메뉴 건너뛰기




Volumn 15, Issue 5-6, 2014, Pages 351-356

Limited role of free TDP-43 as a diagnostic tool in neurodegenerative diseases

Author keywords

Amyotrophic lateral sclerosis; Biomarker; Cerebrospinal fluid; Exosomes; Frontotemporal lobar degeneration; TDP 43

Indexed keywords

TAR DNA BINDING PROTEIN; UREA; DNA BINDING PROTEIN; FLOTILLINS; MEMBRANE PROTEIN; PROTEIN TDP-43;

EID: 84906330760     PISSN: 21678421     EISSN: 21679223     Source Type: Journal    
DOI: 10.3109/21678421.2014.905606     Document Type: Article
Times cited : (116)

References (36)
  • 1
    • 38449102667 scopus 로고    scopus 로고
    • Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease
    • Buratti E, Baralle FE. Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease. Front Biosci. 2008; 13: 867-78
    • (2008) Front Biosci , vol.13 , pp. 867-878
    • Buratti, E.1    Baralle, F.E.2
  • 2
    • 80755153025 scopus 로고    scopus 로고
    • TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies
    • Cohen T J, Lee VM, Trojanowski JQ. TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies. Trends Mol Med. 2011; 17: 659-67
    • (2011) Trends Mol Med , vol.17 , pp. 659-667
    • Cohen, T.J.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 3
    • 80052968310 scopus 로고    scopus 로고
    • Tdp-43 and fus/tls: Cellular functions and implications for neurodegeneration
    • Fiesel F C, Kahle P J. TDP-43 and FUS/TLS: Cellular functions and implications for neurodegeneration. FEBS J. 2011; 278: 3550-68
    • (2011) FEBS J. , vol.278 , pp. 3550-3568
    • Fiesel, F.C.1    Kahle, P.J.2
  • 4
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M, Sampathu DM, Kwong LK, Truax AC, Micsenyi MC, Chou TT, et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science. 2006; 314: 130-3
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3    Truax, A.C.4    Micsenyi, M.C.5    Chou, T.T.6
  • 5
    • 33750716074 scopus 로고    scopus 로고
    • TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Arai T, Hasegawa M, Akiyama H, Ikeda K, Nonaka T, Mori H, et al. TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem Biophys Res Commun. 2006; 351: 602-11
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 602-611
    • Arai, T.1    Hasegawa, M.2    Akiyama, H.3    Ikeda, K.4    Nonaka, T.5    Mori, H.6
  • 6
    • 77949908515 scopus 로고    scopus 로고
    • Phosphorylated and cleaved TDP-43 in ALS, FTLD and other neurodegenerative disorders and in cellular models of TDP-43 proteinopathy
    • Arai T, Hasegawa M, Nonoka T, Kametani F, Yamashita M, Hosokawa M, et al. Phosphorylated and cleaved TDP-43 in ALS, FTLD and other neurodegenerative disorders and in cellular models of TDP-43 proteinopathy. Neuropathology. 2010; 30: 170-81
    • (2010) Neuropathology , vol.30 , pp. 170-181
    • Arai, T.1    Hasegawa, M.2    Nonoka, T.3    Kametani, F.4    Yamashita, M.5    Hosokawa, M.6
  • 7
    • 55949089475 scopus 로고    scopus 로고
    • TDP-43 in cerebrospinal fluid of patients with frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Steinacker P, Hendrich C, Sperfeld A D, Jesse S, von Arnim CA, Lehnert S, et al. TDP-43 in cerebrospinal fluid of patients with frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Arch Neurol. 2008; 65: 1481-7
    • (2008) Arch Neurol , vol.65 , pp. 1481-1487
    • Steinacker, P.1    Hendrich, C.2    Sperfeld, A.D.3    Jesse, S.4    Von Arnim, C.A.5    Lehnert, S.6
  • 8
    • 47949108734 scopus 로고    scopus 로고
    • TDP-43 protein in plasma may index TDP-43 brain pathology in Alzheimer's disease and frontotemporal lobar degeneration
    • Foulds P, McAuley E, Gibbons L, Davidson Y, Pickering-Brown SM, Neary D, et al. TDP-43 protein in plasma may index TDP-43 brain pathology in Alzheimer's disease and frontotemporal lobar degeneration. Acta Neuropathol. 2008; 116: 141-6
