Protein phosphorylation and the regulation of mRNA translation following cerebral ischemia

Progress in Brain Research

Volumn 96, Issue C, 1993, Pages 179-191

  Wieloch, Tadeusz ^a   Bergstedt, Kerstin ^a   Hu, Bing Ren ^a  

^a LUND UNIVERSITY HOSPITAL   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; PROTEIN KINASE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; AUTORADIOGRAPHY; BRAIN ISCHEMIA; CONFERENCE PAPER; NONHUMAN; PROTEIN PHOSPHORYLATION; PROTEIN SYNTHESIS; RAT;

EID: 0027167113     PISSN: 00796123     EISSN: 18757855     Source Type: Book Series    
DOI: 10.1016/S0079-6123(08)63266-5     Document Type: Article

References (101)

1. Ackerman, P., Glover, C.V.C., Osheroff, N., Stimulation of casein kinase II by epidermal growth factor: relationship between the physiological activity of the kinase and the phosphorylation state of its β-subunit. Proc. Natl. Acad. Sci. U.S.A. 87 (1990), 821–825.
2. Aksenova, M.V., Burbaeva, G., Sh. Kandror, K.V., Kapkov, D.V., Stepanov, A.S., The decreased level of casein kinase-2 in brain cortex of schizophrenic and Alzheimer's disease patients. FEBS Lett. 279 (1991), 55–57.
3. Alcazar, A., Mendez, E., Fando, J.L., Salinas, M., Specific phosphorylation of eIF-2 factor from brain by three different protein kinases. Biochem. Biophys. Res. Commun. 153 (1988), 313–320.
4. Alcazar, A., Mendez, E., Martin, M.E., Salinas, M., Purification of a novel eIF-2α protein kinase from calf brain. Biochem. Biophys. Res. Commun. 166 (1990), 1237–1244.
5. Alkon, D.L., Rasmussen, H., A spatial-temporal model of cell activation. Science 239 (1988), 998–1005.
6. Araki, S., Simada, Y., Kaji, K., Hayashi, H., Role of protein kinase C in the inhibition by fibroblast growth factor of apoptosis in serum-depleted endothelial cells. Biochem. Biophys. Res. Commun. 172 (1990), 1081–1085.
7. Araki, T., Kato, H., Kogure, K., Regional impairment of protein synthesis following brief cerebral ischemia in the gerbil. Acta Neuropathol. (Berl.) 79 (1990), 501–505.
8. 14C-leucine incorporation into proteins in the rat brain following 15 minute transient 2-VO ischemia. J. Cereb. Blood Flow Metab., 11, 1991, S188 Suppl. 2.
9. Bodsch, W., Takahashi, K., Barbier, A., Grosse Ophoff, B., Hossmann, K.A., Cerebral protein synthesis and ischemia. Prog. Brain Res. 63 (1985), 197–210.
10. Boris-Möller, F., Smith, M.-L., Siesjö, B.K., Effects of hypothermia on ischemic brain damage: a comparison between preischemic and postischemic cooling. Neurosci. Res. Commun. 5 (1989), 87–94.
11. Buchan, A.M., Li, H., Cho, C., Pulsinelli, W.A., Blockade of the AMPA receptor prevents CA1 hippocampal injury following severe but transient forebrain ischemia in the adult rat. Neurosci. Lett. 132 (1991), 255–258.
12. Buchan, A.M., Xue, D., Huang, Z.-G., Smith, K.H., Lesiuk, H., Delayed AMPA receptor blockade reduces cerebral infarction induced by focal ischemia. Neuroreport 2 (1991), 473–476.
13. Busto, R., Dietrich, W.D., Globus, M.Y.-T., Valdés, I., Scheinberg, P., Ginsberg, M., Small differences in intraischemic brain temperature critically determine the extent of ischemic neuronal injury. J. Cereb. Blood Flow Metab. 7 (1987), 729–738.
