메뉴 건너뛰기




Volumn 2, Issue 9, 2000, Pages 628-636

Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN DEPOLYMERIZING FACTOR; COFILIN;

EID: 0034282106     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/35023579     Document Type: Article
Times cited : (308)

References (50)
  • 1
    • 0030668817 scopus 로고    scopus 로고
    • Cerebral microischemia as a potential precipitant of the neurodegenerative cascade of Alzheimer's disease
    • Richarson, J. S. Cerebral microischemia as a potential precipitant of the neurodegenerative cascade of Alzheimer's disease. Annls N.Y. Acad. Sci. 826, 437-439 (1997).
    • (1997) Annls N.Y. Acad. Sci. , vol.826 , pp. 437-439
    • Richarson, J.S.1
  • 2
    • 0032504657 scopus 로고    scopus 로고
    • Role of mitochondria in oxidative stress and aging
    • Lenaz, G. Role of mitochondria in oxidative stress and aging. Biochim. Biophys. Acta 1366, 53-67 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 53-67
    • Lenaz, G.1
  • 3
    • 0032504708 scopus 로고    scopus 로고
    • Mitochondria and neuronal glutamate excitotoxicity
    • Nicholls, D. G. & Budd, S. L. Mitochondria and neuronal glutamate excitotoxicity. Biochim. Biophys. Acta 1366, 97-112 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 97-112
    • Nicholls, D.G.1    Budd, S.L.2
  • 4
    • 0031776586 scopus 로고    scopus 로고
    • Cytochemical demonstration of oxidative damage in Alzheimer disease by immunochemical enhancement of the carbonyl reaction with 2,4-dinitrophenylhydrazine
    • Smith, M. A. et al. Cytochemical demonstration of oxidative damage in Alzheimer disease by immunochemical enhancement of the carbonyl reaction with 2,4-dinitrophenylhydrazine. J. Histochem. Cytochem. 46, 731-735 (1998).
    • (1998) J. Histochem. Cytochem. , vol.46 , pp. 731-735
    • Smith, M.A.1
  • 5
    • 0032504622 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in neurodegenerative disorders
    • Schapira, A. H. V. Mitochondrial dysfunction in neurodegenerative disorders. Biochim. Biophys. Acta 1366, 225-233 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 225-233
    • Schapira, A.H.V.1
  • 6
    • 0029821150 scopus 로고    scopus 로고
    • Preserved neuron number in the hippocampus of aged rats with spatial learning deficits
    • Rapp, P. R. & Gallagher, M. Preserved neuron number in the hippocampus of aged rats with spatial learning deficits. Proc. Natl Acad. Sci. USA 93, 9926-9930 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 9926-9930
    • Rapp, P.R.1    Gallagher, M.2
  • 7
    • 0030053883 scopus 로고    scopus 로고
    • Memory impaired aged rats. No loss of principal hippocampal and subicular neurons
    • Rasmussen, T., Schliemann, T., Sorensen, J. C., Zimmer, J. & West, M. J. Memory impaired aged rats. No loss of principal hippocampal and subicular neurons. Neurobiol. Aging 17, 143-147 (1996).
    • (1996) Neurobiol. Aging , vol.17 , pp. 143-147
    • Rasmussen, T.1    Schliemann, T.2    Sorensen, J.C.3    Zimmer, J.4    West, M.J.5
  • 8
    • 0024364877 scopus 로고
    • Immunohistochemical quantification of the synapse-related protein synaptophysin in Alzheimer disease
    • Masliah, E., Terry, R. D., DeTeresa, R. M. & Hansen, L. A. Immunohistochemical quantification of the synapse-related protein synaptophysin in Alzheimer disease. Neurosci. Lett. 103, 234-239 (1989).
    • (1989) Neurosci. Lett. , vol.103 , pp. 234-239
    • Masliah, E.1    Terry, R.D.2    DeTeresa, R.M.3    Hansen, L.A.4
  • 9
    • 0033366384 scopus 로고    scopus 로고
    • Slowing of axonal transport is a very early event in the toxicity of ALS-linked sod1 mutants to motor neurons
    • Williamson, T. L. & Cleveland, D.W. Slowing of axonal transport is a very early event in the toxicity of ALS-linked SOD1 mutants to motor neurons. Nature Neurosci. 2, 50-56 (1999).
