback loop in neuroprotection. J. Neurosci. 30, 12210-12218
    • (2010) J. Neurosci. , vol.30 , pp. 12210-12218
    • Bartsch, J.W.1    Wildeboer, D.2    Koller, G.3    Naus, S.4    Rittger, A.5    Moss, M.L.6    Minai, Y.7    Jockusch, H.8
  • 75
    • 67650459027 scopus 로고    scopus 로고
    • Cellular prion protein coupling to TACE-dependent TNF-α shedding controls neurotransmitter catabolism in neuronal cells
    • Pradines, E., Loubet, D., Mouillet-Richard, S., Manivet, P., Launay, J. M., Kellermann, O., and Schneider, B. (2009) Cellular prion protein coupling to TACE-dependent TNF-α shedding controls neurotransmitter catabolism in neuronal cells. J. Neurochem. 110, 912-923
    • (2009) J. Neurochem. , vol.110 , pp. 912-923
    • Pradines, E.1    Loubet, D.2    Mouillet-Richard, S.3    Manivet, P.4    Launay, J.M.5    Kellermann, O.6    Schneider, B.7
  • 76
    • 0036882127 scopus 로고    scopus 로고
    • c triggers caspase 3 activation: Potentiation by proteasome inhibitors and blockade by anti-PrP antibodies
    • DOI 10.1046/j.1471-4159.2002.01234.x
    • Paitel, E., Alves da Costa, C., Vilette, D., Grassi, J., and Checler, F. (2002) Overexpression of PrPc triggers caspase 3 activation: potentiation by proteasome inhibitors and blockade by anti-PrP antibodies. J. Neurochem. 83, 1208-1214 (Pubitemid 35397130)
    • (2002) Journal of Neurochemistry , vol.83 , Issue.5 , pp. 1208-1214
    • Paitel, E.1    Alves, D.C.C.2    Vilette, D.3    Grassi, J.4    Checler, F.5
  • 77
    • 0037855771 scopus 로고    scopus 로고
    • Cellular prion protein sensitizes neurons to apoptotic stimuli through Mdm2-regulated and p53-dependent caspase 3-like activation
    • DOI 10.1074/jbc.M211580200
    • Paitel, E., Fahraeus, R., and Checler, F. (2003) Cellular prion protein sensitizes neurons to apoptotic stimuli through Mdm2-regulated and p53- dependent caspase 3-like activation. J. Biol. Chem. 278, 10061-10066 (Pubitemid 36800261)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.12 , pp. 10061-10066
    • Paitel, E.1    Fahraeus, R.2    Checler, F.3
  • 78
    • 0347683432 scopus 로고    scopus 로고
    • Primary Cultured Neurons Devoid of Cellular Prion Display Lower Responsiveness to Staurosporine through the Control of p53 at Both Transcriptional and Post-transcriptional Levels
    • DOI 10.1074/jbc.M310453200
    • Paitel, E., Sunyach, C., Alves da Costa, C., Bourdon, J. C., Vincent, B., and Checler, F. (2004) Primary cultured neurons devoid of cellular prion display lower responsiveness to staurosporine through the control of p53 at both transcriptional and post-transcriptional levels. J. Biol. Chem. 279, 612-618 (Pubitemid 38044865)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.1 , pp. 612-618
    • Paitel, E.1    Sunyach, C.2    Da, C.C.A.3    Bourdon, J.-C.4    Vincent, B.5    Checler, F.6
  • 79
    • 33748417398 scopus 로고    scopus 로고
    • Dividing roles of prion protein in staurosporine-mediated apoptosis
    • DOI 10.1016/j.bbrc.2006.08.116, PII S0006291X06019127
    • Zhang, Y., Qin, K., Wang, J., Hung, T., and Zhao, R. Y. (2006) Dividing roles of prion protein in staurosporine-mediated apoptosis. Biochem. Biophys. Res. Commun. 349, 759-768 (Pubitemid 44344579)
    • (2006) Biochemical and Biophysical Research Communications , vol.349 , Issue.2 , pp. 759-768
    • Zhang, Y.1    Qin, K.2    Wang, J.3    Hung, T.4    Zhao, R.Y.5
  • 80
    • 34147206506 scopus 로고    scopus 로고
    • C but not prevented DNA fragmentation initiated by serum deprivation
    • DOI 10.1002/jcp.20969
    • Gougoumas, D. D., Vizirianakis, I. S., Triviai, I. N., and Tsiftsoglou, A. S. (2007) Activation of Prn-p gene and stable transfection of Prn-p cDNA in leukemia MEL and neuroblastoma N2a cells increased production of PrP(C) but not prevented DNA fragmentation initiated by serum deprivation. J. Cell. Physiol. 211, 551-559 (Pubitemid 46580109)
    • (2007) Journal of Cellular Physiology , vol.211 , Issue.2 , pp. 551-559
    • Gougoumas, D.D.1    Vizirianakis, I.S.2    Triviai, I.N.3    Tsiftsoglou, A.S.4
  • 81
    • 83755162371 scopus 로고    scopus 로고
    • A naturally occurring C-terminal fragment of the prion protein (PrP) delays disease and acts as a dominant-negative inhibitor of PrPSc formation
    • Westergard, L., Turnbaugh, J. A., and Harris, D. A. (2011) A naturally occurring C-terminal fragment of the prion protein (PrP) delays disease and acts as a dominant-negative inhibitor of PrPSc formation. J. Biol. Chem. 286, 44234-44242
    • (2011) J. Biol. Chem. , vol.286 , pp. 44234-44242
    • Westergard, L.1    Turnbaugh, J.A.2    Harris, D.A.3


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