메뉴 건너뛰기




Volumn 94, Issue , 2016, Pages 18-31

Pathological conformations involving the amino terminus of tau occur early in Alzheimer's disease and are differentially detected by monoclonal antibodies

Author keywords

Alzheimer's disease; Antibodies; Conformation; Neurodegeneration; Protein aggregation; Protein misfolding; Tau; Tauopathies

Indexed keywords

EPITOPE; MONOCLONAL ANTIBODY; RECOMBINANT PROTEIN; TAU PROTEIN; TAU12 PROTEIN; TAU13 PROTEIN; UNCLASSIFIED DRUG;

EID: 84973572645     PISSN: 09699961     EISSN: 1095953X     Source Type: Journal    
DOI: 10.1016/j.nbd.2016.05.016     Document Type: Article
Times cited : (60)

References (50)
  • 1
    • 0036937699 scopus 로고    scopus 로고
    • Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease
    • Augustinack J.C., et al. Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease. Acta Neuropathol. (Berl.) 2002, 103:26-35.
    • (2002) Acta Neuropathol. (Berl.) , vol.103 , pp. 26-35
    • Augustinack, J.C.1
  • 2
    • 0024587074 scopus 로고
    • Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease
    • Bancher C., et al. Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease. Brain Res. 1989, 477:90-99.
    • (1989) Brain Res. , vol.477 , pp. 90-99
    • Bancher, C.1
  • 3
    • 0026030994 scopus 로고
    • Abnormal phosphorylation of tau precedes ubiquitination in neurofibrillary pathology of Alzheimer disease
    • Bancher C., et al. Abnormal phosphorylation of tau precedes ubiquitination in neurofibrillary pathology of Alzheimer disease. Brain Res. 1991, 539:11-18.
    • (1991) Brain Res. , vol.539 , pp. 11-18
    • Bancher, C.1
  • 4
    • 20844439375 scopus 로고    scopus 로고
    • Tau epitope display in progressive supranuclear palsy and corticobasal degeneration
    • Berry R.W., et al. Tau epitope display in progressive supranuclear palsy and corticobasal degeneration. J. Neurocytol. 2004, 33:287-295.
    • (2004) J. Neurocytol. , vol.33 , pp. 287-295
    • Berry, R.W.1
  • 5
    • 0030669037 scopus 로고    scopus 로고
    • Relationships between regional neuronal loss and neurofibrillary changes in the hippocampal formation and duration and severity of Alzheimer disease
    • Bobinski M., et al. Relationships between regional neuronal loss and neurofibrillary changes in the hippocampal formation and duration and severity of Alzheimer disease. J. Neuropathol. Exp. Neurol. 1997, 56:414-420.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 414-420
    • Bobinski, M.1
  • 6
    • 0028345718 scopus 로고
    • Immunohistochemical staging of neurofibrillary degeneration in Alzheimer's disease
    • Bondareff W., et al. Immunohistochemical staging of neurofibrillary degeneration in Alzheimer's disease. J. Neuropathol. Exp. Neurol. 1994, 53:158-164.
    • (1994) J. Neuropathol. Exp. Neurol. , vol.53 , pp. 158-164
    • Bondareff, W.1
  • 7
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak H., Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol. 1991, 82:239-259.
    • (1991) Acta Neuropathol. , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 8
    • 0028362458 scopus 로고
    • A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads
    • Braak E., et al. A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads. Acta Neuropathol. (Berl.) 1994, 87:554-567.
    • (1994) Acta Neuropathol. (Berl.) , vol.87 , pp. 554-567
    • Braak, E.1
  • 9
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain
    • Brandt R., et al. Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain. J. Cell Biol. 1995, 131:1327-1340.
    • (1995) J. Cell Biol. , vol.131 , pp. 1327-1340
    • Brandt, R.1
  • 10
    • 0344838686 scopus 로고    scopus 로고
    • Stereologic analysis of neurofibrillary tangle formation in prefrontal cortex area 9 in aging and Alzheimer's disease
    • Bussiere T., et al. Stereologic analysis of neurofibrillary tangle formation in prefrontal cortex area 9 in aging and Alzheimer's disease. Neuroscience 2003, 117:577-592.