    • (2008) Acta Neuropathol , vol.116 , pp. 141-146
    • Foulds, P.1    McAuley, E.2    Gibbons, L.3    Davidson, Y.4    Pickering-Brown, S.M.5    Neary, D.6
  • 9
    • 70449526407 scopus 로고    scopus 로고
    • Plasma phosphorylated-TDP-43 protein levels correlate with brain pathology in frontotemporal lobar degeneration
    • Foulds PG, Davidson Y, Mishra M, Hobson DJ, Humphreys KM, Taylor M, et al. Plasma phosphorylated-TDP-43 protein levels correlate with brain pathology in frontotemporal lobar degeneration. Acta Neuropathol. 2009; 118: 647-58
    • (2009) Acta Neuropathol , vol.118 , pp. 647-658
    • Foulds, P.G.1    Davidson, Y.2    Mishra, M.3    Hobson, D.J.4    Humphreys, K.M.5    Taylor, M.6
  • 10
    • 57049149602 scopus 로고    scopus 로고
    • Increased TDP-43 protein in cerebrospinal fluid of patients with amyotrophic lateral sclerosis
    • Kasai T, Tokuda T, Ishigami N, Sasayama H, Foulds P, Mitchell DJ, et al. Increased TDP-43 protein in cerebrospinal fluid of patients with amyotrophic lateral sclerosis. Acta Neuropathol. 2009; 117: 55-62
    • (2009) Acta Neuropathol , vol.117 , pp. 55-62
    • Kasai, T.1    Tokuda, T.2    Ishigami, N.3    Sasayama, H.4    Foulds, P.5    Mitchell, D.J.6
  • 12
    • 0016394425 scopus 로고
    • Protein size and cerebrospinal fluid composition
    • Felgenhauer K. Protein size and cerebrospinal fluid composition. Klin Wochenschr. 1974; 52: 1158-64
    • (1974) Klin Wochenschr , vol.52 , pp. 1158-1164
    • Felgenhauer, K.1
  • 13
    • 0028269876 scopus 로고
    • Flow rate of cerebrospinal fluid (CSF): A concept common to normal blood-CSF barrier function and to dysfunction in neurological diseases
    • Reiber H. Flow rate of cerebrospinal fluid (CSF): A concept common to normal blood-CSF barrier function and to dysfunction in neurological diseases. JNeurol Sci. 1994; 122: 189-203
    • (1994) J Neurol Sci , vol.122 , pp. 189-203
    • Reiber, H.1
  • 14
    • 84858156745 scopus 로고    scopus 로고
    • Itraq and multiple reaction monitoring as proteomic tools for biomarker search in cerebrospinal fluid of patients with parkinson's disease dementia
    • Lehnert S, Jesse S, Rist W, Steinacker P, Soininen H, Herukka SK, et al. iTRAQ and multiple reaction monitoring as proteomic tools for biomarker search in cerebrospinal fluid of patients with Parkinson's disease dementia. Exp Neurol. 2012; 234: 499-505
    • (2012) Exp Neurol , vol.234 , pp. 499-505
    • Lehnert, S.1    Jesse, S.2    Rist, W.3    Steinacker, P.4    Soininen, H.5    Herukka, S.K.6
  • 15
    • 33750032901 scopus 로고    scopus 로고
    • Clinical characteristics of amyotrophic lateral sclerosis subsets
    • 62 Spec No 2 4S29-33
    • Pradat P F, Bruneteau G. Clinical characteristics of amyotrophic lateral sclerosis subsets. Rev Neurol (Paris). 2006; 162 Spec No 2: 4S29-33
    • (2006) Rev Neurol (Paris
    • Pradat, P.F.1    Bruneteau, G.2
  • 16
    • 0031672540 scopus 로고    scopus 로고
    • Frontotemporal lobar degeneration: A consensus on clinical diagnostic criteria
    • Neary D, Snowden JS, Gustafson L, Passant U, Stuss D, Black S, et al. Frontotemporal lobar degeneration: A consensus on clinical diagnostic criteria. Neurology. 1998; 51: 1546-54
    • (1998) Neurology , vol.51 , pp. 1546-1554
    • Neary, D.1    Snowden, J.S.2    Gustafson, L.3    Passant, U.4    Stuss, D.5    Black, S.6
  • 17
    • 77950665407 scopus 로고    scopus 로고
    • Frontotemporal lobar degeneration: Epidemiology, pathophysiology, diagnosis and management
    • Rabinovici GD, Miller BL. Frontotemporal lobar degeneration: Epidemiology, pathophysiology, diagnosis and management. CNS Drugs. 2010; 24: 375-98
    • (2010) CNS Drugs , vol.24 , pp. 375-398
    • Rabinovici, G.D.1    Miller, B.L.2
  • 18
    • 80052938441 scopus 로고    scopus 로고
