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Volumn , Issue , 2014, Pages 257-280

Ongoing studies of deimination in neurodegenerative diseases using the F95 antibody

Author keywords

Aging; Alexander disease; Alzheimer's disease; Amyotrophic lateral sclerosis; Creutzfeldt Jakob disease; Diffuse Lewy body disease; Glioma; Parkinson's disease

Indexed keywords


EID: 84929669522     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4614-8317-5_14     Document Type: Chapter
Times cited : (16)

References (40)
  • 1
    • 84861198405 scopus 로고    scopus 로고
    • Neuronal PAD4 expression and protein citrullination: Possible role in production of autoantibodies associated with neurodegenerative disease
    • Acharya NK, Nagele EP, Han M, Coretti NJ, Demarshall C, Kosciuk MC, et al. (2012). Neuronal PAD4 expression and protein citrullination: possible role in production of autoantibodies associated with neurodegenerative disease. J Autoimmun 38: 369-380
    • (2012) J Autoimmun , vol.38 , pp. 369-380
    • Acharya, N.K.1    Nagele, E.P.2    Han, M.3    Coretti, N.J.4    Demarshall, C.5    Kosciuk, M.C.6
  • 2
    • 0030003487 scopus 로고    scopus 로고
    • Granules in glial cells of patients with Alzheimer's disease are immunopositive for C-Terminal sequences of -Amyloid protein
    • Akiyama H, Schwab C, Kondo H, Mori H, Kametani F, Ikeda K, et al. (1996). Granules in glial cells of patients with Alzheimer's disease are immunopositive for C-Terminal sequences of -Amyloid protein. Neurosci Lett 206: 169-172
    • (1996) Neurosci Lett , vol.206 , pp. 169-172
    • Akiyama, H.1    Schwab, C.2    Kondo, H.3    Mori, H.4    Kametani, F.5    Ikeda, K.6
  • 3
    • 0032885575 scopus 로고    scopus 로고
    • Localization of peptidylarginine deiminase type II in a stage-specific immature oligodendrocyte from rat cerebral hemisphere
    • Akiyama K, Sakurai Y, Asou H, Senshu T. (1999). Localization of peptidylarginine deiminase type II in a stage-specific immature oligodendrocyte from rat cerebral hemisphere. Neurosci Lett 274: 53-55
    • (1999) Neurosci Lett , vol.274 , pp. 53-55
    • Akiyama, K.1    Sakurai, Y.2    Asou, H.3    Senshu, T.4
  • 4
    • 0000641404 scopus 로고    scopus 로고
    • Purification of immunoglobulin M and immunoglobulin D
    • Suppl): 2.9.1-2.9.8
    • Andrew SM, Titus JA, Coico R, Amin A. (1997). Purification of immunoglobulin M and immunoglobulin D. Curr Protoc Immunol 21 (Suppl): 2.9.1-2.9.8
    • (1997) Curr Protoc Immunol , vol.21
    • Andrew, S.M.1    Titus, J.A.2    Coico, R.3    Amin, A.4
  • 5
    • 67650388344 scopus 로고    scopus 로고
    • Retinal deimination in aging and disease
    • Bhattacharya SK. (2009). Retinal deimination in aging and disease. IUBMB Life 61: 504-509
    • (2009) IUBMB Life , vol.61 , pp. 504-509
    • Bhattacharya, S.K.1
  • 6
    • 0030293676 scopus 로고    scopus 로고
    • Familial Alzheimer's disease-linked presenilin 1 variants elevate A1-42/1-40 ratio in vitro and in vivo
    • Borchelt DR, Thinakaran G, Eckman CB, Lee MK, Davenport F, Ratovitsky T, et al. (1996). Familial Alzheimer's disease-linked presenilin 1 variants elevate A1-42/1-40 ratio in vitro and in vivo. Neuron 17: 1005-1013
    • (1996) Neuron , vol.17 , pp. 1005-1013
    • Borchelt, D.R.1    Thinakaran, G.2    Eckman, C.B.3    Lee, M.K.4    Davenport, F.5    Ratovitsky, T.6
  • 8
    • 33644830015 scopus 로고    scopus 로고
    • Expression of peptidylarginine deiminase type 4 (PAD4) in various tumors
    • Chang X, Han J. (2006). Expression of peptidylarginine deiminase type 4 (PAD4) in various tumors. Mol Carcinog 45: 183-196
    • (2006) Mol Carcinog , vol.45 , pp. 183-196
    • Chang, X.1    Han, J.2
  • 9
    • 23644436874 scopus 로고    scopus 로고
    • Synovial intracellular citrullinated proteins colocalizing with peptidyl arginine deiminase are pathophysiologically relevant antigenic determinants of rheumatoid arthritis-specific humoral autoimmunity
