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Volumn 6, Issue 1, 2012, Pages 23-25

Two-steps control of cellular prion physiology by the extracellular regulated kinase-1 (ERK1)

Author keywords

ADAM proteases; AP 1; Cellular prion (PrP C); Extracellular regulated kinase 1 (ERK1); N1 fragment; p53; Processing; secretase; Protein kinase C (PKC) isoforms; Transcription

Indexed keywords

ALPHA SECRETASE; AMYLOID PRECURSOR PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; PRION PROTEIN; PROTEIN KINASE C; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME;

EID: 84857230723     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.6.1.18004     Document Type: Note
Times cited : (1)

References (25)
  • 1
    • 0030478022 scopus 로고    scopus 로고
    • Molecular biology and pathogenesis of prion diseases
    • PMID:9009832
    • Prusiner SB. Molecular biology and pathogenesis of prion diseases. Trends Biochem Sci 1996; 21:482-7; PMID:9009832; http://dx.doi.org/10.1016/S0968- 0004(96)10063-3.
    • (1996) Trends Biochem Sci , vol.21 , pp. 482-487
    • Prusiner, S.B.1
  • 2
    • 0032506187 scopus 로고    scopus 로고
    • Prions
    • PMID:9811807
    • Prusiner SB. Prions. Proc Natl Acad Sci USA 1998; 95:13363-83; PMID:9811807; http://dx.doi.org/10.1073/pnas.95.23.13363.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13363-13383
    • Prusiner, S.B.1
  • 3
    • 78649417132 scopus 로고    scopus 로고
    • The prion hypothesis: From biological anomaly to basic regulatory mechanism
    • PMID:21081963
    • Tuite MF, Serio TR. The prion hypothesis: from biological anomaly to basic regulatory mechanism. Nat Rev Mol Cell Biol 2010; 11:823-33; PMID:21081963; http://dx.doi.org/10.1038/nrm3007.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 823-833
    • Tuite, M.F.1    Serio, T.R.2
  • 4
    • 77649202326 scopus 로고    scopus 로고
    • Protein aggregation diseases: Pathogenicity and therapeutic perspectives
    • PMID:20190788
    • Aguzzi A, O'Connor T. Protein aggregation diseases: pathogenicity and therapeutic perspectives. Nat Rev Drug Discov 2010; 9:237-48; PMID:20190788; http://dx.doi.org/10.1038/nrd3050.
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 237-248
    • Aguzzi, A.1    O'Connor, T.2
  • 7
    • 0037855771 scopus 로고    scopus 로고
    • Cellular prion protein sensitizes neurons to apoptotic stimuli through Mdm2-regulated and p53-dependent caspase 3-like activation
    • PMID:12529324
    • Paitel E, Fahraeus R, Checler F. Cellular prion protein sensitizes neurons to apoptotic stimuli through Mdm2-regulated and p53-dependent caspase 3-like activation. J Biol Chem 2003; 278:10061-6; PMID:12529324; http://dx.doi.org/10.1074/jbc.M211580200.
    • (2003) J Biol Chem , vol.278 , pp. 10061-10066
    • Paitel, E.1    Fahraeus, R.2    Checler, F.3
  • 8
    • 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
    • PMID:14570892
    • Paitel E, Sunyach C, Alves da Costa C, Bourdon JC, Vincent B, Checler F. 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 2004; 279:612-8; PMID:14570892; http://dx.doi.org/10.1074/jbc.M310453200.
    • (2004) J Biol Chem , vol.279 , pp. 612-618
    • Paitel, E.1    Sunyach, C.2    Alves Da Costa, C.3    Bourdon, J.C.4    Vincent, B.5    Checler, F.6
  • 9
    • 15244355224 scopus 로고    scopus 로고
    • Combined pharmacological, mutational and cell biology approaches indicate that p53-dependent caspase 3 activation triggered by cellular prion is dependent on its endocytosis
    • PMID:15748158
    • Sunyach C, Checler F. Combined pharmacological, mutational and cell biology approaches indicate that p53-dependent caspase 3 activation triggered by cellular prion is dependent on its endocytosis. J Neurochem 2005; 92:1399-407; PMID:15748158; http://dx.doi.org/10.1111/j.1471-4159.2004.02989.x.
    • (2005) J Neurochem , vol.92 , pp. 1399-1407
    • Sunyach, C.1    Checler, F.2
  • 10
    • 72149127389 scopus 로고    scopus 로고
    • The alpha-secretase-derived N-terminal product of cellular prion, N1, displays neuroprotective function in vitro and in vivo
    • PMID:19850936
    • Guillot-Sestier MV, Sunyach C, Druon C, Scarzello S, Checler F. The alpha-secretase-derived N-terminal product of cellular prion, N1, displays neuroprotective function in vitro and in vivo. J Biol Chem 2009; 284:35973-86; PMID:19850936; http://dx.doi.org/10.1074/jbc.M109.051086.
