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Volumn 1739, Issue 2, 2005, Pages 211-215

Tau modifiers as therapeutic targets for Alzheimer's disease

Author keywords

4 hydroxy 2 nonenal; Alzheimer's disease; Heme oxygenase; Lipid peroxidation; Oxidative stress

Indexed keywords

TAU PROTEIN;

EID: 19944383786     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2004.06.021     Document Type: Review
Times cited : (13)

References (57)
  • 1
    • 0035086103 scopus 로고    scopus 로고
    • Brain degeneration linked to "fatal attractions" of proteins in Alzheimer's disease and related disorders
    • J.Q. Trojanowski, and V.M.Y. Lee Brain degeneration linked to "fatal attractions" of proteins in Alzheimer's disease and related disorders J. Alzheimer's Dis. 3 2001 117 119
    • (2001) J. Alzheimer's Dis. , vol.3 , pp. 117-119
    • Trojanowski, J.Q.1    Lee, V.M.Y.2
  • 2
    • 0028918383 scopus 로고
    • Extracellular neurofibrillary tangles reflect neuronal loss and provide further evidence of extensive protein cross-linking in Alzheimer disease
    • P. Cras, M.A. Smith, P.L. Richey, S.L. Siedlak, P. Mulvihill, and G. Perry Extracellular neurofibrillary tangles reflect neuronal loss and provide further evidence of extensive protein cross-linking in Alzheimer disease Acta Neuropathol. 89 1995 291 295
    • (1995) Acta Neuropathol. , vol.89 , pp. 291-295
    • Cras, P.1    Smith, M.A.2    Richey, P.L.3    Siedlak, S.L.4    Mulvihill, P.5    Perry, G.6
  • 3
  • 7
    • 0033836580 scopus 로고    scopus 로고
    • In Alzheimer's disease, heme oxygenase is coincident with Alz50, an epitope of τ induced by 4-hydroxy-2-nonenal modification
    • A. Takeda, M.A. Smith, J. Avilá, A. Nunomura, S.L. Siedlak, X. Zhu, G. Perry, and L.M. Sayre In Alzheimer's disease, heme oxygenase is coincident with Alz50, an epitope of τ induced by 4-hydroxy-2-nonenal modification J. Neurochem. 75 2000 1234 1241
    • (2000) J. Neurochem. , vol.75 , pp. 1234-1241
    • Takeda, A.1    Smith, M.A.2    Avilá, J.3    Nunomura, A.4    Siedlak, S.L.5    Zhu, X.6    Perry, G.7    Sayre, L.M.8
  • 8
    • 37049048544 scopus 로고
    • Paired helical filaments in electron microscopy of Alzheimer's disease
    • M. Kidd Paired helical filaments in electron microscopy of Alzheimer's disease Nature 197 1963 192 193
    • (1963) Nature , vol.197 , pp. 192-193
    • Kidd, M.1
  • 9
    • 0022257253 scopus 로고
    • Immunologic determinants of tau protein are present in neurofibrillary tangles of Alzheimer's disease
    • J.P. Brion, H. Passarier, J. Nunez, and J. Flament-Durand Immunologic determinants of tau protein are present in neurofibrillary tangles of Alzheimer's disease Arch. Biol. 95 1985 229 235
    • (1985) Arch. Biol. , vol.95 , pp. 229-235
    • Brion, J.P.1    Passarier, H.2    Nunez, J.3    Flament-Durand, J.4
  • 12
    • 0022848472 scopus 로고
    • Alzheimer's paired helical filaments
    • Y. Ihara Alzheimer's paired helical filaments Rinsho Shinkeigaku 26 1986 1287 1289
    • (1986) Rinsho Shinkeigaku , vol.26 , pp. 1287-1289
    • Ihara, Y.1
  • 13
    • 0022724941 scopus 로고
    • Phosphorylated tau protein is integrated into paired helical filaments in Alzheimer's disease
    • Y. Ihara, N. Nukina, R. Miura, and M. Ogawara Phosphorylated tau protein is integrated into paired helical filaments in Alzheimer's disease J. Biochem. 99 1986 1807 1810
