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Volumn 72, Issue 3, 1999, Pages 1294-1306

Hypoxia/ischemia induces dephosphorylation of rat brain neuromodulin/GAP-43 in vivo

Author keywords

Dephosphorylation; In vivo phosphorylation sites; Ischemia hypoxia; Neuromodulin GAP 43; Oxidation

Indexed keywords

NEUROMODULIN;

EID: 0033011718     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1999.0721294.x     Document Type: Article
Times cited : (23)

References (49)
  • 1
    • 0028866034 scopus 로고
    • Overexpression of the neural growth-associated protein GAP-43 induces nerve sprouting in the adult nervous system of transgenic mice
    • Aigner L., Arher S., Kapfhammer J. P., Laux T., Schneider C., Botteri F., Brenner H. R., and Caroni P. (1995) Overexpression of the neural growth-associated protein GAP-43 induces nerve sprouting in the adult nervous system of transgenic mice. Cell 83, 269-278.
    • (1995) Cell , vol.83 , pp. 269-278
    • Aigner, L.1    Arher, S.2    Kapfhammer, J.P.3    Laux, T.4    Schneider, C.5    Botteri, F.6    Brenner, H.R.7    Caroni, P.8
  • 2
    • 0023519487 scopus 로고
    • Calcium-promoted translocation of protein kinase C to synaptic membranes: Relation to the phosphorylation of an endogenous substrate (protein F1) involved in synaptic plasticity
    • Akers R. F. and Routtenberg A. (1987) Calcium-promoted translocation of protein kinase C to synaptic membranes: relation to the phosphorylation of an endogenous substrate (protein F1) involved in synaptic plasticity. J. Neurosci. 7, 3976-3983.
    • (1987) J. Neurosci. , vol.7 , pp. 3976-3983
    • Akers, R.F.1    Routtenberg, A.2
  • 3
    • 0023644790 scopus 로고
    • Regulation of calmodulin binding to P-57. A neurospecific calmodulin binding protein
    • Alexander K. A., Cimler B. M., Meier K. E., and Storm D. R. (1987) Regulation of calmodulin binding to P-57. A neurospecific calmodulin binding protein. J. Biol. Chem. 262, 6108-6113.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6108-6113
    • Alexander, K.A.1    Cimler, B.M.2    Meier, K.E.3    Storm, D.R.4
  • 4
    • 0025239505 scopus 로고
    • Identification of the protein kinase C phosphorylation site in neuromodulin
    • Apel E. D., Byford M. F., Au D., Walsh K. A., and Storm D. R. (1990) Identification of the protein kinase C phosphorylation site in neuromodulin. Biochemistry 29, 2330-2335.
    • (1990) Biochemistry , vol.29 , pp. 2330-2335
    • Apel, E.D.1    Byford, M.F.2    Au, D.3    Walsh, K.A.4    Storm, D.R.5
  • 5
    • 0025883223 scopus 로고
    • Phosphorylation of neuromodulin (GAP-43) by casein kinase II. Identification of phosphorylation sites and regulation by calmodulin
    • Apel E. D., Litchfield D. W., Clark R. H., Krebs E. G., and Storm D. R. (1991) Phosphorylation of neuromodulin (GAP-43) by casein kinase II. Identification of phosphorylation sites and regulation by calmodulin. J. Biol. Chem. 266, 10544-10551.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10544-10551
    • Apel, E.D.1    Litchfield, D.W.2    Clark, R.H.3    Krebs, E.G.4    Storm, D.R.5
  • 6
    • 0023659436 scopus 로고
    • Primary structure and transcriptional regulation of GAP-43, a protein associated with nerve growth
    • Basi G. S., Jacobson R. D., Virag I., Schilling J., and Skene J. H. P. (1987) Primary structure and transcriptional regulation of GAP-43, a protein associated with nerve growth. Cell 49, 785-791.
    • (1987) Cell , vol.49 , pp. 785-791
    • Basi, G.S.1    Jacobson, R.D.2    Virag, I.3    Schilling, J.4    Skene, J.H.P.5
  • 7
    • 0031027044 scopus 로고    scopus 로고
    • GAP-43: An intrinsic determinant of neuronal development and plasticity
    • Benowitz L. I. and Routtenberg A. (1997) GAP-43: an intrinsic determinant of neuronal development and plasticity. Trends Neurosci. 20, 84-91.