    • (1999) Nature Neurosci. , vol.2 , pp. 50-56
    • Williamson, T.L.1    Cleveland, D.W.2
  • 10
    • 0034089887 scopus 로고    scopus 로고
    • Human tau filaments induce microtubule and synapse loss in an in vivo model of neurofibrillary degenerative disease
    • Hall, G. F., Chu, B., Lee, G & Yao, J. Human tau filaments induce microtubule and synapse loss in an in vivo model of neurofibrillary degenerative disease. J. Cell Sci. 113, 1373-1387 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 1373-1387
    • Hall, G.F.1    Chu, B.2    Lee, G.3    Yao, J.4
  • 11
    • 0033853360 scopus 로고    scopus 로고
    • Regulating actin filament dynamics in neuronal growth cones by ADF/cofilin and rho family GTPases
    • Kuhn, T. B. et al. Regulating actin filament dynamics in neuronal growth cones by ADF/cofilin and rho family GTPases. J. Neurobiol. 44, 126-144 (2000).
    • (2000) J. Neurobiol. , vol.44 , pp. 126-144
    • Kuhn, T.B.1
  • 12
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • Bamburg, J.R. Proteins of the ADF/cofilin family: essential regulators of actin dynamics. Annu. Rev. Cell Dev. Biol. 15, 185-230 (1999).
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 13
    • 0033060250 scopus 로고    scopus 로고
    • Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments
    • Blanchoin, L. & Pollard, T.D. Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments. J. Biol. Chem. 274, 15538-15546 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 15538-15546
    • Blanchoin, L.1    Pollard, T.D.2
  • 14
    • 0033588258 scopus 로고    scopus 로고
    • ADF/Cofilin weakens lateral contacts in the actin filament
    • McGough, A. & Chiu, W. ADF/Cofilin weakens lateral contacts in the actin filament. J. Mol. Biol. 291, 513-519 (1999).
    • (1999) J. Mol. Biol. , vol.291 , pp. 513-519
    • McGough, A.1    Chiu, W.2
  • 15
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • Carlier, M-F. et al. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J. Cell Biol. 136, 1307-1322 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 1307-1322
    • Carlier, M.-F.1
  • 16
    • 0034113924 scopus 로고    scopus 로고
    • Actin filaments are severed by both native and recombinant Dictyostelium cofilin but to different extents
    • Ichetovkin, I., Han, J., Pang, K.M., Knecht, D.A. & Condeelis, J.S. Actin filaments are severed by both native and recombinant Dictyostelium cofilin but to different extents. Cell Motil. Cytoskel. 45, 293-306 (2000).
    • (2000) Cell Motil. Cytoskel. , vol.45 , pp. 293-306
    • Ichetovkin, I.1    Han, J.2    Pang, K.M.3    Knecht, D.A.4    Condeelis, J.S.5
  • 17
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • McGough, A., Pope, B., Chiu, W. & Weeds, A. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J. Cell Biol. 138, 771-781 (1997).
    • (1997) J. Cell Biol. , vol.138 , pp. 771-781
    • McGough, A.1    Pope, B.C.W.2    Weeds, A.3
  • 18
    • 0032565962 scopus 로고    scopus 로고
    • Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase
    • Arber, S. et al. Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase. Nature 393, 805-809 (1998).
    • (1998) Nature , vol.393 , pp. 805-809
    • Arber, S.1
  • 19
    • 0032565769 scopus 로고    scopus 로고
    • Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
    • Yang, N. et al. Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature 393, 809-812 (1998).
    • (1998) Nature , vol.393 , pp. 809-812
    • Yang, N.1
  • 20
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. Rho GTPases and the actin cytoskeleton. Science 279, 509-514 (1998).
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 21
    • 0031952055 scopus 로고    scopus 로고
    • Actin depolymerizing factor and cofilin phosphorylation dynamics: Response to signals that regulate neurite extension
    • Meberg, P.J., Ono, S., Minamide, L.S., Takahashi, M. & Bamburg, J.R. Actin depolymerizing factor and cofilin phosphorylation dynamics: response to signals that regulate neurite extension. Cell Motil. Cytoskel. 39, 172-190 (1998).