    • De Rycke L, Nicholas AP, Cantaert T, Kruithof E, Echols JD, Vandekerckhove B, et al. (2005). Synovial intracellular citrullinated proteins colocalizing with peptidyl arginine deiminase are pathophysiologically relevant antigenic determinants of rheumatoid arthritis-specific humoral autoimmunity. Arthritis Rheum 52: 2323-2330
    • (2005) Arthritis Rheum , vol.52 , pp. 2323-2330
    • De Rycke, L.1    Nicholas, A.P.2    Cantaert, T.3    Kruithof, E.4    Echols, J.D.5    Vandekerckhove, B.6
  • 10
    • 0345119026 scopus 로고    scopus 로고
    • Caught in the act: A-synuclein is the culprit in Parkinson's disease
    • Eriksen JL, Dawson TM, Dickson DW, Petrucelli L. (2003). Caught in the act: a-synuclein is the culprit in Parkinson's disease. Neuron 40: 453-456
    • (2003) Neuron , vol.40 , pp. 453-456
    • Eriksen, J.L.1    Dawson, T.M.2    Dickson, D.W.3    Petrucelli, L.4
  • 11
    • 0026635173 scopus 로고
    • Phagocytosis and deposition of vascular beta-Amyloid in rat brains injected with Alzheimer beta-Amyloid
    • Frautschy SA, Cole GM, Baird A. (1992). Phagocytosis and deposition of vascular beta-Amyloid in rat brains injected with Alzheimer beta-Amyloid. Am J Pathol 140: 1389-1399
    • (1992) Am J Pathol , vol.140 , pp. 1389-1399
    • Frautschy, S.A.1    Cole, G.M.2    Baird, A.3
  • 12
    • 34547190677 scopus 로고    scopus 로고
    • Post-Translational modifications in the rat lumbar spinal cord in experimental autoimmune encephalomyelitis
    • Grant JE, Hu J, Liu T, Jain MR, Elkabes S, Li H. (2007). Post-Translational modifications in the rat lumbar spinal cord in experimental autoimmune encephalomyelitis. J Proteome Res 6: 2786-2791
    • (2007) J Proteome Res , vol.6 , pp. 2786-2791
    • Grant, J.E.1    Hu, J.2    Liu, T.3    Jain, M.R.4    Elkabes, S.5    Li, H.6
  • 13
    • 33846927285 scopus 로고    scopus 로고
    • A tale of two citrullines-structural and functional aspects of myelin basic protein deimination in health and disease
    • Harauz G, Musse AA. (2007). A tale of two citrullines-structural and functional aspects of myelin basic protein deimination in health and disease. Neurochem Res 32: 137-158
    • (2007) Neurochem Res , vol.32 , pp. 137-158
    • Harauz, G.1    Musse, A.A.2
  • 15
    • 20244368810 scopus 로고    scopus 로고
    • Abnormal accumulation of citrullinated proteins catalyzed by peptidylarginine deiminase in hippocampal extracts from patients with Alzheimer's disease
    • Ishigami A, Ohsawa T, Hiratsuka M, Taguchi H, Kobayashi S, Saito Y, et al. (2005). Abnormal accumulation of citrullinated proteins catalyzed by peptidylarginine deiminase in hippocampal extracts from patients with Alzheimer's disease. J Neurosci Res 80: 120-128
    • (2005) J Neurosci Res , vol.80 , pp. 120-128
    • Ishigami, A.1    Ohsawa, T.2    Hiratsuka, M.3    Taguchi, H.4    Kobayashi, S.5    Saito, Y.6
  • 16
    • 77449101433 scopus 로고    scopus 로고
    • Involvement of peptidylarginine deiminase-mediated post-Translational citrullination in pathogenesis of sporadic Creutzfeldt-Jakob disease
    • Jang B, Jin JK, Jeon YC, Cho HJ, Ishigami A, Choi KC, et al. (2010). Involvement of peptidylarginine deiminase-mediated post-Translational citrullination in pathogenesis of sporadic Creutzfeldt-Jakob disease. Acta Neuropathol 119: 199-210
    • (2010) Acta Neuropathol , vol.119 , pp. 199-210
    • Jang, B.1    Jin, J.K.2    Jeon, Y.C.3    Cho, H.J.4    Ishigami, A.5    Choi, K.C.6
  • 17
    • 38149063361 scopus 로고    scopus 로고
    • Expression pattern of peptidylarginine deiminase in rat and human Schwann cells
    • Keilhoff G, Prell T, Langnaese K, Mawrin C, Simon M, Fansa H, et al. (2008). Expression pattern of peptidylarginine deiminase in rat and human Schwann cells. Dev Neurobiol 68: 101-114
    • (2008) Dev Neurobiol , vol.68 , pp. 101-114
    • Keilhoff, G.1    Prell, T.2    Langnaese, K.3    Mawrin, C.4    Simon, M.5    Fansa, H.6