    • (1986) J. Biochem. , vol.99 , pp. 1807-1810
    • Ihara, Y.1    Nukina, N.2    Miura, R.3    Ogawara, M.4
  • 14
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease
    • K.S. Kosik, C.L. Joachim, and D.J. Selkoe Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease Proc. Natl. Acad. Sci. U. S. A. 83 1986 4044 4048
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 16
    • 0022530987 scopus 로고
    • High molecular weight microtubule-associated proteins: Purification by electro-elution and amino acid compositions
    • K.S. Kosik, S.F. Bakalis, D.J. Selkoe, M.W. Pierce, and L.K. Duffy High molecular weight microtubule-associated proteins: purification by electro-elution and amino acid compositions J. Neurosci. Res. 15 1986 543 551
    • (1986) J. Neurosci. Res. , vol.15 , pp. 543-551
    • Kosik, K.S.1    Bakalis, S.F.2    Selkoe, D.J.3    Pierce, M.W.4    Duffy, L.K.5
  • 17
    • 0023687214 scopus 로고
    • A modified form of microtubule-associated tau protein is the main component of paired helical filaments
    • A. Nieto, I. Correas, E. Montejo de Garcini, and J. Avila A modified form of microtubule-associated tau protein is the main component of paired helical filaments Biochem. Biophys. Res. Commun. 154 1988 660 667
    • (1988) Biochem. Biophys. Res. Commun. , vol.154 , pp. 660-667
    • Nieto, A.1    Correas, I.2    Montejo De Garcini, E.3    Avila, J.4
  • 20
    • 0024804051 scopus 로고
    • Neurofibrillary degeneration and neuronal loss in Alzheimer's disease
    • W. Bondareff, C.Q. Mountjoy, M. Roth, and D.L. Hauser Neurofibrillary degeneration and neuronal loss in Alzheimer's disease Neurobiol. Aging 10 1989 709 715
    • (1989) Neurobiol. Aging , vol.10 , pp. 709-715
    • Bondareff, W.1    Mountjoy, C.Q.2    Roth, M.3    Hauser, D.L.4
  • 21
    • 0025909019 scopus 로고
    • Basic fibroblast growth factor binding is a marker for extracellular neurofibrillary tangles in Alzheimer disease
    • S.L. Siedlak, P. Cras, M. Kawai, P. Richey, and G. Perry Basic fibroblast growth factor binding is a marker for extracellular neurofibrillary tangles in Alzheimer disease J. Histochem. Cytochem. 39 1991 899 904
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 899-904
    • Siedlak, S.L.1    Cras, P.2    Kawai, M.3    Richey, P.4    Perry, G.5
  • 23
    • 0033600084 scopus 로고    scopus 로고
    • Alzheimer's disease. Pinning down phosphorylated tau
    • M. Goedert Alzheimer's disease. Pinning down phosphorylated tau Nature 399 1999 739 740
    • (1999) Nature , vol.399 , pp. 739-740
    • Goedert, M.1
  • 24
    • 0028593606 scopus 로고
    • Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404
    • L. Otvos Jr., L. Feiner, E. Lang, G.I. Szendrei, M. Goedert, and V.M. Lee Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404 J. Neurosci. Res. 39 1994 669 673
    • (1994) J. Neurosci. Res. , vol.39 , pp. 669-673
    • Otvos Jr., L.1    Feiner, L.2    Lang, E.3    Szendrei, G.I.4    Goedert, M.5    Lee, V.M.6
  • 25
    • 0030062245 scopus 로고    scopus 로고
    • Mitotic mechanisms in Alzheimer's disease
    • I. Vincent, M. Rosado, and P. Davies Mitotic mechanisms in Alzheimer's disease J. Cell Biol. 132 1996 413 425
    • (1996) J. Cell Biol. , vol.132 , pp. 413-425
    • Vincent, I.1    Rosado, M.2    Davies, P.3
  • 26
    • 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
