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Volumn 66, Issue 1, 1996, Pages 286-295

Changes in phosphorylation of τ during ischemia and reperfusion in the rabbit spinal cord

Author keywords

Cytoskeleton; Ischemia; Rabbit spinal cord; Reperfusion; Stroke;

Indexed keywords

ANIMAL TISSUE; ARTICLE; CALCIUM CELL LEVEL; DEPHOSPHORYLATION; ENZYME ACTIVITY; ISCHEMIA; LUMBAR SPINE; MICROTUBULE ASSEMBLY; NERVE CELL PLASTICITY; NERVE FIBER GROWTH; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; REPERFUSION INJURY; SPINAL CORD;

EID: 0030033901     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.66010286.x     Document Type: Article
Times cited : (34)

References (51)
  • 1
    • 0023630392 scopus 로고
    • Phosphorylation of tau proteins to a state like that in Alzheimer's brain is catalyzed by a calcium/calmodulin-dependent kinase and modulated by phospholipids
    • Baudier J. and Cole R. D. (1987) Phosphorylation of tau proteins to a state like that in Alzheimer's brain is catalyzed by a calcium/calmodulin-dependent kinase and modulated by phospholipids. J. Biol. Chem. 262, 17577-17583.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17577-17583
    • Baudier, J.1    Cole, R.D.2
  • 3
    • 0027338266 scopus 로고
    • 262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding
    • 262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding. Neuron 11, 153-163.
    • (1993) Neuron , vol.11 , pp. 153-163
    • Biemat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 4
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • Binder L. I., Frankfurter A., and Rebhun L. I. (1985) The distribution of tau in the mammalian central nervous system. J. Cell Biol. 101, 1371-1378.
    • (1985) J. Cell Biol. , vol.101 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 5
    • 0026578425 scopus 로고
    • Regions with abundant neurofibrillary pathology in human brain exhibit a selective reduction in levels of binding-competent τ and accumulation of abnormal τ-isoforms (A68 proteins)
    • Bramblett G. L., Trojanowski J. Q., and Lee V. M. (1992) Regions with abundant neurofibrillary pathology in human brain exhibit a selective reduction in levels of binding-competent τ and accumulation of abnormal τ-isoforms (A68 proteins). Lab. Invest. 66, 212-222.
    • (1992) Lab. Invest. , vol.66 , pp. 212-222
    • Bramblett, G.L.1    Trojanowski, J.Q.2    Lee, V.M.3
  • 6
    • 0028945978 scopus 로고
    • Activation of a neurofilament kinase, a tau kinase, and a tau phosphatase by decreased ATP levels in nerve growth factor-differentiated PC-12 cells
    • Bush M. L., Miyashiro J. S., and Ingram V. M. (1995) Activation of a neurofilament kinase, a tau kinase, and a tau phosphatase by decreased ATP levels in nerve growth factor-differentiated PC-12 cells. Proc. Natl. Acad. Sci. USA 92, 1861-1865.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1861-1865
    • Bush, M.L.1    Miyashiro, J.S.2    Ingram, V.M.3
  • 7
    • 0026730122 scopus 로고
    • Tyrosine phosphorylation of microtubule-associated protein kinase after transient ischemia in the gerbil brain
    • Campos-González R. and Kindy M. S. (1992) Tyrosine phosphorylation of microtubule-associated protein kinase after transient ischemia in the gerbil brain. J. Neurochem. 59, 1955-1958.
    • (1992) J. Neurochem. , vol.59 , pp. 1955-1958
    • Campos-González, R.1    Kindy, M.S.2
  • 8
    • 0027443741 scopus 로고
    • Reversible heat stress-related loss of phosphorylated Alzheimer-type epitopes in tau proteins of human neuroblastoma cells
    • Chiang M. F., Liu W.-K., and Yen S.-H. (1993) Reversible heat stress-related loss of phosphorylated Alzheimer-type epitopes in tau proteins of human neuroblastoma cells. J. Neurosci. 13, 4854-4860.
    • (1993) J. Neurosci. , vol.13 , pp. 4854-4860
    • Chiang, M.F.1    Liu, W.-K.2    Yen, S.-H.3
  • 10
    • 0027359805 scopus 로고
    • Alz-50 and ubiquitin immunoreactivity is induced by permanent focal cerebral ischaemia in the cat
    • Dewar D., Graham D. I., Teasdale G. M., and McCulloch J. (1993) Alz-50 and ubiquitin immunoreactivity is induced by permanent focal cerebral ischaemia in the cat. Acta Neuropathol. 86, 623-629.