    • (1998) Cell Motil. Cytoskel. , vol.39 , pp. 172-190
    • Meberg, P.J.1    Ono, S.2    Minamide, L.S.3    Takahashi, M.4    Bamburg, J.R.5
  • 22
    • 0023387681 scopus 로고
    • Cofilin is a component of intranuclear and cytoplasmic rods induced in cultured cells
    • Nishida, E., Iida, K., Yonezawa, N., Koyasu, I. & Sakai, H. Cofilin is a component of intranuclear and cytoplasmic rods induced in cultured cells. Proc. Natl Acad. Sci. USA 84, 5262-5266 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 5262-5266
    • Nishida, E.1    Iida, K.2    Yonezawa, N.3    Koyasu, I.4    Sakai, H.5
  • 23
    • 0018938686 scopus 로고
    • Destruction of microfilament bundles in mouse embryo fibroblasts treated with inhibitors of energy metabolism
    • Bershadsky, A.D., Gelfand, V.I., Svitkina, T.M. & Tint, I.S. Destruction of microfilament bundles in mouse embryo fibroblasts treated with inhibitors of energy metabolism. Exp. Cell Res. 127, 421-429 (1980).
    • (1980) Exp. Cell Res. , vol.127 , pp. 421-429
    • Bershadsky, A.D.1    Gelfand, V.I.2    Svitkina, T.M.3    Tint, I.S.4
  • 24
    • 0033608731 scopus 로고    scopus 로고
    • A quantitative analysis of G-actin binding proteins and the G-actin pool in developing chick brain
    • Devineni, N. et al. A quantitative analysis of G-actin binding proteins and the G-actin pool in developing chick brain. Brain Res. 823, 129-140 (1999).
    • (1999) Brain Res. , vol.823 , pp. 129-140
    • Devineni, N.1
  • 25
  • 26
    • 0032520191 scopus 로고    scopus 로고
    • Heterogeneity in the molecular composition of excitatory postsynaptic sites during development of hippocampal neurons in culture
    • Rao, A., Kim, E., Shang, M. & Craig, A.M. Heterogeneity in the molecular composition of excitatory postsynaptic sites during development of hippocampal neurons in culture. J. Neurosci. 18, 1217-1229 (1998).
    • (1998) J. Neurosci. , vol.18 , pp. 1217-1229
    • Rao, A.1    Kim, E.2    Shang, M.3    Craig, A.M.4
  • 27
    • 0027226219 scopus 로고
    • Optimized survival of hippocampal neurons in B27-supplemented neurobasal, a new serum-free medium combination
    • Brewer, G.J., Torricelli, J.R., Evege, E.K. & Price, P.J. Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination. J. Neurosci. Res. 35, 567-576 (1993).
    • (1993) J. Neurosci. Res. , vol.35 , pp. 567-576
    • Brewer, G.J.1    Torricelli, J.R.2    Evege, E.K.3    Price, P.J.4
  • 28
    • 0027686249 scopus 로고
    • Oxidative stress, glutamate and neurodegenerative disorders
    • Coyle, J.T. & Puttfarcken, P. Oxidative stress, glutamate and neurodegenerative disorders. Science 262, 689-695 (1993).
    • (1993) Science , vol.262 , pp. 689-695
    • Coyle, J.T.1    Puttfarcken, P.2
  • 29
    • 0038233014 scopus 로고    scopus 로고
    • Nitric oxide-mediated mitochondrial damage in the brain: Mechanisms and implications for neurodegenerative diseases
    • Bolanos, J.P. et al. Nitric oxide-mediated mitochondrial damage in the brain: mechanisms and implications for neurodegenerative diseases. J. Neurochem. 68, 2227-2240 (1997).
    • (1997) J. Neurochem. , vol.68 , pp. 2227-2240
    • Bolanos, J.P.1
  • 30
    • 0034175588 scopus 로고    scopus 로고
    • Increase in neurite outgrowth mediated by overexpression of actin depolymerizing factor
    • Meberg, P.J. & Bamburg, J.R. Increase in neurite outgrowth mediated by overexpression of actin depolymerizing factor. J. Neurosci. 20, 2459-2469 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 2459-2469
    • Meberg, P.J.1    Bamburg, J.R.2
  • 32
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease and oxidative stress
    • Berlett, B.B. & Stadtman, E.R. Protein oxidation in aging, disease and oxidative stress. J. Biol. Chem. 272, 20313-20316 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.B.1    Stadtman, E.R.2
  • 33
    • 0030008721 scopus 로고    scopus 로고
    • Assessment of the role of the glutathione and pentose phosphate pathways in the protection of primary cerebrocortical cultures from oxidative stress
    • Ben-Yoseph, O., Boxer, P.A. & Ross, B.D. Assessment of the role of the glutathione and pentose phosphate pathways in the protection of primary cerebrocortical cultures from oxidative stress. J. Neurochem. 66, 2329-2337 (1996).