    • (2003) Neuroscience , vol.117 , pp. 577-592
    • Bussiere, T.1
  • 11
    • 12644260802 scopus 로고    scopus 로고
    • The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology
    • Carmel G., et al. The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology. J. Biol. Chem. 1996, 271:32789-32795.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32789-32795
    • Carmel, G.1
  • 12
    • 0026451030 scopus 로고
    • Immunocytochemistry of neurofibrillary tangles with antibodies to subregions of tau protein: identification of hidden and cleaved tau epitopes and a new phosphorylation site
    • Dickson D.W., et al. Immunocytochemistry of neurofibrillary tangles with antibodies to subregions of tau protein: identification of hidden and cleaved tau epitopes and a new phosphorylation site. Acta Neuropathol. 1992, 84:596-605.
    • (1992) Acta Neuropathol. , vol.84 , pp. 596-605
    • Dickson, D.W.1
  • 13
    • 0027534862 scopus 로고
    • Lack of the carboxyl terminal sequence of tau in ghost tangles of Alzheimer's disease
    • Endoh R., et al. Lack of the carboxyl terminal sequence of tau in ghost tangles of Alzheimer's disease. Brain Res. 1993, 601:164-172.
    • (1993) Brain Res. , vol.601 , pp. 164-172
    • Endoh, R.1
  • 14
    • 11144321178 scopus 로고    scopus 로고
    • Potential structure/function relationships of predicted secondary structural elements of tau
    • Gamblin T.C. Potential structure/function relationships of predicted secondary structural elements of tau. Biochim. Biophys. Acta 2005, 1739:140-149.
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 140-149
    • Gamblin, T.C.1
  • 15
    • 0034705192 scopus 로고    scopus 로고
    • In vitro polymerization of tau protein monitored by laser light scattering: method and application to the study of FTDP-17 mutants
    • Gamblin T.C., et al. In vitro polymerization of tau protein monitored by laser light scattering: method and application to the study of FTDP-17 mutants. Biochemistry 2000, 39:6136-6144.
    • (2000) Biochemistry , vol.39 , pp. 6136-6144
    • Gamblin, T.C.1
  • 16
    • 0342368728 scopus 로고    scopus 로고
    • The extent of neurofibrillary pathology in perforant pathway neurons is the key determinant of dementia in the very old
    • Garcia-Sierra F., et al. The extent of neurofibrillary pathology in perforant pathway neurons is the key determinant of dementia in the very old. Acta Neuropathol. (Berl.) 2000, 100:29-35.
    • (2000) Acta Neuropathol. (Berl.) , vol.100 , pp. 29-35
    • Garcia-Sierra, F.1
  • 17
    • 0038291981 scopus 로고    scopus 로고
    • Conformational changes and truncation of tau protein during tangle evolution in Alzheimer's disease
    • Garcia-Sierra F., et al. Conformational changes and truncation of tau protein during tangle evolution in Alzheimer's disease. J. Alzheimers Dis. 2003, 5:65-77.
    • (2003) J. Alzheimers Dis. , vol.5 , pp. 65-77
    • Garcia-Sierra, F.1
  • 18
    • 0036434880 scopus 로고    scopus 로고
    • Tau conformational changes correspond to impairments of episodic memory in mild cognitive impairment and Alzheimer's disease
    • Ghoshal N., et al. Tau conformational changes correspond to impairments of episodic memory in mild cognitive impairment and Alzheimer's disease. Exp. Neurol. 2002, 177:475-493.
    • (2002) Exp. Neurol. , vol.177 , pp. 475-493
    • Ghoshal, N.1
  • 19
    • 0028946744 scopus 로고
    • Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205
    • Goedert M., et al. Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205. Neurosci. Lett. 1995, 189:167-169.
    • (1995) Neurosci. Lett. , vol.189 , pp. 167-169
    • Goedert, M.1
  • 20
    • 0344653664 scopus 로고    scopus 로고
    • Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease
    • Gomez-Isla T., et al. Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease. Ann. Neurol. 1997, 41:17-24.