14. Buszaki, G., Freund, T.F., Bayardo, F., Somogyi, P., Ischemia-induced changes in the electrical activity of the hippocampus. Exp. Brain Res. 78 (1989), 268–278.
15. Cardell, M., Bingren, H., Wieloch, T., Zivin, J., Saitoh, T., Protein kinase C is translocated to cell membranes during cerebral ischemia. Neurosci. Lett. 119 (1990), 228–232.
16. Cardell, M., Boris-Möller, F., Wieloch, T., Hypothermia prevents the ischemia-induced translocation and inhibition of protein kinase C in the rat striatum. J. Neurochem. 57 (1991), 1814–1817.
17. Chopp, H.S., Sasaki, T., Kassell, N.F., Hippocampal unit activity after transient cerebral ischemia in rats. Stroke 20 (1989), 1051–1058.
18. Churn, S.B., Taft, W.C., Billingsley, M.L., Blair, R.E., De Lorenzo, R.J., Temperature modulation of ischemia-induced neuronal death and ischemia-induced inhibition of calcium/calmodulin dependent protein kinase II in gerbils. Stroke 21 (1990), 1715–1721.
19. Clemens, M.J., Regulatory mechanisms in translational control. Curr. Opinion Cell Biol. 1 (1989), 1160–1197.
20. Cooper, H.K., Zalewski, T., Kawakami, S., Hossmann, K.-A., Kleihues, P., The effect of ischemia and recirculation on protein synthesis in the rat brain. J. Neurochem. 28 (1977), 929–934.
21. De Leo, J., Toth, L., Schubert, P., Rudolphi, K., Kreutzberg, G.W., Ischemia-induced neuronal cell death, calcium accumulation, and glial response in the hippocampus of the Mongolian gerbil and protection by propentofylline. (HWA 285). J. Cereb. Blood Flow Metab. 7 (1987), 745–751.
22. Desphande, J., Bergstedt, K., Lindén, T., Kalimo, H., Wieloch, T., Ultrastructural changes in the hippocampal CA1 region following transient cerebral ischemia: evidence against programmed cell death. Exp. Brain Res. 88 (1992), 91–105.
23. Dholakia, J.N., Wahba, A.J., Phosphorylation of the guanine nucleotide exchange factor from rabbit reticulocytes regulates its activity in polypeptide chain initiation. Proc. Natl. Acad. Sci. U.S.A. 85 (1988), 51–54.
24. Dienel, G.A., Pulsinelli, W.A., Duffy, T.E., Regional protein synthesis in rat brain following acute hemispheric ischemia. J. Neurochem. 35 (1980), 1216–1226.
25. Dienel, G.A., Cruz, N.F., Rosenfeld, S.J., Temporal profiles of proteins responsive to transient ischemia. J. Neurochem. 44 (1985), 600–610.
26. Dumuis, A., Pin, J.P., Oomagari, K., Sebben, M., Bockaert, J., Arachidonic acid released from striatal neurons by joint stimulation of ionotropic and metabotropic quisqualate receptors. Nature 347 (1990), 182–183.
27. Duncan, R., Protein synthesis initiation factor modifications during viral infection: implication for translational control. Electrophoresis 11 (1990), 219–227.
28. Duncan, R., Hershey, J., Heat shock-induced translational alterations in HeLa cells. J. Biol. Chem. 259 (1984), 11882–11889.
29. Duncan, R., Hershey, J., Regulation of initiation factors during translational repression caused by serum depletion. J. Biol. Chem. 260 (1985), 5493–5497.
30. Duncan, R., Milburn, S.C., Hershey, J.W.B., Regulated phosphorylation and low abundance of HeLa cell initiation factor eIF-4F suggests a role in translational control. J. Biol. Chem. 262 (1987), 380–388.
31. Edelman, A.M., Blumenthal, D.K., Krebs, E.G., Protein serine/threonine kinases. Annu. Rev. Biochem. 56 (1987), 567–613.