    • (1996) J. Neurochem. , vol.66 , pp. 2329-2337
    • Ben-Yoseph, O.1    Boxer, P.A.2    Ross, B.D.3
  • 34
    • 0018428638 scopus 로고
    • Nuclear actin bundles in Amoeba, Dictyostelium and human HeLa cells induced by dimethyl sulfoxide
    • Fukui, Y. & Katsumaru, H. Nuclear actin bundles in Amoeba, Dictyostelium and human HeLa cells induced by dimethyl sulfoxide. Exp. Cell Res. 120, 452-455 (1979).
    • (1979) Exp. Cell Res. , vol.120 , pp. 452-455
    • Fukui, Y.1    Katsumaru, H.2
  • 35
    • 0033560132 scopus 로고    scopus 로고
    • Myelin and collapsin-1 induce motor neuron growth cone collapse through different pathways: Inhibition of collapse by opposing mutants of rac1
    • Kuhn, T.B., Brown, M.D., Wilcox, C.L., Raper, J.A. & Bamburg, J.R. Myelin and collapsin-1 induce motor neuron growth cone collapse through different pathways: inhibition of collapse by opposing mutants of rac1. J. Neurosci. 19, 1965-1975 (1999).
    • (1999) J. Neurosci. , vol.19 , pp. 1965-1975
    • Kuhn, T.B.1    Brown, M.D.2    Wilcox, C.L.3    Raper, J.A.4    Bamburg, J.R.5
  • 36
    • 0032495144 scopus 로고    scopus 로고
    • Striation is the characteristic neuritic abnormality in Alzheimer disease
    • Velasco, M.E., Smith, M.A., Siedlak, S.L., Nunomura, A. & Perry, G. Striation is the characteristic neuritic abnormality in Alzheimer disease. Brain Res. 813, 329-333 (1998).
    • (1998) Brain Res. , vol.813 , pp. 329-333
    • Velasco, M.E.1    Smith, M.A.2    Siedlak, S.L.3    Nunomura, A.4    Perry, G.5
  • 37
    • 0027439319 scopus 로고
    • The interaction of human actin depolymerizing factor with actin is pH regulated
    • Hawkins, M., Pope, B., Maciver, S.K. & Weeds, A.G. The interaction of human actin depolymerizing factor with actin is pH regulated. Biochemistry 32, 9985-9993 (1993).
    • (1993) Biochemistry , vol.32 , pp. 9985-9993
    • Hawkins, M.1    Pope, B.2    Maciver, S.K.3    Weeds, A.G.4
  • 38
    • 0021964668 scopus 로고
    • Opposite effects of cofilin and profilin from porcine brain on rate of exchange of actin-bound adenosine 5'-triphosphate
    • Nishida, E. Opposite effects of cofilin and profilin from porcine brain on rate of exchange of actin-bound adenosine 5'-triphosphate. Biochemistry 24, 1160-1164 (1985).
    • (1985) Biochemistry , vol.24 , pp. 1160-1164
    • Nishida, E.1
  • 40
    • 0032749566 scopus 로고    scopus 로고
    • Differential expression of multiple trans-glutaminases in human brain. Increased expression and cross-linking by transglutaminases 1 and 2 in Alzheimer's disease
    • Kim, S-Y., Grant, P., Lee, J-H., Pant, H.C. & Steinert, P.M. Differential expression of multiple trans-glutaminases in human brain. Increased expression and cross-linking by transglutaminases 1 and 2 in Alzheimer's disease. J. Biol. Chem. 274, 30715-30721 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 30715-30721
    • Kim, S.-Y.1    Grant, P.2    Lee, J.-H.3    Pant, H.C.4    Steinert, P.M.5
  • 41
    • 0030827975 scopus 로고    scopus 로고
    • Reactive oxygen species and Alzheimer's disease
    • Multhaup, G. et al. Reactive oxygen species and Alzheimer's disease. Biochem. Pharmacol. 54, 533-539 (1997).