    • G.A. Jicha, R. Bowser, I.G. Kazam, and P. Davies Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau J. Neurosci. Res. 48 1997 128 132
    • (1997) J. Neurosci. Res. , vol.48 , pp. 128-132
    • Jicha, G.A.1    Bowser, R.2    Kazam, I.G.3    Davies, P.4
  • 27
    • 0034282067 scopus 로고    scopus 로고
    • Conformational change as one of the earliest alterations of tau in Alzheimer's disease
    • C.L. Weaver, M. Espinoza, Y. Kress, and P. Davies Conformational change as one of the earliest alterations of tau in Alzheimer's disease Neurobiol. Aging 21 2000 719 727
    • (2000) Neurobiol. Aging , vol.21 , pp. 719-727
    • Weaver, C.L.1    Espinoza, M.2    Kress, Y.3    Davies, P.4
  • 28
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
    • P.V. Arriagada, J.H. Growdon, E.T. Hedley-Whyte, and B.T. Hyman Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease Neurology 42 1992 631 639
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 29
    • 0026743110 scopus 로고
    • Distribution of Alzheimer-type pathologic changes in nondemented elderly individuals matches the pattern in Alzheimer's disease
    • P.V. Arriagada, K. Marzloff, and B.T. Hyman Distribution of Alzheimer-type pathologic changes in nondemented elderly individuals matches the pattern in Alzheimer's disease Neurology 42 1992 1681 1688
    • (1992) Neurology , vol.42 , pp. 1681-1688
    • Arriagada, P.V.1    Marzloff, K.2    Hyman, B.T.3
  • 31
    • 0029999787 scopus 로고    scopus 로고
    • Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules
    • A.C. Alonso, I. Grundke-Iqbal, and K. Iqbal Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules Nat. Med. 2 1996 783 787
    • (1996) Nat. Med. , vol.2 , pp. 783-787
    • Alonso, A.C.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 32
    • 0037303935 scopus 로고    scopus 로고
    • Traffic at the intersection of neurotrophic factor signaling and neurodegeneration
    • A. Salehi, J.D. Delcroix, and W.C. Mobley Traffic at the intersection of neurotrophic factor signaling and neurodegeneration Trends Neurosci. 26 2003 73 80
    • (2003) Trends Neurosci. , vol.26 , pp. 73-80
    • Salehi, A.1    Delcroix, J.D.2    Mobley, W.C.3
  • 33
    • 0035851157 scopus 로고    scopus 로고
    • Interaction of tau isoforms with Alzheimer's disease abnormally hyperphosphorylated tau and in vitro phosphorylation into the disease-like protein
    • A.D. Alonso, T. Zaidi, M. Novak, H.S. Barra, I. Grundke-Iqbal, and K. Iqbal Interaction of tau isoforms with Alzheimer's disease abnormally hyperphosphorylated tau and in vitro phosphorylation into the disease-like protein J. Biol. Chem. 276 2001 37967 37973
    • (2001) J. Biol. Chem. , vol.276 , pp. 37967-37973
    • Alonso, A.D.1    Zaidi, T.2    Novak, M.3    Barra, H.S.4    Grundke-Iqbal, I.5    Iqbal, K.6
  • 35
    • 0023140474 scopus 로고
    • Ubiquitin is a component of paired helical filaments in Alzheimer's disease
    • H. Mori, J. Kondo, and Y. Ihara Ubiquitin is a component of paired helical filaments in Alzheimer's disease Science 235 1987 1641 1644
    • (1987) Science , vol.235 , pp. 1641-1644
    • Mori, H.1    Kondo, J.2    Ihara, Y.3
  • 36
    • 0026053022 scopus 로고
    • Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51