32. Gage, F.H., Batchelor, P., Chen, K.S., Chin, D., Higgins, G.A., Koh, S., Deputy, S., Rosenberg, M.B., Fischer, W., Björklund, A., NGF receptor reexpression and NGF-mediated cholinergic neuronal hypertrophy in the damaged adult neostriatum. Neuron 2 (1989), 1177–1184.
33. Gilad, G., Gilad, V.H., Polyamines can protect against ischemia-induced nerve cell death in gerbil forebrain. Exp. Neurol. 111 (1991), 349–355.
34. Gill, R., Lodge, D., The neuroprotective action of 2,3-dihydoxy-6-nitro-7-sulfamoyl-benzo(F)quinnoxaline (NBQX) in a rat focal ischemia model. J. Cereb. Blood Flow Metab., 11, 1991, S224 Suppl. 2.
35. Gonzalez, M.F., Lowenstein, D., Fernyak, S., Hisanaga, K., Simon, R., Sharp, F., Induction of heat shock protein 72-like immunoreactivity in the hippocampal formation following transient global ischemia. Brain Res. Bull. 26 (1991), 241–250.
36. Gustafson, I., Miyauchi, Y., Wieloch, T., Postischemic administration of Idazoxan, an α-2 adrenergic receptor antagonist, decreases neuronal damage in the rat brain. J. Cereb. Blood Flow Metab. 9 (1989), 171–174.
37. Hama, T., Huang, K.-P., Guroff, G., Protein kinase C as a component of nerve growth factor sensitive phosphorylation system in PC 12 cells. Proc. Natl. Acad. Sci. U.S.A. 83 (1986), 2353–2357.
38. Hansen, A.J., Effects of anoxia on ionic distribution in the brain. Physiol Rev. 65 (1985), 101–135.
39. Hathaway, G.M., Traugh, J.A., Casein kinases - multipotential protein kinases. Stadtman, E., Horecker, B., (eds.) Current Topics in Cellular Regulation, 1982, Academic Press, New York, 101–127.
40. Heidenreich, K.A., Toledo, S.P., Insulin receptors mediate growth effects in cultured neurons. I. Rapid stimulation of protein synthesis. Endocrinology 125 (1989), 1451–1457.
41. Hershey, J.W., Translation control in mammalian cells. Annu. Rev. Biochem. 60 (1991), 717–755.
42. Houslay, M.D., “Crosstalk”: a pivotal role for protein kinase C in modulating relationships between signal transduction pathways. Eur. J. Biochem. 195 (1991), 9–27.
43. Hu, B.G., Wieloch, T., Stress-induced inhibition of protein synthesis initiation. Modulation of initiation factor 2 and guanine exchange factor activities following transient cerebral ischemia in the rat. J. Neurosci., 1993 in press.
44. Hu, B.G., Wieloch, T., Casein kinase II activity in the postischemic rat brain increases in brain regions resistant to ischemia but decreases in vulnerable areas. J. Neurochem., 1993 in press.
45. Huang, K.-P., The mechanism of protein kinase C activation. Trends Neurosci. 12 (1989), 425–432.
46. Hultmark, D., Klemenz, R., Gehring, W.J., Translational and transcriptional control elements in the untranslated leader of the heat-shock genehsp 22. Cell 44 (1986), 429–438.
47. Hunter, T., Protein modification: phosphorylation on tyrosine residues. Curr. Opinion Cell Biol. 1 (1989), 1168–1181.
48. Hunter, T., Cooper, J., Protein-tyrosine kinases. Annu. Rev. Biochem. 54 (1985), 897–930.
49. Imoto, D.S., Masliah, E., De Teresa, R., Terry, R.D., Saitoh, T., Aberrant casein kinase II in Alzheimer's disease. Brain Res. 507 (1989), 273–280.