    • (1997) Biochem. Pharmacol. , vol.54 , pp. 533-539
    • Multhaup, G.1
  • 42
    • 0028803993 scopus 로고
    • Two actin binding proteins, actin depolymerizing factor and cofilin, are associated with Hirano bodies
    • Maciver, S.K. & Harrington, C.R. Two actin binding proteins, actin depolymerizing factor and cofilin, are associated with Hirano bodies. Neuroreport 6, 1985-1988 (1995).
    • (1995) Neuroreport , vol.6 , pp. 1985-1988
    • Maciver, S.K.1    Harrington, C.R.2
  • 43
    • 0028286860 scopus 로고
    • Hirano bodies and related neuronal inclusions
    • Hirano, A. Hirano bodies and related neuronal inclusions. Neuropathol. Appl. Neurobiol. 20, 3-11 (1994).
    • (1994) Neuropathol. Appl. Neurobiol. , vol.20 , pp. 3-11
    • Hirano, A.1
  • 44
    • 0015398272 scopus 로고
    • Intranuclear rods and sheets in rat cochlear nucleus
    • Feldman, M.L. & Peters, A. Intranuclear rods and sheets in rat cochlear nucleus. J. Neurol. 1, 109-127 (1972).
    • (1972) J. Neurol. , vol.1 , pp. 109-127
    • Feldman, M.L.1    Peters, A.2
  • 45
    • 13044287361 scopus 로고    scopus 로고
    • Plaque-independent disruption of neuronal circuits in Alzheimer's disease mouse models
    • Hsia, A.Y. et al. Plaque-independent disruption of neuronal circuits in Alzheimer's disease mouse models. Proc. Natl Acad. Sci. USA 96, 3228-3233 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3228-3233
    • Hsia, A.Y.1
  • 46
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl, C., Davis, J.B., Lesley, R. & Schubart, D. Hydrogen peroxide mediates amyloid β protein toxicity. Cell 77, 817-827 (1994).
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubart, D.4
  • 47
    • 0021629684 scopus 로고
    • An electron microscopic study of the development of axons and dendrites by hippocampal neurons in culture. I. Cells which develop without intercellular contacts
    • Bartlett, W.P. & Banker, G.A. An electron microscopic study of the development of axons and dendrites by hippocampal neurons in culture. I. Cells which develop without intercellular contacts. J. Neurosci. 4, 1944-1953 (1984).
    • (1984) J. Neurosci. , vol.4 , pp. 1944-1953
    • Bartlett, W.P.1    Banker, G.A.2
  • 48
    • 0023798578 scopus 로고
    • Isolated hippocampal neurons in cryopreserved long-term cultures: Development of neuroarchitecture and sensitivity to NMDA
    • Mattson, M.P. & Kater, S.B. Isolated hippocampal neurons in cryopreserved long-term cultures: development of neuroarchitecture and sensitivity to NMDA. Int. J. Dev. Neurosci. 6, 439-452 (1988).
    • (1988) Int. J. Dev. Neurosci. , vol.6 , pp. 439-452
    • Mattson, M.P.1    Kater, S.B.2
  • 49
    • 0025108764 scopus 로고
    • Sequence of cDNAs encoding actin depolymerizing factor and cofilin of embryonic chicken skeletal muscle: Two functionally distinct actin-regulatory proteins exhibit high structural homology
    • Abe, H., Endo, T., Yamamoto, K. & Obinata, T. Sequence of cDNAs encoding actin depolymerizing factor and cofilin of embryonic chicken skeletal muscle: two functionally distinct actin-regulatory proteins exhibit high structural homology. Biochemistry 29, 7420-7425 (1990).
    • (1990) Biochemistry , vol.29 , pp. 7420-7425
    • Abe, H.1    Endo, T.2    Yamamoto, K.3    Obinata, T.4
  • 50
    • 0021211607 scopus 로고
    • Morphology and distribution of Alzheimer neuritic (senile) and amyloid plaques in striatum and diencephalon
    • Rudelli, R.D., Ambler, M.W. & Wisniewski, H.M. Morphology and distribution of Alzheimer neuritic (senile) and amyloid plaques in striatum and diencephalon. Acta Neuropathol. 64, 273-281 (1984).
    • (1984) Acta Neuropathol. , vol.64 , pp. 273-281
    • Rudelli, R.D.1    Ambler, M.W.2    Wisniewski, H.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.