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Volumn 6, Issue 3, 2016, Pages 503-517

Nilotinib effects in Parkinson's disease and dementia with lewy bodies

Author keywords

dopamine; homovanillic acid; Lewy bodies; Nilotinib; Parkinson; synuclein; tau

Indexed keywords

ABELSON KINASE; ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; BIOLOGICAL MARKER; DJ 1 PROTEIN; DOPAMINE; HOMOVANILLIC ACID; NILOTINIB; RASAGILINE; SELEGILINE; TAU PROTEIN; 4-METHYL-N-(3-(4-METHYLIMIDAZOL-1-YL)-5-(TRIFLUOROMETHYL)PHENYL)-3-((4-PYRIDIN-3-YLPYRIMIDIN-2-YL)AMINO)BENZAMIDE; PYRIMIDINE DERIVATIVE;

EID: 84983738240     PISSN: 18777171     EISSN: 1877718X     Source Type: Journal    
DOI: 10.3233/JPD-160867     Document Type: Article
Times cited : (218)

References (48)
  • 1
    • 49049096562 scopus 로고    scopus 로고
    • Autophagy induction and autophagosome clearance in neurons: Relationship to autophagic pathology in Alzheimer's disease
    • Boland B, Kumar A, Lee S, Platt FM, Wegiel J, Yu WH, & NixonRA(2008) Autophagy induction and autophagosome clearance in neurons: Relationship to autophagic pathology in Alzheimer's disease. J Neurosci, 28, 6926-6937.
    • (2008) J Neurosci , vol.28 , pp. 6926-6937
    • Boland, B.1    Kumar, A.2    Lee, S.3    Platt, F.M.4    Wegiel, J.5    Yu, W.H.6    Nixon, R.A.7
  • 2
    • 0034307476 scopus 로고    scopus 로고
    • Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy
    • Kegel KB, Kim M, Sapp E, McIntyre C, Castano JG, Aronin N, &DiFigliaM(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
  • 4
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar B, Duden R, & Rubinsztein DC (2002) Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum Mol Genet, 11, 1107-1117.
    • (2002) Hum Mol Genet , vol.11 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 5
    • 33747819801 scopus 로고    scopus 로고
    • Mtor and cancer: Insights into a complex relationship
    • SabatiniDM(2006) mTOR and cancer: Insights into a complex relationship. Nat Rev Cancer, 6, 729-734.
    • (2006) Nat Rev Cancer , vol.6 , pp. 729-734
    • Sabatini, D.M.1
  • 6
    • 0035894855 scopus 로고    scopus 로고
    • Expression of a53t mutant but not wild-type alphasynuclein in pc12 cells induces alterations of the ubiquitindependent degradation system, loss of dopamine release, and autophagic cell death
    • Stefanis L, Larsen KE, Rideout HJ, Sulzer D, & Greene LA (2001) Expression of A53T mutant but not wild-type alphasynuclein in PC12 cells induces alterations of the ubiquitindependent degradation system, loss of dopamine release, and autophagic cell death. J Neurosci, 21, 9549-9560.
    • (2001) J Neurosci , vol.21 , pp. 9549-9560
    • Stefanis, L.1    Larsen, K.E.2    Rideout, H.J.3    Sulzer, D.4    Greene, L.A.5
  • 8
    • 84882254367 scopus 로고    scopus 로고
    • The role of autophagy in neurodegenerative disease
    • Nixon RA (2013) The role of autophagy in neurodegenerative disease. Nat Med, 19, 983-997.
    • (2013) Nat Med , vol.19 , pp. 983-997
    • Nixon, R.A.1
  • 9
    • 57749173855 scopus 로고    scopus 로고
    • Nilotinib: A second-generation tyrosine kinase inhibitor for the treatment of chronic myelogenous leukemia
    • Deremer DL, Ustun C, & Natarajan K (2008) Nilotinib: A second-generation tyrosine kinase inhibitor for the treatment of chronic myelogenous leukemia. Clin Ther, 30, 1956-1975.
    • (2008) Clin Ther , vol.30 , pp. 1956-1975
    • Deremer, D.L.1    Ustun, C.2    Natarajan, K.3
  • 10
    • 82255186664 scopus 로고    scopus 로고
    • Bcr-Abl1 kinase: Hunting an elusive target with new weapons
    • Skorski T (2011) BCR-ABL1 kinase: Hunting an elusive target with new weapons. Chem Biol, 18, 1352-1353.
    • (2011) Chem Biol , vol.18 , pp. 1352-1353