    • (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
  • 11
    • 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
    • PMID:17121821
    • Sunyach C, Cisse MA, da Costa CA, Vincent B, Checler F. 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 2007; 282:1956-63; PMID:17121821; http://dx.doi.org/10.1074/jbc.M609663200.
    • (2007) J Biol Chem , vol.282 , pp. 1956-1963
    • Sunyach, C.1    Cisse, M.A.2    Da Costa, C.A.3    Vincent, B.4    Checler, F.5
  • 12
    • 0029027854 scopus 로고
    • Truncated forms of the human prion protein in normal brain and in prion disease
    • PMID:7642585
    • Chen SG, Teplow DB, Parchi P, Teller JK, Gambetti P, Autilio-Gambetti L. Truncated forms of the human prion protein in normal brain and in prion disease. J Biol Chem 1995; 270:19173-80; PMID:7642585; http://dx.doi.org/10.1074/jbc. 270.32.19173.
    • (1995) J Biol Chem , vol.270 , pp. 19173-19180
    • Chen, S.G.1    Teplow, D.B.2    Parchi, P.3    Teller, J.K.4    Gambetti, P.5    Autilio-Gambetti, L.6
  • 13
    • 0030667339 scopus 로고    scopus 로고
    • α-secretase-derived product of β-amyloid precursor protein is decreased by presenilin 1 mutations linked to familial Alzheimer's disease
    • PMID:9375682
    • Ancolio K, Marambaud P, Dauch P, Checler F. α-secretase-derived product of β-amyloid precursor protein is decreased by presenilin 1 mutations linked to familial Alzheimer's disease. J Neurochem 1997; 69:2494-9; PMID:9375682; http://dx.doi.org/10.1046/j.1471-4159.1997.69062494.x.
    • (1997) J Neurochem , vol.69 , pp. 2494-2499
    • Ancolio, K.1    Marambaud, P.2    Dauch, P.3    Checler, F.4
  • 14
    • 0035089318 scopus 로고    scopus 로고
    • Constitutive alpha-secretase cleavage of the beta-amyloid precursor protein in the furin-deficient LoVo cell line: Involvement of the pro-hormone convertase 7 and the disintegrin metalloprotease ADAM10
    • PMID:11238737
    • Lopez-Perez E, Zhang Y, Frank SJ, Creemers J, Seidah N, Checler F. Constitutive alpha-secretase cleavage of the beta-amyloid precursor protein in the furin-deficient LoVo cell line: involvement of the pro-hormone convertase 7 and the disintegrin metalloprotease ADAM10. J Neurochem 2001; 76:1532-9; PMID:11238737; http://dx.doi.org/10.1046/j.1471-4159.2001.00180.x.
    • (2001) J Neurochem , vol.76 , pp. 1532-1539
    • Lopez-Perez, E.1    Zhang, Y.2    Frank, S.J.3    Creemers, J.4    Seidah, N.5    Checler, F.6
  • 15
    • 0030667097 scopus 로고    scopus 로고
    • Constitutive and protein kinase C-regulated secretory cleavage of Alzheimer's β amyloid precursor protein: Different control of early and late events by the proteasome
    • PMID:9375683
    • Marambaud P, Lopez-Perez E, Wilk S, Checler F. Constitutive and protein kinase C-regulated secretory cleavage of Alzheimer's β amyloid precursor protein: different control of early and late events by the proteasome. J Neurochem 1997; 69:2500-5; PMID:9375683; http://dx.doi.org/10.1046/j.1471-4159. 1997.69062500.x.
    • (1997) J Neurochem , vol.69 , pp. 2500-2505
    • Marambaud, P.1    Lopez-Perez, E.2    Wilk, S.3    Checler, F.4
  • 16
    • 0033616716 scopus 로고    scopus 로고
    • Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease
    • PMID:10097139
    • Lammich S, Kojro E, Postina R, Gilbert S, Pfeiffer R, Jasionowski M, et al. Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. Proc Natl Acad Sci USA 1999; 96:3922-7; PMID:10097139; http://dx.doi.org/10.1073/pnas.96.7.3922.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3922-3927
    • Lammich, S.1    Kojro, E.2    Postina, R.3    Gilbert, S.4    Pfeiffer, R.5    Jasionowski, M.6
  • 17
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor α converting enzyme is involved in regulated α-secretase cleavage of the Alzheimer amyloid protein precursor
    • PMID:9774383
    • Buxbaum JD, Liu KN, Luo Y, Slack JL, Stocking KL, Peschon JJ, et al. Evidence that tumor necrosis factor α converting enzyme is involved in regulated α-secretase cleavage of the Alzheimer amyloid protein precursor. J Biol Chem 1998; 273:27765-7; PMID:9774383; http://dx.doi.org/10.1074/jbc.273. 43.27765.
    • (1998) J Biol Chem , vol.273 , pp. 27765-27767