    • (1997) Trends Neurosci. , vol.20 , pp. 84-91
    • Benowitz, L.I.1    Routtenberg, A.2
  • 8
    • 0026692124 scopus 로고
    • Mass spectrometry of peptides and proteins
    • Biemann K. (1992) Mass spectrometry of peptides and proteins. Annu. Rev. Biochem. 61, 977-1010.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 977-1010
    • Biemann, K.1
  • 10
    • 0029888311 scopus 로고    scopus 로고
    • Role of oxidants in ischemic brain damage
    • Chan P. H. (1996) Role of oxidants in ischemic brain damage. Stroke 27, 1124-1129.
    • (1996) Stroke , vol.27 , pp. 1124-1129
    • Chan, P.H.1
  • 11
    • 0025216913 scopus 로고
    • Purification of the growth-associated protein GAP-43 by reversed phase chromatography: Amino acid sequence analysis and cDNA identification
    • Changelian P. S., Meiri K., Soppet D., Valenza H., Loewy A., and Willard M. (1990) Purification of the growth-associated protein GAP-43 by reversed phase chromatography: amino acid sequence analysis and cDNA identification. Brain Res. 510, 259-268.
    • (1990) Brain Res. , vol.510 , pp. 259-268
    • Changelian, P.S.1    Meiri, K.2    Soppet, D.3    Valenza, H.4    Loewy, A.5    Willard, M.6
  • 12
    • 0028016077 scopus 로고
    • Glutamate receptors and the induction of excitotoxic neuronal death
    • Choi D. W. (1994) Glutamate receptors and the induction of excitotoxic neuronal death. Prog. Brain Res. 100, 47-51.
    • (1994) Prog. Brain Res. , vol.100 , pp. 47-51
    • Choi, D.W.1
  • 13
    • 0024425969 scopus 로고
    • Evidence for a single protein kinase C-mediated phosphorylation site in rat brain protein B-50
    • Coggins P. J. and Zwiers H. (1989) Evidence for a single protein kinase C-mediated phosphorylation site in rat brain protein B-50. J. Neurochem. 53, 1895-1901.
    • (1989) J. Neurochem. , vol.53 , pp. 1895-1901
    • Coggins, P.J.1    Zwiers, H.2
  • 15
    • 0030575196 scopus 로고    scopus 로고
    • Determination of the endogenous phosphorylation state of B-5Ü/GAP-43 and neurogranin in different brain regions by electrospray mass spectrometry
    • Di Luca M., Pastorino L., Raverdino V., De Graan P. N. E., Caputi A., Gispen W. H., and Cattabeni F. (1996) Determination of the endogenous phosphorylation state of B-5Ü/GAP-43 and neurogranin in different brain regions by electrospray mass spectrometry. FEBS Lett. 389, 309-313.
    • (1996) FEBS Lett. , vol.389 , pp. 309-313
    • Di Luca, M.1    Pastorino, L.2    Raverdino, V.3    De Graan, P.N.E.4    Caputi, A.5    Gispen, W.H.6    Cattabeni, F.7
  • 17
    • 0027184141 scopus 로고
    • P42 mitogen-activated protein kinase in brain: Prominent localization in neuronal cell bodies and dendrites
    • Fiore R. S., Bayer V. E., Pelech S. L., Posada J., Cooper J. A., and Baraban J. M. (1993) p42 mitogen-activated protein kinase in brain: prominent localization in neuronal cell bodies and dendrites. Neuroscience 55, 463-472.
    • (1993) Neuroscience , vol.55 , pp. 463-472
    • Fiore, R.S.1    Bayer, V.E.2    Pelech, S.L.3    Posada, J.4    Cooper, J.A.5    Baraban, J.M.6
  • 18
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localization of the kinase
    • Hanger D. P., Hughes K., Woodgett J. R., Brion J.-P., and Anderton B. H. (1992) Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: generation of paired helical filament epitopes and neuronal localization of the kinase. Neurosci. Lett. 147, 58-62.
    • (1992) Neurosci. Lett. , vol.147 , pp. 58-62
    • Hanger, D.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.-P.4    Anderton, B.H.5
  • 19
    • 0027982679 scopus 로고
    • Viability thresholds and the penumbra of focal ischemia
    • Hossmann K. A. (1994) Viability thresholds and the penumbra of focal ischemia. Ann. Neurol. 36, 557-565.