    • Skorski, T.1
  • 12
    • 70349638918 scopus 로고    scopus 로고
    • Targeted therapies and autophagy: New insights from chronic myeloid leukemia
    • Salomoni P, & Calabretta B (2009) Targeted therapies and autophagy: New insights from chronic myeloid leukemia. Autophagy, 5, 1050-1051.
    • (2009) Autophagy , vol.5 , pp. 1050-1051
    • Salomoni, P.1    Calabretta, B.2
  • 13
    • 84881250979 scopus 로고    scopus 로고
    • Nilotinib reverses loss of dopamine neurons and improves motor behavior via autophagic degradation of alpha-synuclein in Parkinson's disease models
    • Hebron ML, Lonskaya I, & Moussa CE (2013) Nilotinib reverses loss of dopamine neurons and improves motor behavior via autophagic degradation of alpha-synuclein in Parkinson's disease models. Hum Mol Genet, 22, 3315-3328.
    • (2013) Hum Mol Genet , vol.22 , pp. 3315-3328
    • Hebron, M.L.1    Lonskaya, I.2    Moussa, C.E.3
  • 14
    • 84881490638 scopus 로고    scopus 로고
    • Tyrosine kinase inhibition increases functional parkin-beclin-1 interaction and enhances amyloid clearance and cognitive performance
    • Lonskaya I, Hebron ML, Desforges NM, Franjie A, & Moussa CE (2013) Tyrosine kinase inhibition increases functional parkin-Beclin-1 interaction and enhances amyloid clearance and cognitive performance. EMBO Mol Med, 5, 1247-1262.
    • (2013) EMBO Mol Med , vol.5 , pp. 1247-1262
    • Lonskaya, I.1    Hebron, M.L.2    Desforges, N.M.3    Franjie, A.4    Moussa, C.E.5
  • 15
    • 84873615689 scopus 로고    scopus 로고
    • Parkin ubiquitinates tar-DNA binding protein-43 (tdp-43) and promotes its cytosolic accumulation via interaction with histone deacetylase 6 (hdac6
    • Hebron ML, Lonskaya I, Sharpe K, Weerasinghe PP, Algarzae NK, Shekoyan AR, & Moussa CE (2013) Parkin ubiquitinates Tar-DNA binding protein-43 (TDP-43) and promotes its cytosolic accumulation via interaction with histone deacetylase 6 (HDAC6). J Biol Chem, 288, 4103-4115.
    • (2013) J Biol Chem , vol.288 , pp. 4103-4115
    • Hebron, M.L.1    Lonskaya, I.2    Sharpe, K.3    Weerasinghe, P.P.4    Algarzae, N.K.5    Shekoyan, A.R.6    Moussa, C.E.7
  • 16
    • 84983734366 scopus 로고    scopus 로고
    • Tyrosine kinase inhibition regulates early systemic immune changes and modulates the neuroimmune response in alpha-synucleinopathy
    • Hebron ML, Lonskaya I, Olopade P, Selby ST, Pagan F, & Moussa CE (2014) Tyrosine Kinase Inhibition Regulates Early Systemic Immune Changes and Modulates the Neuroimmune Response in alpha-Synucleinopathy. J Clin Cell Immunol, 5, 259.
    • (2014) J Clin Cell Immunol , vol.5 , pp. 259
    • Hebron, M.L.1    Lonskaya, I.2    Olopade, P.3    Selby, S.T.4    Pagan, F.5    Moussa, C.E.6
  • 17
    • 84898487614 scopus 로고    scopus 로고
    • Nilotinib-induced autophagic changes increase endogenous parkin level and ubiquitination, leading to amyloid clearance
    • Lonskaya I, Hebron M, Desforges NM, Schachter JB, & Moussa CE (2014) Nilotinib-induced autophagic changes increase endogenous parkin level and ubiquitination, leading to amyloid clearance. J Mol Med, 92, 373-386.
    • (2014) J Mol Med , vol.92 , pp. 373-386
    • Lonskaya, I.1    Hebron, M.2    Desforges, N.M.3    Schachter, J.B.4    Moussa, C.E.5
  • 18
    • 84891300736 scopus 로고    scopus 로고
    • Ubiquitination increases parkin activity to promote autophagic alpha-synuclein clearance
    • Lonskaya I, Desforges NM, Hebron ML, & Moussa CE (2013) Ubiquitination increases parkin activity to promote autophagic alpha-synuclein clearance. PLoS One, 8, e83914.
    • (2013) PLoS One , vol.8 , pp. e83914
    • Lonskaya, I.1    Desforges, N.M.2    Hebron, M.L.3    Moussa, C.E.4
  • 19
    • 84898487614 scopus 로고    scopus 로고