    • (1993) Acta Neuropathol. , vol.86 , pp. 623-629
    • Dewar, D.1    Graham, D.I.2    Teasdale, G.M.3    McCulloch, J.4
  • 11
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • Drechsel D. N., Hyman A. A., Cobb M. H., and Kirschner M. W. (1992) Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol. Biol. Cell 3, 1141-1154.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 13
    • 0027309252 scopus 로고
    • Corticosterone exacerbates kainate-induced alterations in hippocampal tau immunoreactivity and spectrin proteolysis in vivo
    • Elliott E. M., Mattson M. P., Vanderklish P., Lynch G., Chang I., and Sapolsky R. M. (1993) Corticosterone exacerbates kainate-induced alterations in hippocampal tau immunoreactivity and spectrin proteolysis in vivo. J. Neurochem. 61, 57-67.
    • (1993) J. Neurochem. , vol.61 , pp. 57-67
    • Elliott, E.M.1    Mattson, M.P.2    Vanderklish, P.3    Lynch, G.4    Chang, I.5    Sapolsky, R.M.6
  • 15
    • 0028321947 scopus 로고
    • Alterations in τ immunostaining in the rat hippocampus following transient cerebral ischemia
    • Geddes J. W., Schwab C., Craddock S., Wilson J. L., and Pettigrew L. C. (1994) Alterations in τ immunostaining in the rat hippocampus following transient cerebral ischemia. J. Cereb. Blood Flow Metab. 14, 554-564.
    • (1994) J. Cereb. Blood Flow Metab. , vol.14 , pp. 554-564
    • Geddes, J.W.1    Schwab, C.2    Craddock, S.3    Wilson, J.L.4    Pettigrew, L.C.5
  • 16
    • 0027264771 scopus 로고
    • Expression of high molecular weight tau in the central and peripheral nervous systems
    • Georgieff I. S., Liem R. K., Couchic D., Mavilia C., Nunez J., and Shelanski M. L. (1993) Expression of high molecular weight tau in the central and peripheral nervous systems. J. Cell Sci. 105, 729-737.
    • (1993) J. Cell Sci. , vol.105 , pp. 729-737
    • Georgieff, I.S.1    Liem, R.K.2    Couchic, D.3    Mavilia, C.4    Nunez, J.5    Shelanski, M.L.6
  • 17
    • 0025853691 scopus 로고
    • Localization of the Alz-50 epitope in recombinant human microtubule-associated protein tau
    • Goedert M., Spillantini M. G., and Jakes R. (1991) Localization of the Alz-50 epitope in recombinant human microtubule-associated protein tau. Neurosci. Lett. 126, 149-154.
    • (1991) Neurosci. Lett. , vol.126 , pp. 149-154
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3
  • 18
    • 0026512915 scopus 로고
    • Cloning of a big tau microtubule-associated protein characteristic of the peripheral nervous system
    • Goedert M., Spillantini M. G., and Crowther R. A. (1992) Cloning of a big tau microtubule-associated protein characteristic of the peripheral nervous system. Proc. Natl. Acad. Sci. USA 89, 1983-1987.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1983-1987
    • Goedert, M.1    Spillantini, M.G.2    Crowther, R.A.3
  • 20
    • 0028118917 scopus 로고
    • Microtubule organization and dynamics dependent on microtubule-associated proteins
    • Hirokawa N. (1994) Microtubule organization and dynamics dependent on microtubule-associated proteins. Curr. Opin. Cell Biol. 6, 74-81.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 74-81
    • Hirokawa, N.1
  • 21
    • 0028353865 scopus 로고
    • Tyrosine phosphorylation and activation of mitogen-activated protein kinase in the rat brain following transient cerebral ischemia
    • Hu B.-R. and Wieloch T. (1994) Tyrosine phosphorylation and activation of mitogen-activated protein kinase in the rat brain following transient cerebral ischemia. J. Neurochem. 62, 1357-1367.
    • (1994) J. Neurochem. , vol.62 , pp. 1357-1367
    • Hu, B.-R.1    Wieloch, T.2
  • 23
    • 0028136879 scopus 로고
    • Heat shock proteins protect against stress-related phosphorylation of tau in neuronal PC12 cells that have acquired thermotolerance
    • Kirby B. A., Merril C. R., Ghanbari H., and Wallace W. C. (1994) Heat shock proteins protect against stress-related phosphorylation of tau in neuronal PC12 cells that have acquired thermotolerance. J. Neurosci. 14, 5687-5693.
    • (1994) J. Neurosci. , vol.14 , pp. 5687-5693