    • (1994) Ann. Neurol. , vol.36 , pp. 557-565
    • Hossmann, K.A.1
  • 20
    • 0027180072 scopus 로고
    • Characterization of a 7.5-kDa protein kinase C substrate (RC3 protein, neurogranin) from rat brain
    • Huang K.-P., Huang F. L., and Chen H.-C. (1993) Characterization of a 7.5-kDa protein kinase C substrate (RC3 protein, neurogranin) from rat brain. Arch. Biochem. Biophys. 305, 570-580.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 570-580
    • Huang, K.-P.1    Huang, F.L.2    Chen, H.-C.3
  • 21
    • 0023180044 scopus 로고
    • Cloning and complementary DNA for GAP-43, a neuronal growth-related protein
    • Karns L. R., Ng S. C., Freeman J. A., and Fishman M. C. (1987) Cloning and complementary DNA for GAP-43, a neuronal growth-related protein. Science 236, 597-600.
    • (1987) Science , vol.236 , pp. 597-600
    • Karns, L.R.1    Ng, S.C.2    Freeman, J.A.3    Fishman, M.C.4
  • 22
    • 0024727509 scopus 로고
    • Selective conservation of GAP-43 structure in vertebrate evolution
    • LaBate M. E. and Skene J. H. P. (1989) Selective conservation of GAP-43 structure in vertebrate evolution. Neuron 3, 299-310.
    • (1989) Neuron , vol.3 , pp. 299-310
    • LaBate, M.E.1    Skene, J.H.P.2
  • 23
    • 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
  • 24
    • 0024307526 scopus 로고
    • Dephosphorylation of neuromodulin by calcineurin
    • Liu Y. and Storm D. R. (1989) Dephosphorylation of neuromodulin by calcineurin. J. Biol. Chem. 264, 12800-12804.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12800-12804
    • Liu, Y.1    Storm, D.R.2
  • 25
    • 0025346896 scopus 로고
    • Regulation of free calmodulin levels by neuromodulin: Neuron growth and regeneration
    • Liu Y. and Storm D. R. (1990) Regulation of free calmodulin levels by neuromodulin: neuron growth and regeneration. Trends Pharmacol. Sci. 11, 107-111.
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 107-111
    • Liu, Y.1    Storm, D.R.2
  • 26
    • 0027368868 scopus 로고
    • Analysis of the palmitoylation and membrane targeting domain of neuromodulin (GAP-43) by site-specific mutagenesis
    • Liu Y., Fisher D. A., and Storm D. R. (1993) Analysis of the palmitoylation and membrane targeting domain of neuromodulin (GAP-43) by site-specific mutagenesis. Biochemistry 32, 10714-10719.
    • (1993) Biochemistry , vol.32 , pp. 10714-10719
    • Liu, Y.1    Fisher, D.A.2    Storm, D.R.3
  • 27
    • 0031029260 scopus 로고    scopus 로고
    • Identification of NAP-22 and GAP-43 (neuromodulin) as major protein components in a Triton insoluble low density fraction of rat brain
    • Maekawa S., Kumanogoh H., Funatsu N., Takei N., Inoue K., Endo Y., Hamada K., and Sokawa Y. (1997) Identification of NAP-22 and GAP-43 (neuromodulin) as major protein components in a Triton insoluble low density fraction of rat brain. Biochim. Biophys. Acta 1323, 1-5.
    • (1997) Biochim. Biophys. Acta , vol.1323 , pp. 1-5
    • Maekawa, S.1    Kumanogoh, H.2    Funatsu, N.3    Takei, N.4    Inoue, K.5    Endo, Y.6    Hamada, K.7    Sokawa, Y.8
  • 28
    • 0025190597 scopus 로고
    • GAP-43 in growth cones is associated with areas of membrane that are tightly bound to substrate and is a component of a membrane skeleton subcellular fraction
    • Meiri K. F. and Gordon-Weeks P. R. (1990) GAP-43 in growth cones is associated with areas of membrane that are tightly bound to substrate and is a component of a membrane skeleton subcellular fraction. J. Neurosci. 10, 256-266.