    • Nilotinib-induced autophagic changes increase endogenous parkin level and ubiquitination, leading to amyloid clearance
    • Lonskaya I, Hebron ML, Desforges NM, Schachter JB, & Moussa CE (2014) Nilotinib-induced autophagic changes increase endogenous parkin level and ubiquitination, leading to amyloid clearance. J Mol Med (Berl), 92, 373-386.
    • (2014) J Mol Med (Berl , vol.92 , pp. 373-386
    • Lonskaya, I.1    Hebron, M.L.2    Desforges, N.M.3    Schachter, J.B.4    Moussa, C.E.5
  • 20
    • 84964312590 scopus 로고    scopus 로고
    • Tau deletion impairs intracellular beta-Amyloid-42 clearance and leads to more extracellular plaque deposition in gene transfer models
    • Lonskaya I, Hebron M, Chen W, Schachter J, & Moussa C (2014) Tau deletion impairs intracellular beta-Amyloid-42 clearance and leads to more extracellular plaque deposition in gene transfer models. Mol Neurodegener, 9, 46.
    • (2014) Mol Neurodegener , vol.9 , pp. 46
    • Lonskaya, I.1    Hebron, M.2    Chen, W.3    Schachter, J.4    Moussa, C.5
  • 21
    • 84899892500 scopus 로고    scopus 로고
    • The c-Abl inhibitor, nilotinib, protects dopaminergic neurons in a preclinical animal model of Parkinson's disease
    • Karuppagounder SS, Brahmachari S, Lee Y, Dawson VL, Dawson TM, &Ko HS (2014) The c-Abl inhibitor, nilotinib, protects dopaminergic neurons in a preclinical animal model of Parkinson's disease. Sci Rep, 4, 4874.
    • (2014) Sci Rep , vol.4 , pp. 4874
    • Karuppagounder, S.S.1    Brahmachari, S.2    Lee, Y.3    Dawson, V.L.4    Dawson, T.M.5    Ko, H.S.6
  • 25
    • 44649188448 scopus 로고    scopus 로고
    • Oxidative insults induce dj-1 upregulation and redistribution: Implications for neuroprotection
    • Lev N, Ickowicz D, Melamed E, & Offen D (2008) Oxidative insults induce DJ-1 upregulation and redistribution: Implications for neuroprotection. Neurotoxicology, 29, 397-405.
    • (2008) Neurotoxicology , vol.29 , pp. 397-405
    • Lev, N.1    Ickowicz, D.2    Melamed, E.3    Offen, D.4
  • 27
    • 84895832137 scopus 로고    scopus 로고
    • The capable abl: What is its biological function?
    • Wang JY (2014) The capable ABL: What is its biological function? Mol Cell Biol, 34, 1188-1197.
    • (2014) Mol Cell Biol , vol.34 , pp. 1188-1197
    • Wang, J.Y.1
  • 28
    • 73949087519 scopus 로고    scopus 로고
    • Neuronal and glial cerebrospinal fluid protein biomarkers are elevated after west nile virus infection
    • Petzold A, Groves M, Leis AA, Scaravilli F, & Stokic DS (2010) Neuronal and glial cerebrospinal fluid protein biomarkers are elevated after West Nile virus infection. Muscle Nerve, 41, 42-49.
    • (2010) Muscle Nerve , vol.41 , pp. 42-49
    • Petzold, A.1    Groves, M.2    Leis, A.A.3    Scaravilli, F.4    Stokic, D.S.5
  • 29
    • 45449091744 scopus 로고    scopus 로고
    • Glial and axonal body fluid biomarkers are related to infarct volume, severity, and outcome
    • Petzold A, Michel P, Stock M, &SchluepM(2008) Glial and axonal body fluid biomarkers are related to infarct volume, severity, and outcome. J Stroke Cerebrovasc Dis, 17, 196-203.
    • (2008) J Stroke Cerebrovasc Dis , vol.17 , pp. 196-203
    • Petzold, A.1    Michel, P.2    Stock, M.3    Schluep, M.4
  • 30
    • 33748988163 scopus 로고    scopus 로고
    • Association of serial biochemical markers with acute ischemic stroke: The national institute of neurological disorders and stroke recombinant tissue plasminogen activator stroke study
    • Jauch EC, Lindsell C, Broderick J, Fagan SC, Tilley BC, Levine SR, & Group Nr-PSS (2006) Association of serial biochemical markers with acute ischemic stroke: The National Institute of Neurological Disorders and Stroke recombinant tissue plasminogen activator Stroke Study. Stroke, 37, 2508-2513.
    • (2006) Stroke , vol.37 , pp. 2508-2513