    • M. Novak, R. Jakes, P.C. Edwards, C. Milstein, and C.M. Wischik Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51 Proc. Natl. Acad. Sci. U. S. A. 88 1991 5837 5841
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 5837-5841
    • Novak, M.1    Jakes, R.2    Edwards, P.C.3    Milstein, C.4    Wischik, C.M.5
  • 37
    • 0028065142 scopus 로고
    • Analysis of microtubule-associated protein tau glycation in paired helical filaments
    • M.D. Ledesma, P. Bonay, C. Colaco, and J. Avila Analysis of microtubule-associated protein tau glycation in paired helical filaments J. Biol. Chem. 269 1994 21614 21619
    • (1994) J. Biol. Chem. , vol.269 , pp. 21614-21619
    • Ledesma, M.D.1    Bonay, P.2    Colaco, C.3    Avila, J.4
  • 39
    • 0029114196 scopus 로고
    • Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments
    • O. Schweers, E.M. Mandelkow, J. Biernat, and E. Mandelkow Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments Proc. Natl. Acad. Sci. U. S. A. 92 1995 8463 8467
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 8463-8467
    • Schweers, O.1    Mandelkow, E.M.2    Biernat, J.3    Mandelkow, E.4
  • 41
    • 0029037264 scopus 로고
    • Degenerative and protective signaling mechanisms in the neurofibrillary pathology of AD
    • M.P. Mattson Degenerative and protective signaling mechanisms in the neurofibrillary pathology of AD Neurobiol. Aging 16 1995 447 457
    • (1995) Neurobiol. Aging , vol.16 , pp. 447-457
    • Mattson, M.P.1
  • 42
    • 0035060129 scopus 로고    scopus 로고
    • PHF and PHF-like fibrils-cause or consequence?
    • Y. Ihara PHF and PHF-like fibrils-cause or consequence? Neurobiol. Aging 22 2001 123 126
    • (2001) Neurobiol. Aging , vol.22 , pp. 123-126
    • Ihara, Y.1
  • 44
    • 0036955813 scopus 로고    scopus 로고
    • Neuron loss from the hippocampus of Alzheimer's disease exceeds extracellular neurofibrillary tangle formation
    • J.J. Kril, S. Patel, A.J. Harding, and G.M. Halliday Neuron loss from the hippocampus of Alzheimer's disease exceeds extracellular neurofibrillary tangle formation Acta Neuropathol. (Berl.) 103 2002 370 376
    • (2002) Acta Neuropathol. (Berl.) , vol.103 , pp. 370-376
    • Kril, J.J.1    Patel, S.2    Harding, A.J.3    Halliday, G.M.4
  • 45
    • 0034920836 scopus 로고    scopus 로고
    • Relationship between DNA fragmentation, morphological changes and neuronal loss in Alzheimer's disease and dementia with Lewy bodies
    • M. Broe, C.E. Shepherd, E.A. Milward, and G.M. Halliday Relationship between DNA fragmentation, morphological changes and neuronal loss in Alzheimer's disease and dementia with Lewy bodies Acta Neuropathol. (Berl.) 101 2001 616 624
    • (2001) Acta Neuropathol. (Berl.) , vol.101 , pp. 616-624
    • Broe, M.1    Shepherd, C.E.2    Milward, E.A.3    Halliday, G.M.4
  • 46
    • 0033964859 scopus 로고    scopus 로고
    • In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: A central role for bound transition metals
    • L.M. Sayre, G. Perry, P.L.R. Harris, Y. Liu, K.A. Schubert, and M.A. Smith In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: a central role for bound transition metals J. Neurochem. 74 2000 270 279
    • (2000) J. Neurochem. , vol.74 , pp. 270-279
    • Sayre, L.M.1    Perry, G.2    Harris, P.L.R.3    Liu, Y.4    Schubert, K.A.5    Smith, M.A.6
  • 49
    • 0034797352 scopus 로고    scopus 로고