  • 18
    • 0036174969 scopus 로고    scopus 로고
    • The effects of long-Term treatment with metrifonate, a cholinesterase inhibitor, on cholinergic activity, amyloid pathology, and cognitive function in APP and PS1 doubly transgenic mice
    • Liu L, Ikonen S, Heikkinen T, Tapiola T, van Groen T, Tanila H. (2002). The effects of long-Term treatment with metrifonate, a cholinesterase inhibitor, on cholinergic activity, amyloid pathology, and cognitive function in APP and PS1 doubly transgenic mice. Exp Neurol 173: 196-204
    • (2002) Exp Neurol , vol.173 , pp. 196-204
    • Liu, L.1    Ikonen, S.2    Heikkinen, T.3    Tapiola, T.4    Van Groen, T.5    Tanila, H.6
  • 19
    • 71749088420 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosislinked mutant SOD1 sequesters Hu antigen R (HuR) and TIA-1-related protein (TIAR): Implications for impaired post-Transcriptional regulation of vascular endothelial growth factor
    • Lu L, Wang S, Zheng L, Li X, Suswam EA, Zhang X, et al. (2009). Amyotrophic lateral sclerosislinked mutant SOD1 sequesters Hu antigen R (HuR) and TIA-1-related protein (TIAR): implications for impaired post-Transcriptional regulation of vascular endothelial growth factor. J Biol Chem 284: 33989-33998
    • (2009) J Biol Chem , vol.284 , pp. 33989-33998
    • Lu, L.1    Wang, S.2    Zheng, L.3    Li, X.4    Suswam, E.A.5    Zhang, X.6
  • 23
    • 84856905668 scopus 로고    scopus 로고
    • Current and prospective disease-modifying therapies for amyotrophic lateral sclerosis
    • Morren JA, Galvez-Jimenez N. (2012). Current and prospective disease-modifying therapies for amyotrophic lateral sclerosis. Expert Opin Investig Drugs 21: 297-320
    • (2012) Expert Opin Investig Drugs , vol.21 , pp. 297-320
    • Morren, J.A.1    Galvez-Jimenez, N.2
  • 25
    • 0026612499 scopus 로고
    • Affinity chromatographic purification of immunoglobulin M antibodies utilizing immobilized mannan binding protein
    • Nevens JR, Mallia AK, Wendt MW, Smith PK. (1992). Affinity chromatographic purification of immunoglobulin M antibodies utilizing immobilized mannan binding protein. J Chromatogr 597: 247-256
    • (1992) J Chromatogr , vol.597 , pp. 247-256
    • Nevens, J.R.1    Mallia, A.K.2    Wendt, M.W.3    Smith, P.K.4
  • 26
    • 79955025436 scopus 로고    scopus 로고
    • Dual immunofluorescence study of citrullinated proteins in Parkinson diseased substantia nigra
    • Nicholas AP. (2011). Dual immunofluorescence study of citrullinated proteins in Parkinson diseased substantia nigra. Neurosci Lett 495: 26-29
    • (2011) Neurosci Lett , vol.495 , pp. 26-29
    • Nicholas, A.P.1
  • 27
    • 84878554880 scopus 로고    scopus 로고
    • Dual immunofluorescence study of citrullinated proteins in Alzheimer diseased frontal cortex
    • Nicholas AP. (2013). Dual immunofluorescence study of citrullinated proteins in Alzheimer diseased frontal cortex. Neurosci Lett 545: 107-111
    • (2013) Neurosci Lett , vol.545 , pp. 107-111
    • Nicholas, A.P.1
  • 28
    • 0037085720 scopus 로고    scopus 로고
    • Preparation of a monoclonal antibody to citrullinated epitopes: Its characterization and some applications to immunohistochemistry in human brain
    • Nicholas AP, Whitaker JN. (2002). Preparation of a monoclonal antibody to citrullinated epitopes: its characterization and some applications to immunohistochemistry in human brain. Glia 37: 328-336
    • (2002) Glia , vol.37 , pp. 328-336
    • Nicholas, A.P.1    Whitaker, J.N.2
  • 30
    • 1942452851 scopus 로고    scopus 로고
    • Increased citrullinated glial fibrillary acidic protein in secondary progressive multiple sclerosis
    • Nicholas AP, Sambandam T, Echols JD, Tourtellotte WW. (2004). Increased citrullinated glial fibrillary acidic protein in secondary progressive multiple sclerosis. J Comp Neurol 473: 128-136
    • (2004) J Comp Neurol , vol.473 , pp. 128-136