    • Jauch, E.C.1    Lindsell, C.2    Broderick, J.3    Fagan, S.C.4    Tilley, B.C.5    Levine, S.R.6
  • 31
    • 0023195783 scopus 로고
    • S-100 protein and neuron-specific enolase in cerebrospinal fluid and serum: Markers of cell damage in human central nervous system
    • Persson L, Hardemark HG, Gustafsson J, Rundstrom G, Mendel-Hartvig I, Esscher T, & Pahlman S (1987) S-100 protein and neuron-specific enolase in cerebrospinal fluid and serum: Markers of cell damage in human central nervous system. Stroke, 18, 911-918.
    • (1987) Stroke , vol.18 , pp. 911-918
    • Persson, L.1    Hardemark, H.G.2    Gustafsson, J.3    Rundstrom, G.4    Mendel-Hartvig, I.5    Esscher, T.6    Pahlman, S.7
  • 34
    • 84865756966 scopus 로고    scopus 로고
    • Alpha-synuclein in the cerebrospinal fluid differentiates synucleinopathies (Parkinson disease, dementia with lewy bodies, multiple system atrophy) from Alzheimer disease
    • Tateno F, Sakakibara R, Kawai T, Kishi M, & Murano T (2012) Alpha-synuclein in the cerebrospinal fluid differentiates synucleinopathies (Parkinson Disease, dementia with Lewy bodies, multiple system atrophy) from Alzheimer disease. Alzheimer Dis Assoc Disord, 26, 213-216.
    • (2012) Alzheimer Dis Assoc Disord , vol.26 , pp. 213-216
    • Tateno, F.1    Sakakibara, R.2    Kawai, T.3    Kishi, M.4    Murano, T.5
  • 36
    • 0022972558 scopus 로고
    • Cerebrospinal fluid levels of angiotensin-converting enzyme, acetylcholinesterase, and dopamine metabolites in dementia associated with Alzheimer's disease and Parkinson's disease: A correlative study
    • Zubenko GS, Marquis JK, Volicer L, Direnfeld LK, Langlais PJ, & Nixon RA (1986) Cerebrospinal fluid levels of angiotensin-converting enzyme, acetylcholinesterase, and dopamine metabolites in dementia associated with Alzheimer's disease and Parkinson's disease: A correlative study. Biol Psychiatry, 21, 1365-1381.
    • (1986) Biol Psychiatry , vol.21 , pp. 1365-1381
    • Zubenko, G.S.1    Marquis, J.K.2    Volicer, L.3    Direnfeld, L.K.4    Langlais, P.J.5    Nixon, R.A.6
  • 37
    • 84861547965 scopus 로고    scopus 로고
    • Cerebrospinal fluid biomarkers of central catecholamine deficiency in Parkinson's disease and other synucleinopathies
    • Goldstein DS, Holmes C, &SharabiY(2012) Cerebrospinal fluid biomarkers of central catecholamine deficiency in Parkinson's disease and other synucleinopathies. Brain, 135, 1900-1913.
    • (2012) Brain , vol.135 , pp. 1900-1913
    • Goldstein, D.S.1    Holmes, C.2    Sharabi, Y.3
  • 38
    • 79952035031 scopus 로고    scopus 로고
    • Parkin degrades estrogen-related receptors to limit the expression of monoamine oxidases
    • Ren Y, Jiang H, Ma D, Nakaso K, & Feng J (2011) Parkin degrades estrogen-related receptors to limit the expression of monoamine oxidases. Hum Mol Genet, 20, 1074-1083.
    • (2011) Hum Mol Genet , vol.20 , pp. 1074-1083
    • Ren, Y.1    Jiang, H.2    Ma, D.3    Nakaso, K.4    Feng, J.5
  • 44
  • 46
    • 32544446902 scopus 로고    scopus 로고
    • Total tau protein, phosphorylated tau (181p) protein, betaamyloid( 1-42), and beta-Amyloid 1-40) in cerebrospinal fluid of patients with dementia with lewybodies
    • Mollenhauer B, Bibl M, Wiltfang J, Steinacker P, Ciesielczyk B, Neubert K, Trenkwalder C, & Otto M (2006) Total tau protein, phosphorylated tau (181p) protein, betaamyloid( 1-42), and beta-Amyloid(1-40) in cerebrospinal fluid of patients with dementia with Lewybodies. Clin Chem Lab Med, 44, 192-195.
    • (2006) Clin Chem Lab Med , vol.44 , pp. 192-195
    • Mollenhauer, B.1    Bibl, M.2    Wiltfang, J.3    Steinacker, P.4    Ciesielczyk, B.5    Neubert, K.6    Trenkwalder, C.7    Otto, M.8


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