50. Kirino, T., Sano, K., Selective vulnerability in the gerbil hippocampus following transient ischemia. Acta Neuropathol. (Berl.) 62 (1984), 201–208.
51. Kirino, T., Robinson, H.P.C., Miwa, A., Tamura, A., Kawai, N., Disturbances of membrane function preceding ischemic delayed neuronal death in the gerbil hippocampus. J. Cereb. Blood Flow Metab. 12 (1992), 408–418.
52. Klarlund, J., Czech, M.P., Insulin-like growth factor I and insulin rapidly increase casein kinase II activity in BALB/c3T3 fibroblasts. J. Biol. Chem. 263 (1988), 15872–15877.
53. Kochhar, A., Saitoh, T., Zivin, J., Reduced protein kinase C activity in ischemic spinal cord. J. Neurochem. 53 (1989), 946–952.
54. Kozak, M., Comparison of initiation of protein synthesis in procaryotes, eucaryotes and organelles. Microbiol. Rev. 47 (1983), 1–49.
55. Kozuka, M., Smith, M.-L., Siesjö, B.K., Preischemic hyperglycemia enhances postischemic depression of cerebral metabolic rate. J. Cereb. Blood Flow Metab. 9 (1989), 478–490.
56. Kromer, L., Nerve growth factor treatment after brain injury prevents neuronal death. Science 235 (1987), 214–216.
57. Lamphear, B.J., Panniers, R., Heat shock impairs the interaction of cap-binding protein complex with 5′ mRNA cap. J. Biol. Chem. 266 (1991), 2789–2794.
58. Lau, K.-H.W., Farley, J., Baylink, D., Phosphotyrosyl protein phosphatases. Biochem. J. 257 (1989), 23–36.
59. Le Peillet, E., Arvin, B., Moncada, C., Meldrum, B.S., The non-NMDA antagonists, NBQX and GYKI 53466, protect against cortical and striatal cell loss following transient global ischemia in the rat. Brain Res. 571 (1992), 115–120.
60. Llinás, R., McGuinness, T.L., Leonard, C.S., Sugimori, M., Greengard, P., Intraterminal injection of synapsin I or calcium/calmodulin-dependent protein kinase II alters neurotransmitter release at the squid giant synapse. Proc. Natl. Acad. Sci. U.S.A. 82 (1985), 3035–3039.
61. Louis, J.-C., Magal, E., Yavin, E., Protein kinase C alterations in the fetal rat brain after global ischemia. J. Biol. Chem. 263 (1988), 19282–19285.
62. Mattson, M.P., Murrain, M., Guthrie, P.B., Kater, S.B., Fibroblast growth factor and glutamate: opposing roles in the generation and degeneration of hippocampal neuroarchitecture. J. Neurosci. 9 (1989), 3728–3740.
63. Minamisawa, H., Nordström, C.-H., Smith, M.-L., Siesjö, B.K., The influence of mild body and brain hypothermia on ischemic brain damage. J. Cereb. Blood Flow Metab. 10 (1990), 365–374.
64. Montine, K.S., Henshaw, E.C., Serum growth factors cause rapid stimulation of protein synthesis and dephosphorylation of eIF-2 in serum deprived Ehrlich cells. Biochim. Biophys. Acta 1014 (1989), 282–288.
65. Morley, S.J., Thomas, G., Intracellular messengers and the control of protein synthesis. Pharmacol. Ther. 50 (1991), 291–319.
66. Morley, S.J., Dever, T.E., Etchison, D., Traugh, J.A., Phosphorylation of eIF-4F by protein kinase C or multipotential S6 kinase stimulates protein synthesis at initiation. J. Biol. Chem. 266 (1991), 4669–4672.
67. Mulner-Lorillon, O., Cormier, P., Labbé, J.-C., Dorée, M., Poulhe, R., Osborn, H., Bellé, R., M-phase-specific cdc2 protein kinase phosphorylates the β-subunit of casien kinase II and increases kinase II activity. Eur. J. Biochem. 193 (1990), 529–534.