    • (1990) J. Neurosci. , vol.10 , pp. 256-266
    • Meiri, K.F.1    Gordon-Weeks, P.R.2
  • 29
    • 0029670673 scopus 로고    scopus 로고
    • Mutagenesis of ser41 to ala inhibits the association of GAP-43 with the membrane skeleton of GAP-43-deficient PC12B cells: Effects on cell adhesion and the composition of neurite cytoskeleton and membrane
    • Meiri K. F., Hammang J. P., Dent E. W., and Baetge E. E. (1996) Mutagenesis of ser41 to ala inhibits the association of GAP-43 with the membrane skeleton of GAP-43-deficient PC12B cells: effects on cell adhesion and the composition of neurite cytoskeleton and membrane. J. Neurobiol. 29, 213-232.
    • (1996) J. Neurobiol. , vol.29 , pp. 213-232
    • Meiri, K.F.1    Hammang, J.P.2    Dent, E.W.3    Baetge, E.E.4
  • 30
    • 0025220605 scopus 로고
    • Chicken growth-associated protein GAP-43 is tightly bound to the actin-rich neuronal membrane skeleton
    • Moss D. J., Fernyhough P., Chapman K., Baizer L., Bray D., and Allsopp T. (1990) Chicken growth-associated protein GAP-43 is tightly bound to the actin-rich neuronal membrane skeleton. J. Neurochem. 54, 729-736.
    • (1990) J. Neurochem. , vol.54 , pp. 729-736
    • Moss, D.J.1    Fernyhough, P.2    Chapman, K.3    Baizer, L.4    Bray, D.5    Allsopp, T.6
  • 33
    • 0029888940 scopus 로고    scopus 로고
    • Phosphorylation of GAP-43 (growth-associated protein of 43 kDa) by conventional, novel and atypical isotypes of the protein kinase C gene family: Differences between oligopeptide and polypeptide phosphorylation
    • Oehrlein S. A., Parker P. J., and Herget T. (1996) Phosphorylation of GAP-43 (growth-associated protein of 43 kDa) by conventional, novel and atypical isotypes of the protein kinase C gene family: differences between oligopeptide and polypeptide phosphorylation. Biochem. J. 317, 219-224.
    • (1996) Biochem. J. , vol.317 , pp. 219-224
    • Oehrlein, S.A.1    Parker, P.J.2    Herget, T.3
  • 34
    • 0027499934 scopus 로고
    • Phosphorylase kinase phosphorylates the calmodulin-binding regulatory regions of neuronal tissue-specific protein B-50 (GAP-43) and neurogranin
    • Paudel H. K., Zwiers H., and Wang J. H. (1993) Phosphorylase kinase phosphorylates the calmodulin-binding regulatory regions of neuronal tissue-specific protein B-50 (GAP-43) and neurogranin. J. Biol. Chem. 268, 6207-6213.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6207-6213
    • Paudel, H.K.1    Zwiers, H.2    Wang, J.H.3
  • 35
    • 0023718841 scopus 로고
    • Phosphorylation of protein B-50 (GAP-43) from adult rat brain cortex by casein kinase II
    • Pisano M. R., Hegazy M. G., Reimann E. M., and Dokas L. A. (1988) Phosphorylation of protein B-50 (GAP-43) from adult rat brain cortex by casein kinase II. Biochem. Biophys. Res. Commun. 155, 1207-1212.
    • (1988) Biochem. Biophys. Res. Commun. , vol.155 , pp. 1207-1212
    • Pisano, M.R.1    Hegazy, M.G.2    Reimann, E.M.3    Dokas, L.A.4
  • 37
    • 0029049719 scopus 로고
    • 644) in the control of rabbit muscle glycogen synthase
    • 644) in the control of rabbit muscle glycogen synthase. J. Biol. Chem. 270, 12491-12497.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12491-12497
    • Scared, A.V.1    Roach, P.J.2
  • 38
    • 0028931985 scopus 로고
    • Dephosphorylation of protein kinase C substrates, neurogranin, neuromodulin, and MARCKS, by calcineurin and protein phosphatases 1 and 2A
    • Seki K., Chen H.-C. and Huang K.-P. (1995) Dephosphorylation of protein kinase C substrates, neurogranin, neuromodulin, and MARCKS, by calcineurin and protein phosphatases 1 and 2A. Arch. Biochem. Biophys. 316, 673-679.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 673-679
    • Seki, K.1    Chen, H.-C.2    Huang, K.-P.3
  • 39
    • 0029787497 scopus 로고    scopus 로고
    • Nitric oxide modification of rat brain neurogranin affects its phosphorylation by protein kinase C and affinity for calmodulin
    • Sheu F.-S., Mahoney C. W., Seki K., and Huang K.-P. (1996) Nitric oxide modification of rat brain neurogranin affects its phosphorylation by protein kinase C and affinity for calmodulin. J. Biol. Chem. 271, 22407-22413.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22407-22413
    • Sheu, F.-S.1    Mahoney, C.W.2    Seki, K.3    Huang, K.-P.4
  • 40
    • 0024508661 scopus 로고
    • Axonal growth-associated proteins
    • Skene J. H. P. (1989) Axonal growth-associated proteins. Annu. Rev. Neurosci. 12, 127-156.