    • Kirby, B.A.1    Merril, C.R.2    Ghanbari, H.3    Wallace, W.C.4
  • 25
    • 0024109687 scopus 로고
    • Epitopes that span the tau molecule are shared with paired helical filaments
    • Kosik K. S., Orecchio L. D., Binder L., Trojanowski J. Q., Lee V. M., and Lee G. (1988) Epitopes that span the tau molecule are shared with paired helical filaments. Neuron 1, 817-825.
    • (1988) Neuron , vol.1 , pp. 817-825
    • Kosik, K.S.1    Orecchio, L.D.2    Binder, L.3    Trojanowski, J.Q.4    Lee, V.M.5    Lee, G.6
  • 26
    • 0023626638 scopus 로고
    • Axonal disruption and aberrant localization of tau protein characterize the neuropil pathology of Alzheimer's disease
    • Kowall N. W. and Kosik K. S. (1987) Axonal disruption and aberrant localization of tau protein characterize the neuropil pathology of Alzheimer's disease. Ann. Neurol. 22, 639-643.
    • (1987) Ann. Neurol. , vol.22 , pp. 639-643
    • Kowall, N.W.1    Kosik, K.S.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli U. K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0025341754 scopus 로고
    • Tau protein: An update on structure and function
    • Lee G. (1990) Tau protein: an update on structure and function. Cell Motil. Cytoskeleton 15, 199-203.
    • (1990) Cell Motil. Cytoskeleton , vol.15 , pp. 199-203
    • Lee, G.1
  • 30
    • 0026941497 scopus 로고
    • The disordered neuronal cytoskeleton in Alzheimer's disease
    • Lee V. M. and Trojanowski J. Q. (1992) The disordered neuronal cytoskeleton in Alzheimer's disease. Curr. Opin. Neurobiol. 2, 653-656.
    • (1992) Curr. Opin. Neurobiol. , vol.2 , pp. 653-656
    • Lee, V.M.1    Trojanowski, J.Q.2
  • 31
    • 0028924918 scopus 로고
    • Neuronal cdc2-like kinase
    • Lew J. and Wang J. H. (1995) Neuronal cdc2-like kinase. Trends Biochem. Sci. 20, 33-37.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 33-37
    • Lew, J.1    Wang, J.H.2
  • 32
    • 0021338217 scopus 로고
    • Phosphorylation affects the ability of tau protein to promote microtubule assembly
    • Lindwall G. and Cole R. D. (1984) Phosphorylation affects the ability of tau protein to promote microtubule assembly. J. Biol. Chem. 259, 5301-5305.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5301-5305
    • Lindwall, G.1    Cole, R.D.2
  • 34
    • 0027376632 scopus 로고
    • Tau as a marker for Alzheimer's disease
    • Mandelkow E. and Mandelkow E. (1993) Tau as a marker for Alzheimer's disease. Trends Biochem. Sci. 18, 480-483.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 480-483
    • Mandelkow, E.1    Mandelkow, E.2
  • 35
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P. (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262, 10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 36
    • 0027945346 scopus 로고
    • Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau
    • Matsuo E. S., Shin R., Billingsley M. L., Van deVoorde A., O'Connor M., Trojanowski J. Q., and Lee V. M. (1994) Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau. Neuron 13, 989-1002.
    • (1994) Neuron , vol.13 , pp. 989-1002
    • Matsuo, E.S.1    Shin, R.2    Billingsley, M.L.3    Van DeVoorde, A.4    O'Connor, M.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 37
    • 0025273543 scopus 로고
    • 2+ influx in cultured hippocampal neurons
    • 2+ influx in cultured hippocampal neurons. Neuron 2, 105-117.
    • (1990) Neuron , vol.2 , pp. 105-117
    • Mattson, M.P.1
  • 38
    • 0026349379 scopus 로고
    • Effects of elevated intracellular calcium levels on the cytoskeleton and tau in cultured human cortical neurons
    • Mattson M. P., Engle M. G., and Rychlik B. (1991) Effects of elevated intracellular calcium levels on the cytoskeleton and tau in cultured human cortical neurons. Mol. Chem. Neuropathol. 15, 117-142.
    • (1991) Mol. Chem. Neuropathol. , vol.15 , pp. 117-142
    • Mattson, M.P.1    Engle, M.G.2    Rychlik, B.3
  • 40
    • 0028129138 scopus 로고
    • Compromised mitochondrial function results in dephosphorylation of tau through a calcium-dependent process in rat brain cerebral cortical slices