68. Munekata, K., Hossmann, K.A., Xie, Y., Seo, K., Oschlies, U., Selective vulnerability of hippocampus: ribosomal aggregation, protein synthesis, and tissue pH. Cerebrovascular Disease, 1987, Raven Press, New York, 107–117.
69. Nellgård, B., Wieloch, T., Postischemia blockade of AMPA but not NMDA receptors mitigates neuronal damage in the rat brain following transient cerebral ischemia. J. Cereb. Blood Flow Metab. 11 (1992), 1–12.
70. Nishizuka, Y., Studies and perspectives of protein kinase C. Science 233 (1986), 305–312.
71. Ochoa, S., Regulation of protein synthesis initiation in eurocaryotes. Arch. Biochem. Biophys. 223 (1983), 325–349.
72. 2+/calmodulin-dependent protein kinase II immunoreactivity in the rat hippocampus after forebrain ischemia. Neurosci. Lett. 113 (1990), 134–138.
73. Padmanabha, R., Chen-Wu, J.L.P., Hanna, D.E., Glover, C.V.C., Isolation, sequencing and distribution of the yeastCKA2 gene: casein kinase II is essential for viability inSaccharomyces cerevisiae. Mol. Cell. Biol. 10 (1990), 4089–4099.
74. Panniers, R., Henshaw, E.C., A GDP/GTP exchange factor essential for eukaryotic initiation factor 2 cycling in Ehrlich ascites tumor cells and its regulation by eukarotic initiation factor 2 phosphorylation. J. Biol. Chem. 258:13 (1983), 7928–7934.
75. Paschen, W., Hallmayer, J., Röhn, G., Regional changes of polyamine profiles after reversible cerebral ischemia in mongolian gerbils: effects of nimodipine and barbiturate. Neurochem. Pathol. 8 (1988), 27–41.
76. Petito, C., Pulsinelli, W., Delayed neuronal recovery and neuronal death in rat hippocampus following severe cerebral ischemia: possible relationship to abnormalities in neuronal processes. J. Cereb. Blood Flow Metab. 4 (1984), 194–205.
77. Proud, C.G., Guanine nucleotides, protein phosphorylation and the control of translation. Trends Biochem. Sci. 11 (1986), 73–77.
78. Pulsinelli, W.A., Duffy, T.E., Regional energy balance in rat brain after transient forebrain ischemia. J. Neurochem. 40 (1983), 1500–1503.
79. Pulsinelli, W.A., Levy, D.E., Duffy, T.E., Regional cerebral blood flow and glucose metabolism following transient forebrain ischemia. Ann. Neurol. 11 (1982), 499–509.
80. Rhoads, R.E., Protein synthesis, cell growth and on-cogenesis. Curr. Opinion Cell Biol. 3 (1991), 1019–1024.
81. Rostas, J.A.P., Weinberger, R.P., Dunkley, P.R., Multiple pools and multiple forms of calmodulin-stimulated protein kinase during development: relationship to postsynaptic densities. Prog. Brain Res. 69 (1986), 355–371.
82. Rowlands, A.G., Panniers, R., Henshaw, E.G., The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2. J. Biol. Chem. 263 (1988), 5526–5533.
83. Ryazanov, A.G., Shestakova, E.A., Natapov, P.G., Phosphorylation of elongation factor 2 by EF-2 kinase effects rate of translation. Nature 334 (1988), 170–173.
84. Saitoh, T., Masliah, E., Jin, L.W., Cole, G.M., Wieloch, T., Shapiro, I.P., Biology of disease. Protein kinases and phosphorylation in neurological disorders and cell death. Lab. Invest. 64 (1991), 596–616.
85. Sarre, T.F., Hermann, M., Bader, M., Differential effect of hemin-controlled eIF-2α kinases from mouse erythroleukemia cells on protein synthesis. Eur. J. Biochem. 183 (1989), 137–143.