    • Sensitivity of revised diagnostic criteria for the behavioural variant of frontotemporal dementia
    • Rascovsky K, Hodges JR, Knopman D, Mendez MF, Kramer JH, Neuhaus J, et al. Sensitivity of revised diagnostic criteria for the behavioural variant of frontotemporal dementia. Brain. 2011; 134: 2456-77
    • (2011) Brain , vol.134 , pp. 2456-2477
    • Rascovsky, K.1    Hodges, J.R.2    Knopman, D.3    Mendez, M.F.4    Kramer, J.H.5    Neuhaus, J.6
  • 20
    • 33947709328 scopus 로고    scopus 로고
    • Packaging of prions into exosomes is associated with a novel pathway of PrP processing
    • Vella LJ, Sharples RA, Lawson VA, Masters CL, Cappai R, Hill AF. Packaging of prions into exosomes is associated with a novel pathway of PrP processing. JPathol. 2007; 211: 582-90
    • (2007) J Pathol , vol.211 , pp. 582-590
    • Vella, L.J.1    Sharples, R.A.2    Lawson, V.A.3    Masters, C.L.4    Cappai, R.5    Hill, A.F.6
  • 21
    • 68849129712 scopus 로고    scopus 로고
    • Membrane vesicles as conveyors of immune responses
    • Thery C, Ostrowski M, Segura E. Membrane vesicles as conveyors of immune responses. Nat Rev Immunol. 2009; 9: 581-93
    • (2009) Nat Rev Immunol , vol.9 , pp. 581-593
    • Thery, C.1    Ostrowski, M.2    Segura, E.3
  • 22
    • 33751199883 scopus 로고    scopus 로고
    • Exosomes: From biogenesis and secretion to biological function
    • Keller S, Sanderson M P, Stoeck A, Altevogt P. Exosomes: From biogenesis and secretion to biological function. Immunol Lett. 2006; 107: 102-8
    • (2006) Immunol Lett , vol.107 , pp. 102-108
    • Keller, S.1    Sanderson, M.P.2    Stoeck, A.3    Altevogt, P.4
  • 23
    • 39749162770 scopus 로고    scopus 로고
    • The role of exosomes in the processing of proteins associated with neurodegenerative diseases
    • Vella LJ, Sharples RA, Nisbet RM, Cappai R, Hill AF. The role of exosomes in the processing of proteins associated with neurodegenerative diseases. Eur Biophys J. 2008; 37: 323-32
    • (2008) Eur Biophys J. , vol.37 , pp. 323-332
    • Vella, L.J.1    Sharples, R.A.2    Nisbet, R.M.3    Cappai, R.4    Hill, A.F.5
  • 24
    • 0033485648 scopus 로고    scopus 로고
    • Activated platelets release two types of membrane vesicles: Microvesicles by surface shedding and exosomes derived from exocytosis of multivesicular bodies and alpha-granules
    • Heijnen HF, Schiel A E, Fijnheer R, Geuze HJ, Sixma JJ. Activated platelets release two types of membrane vesicles: Microvesicles by surface shedding and exosomes derived from exocytosis of multivesicular bodies and alpha-granules. Blood. 1999; 94: 3791-9
    • (1999) Blood , vol.94 , pp. 3791-3799
    • Heijnen, H.F.1    Schiel, A.E.2    Fijnheer, R.3    Geuze, H.J.4    Sixma, J.J.5
  • 26
    • 55749111850 scopus 로고    scopus 로고
    • Cerebrospinal fluid-optimized two-dimensional difference gel electrophoresis (2-D DIGE) facilitates the differential diagnosis of Creutzfeldt-Jakob disease
    • Brechlin P, Jahn O, Steinacker P, Cepek L, Kratzin H, Lehnert S, et al. Cerebrospinal fluid-optimized two-dimensional difference gel electrophoresis (2-D DIGE) facilitates the differential diagnosis of Creutzfeldt-Jakob disease. Proteomics. 2008; 8: 4357-66
    • (2008) Proteomics , vol.8 , pp. 4357-4366
    • Brechlin, P.1    Jahn, O.2    Steinacker, P.3    Cepek, L.4    Kratzin, H.5    Lehnert, S.6
  • 27
    • 84858156745 scopus 로고    scopus 로고
    • Itraq and multiple reaction monitoring as proteomic tools for biomarker search in cerebrospinal fluid of patients with parkinson's disease dementia
    • Lehnert S, Jesse S, Rist W, Steinacker P, Soininen H, Herukka SK, et al. iTRAQ and multiple reaction monitoring as proteomic tools for biomarker search in cerebrospinal fluid of patients with Parkinson's disease dementia. Exp Neurol. 2012; 234: 499-505