    • (1989) Annu. Rev. Neurosci. , vol.12 , pp. 127-156
    • Skene, J.H.P.1
  • 41
    • 0024576943 scopus 로고
    • Posttranslational membrane attachment and dynamic fatty acylation of a neuronal growth cone protein, GAP-43
    • Skene J. H. P. and Virag I. (1989) Posttranslational membrane attachment and dynamic fatty acylation of a neuronal growth cone protein, GAP-43. J. Cell Biol. 108, 613-624.
    • (1989) J. Cell Biol. , vol.108 , pp. 613-624
    • Skene, J.H.P.1    Virag, I.2
  • 42
    • 0026806135 scopus 로고
    • GAP-43, a protein associated with axon growth, is phosphorylated at 3 sites in cultured neurons and rat brain
    • Spencer S. A., Schuh S. M., Liu W.-S., and Willard M. B. (1992) GAP-43, a protein associated with axon growth, is phosphorylated at 3 sites in cultured neurons and rat brain. J. Biol. Chem. 267, 9059-9064.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9059-9064
    • Spencer, S.A.1    Schuh, S.M.2    Liu, W.-S.3    Willard, M.B.4
  • 44
    • 0028853240 scopus 로고
    • Neuronal pathfinding is abnormal in mice lacking the neuronal growth cone protein GAP-43
    • Strittmatter S. M., Fankhauser C., Huang P. L., Mashimo H., and Fishman M. C. (1995) Neuronal pathfinding is abnormal in mice lacking the neuronal growth cone protein GAP-43. Cell 80, 445-452.
    • (1995) Cell , vol.80 , pp. 445-452
    • Strittmatter, S.M.1    Fankhauser, C.2    Huang, P.L.3    Mashimo, H.4    Fishman, M.C.5
  • 45
    • 0028021757 scopus 로고
    • A mass spectrometric study on the in vivo posttranslational modification of GAP-43
    • Taniguchi H., Suzuki M., Manenti S., and Titani K. (1994) A mass spectrometric study on the in vivo posttranslational modification of GAP-43. J. Biol. Chem. 269, 22481-22484.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22481-22484
    • Taniguchi, H.1    Suzuki, M.2    Manenti, S.3    Titani, K.4
  • 46
    • 0026039891 scopus 로고
    • Casein kinase I and II -multipotential serine protein kinases: Structure, function, and regulation
    • Tuazon P. T. and Traugh J. A. (1991) Casein kinase I and II -multipotential serine protein kinases: structure, function, and regulation. Adv. Second Messenger Phosphoprotein Res. 23, 123-164.
    • (1991) Adv. Second Messenger Phosphoprotein Res. , vol.23 , pp. 123-164
    • Tuazon, P.T.1    Traugh, J.A.2
  • 47
    • 0021799736 scopus 로고
    • Modulation of the activity of purified phosphatidylinositol-4-phosphate kinase by phosphorylated B-50 protein
    • Van Dongen C. J., Zwiers H., De Graan P. N. E., and Gispen W. H. (1985) Modulation of the activity of purified phosphatidylinositol-4-phosphate kinase by phosphorylated B-50 protein. Biochem. Biophys. Res. Commun. 128, 1219-1227.
    • (1985) Biochem. Biophys. Res. Commun. , vol.128 , pp. 1219-1227
    • Van Dongen, C.J.1    Zwiers, H.2    De Graan, P.N.E.3    Gispen, W.H.4
  • 48
  • 49
    • 0024956319 scopus 로고
    • A membrane-targeting signal in the amino terminus of the neuronal protein GAP-43
    • Zuber M. X., Strittmatter S. M., and Fishman M. C. (1989) A membrane-targeting signal in the amino terminus of the neuronal protein GAP-43. Nature 341, 345-348.
    • (1989) Nature , vol.341 , pp. 345-348
    • Zuber, M.X.1    Strittmatter, S.M.2    Fishman, M.C.3


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