    • (1997) Ann. Neurol. , vol.41 , pp. 17-24
    • Gomez-Isla, T.1
  • 21
    • 0026501888 scopus 로고
    • Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau
    • Greenberg S.G., et al. Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau. J. Biol. Chem. 1992, 267:564-569.
    • (1992) J. Biol. Chem. , vol.267 , pp. 564-569
    • Greenberg, S.G.1
  • 22
    • 3242811902 scopus 로고    scopus 로고
    • Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease
    • Guo H., et al. Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease. Am. J. Pathol. 2004, 165:523-531.
    • (2004) Am. J. Pathol. , vol.165 , pp. 523-531
    • Guo, H.1
  • 23
    • 0022521851 scopus 로고
    • Use of monoclonal antibodies to detect conformational alterations in lactate dehydrogenase isoenzyme 5 on heat denaturation and on adsorption to polystyrene plates
    • Hollander Z., Katchalski-Katzir E. Use of monoclonal antibodies to detect conformational alterations in lactate dehydrogenase isoenzyme 5 on heat denaturation and on adsorption to polystyrene plates. Mol. Immunol. 1986, 23:927-933.
    • (1986) Mol. Immunol. , vol.23 , pp. 927-933
    • Hollander, Z.1    Katchalski-Katzir, E.2
  • 24
    • 4544248870 scopus 로고    scopus 로고
    • Early N-terminal changes and caspase-6 cleavage of tau in Alzheimer's disease
    • Horowitz P.M., et al. Early N-terminal changes and caspase-6 cleavage of tau in Alzheimer's disease. J. Neurosci. 2004, 24:7895-7902.
    • (2004) J. Neurosci. , vol.24 , pp. 7895-7902
    • Horowitz, P.M.1
  • 25
    • 33750380827 scopus 로고    scopus 로고
    • N-terminal fragments of tau inhibit full-length tau polymerization in vitro
    • Horowitz P.M., et al. N-terminal fragments of tau inhibit full-length tau polymerization in vitro. Biochemistry 2006, 45:12859-12866.
    • (2006) Biochemistry , vol.45 , pp. 12859-12866
    • Horowitz, P.M.1
  • 26
    • 0023940185 scopus 로고
    • Alz-50 antibody recognizes Alzheimer-related neuronal changes
    • Hyman B.T., et al. Alz-50 antibody recognizes Alzheimer-related neuronal changes. Ann. Neurol. 1988, 23:371-379.
    • (1988) Ann. Neurol. , vol.23 , pp. 371-379
    • Hyman, B.T.1
  • 27
    • 33144463940 scopus 로고    scopus 로고
    • Global hairpin folding of tau in solution
    • Jeganathan S., et al. Global hairpin folding of tau in solution. Biochemistry 2006, 45:2283-2293.
    • (2006) Biochemistry , vol.45 , pp. 2283-2293
    • Jeganathan, S.1
  • 28
    • 57649129018 scopus 로고    scopus 로고
    • Proline-directed pseudo-phosphorylation at AT8 and PHF1 epitopes induces a compaction of the paperclip folding of tau and generates a pathological (MC-1) conformation
    • Jeganathan S., et al. Proline-directed pseudo-phosphorylation at AT8 and PHF1 epitopes induces a compaction of the paperclip folding of tau and generates a pathological (MC-1) conformation. J. Biol. Chem. 2008, 283:32066-32076.
    • (2008) J. Biol. Chem. , vol.283 , pp. 32066-32076
    • Jeganathan, S.1
  • 29
    • 0030936599 scopus 로고    scopus 로고
    • Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau
    • Jicha G.A., et al. Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau. J. Neurosci. Res. 1997, 48:128-132.
    • (1997) J. Neurosci. Res. , vol.48 , pp. 128-132
    • Jicha, G.A.1
  • 30
    • 0033558929 scopus 로고    scopus 로고
    • Sequence requirements for formation of conformational variants of tau similar to those found in Alzheimer's disease
    • Jicha G.A., et al. Sequence requirements for formation of conformational variants of tau similar to those found in Alzheimer's disease. J. Neurosci. Res. 1999, 55:713-723.