    • (2012) Exp Neurol , vol.234 , pp. 499-505
    • Lehnert, S.1    Jesse, S.2    Rist, W.3    Steinacker, P.4    Soininen, H.5    Herukka, S.K.6
  • 28
    • 0030951595 scopus 로고    scopus 로고
    • Improved electrophoretic separation and immunoblotting of beta-Amyloid (A beta) peptides 1-40, 1-42, and 1-43
    • Wiltfang J, Smirnov A, Schnierstein B, Kelemen G, Matthies U, Klafki HW, et al. Improved electrophoretic separation and immunoblotting of beta-Amyloid (A beta) peptides 1-40, 1-42, and 1-43. Electrophoresis. 1997; 18: 527-32
    • (1997) Electrophoresis , vol.18 , pp. 527-532
    • Wiltfang, J.1    Smirnov, A.2    Schnierstein, B.3    Kelemen, G.4    Matthies, U.5    Klafki, H.W.6
  • 29
    • 0040089526 scopus 로고    scopus 로고
    • Molecular characterization of dendritic cell-derived exosomes Selective accumulation of the heat shock protein hsc73
    • Thery C, Regnault A, Garin J, Wolfers J, Zitvogel L, Ricciardi-Castagnoli P, et al. Molecular characterization of dendritic cell-derived exosomes. Selective accumulation of the heat shock protein hsc73. JCell Biol. 1999; 147: 599-610
    • (1999) JCell Biol , vol.147 , pp. 599-610
    • Thery, C.1    Regnault, A.2    Garin, J.3    Wolfers, J.4    Zitvogel, L.5    Ricciardi-Castagnoli, P.6
  • 31
    • 79958141527 scopus 로고    scopus 로고
    • Cytoplasmic accumulation of tdp-43 in circulating lymphomonocytes of als patients with and without tardbp mutations
    • de Marco G, Lupino E, Calvo A, Moglia C, Buccinna B, Grifoni S, et al. Cytoplasmic accumulation of TDP-43 in circulating lymphomonocytes of ALS patients with and without TARDBP mutations. Acta Neuropathol. 2011; 121: 611-22
    • (2011) Acta Neuropathol , vol.121 , pp. 611-622
    • De Marco, G.1    Lupino, E.2    Calvo, A.3    Moglia, C.4    Buccinna, B.5    Grifoni, S.6
  • 32
    • 82755161867 scopus 로고    scopus 로고
    • Alteration in cell cycle-related proteins in lymphoblasts from carriers of the c.709-1G-A PGRN mutation associated with FTLD-TDP dementia
    • e7-20
    • Alquezar C, Esteras N, Bartolome F, Merino JJ, Alzualde A, Munain AL, et al. Alteration in cell cycle-related proteins in lymphoblasts from carriers of the c.709-1G-A PGRN mutation associated with FTLD-TDP dementia. Neurobiol Aging. 2012; 33: 429.e7-20
    • (2012) Neurobiol Aging , vol.33 , pp. 429
    • Alquezar, C.1    Esteras, N.2    Bartolome, F.3    Merino, J.J.4    Alzualde, A.5    Munain, A.L.6
  • 33
    • 84875234646 scopus 로고    scopus 로고
    • Exosomes: Vesicular carriers for intercellular communication in neurodegenerative disorders
    • Schneider A, Simons M. Exosomes: Vesicular carriers for intercellular communication in neurodegenerative disorders. Cell Tissue Res. 2013; 352: 33-47
    • (2013) Cell Tissue Res , vol.352 , pp. 33-47
    • Schneider, A.1    Simons, M.2
  • 34
    • 84866426167 scopus 로고    scopus 로고
    • Exosomes: Vehicles for the transfer of toxic proteins associated with neurodegenerative diseases
    • Bellingham SA, Guo BB, Coleman BM, Hill A F. Exosomes: Vehicles for the transfer of toxic proteins associated with neurodegenerative diseases? Front Physiol. 2012; 3: 124
    • (2012) Front Physiol , vol.3 , pp. 124
    • Bellingham, S.A.1    Guo, B.B.2    Coleman, B.M.3    Hill, A.F.4
  • 35
    • 0023645106 scopus 로고
    • Vesicle formation during reticulocyte maturation association of plasma membrane activities with released vesicles (exosomes)
    • Johnstone RM, Adam M, Hammond JR, Orr L, Turbide C. Vesicle formation during reticulocyte maturation. Association of plasma membrane activities with released vesicles (exosomes). JBiol Chem. 1987; 262: 9412-20
    • (1987) JBiol Chem , vol.262 , pp. 9412-9420
    • Johnstone, R.M.1    Adam, M.2    Hammond, J.R.3    Orr, L.4    Turbide, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.