86. Scorsone, K.A., Panniers, R., Rowlands, A.G., Henshaw, E.C., Phosphorylation of eukaryotic initiation factor 2 during physiological stresses which affect protein synthesis. J. Biol. Chem. 262 (1987), 14538–14543.
87. Sheardown, M.J., Nielsen, E.Ø., Hansen, A.J., Jacobsen, P., Honoré, T., 2,3-Dihydroxy-6-nitro-7-sulfamoyl-benzo(F)quinoxaline: a neuroprotectant for cerebral ischemia. Science 247 (1990), 571–574.
88. Shenolikar, S., Nairn, A., Protein phosphatases: recent progress. Greengard, P., Robinson, G., (eds.) Advances in Second Messenger and Phosphoprotein Research, 1991, Raven Press, New York, 1–119.
89. Shigeno, T., Mima, T., Takakura, K., Graham, D.I., Kato, G., Hashimoto, Y., Furukawa, S., Amelioration of delayed neuronal death in the hippocampus by nerve growth factor. J. Neurosci. 11 (1991), 2914–2919.
90. Siesjö, B.K., Mechanisms of ischemic brain damage. Crit. Care Med. 16 (1988), 954–963.
91. Sommercorn, J., Mulligan, J.A., Lozeman, F., Krebs, E.G., Activation of casein kinase II in response to insulin and to epidermal growth factor. Proc. Natl. Acad. Sci. U.S.A. 84 (1987), 8834–8838.
92. Thilmann, R., Xie, Y., Kleihues, P., Kiessling, M., Persistent inhibition of protein synthesis precedes delayed neuronal death in postischemic gerbil hippocampus. Acta Neuropathol. (Berl.) 71 (1987), 88–93.
93. Thomas, N.S.B., Matts, R.L., Petryshyn, R., London, I.M., Distribution of reversing factor in reticulocyte lysates during active protein synthesis and on inhibition by heme deprivation or double stranded RNA. Proc. Natl. Acad. Sci. U.S.A. 81 (1984), 6998–7002.
94. Tuazon, P.T., Traugh, J.A., Casein kinase I and II. Multipotential serine protein kinases: structure, function and regulation. Adv. Second Messengers Phosphoprotein Res. 23 (1991), 124–164.
95. Tuazon, P., Merrick, W., Traugh, J., Comparative analysis of phosphorylation of translational initiation and elongation factors by seven protein kinases. J. Biol. Chem. 264 (1989), 2773–2777.
96. 14C]Leucine incorporation into brain proteins in gerbils after transient ischemia: relationship to selective vulnerability of hippocampus. J. Neurochem. 56 (1991), 789–796.
97. Wieloch, T., Neurochemical correlates to selective neuronal vulnerability. Prog. Brain Res. 63 (1985), 69–85.
98. Wieloch, T., Koide, T., Westerberg, E., Inhibitory neurotransmitters and neuromodulators as protective agents against ischemic brain damage. Krieglstein, K., (eds.) The Pharmacology of Ischemic Brain Damage, 1986, Elsevier, Amsterdam, 191–197.
99. Wieloch, T., Cardell, M., Bingren, H., Zivin, J., Saitoh, T., Changes in the activity of protein kinase C and the subcellular redistribution of its isozymes during and following forebrain ischemia. J. Neurochem. 56 (1991), 1227–1235.
100. Yamamoto, H., Fukunaga, K., Lee, K., Soderling, T., Ischemia-induced loss of brain calcium/calmodulin dependent protein kinase II. J. Neurochem. 58 (1992), 1110–1117.
101. Yoshida, S., Inoh, S., Asano, T., Sano, K., Kubota, M., Shimazaki, H., Ueta, N., Effect of transient ischemia on free fatty acids and phospholipids in gerbil brain. Lipid peroxidation as possible cause of postischemic injury. J. Neurosurg. 53 (1980), 232–331.