    • (1999) J. Neurosci. Res. , vol.55 , pp. 713-723
    • Jicha, G.A.1
  • 31
    • 79960032374 scopus 로고    scopus 로고
    • Pathogenic forms of tau inhibit kinesin-dependent axonal transport through a mechanism involving activation of axonal phosphotransferases
    • Kanaan N.M., et al. Pathogenic forms of tau inhibit kinesin-dependent axonal transport through a mechanism involving activation of axonal phosphotransferases. J. Neurosci. 2011, 31:9858-9868.
    • (2011) J. Neurosci. , vol.31 , pp. 9858-9868
    • Kanaan, N.M.1
  • 32
    • 84856954738 scopus 로고    scopus 로고
    • Phosphorylation in the amino terminus of tau prevents inhibition of anterograde axonal transport
    • Kanaan N.M., et al. Phosphorylation in the amino terminus of tau prevents inhibition of anterograde axonal transport. Neurobiol. Aging 2012, 33(826):e15-e30.
    • (2012) Neurobiol. Aging , vol.33 , Issue.826
    • Kanaan, N.M.1
  • 33
    • 84973521894 scopus 로고    scopus 로고
    • Characterization of early pathological tau conformations and phosphorylation in chronic traumatic encephalopathy
    • Kanaan N.M., et al. Characterization of early pathological tau conformations and phosphorylation in chronic traumatic encephalopathy. J. Neuropathol. Exp. Neurol. 2015.
    • (2015) J. Neuropathol. Exp. Neurol.
    • Kanaan, N.M.1
  • 34
    • 0028827080 scopus 로고
    • DAPI: a DNA-specific fluorescent probe
    • Kapuscinski J. DAPI: a DNA-specific fluorescent probe. Biotech. Histochem. 1995, 70:220-233.
    • (1995) Biotech. Histochem. , vol.70 , pp. 220-233
    • Kapuscinski, J.1
  • 35
    • 62849088641 scopus 로고    scopus 로고
    • The amino terminus of tau inhibits kinesin-dependent axonal transport: implications for filament toxicity
    • LaPointe N.E., et al. The amino terminus of tau inhibits kinesin-dependent axonal transport: implications for filament toxicity. J. Neurosci. Res. 2009, 87:440-451.
    • (2009) J. Neurosci. Res. , vol.87 , pp. 440-451
    • LaPointe, N.E.1
  • 36
    • 38049030324 scopus 로고    scopus 로고
    • Earliest stages of tau conformational changes are related to the appearance of a sequence of specific phospho-dependent tau epitopes in Alzheimer's disease
    • Luna-Munoz J., et al. Earliest stages of tau conformational changes are related to the appearance of a sequence of specific phospho-dependent tau epitopes in Alzheimer's disease. J. Alzheimers Dis. 2007, 12:365-375.
    • (2007) J. Alzheimers Dis. , vol.12 , pp. 365-375
    • Luna-Munoz, J.1
  • 37
    • 0028798197 scopus 로고
    • Monitoring pathological assembly of tau and beta-amyloid proteins in Alzheimer's disease
    • Mena R., et al. Monitoring pathological assembly of tau and beta-amyloid proteins in Alzheimer's disease. Acta Neuropathol. 1995, 89:50-56.
    • (1995) Acta Neuropathol. , vol.89 , pp. 50-56
    • Mena, R.1
  • 38
    • 0026758096 scopus 로고
    • Monoclonal antibodies with selective specificity for Alzheimer tau are directed against phosphatase-sensitive epitopes
    • Mercken M., et al. Monoclonal antibodies with selective specificity for Alzheimer tau are directed against phosphatase-sensitive epitopes. Acta Neuropathol. 1992, 84:265-272.
    • (1992) Acta Neuropathol. , vol.84 , pp. 265-272
    • Mercken, M.1
  • 39
    • 0033028074 scopus 로고    scopus 로고
    • Neurons may live for decades with neurofibrillary tangles
    • Morsch R., et al. Neurons may live for decades with neurofibrillary tangles. J. Neuropathol. Exp. Neurol. 1999, 58:188-197.
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 188-197
    • Morsch, R.1
  • 40
    • 61349120815 scopus 로고    scopus 로고
    • Structural polymorphism of 441-residue tau at single residue resolution
    • Mukrasch M.D., et al. Structural polymorphism of 441-residue tau at single residue resolution. PLoS Biol. 2009, 7.