    • Norman S. G. P. and Johnson G. V. W. (1994) Compromised mitochondrial function results in dephosphorylation of tau through a calcium-dependent process in rat brain cerebral cortical slices. Neurochem. Res. 19, 1151-1158.
    • (1994) Neurochem. Res. , vol.19 , pp. 1151-1158
    • Norman, S.G.P.1    Johnson, G.V.W.2
  • 41
    • 0023505501 scopus 로고
    • Phosphorylation determines two distinct species of tau in the central nervous system
    • Papasozomenos S. C. and Binder L. I. (1987) Phosphorylation determines two distinct species of tau in the central nervous system. Cell Motil Cytoskeleton 8, 210-226.
    • (1987) Cell Motil Cytoskeleton , vol.8 , pp. 210-226
    • Papasozomenos, S.C.1    Binder, L.I.2
  • 42
    • 0025810513 scopus 로고
    • Altered phosphorylation of τ protein in heat-shocked rats and patients with Alzheimer disease
    • Papasozomenos S. C. and Su Y. (1991) Altered phosphorylation of τ protein in heat-shocked rats and patients with Alzheimer disease. Proc. Natl. Acad. Sci. USA 88, 4543-4547.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4543-4547
    • Papasozomenos, S.C.1    Su, Y.2
  • 43
    • 0027291906 scopus 로고
    • 2+/calmodutin-dependent protein kinase II following spinal cord ischemia
    • 2+/calmodutin-dependent protein kinase II following spinal cord ischemia. J. Neurochem. 61, 738-747.
    • (1993) J. Neurochem. , vol.61 , pp. 738-747
    • Shackelford, D.A.1    Yeh, R.2    Zivin, J.A.3
  • 44
    • 0028173843 scopus 로고
    • Glutamate increases tau phosphorylation in primary neuronal cultures from fetal rat cerebral cortex
    • Sindou P., Lesort M., Couratier P., Yardin C., Esclaire F., and Hugon J. (1994) Glutamate increases tau phosphorylation in primary neuronal cultures from fetal rat cerebral cortex. Brain Res. 646, 124-128.
    • (1994) Brain Res. , vol.646 , pp. 124-128
    • Sindou, P.1    Lesort, M.2    Couratier, P.3    Yardin, C.4    Esclaire, F.5    Hugon, J.6
  • 46
    • 0027388775 scopus 로고
    • Recognition of the minimal epitope of monoclonal antibody tau-1 depends upon the presence of a phosphate group but not its location
    • Szendrei G. I., Lee V. M., and Otvos L. Jr. (1993) Recognition of the minimal epitope of monoclonal antibody tau-1 depends upon the presence of a phosphate group but not its location. J. Neurosci. Res. 34, 243-249.
    • (1993) J. Neurosci. Res. , vol.34 , pp. 243-249
    • Szendrei, G.I.1    Lee, V.M.2    Otvos Jr., L.3
  • 47
    • 13344288373 scopus 로고
    • Phosphorylation/dephosphorylation of tau after heat shock in neuronal PC12 cells: Comparison of newly synthesized vs mature forms
    • Wallace W. C., Lyons W. E., Mamounas L. A., and Merril C. R. (1994) Phosphorylation/dephosphorylation of tau after heat shock in neuronal PC12 cells: comparison of newly synthesized vs mature forms. Soc. Neurosci. Abstr. 20, 648.
    • (1994) Soc. Neurosci. Abstr. , vol.20 , pp. 648
    • Wallace, W.C.1    Lyons, W.E.2    Mamounas, L.A.3    Merril, C.R.4
  • 49
    • 0025071270 scopus 로고
    • Differential vulnerability of microtubule components in cerebral ischemia
    • Yanagihara T., Brengman J. W., and Mushynski W. E. (1990) Differential vulnerability of microtubule components in cerebral ischemia. Acta Neuropathol. 80, 499-505.
    • (1990) Acta Neuropathol. , vol.80 , pp. 499-505
    • Yanagihara, T.1    Brengman, J.W.2    Mushynski, W.E.3
  • 50
    • 0022531680 scopus 로고
    • Studies of the influence of biogenic amines on central nervous system ischemia
    • Zivin J. A. and DeGirolami U. (1986) Studies of the influence of biogenic amines on central nervous system ischemia. Stroke 17, 509-516.
    • (1986) Stroke , vol.17 , pp. 509-516
    • Zivin, J.A.1    DeGirolami, U.2
  • 51
    • 0019942376 scopus 로고
    • A quantitative study of the spectrum of neurological deficits in experimental nervous system ischemia
    • Zivin J. A., DeGirolami U., and Hurwitz E. L. (1982) A quantitative study of the spectrum of neurological deficits in experimental nervous system ischemia. Arch. Neurol 39, 408-412.
    • (1982) Arch. Neurol , vol.39 , pp. 408-412
    • Zivin, J.A.1    DeGirolami, U.2    Hurwitz, E.L.3


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