    • Nicholas, A.P.1    Sambandam, T.2    Echols, J.D.3    Tourtellotte, W.W.4
  • 31
    • 17844411445 scopus 로고    scopus 로고
    • Expression of citrullinated proteins in murine experimental autoimmune encephalomyelitis
    • Nicholas AP, Sambandam T, Echols JD, Barnum SR. (2005). Expression of citrullinated proteins in murine experimental autoimmune encephalomyelitis. J Comp Neurol 486: 254-266
    • (2005) J Comp Neurol , vol.486 , pp. 254-266
    • Nicholas, A.P.1    Sambandam, T.2    Echols, J.D.3    Barnum, S.R.4
  • 32
    • 33746485560 scopus 로고    scopus 로고
    • The Alexander diseasecausing glial fibrillary acidic protein mutant, R416W, accumulates into Rosenthal fibers by a pathway that involves filament aggregation and the association of aB-crystallin and HSP27
    • Perng MD, Su M, Wen SF, Li R, Gibbon T, Prescott AR, et al. (2006). The Alexander diseasecausing glial fibrillary acidic protein mutant, R416W, accumulates into Rosenthal fibers by a pathway that involves filament aggregation and the association of aB-crystallin and HSP27. Am J Hum Genet 79: 197-213
    • (2006) Am J Hum Genet , vol.79 , pp. 197-213
    • Perng, M.D.1    Su, M.2    Wen, S.F.3    Li, R.4    Gibbon, T.5    Prescott, A.R.6
  • 34
    • 76549127361 scopus 로고    scopus 로고
    • Developmental and age-related changes of peptidylarginine deiminase 2 in the mouse brain
    • Shimada N, Handa S, Uchida Y, Fukuda M, Maruyama N, Asaga H, et al. (2010). Developmental and age-related changes of peptidylarginine deiminase 2 in the mouse brain. J Neurosci Res 88: 798-806
    • (2010) J Neurosci Res , vol.88 , pp. 798-806
    • Shimada, N.1    Handa, S.2    Uchida, Y.3    Fukuda, M.4    Maruyama, N.5    Asaga, H.6
  • 35
    • 33747153860 scopus 로고    scopus 로고
    • Deposition of mouse amyloid in human APP/PS1 double and single AD model transgenic mice
    • van Groen T, Kiliaan AJ, Kadish I. (2006). Deposition of mouse amyloid in human APP/PS1 double and single AD model transgenic mice. Neurobiol Dis 23: 653-662
    • (2006) Neurobiol Dis , vol.23 , pp. 653-662
    • Van Groen, T.1    Kiliaan, A.J.2    Kadish, I.3
  • 36
    • 84866490231 scopus 로고    scopus 로고
    • The molecular basis of the frontotemporal lobar degeneration-Amyotrophic lateral sclerosis spectrum
    • Van Langenhove T, van der Zee J, Van Broeckhoven C. (2012). The molecular basis of the frontotemporal lobar degeneration-Amyotrophic lateral sclerosis spectrum. Ann Med 44: 817-828
    • (2012) Ann Med , vol.44 , pp. 817-828
    • Van Langenhove, T.1    Van Der Zee, J.2    Van Broeckhoven, C.3
  • 37
    • 0026544923 scopus 로고
    • Immunohistochemical localization of peptidylarginine deiminase in rat brain
    • Vincent SR, Leung E, Watanabe K. (1992). Immunohistochemical localization of peptidylarginine deiminase in rat brain. J Chem Neuroanat 5: 159-168
    • (1992) J Chem Neuroanat , vol.5 , pp. 159-168
    • Vincent, S.R.1    Leung, E.2    Watanabe, K.3
  • 38
    • 0034295217 scopus 로고    scopus 로고
    • Microglia cells are the driving force in fibrillar plaque formation, whereas astrocytes are a leading factor in plaque degradation
    • Wegiel J, Wang KC, Tarnawski M, Lach B. (2000). Microglia cells are the driving force in fibrillar plaque formation, whereas astrocytes are a leading factor in plaque degradation. Acta Neuropathol 100: 356-364
    • (2000) Acta Neuropathol , vol.100 , pp. 356-364
    • Wegiel, J.1    Wang, K.C.2    Tarnawski, M.3    Lach, B.4
  • 40
    • 0033557276 scopus 로고    scopus 로고
    • Glial fibrillary acidic protein is necessary for mature astrocytes to react to beta-Amyloid
    • Xu K, Malouf AT, Messing A, Silver J. (1999). Glial fibrillary acidic protein is necessary for mature astrocytes to react to beta-Amyloid. Glia 25: 390-403
    • (1999) Glia , vol.25 , pp. 390-403
    • Xu, K.1    Malouf, A.T.2    Messing, A.3    Silver, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.