    • (2009) PLoS Biol. , vol.7
    • Mukrasch, M.D.1
  • 41
    • 0028593606 scopus 로고
    • Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404
    • Otvos L., et al. Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404. J. Neurosci. Res. 1994, 39:669-673.
    • (1994) J. Neurosci. Res. , vol.39 , pp. 669-673
    • Otvos, L.1
  • 42
    • 0023505501 scopus 로고
    • Phosphorylation determines two distinct species of tau in the central nervous system
    • Papasozomenos S.C., Binder L.I. Phosphorylation determines two distinct species of tau in the central nervous system. Cell Motil. Cytoskeleton 1987, 8:210-226.
    • (1987) Cell Motil. Cytoskeleton , vol.8 , pp. 210-226
    • Papasozomenos, S.C.1    Binder, L.I.2
  • 43
    • 79959571777 scopus 로고    scopus 로고
    • Characterization of prefibrillar Tau oligomers in vitro and in Alzheimer disease
    • Patterson K.R., et al. Characterization of prefibrillar Tau oligomers in vitro and in Alzheimer disease. J Biol Chem. 2011, 286:23063-23076.
    • (2011) J Biol Chem. , vol.286 , pp. 23063-23076
    • Patterson, K.R.1
  • 44
    • 81855190900 scopus 로고    scopus 로고
    • Heat shock protein 70 prevents both tau aggregation and the inhibitory effects of preexisting tau aggregates on fast axonal transport
    • Patterson K.R., et al. Heat shock protein 70 prevents both tau aggregation and the inhibitory effects of preexisting tau aggregates on fast axonal transport. Biochemistry. 2011, 50:10300-10310.
    • (2011) Biochemistry. , vol.50 , pp. 10300-10310
    • Patterson, K.R.1
  • 45
    • 84900429512 scopus 로고    scopus 로고
    • Specificity of anti-tau antibodies when analyzing mice models of Alzheimer's disease: problems and solutions
    • Petry F.R., et al. Specificity of anti-tau antibodies when analyzing mice models of Alzheimer's disease: problems and solutions. PLoS One 2014, 9.
    • (2014) PLoS One , vol.9
    • Petry, F.R.1
  • 46
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • Santacruz K., et al. Tau suppression in a neurodegenerative mouse model improves memory function. Science 2005, 309:476-481.
    • (2005) Science , vol.309 , pp. 476-481
    • Santacruz, K.1
  • 47
    • 0025870805 scopus 로고
    • An appraisal of polystyrene-(ELISA) and nitrocellulose-based (ELIFA) enzyme immunoassay systems using monoclonal antibodies reactive toward antigenically distinct forms of human C-reactive protein
    • Shields M.J., et al. An appraisal of polystyrene-(ELISA) and nitrocellulose-based (ELIFA) enzyme immunoassay systems using monoclonal antibodies reactive toward antigenically distinct forms of human C-reactive protein. J. Immunol. Methods 1991, 141:253-261.
    • (1991) J. Immunol. Methods , vol.141 , pp. 253-261
    • Shields, M.J.1
  • 48
    • 38549120646 scopus 로고    scopus 로고
    • In vivo imaging reveals dissociation between caspase activation and acute neuronal death in tangle-bearing neurons
    • Spires-Jones T.L., et al. In vivo imaging reveals dissociation between caspase activation and acute neuronal death in tangle-bearing neurons. J. Neurosci. 2008, 28:862-867.
    • (2008) J. Neurosci. , vol.28 , pp. 862-867
    • Spires-Jones, T.L.1
  • 49
    • 0035958642 scopus 로고    scopus 로고
    • Tauopathy in drosophila: neurodegeneration without neurofibrillary tangles
    • Wittmann C.W., et al. Tauopathy in drosophila: neurodegeneration without neurofibrillary tangles. Science 2001, 293:711-714.
    • (2001) Science , vol.293 , pp. 711-714
    • Wittmann, C.W.1
  • 50
    • 33846538660 scopus 로고    scopus 로고
    • Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model
    • Yoshiyama Y., et al. Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model. Neuron 2007, 53:337-351.
    • (2007) Neuron , vol.53 , pp. 337-351
    • Yoshiyama, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.