    • Differential activation of neuronal ERK, JNK/SAPK and p38 in Alzheimer disease: The "two hit" hypothesis
    • X. Zhu, R.J. Castellani, A. Takeda, A. Nunomura, C.S. Atwood, G. Perry, and M.A. Smith Differential activation of neuronal ERK, JNK/SAPK and p38 in Alzheimer disease: the "two hit" hypothesis Mech. Ageing Dev. 123 2001 39 46
    • (2001) Mech. Ageing Dev. , vol.123 , pp. 39-46
    • Zhu, X.1    Castellani, R.J.2    Takeda, A.3    Nunomura, A.4    Atwood, C.S.5    Perry, G.6    Smith, M.A.7
  • 50
    • 0037380952 scopus 로고    scopus 로고
    • JKK1, an upstream activator of JNK/SAPK, is activated in Alzheimer's disease
    • X. Zhu, O. Ogawa, Y. Wang, G. Perry, and M.A. Smith JKK1, an upstream activator of JNK/SAPK, is activated in Alzheimer's disease J. Neurochem. 85 2003 87 93
    • (2003) J. Neurochem. , vol.85 , pp. 87-93
    • Zhu, X.1    Ogawa, O.2    Wang, Y.3    Perry, G.4    Smith, M.A.5
  • 53
    • 0036752026 scopus 로고    scopus 로고
    • The p38 pathway is activated in Pick disease and progressive supranuclear palsy: A mechanistic link between mitogenic pathways, oxidative stress, and tau
    • A.W. Hartzler, X. Zhu, S.L. Siedlak, R.J. Castellani, J. Avilá, G. Perry, and M.A. Smith The p38 pathway is activated in Pick disease and progressive supranuclear palsy: a mechanistic link between mitogenic pathways, oxidative stress, and tau Neurobiol. Aging 23 2002 855 859
    • (2002) Neurobiol. Aging , vol.23 , pp. 855-859
    • Hartzler, A.W.1    Zhu, X.2    Siedlak, S.L.3    Castellani, R.J.4    Avilá, J.5    Perry, G.6    Smith, M.A.7
  • 55
    • 0024550480 scopus 로고
    • Immunoaffinity demonstration that paired helical filaments of Alzheimer disease share epitopes with neurofilaments, MAP2 and tau
    • P. Mulvihill, and G. Perry Immunoaffinity demonstration that paired helical filaments of Alzheimer disease share epitopes with neurofilaments, MAP2 and tau Brain Res. 484 1989 150 156
    • (1989) Brain Res. , vol.484 , pp. 150-156
    • Mulvihill, P.1    Perry, G.2
  • 56
    • 0032482231 scopus 로고    scopus 로고
    • Absence of the mid-sized neurofilament subunit decreases axonal calibres, levels of light neurofilament (NF-L), and neurofilament content
    • G.A. Elder, V.L. Friedrich Jr., P. Bosco, C. Kang, A. Gourov, P.H. Tu, V.M. Lee, and R.A. Lazzarini Absence of the mid-sized neurofilament subunit decreases axonal calibres, levels of light neurofilament (NF-L), and neurofilament content J. Cell Biol. 141 1998 727 739
    • (1998) J. Cell Biol. , vol.141 , pp. 727-739
    • Elder, G.A.1    Friedrich Jr., V.L.2    Bosco, P.3    Kang, C.4    Gourov, A.5    Tu, P.H.6    Lee, V.M.7    Lazzarini, R.A.8
  • 57
    • 0032487499 scopus 로고    scopus 로고
    • Neurofilament-dependent radial growth of motor axons and axonal organization of neurofilaments does not require the neurofilament heavy subunit (NF-H) or its phosphorylation
    • M.V. Rao, M.K. Houseweart, T.L. Williamson, T.O. Crawford, J. Folmer, and D.W. Cleveland Neurofilament-dependent radial growth of motor axons and axonal organization of neurofilaments does not require the neurofilament heavy subunit (NF-H) or its phosphorylation J. Cell Biol. 143 1998 171 181
    • (1998) J. Cell Biol. , vol.143 , pp. 171-181
    • Rao, M.V.1    Houseweart, M.K.2    Williamson, T.L.3    Crawford, T.O.4    Folmer, J.5    Cleveland, D.W.6


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