    • Buxbaum, J.D.1    Liu, K.N.2    Luo, Y.3    Slack, J.L.4    Stocking, K.L.5    Peschon, J.J.6
  • 18
    • 84874934734 scopus 로고    scopus 로고
    • α-secretase in Alzheimer's disease and beyond: Mechanistic, regulation and function
    • In press; PMID:21605031
    • Vincent B, Checler F. α-secretase in Alzheimer's disease and beyond: mechanistic, regulation and function. Curr Alzheimer Res 2011; In press; PMID:21605031.
    • (2011) Curr Alzheimer Res
    • Vincent, B.1    Checler, F.2
  • 19
    • 0034634655 scopus 로고    scopus 로고
    • Phorbol ester-regulated cleavage of normal prion protein in HEK293 human cells and murine neurons
    • PMID:10952979
    • Vincent B, Paitel E, Frobert Y, Lehmann S, Grassi J, Checler F. Phorbol ester-regulated cleavage of normal prion protein in HEK293 human cells and murine neurons. J Biol Chem 2000; 275:35612-6; PMID:10952979; http://dx.doi.org/10.1074/jbc.M004628200.
    • (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
  • 20
    • 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
    • PMID:11477090
    • Vincent B, Paitel E, Saftig P, Frobert Y, Hartmann D, De Strooper B, et al. The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. J Biol Chem 2001; 276:37743-6; PMID:11477090.
    • (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
  • 21
    • 80051685988 scopus 로고    scopus 로고
    • The extracellular regulated kinase-1 (ERK1) controls regulated {alpha}-secretase-mediated processing, promoter transactivation and mRNA levels of the cellular prion protein
    • PMID:21586567
    • Cissé M, Duplan E, Guillot-Sestier MV, Rumigny J, Bauer C, Pages G, et al. The extracellular regulated kinase-1 (ERK1) controls regulated {alpha}-secretase-mediated processing, promoter transactivation and mRNA levels of the cellular prion protein. J Biol Chem 2011; 286:29192-206; PMID:21586567; http://dx.doi.org/10.1074/jbc.M110.208249.
    • (2011) J Biol Chem , vol.286 , pp. 29192-29206
    • Cissé, M.1    Duplan, E.2    Guillot-Sestier, M.V.3    Rumigny, J.4    Bauer, C.5    Pages, G.6
  • 22
    • 54049141728 scopus 로고    scopus 로고
    • Mitogen-activated protein (MAP) kinase/MAP kinase phosphatase regulation: Roles in cell growth, death and cancer
    • PMID:18922965
    • Boutros T, Chevet E, Metrakos P. Mitogen-activated protein (MAP) kinase/MAP kinase phosphatase regulation: roles in cell growth, death and cancer. Pharmacol Rev 2008; 60:261-310; PMID:18922965; http://dx.doi.org/10. 1124/pr.107.00106.
    • (2008) Pharmacol Rev , vol.60 , pp. 261-310
    • Boutros, T.1    Chevet, E.2    Metrakos, P.3
  • 23
    • 0036890486 scopus 로고    scopus 로고
    • Alzheimer's and prion diseases: Distinct pathologies, common proteolytic denominators
    • PMID:12446128
    • Checler F, Vincent B. Alzheimer's and prion diseases: distinct pathologies, common proteolytic denominators. Trends Neurosci 2002; 25:616-20; PMID:12446128; http://dx.doi.org/10.1016/S0166-2236(02)02263-4.
    • (2002) Trends Neurosci , vol.25 , pp. 616-620
    • Checler, F.1    Vincent, B.2
  • 24
    • 53849113627 scopus 로고    scopus 로고
    • Isoform-specific contribution of protein kinase C to prion processing
    • PMID:18722532
    • Alfa Cissé M, Louis K, Braun U, Mari B, Leitges M, Slack BE, et al. Isoform-specific contribution of protein kinase C to prion processing. Mol Cell Neurosci 2008; 39:400-10; PMID:18722532; http://dx.doi.org/10.1016/j.mcn. 2008.07.013.
    • (2008) Mol Cell Neurosci , vol.39 , pp. 400-410
    • Alfa Cissé, M.1    Louis, K.2    Braun, U.3    Mari, B.4    Leitges, M.5    Slack, B.E.6
  • 25
    • 79957646992 scopus 로고    scopus 로고
    • ERK1-independent alpha-secretase cut of beta-amyloid precursor protein via M1 muscarinic receptors and PKCalpha/epsilon
    • PMID:21570469
    • Cisse M, Braun U, Leitges M, Fisher A, Pages G, Checler F, et al. ERK1-independent alpha-secretase cut of beta-amyloid precursor protein via M1 muscarinic receptors and PKCalpha/epsilon. Mol Cell Neurosci 2011; 47:223-32; PMID:21570469; http://dx.doi.org/10.1016/j.mcn.2011.04.008.
    • (2011) Mol Cell Neurosci , vol.47 , pp. 223-232
    • Cisse, M.1    Braun, U.2    Leitges, M.3    Fisher, A.4    Pages, G.5    Checler, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.