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Volumn 40, Issue 1, 2003, Pages 129-137

Carbon monoxide neurotransmission activated by CK2 phosphorylation of heme oxygenase-2

Author keywords

[No Author keywords available]

Indexed keywords

4,5,6,7 TETRABROMOBENZOTRIAZOLE; CARBON MONOXIDE; CASEIN KINASE II; CYCLIC GMP; HEME OXYGENASE; HEME OXYGENASE 2; PHORBOL ESTER; PROTEIN KINASE C; TRIAZOLE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0141750449     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(03)00596-8     Document Type: Article
Times cited : (133)

References (47)
  • 1
    • 0035949667 scopus 로고    scopus 로고
    • Neural roles for heme oxygenase: Contrasts to nitric oxide synthase
    • Baranano D.E., Snyder S.H. Neural roles for heme oxygenase. contrasts to nitric oxide synthase Proc. Natl. Acad. Sci. USA. 98:2001;10996-11002.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10996-11002
    • Baranano, D.E.1    Snyder, S.H.2
  • 4
    • 0031862763 scopus 로고    scopus 로고
    • Neurotrophin-induced activation of casein kinase 2 in rat hippocampal slices
    • Blanquet P.R. Neurotrophin-induced activation of casein kinase 2 in rat hippocampal slices. Neuroscience. 86:1998;739-749.
    • (1998) Neuroscience , vol.86 , pp. 739-749
    • Blanquet, P.R.1
  • 5
    • 0033991008 scopus 로고    scopus 로고
    • Casein kinase 2 as a potentially important enzyme in the nervous system
    • a
    • Blanquet P.R. Casein kinase 2 as a potentially important enzyme in the nervous system. Prog. Neurobiol. 60:2000;211-246. a.
    • (2000) Prog. Neurobiol. , vol.60 , pp. 211-246
    • Blanquet, P.R.1
  • 6
    • 0032761316 scopus 로고    scopus 로고
    • Identification of two persistently activated neurotrophin-regulated pathways in rat hippocampus
    • b
    • Blanquet P.R. Identification of two persistently activated neurotrophin-regulated pathways in rat hippocampus. Neuroscience. 95:2000;705-719. b.
    • (2000) Neuroscience , vol.95 , pp. 705-719
    • Blanquet, P.R.1
  • 7
    • 0025191219 scopus 로고
    • Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme
    • Bredt D.S., Snyder S.H. Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme. Proc. Natl. Acad. Sci. USA. 87:1990;682-685.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 682-685
    • Bredt, D.S.1    Snyder, S.H.2
  • 8
    • 0025941639 scopus 로고
    • Nitric oxide synthase protein and mRNA are discretely localized in neuronal populations of the mammalian CNS together with NADPH diaphorase
    • Bredt D.S., Glatt C.E., Hwang P.M., Fotuhi M., Dawson T.M., Snyder S.H. Nitric oxide synthase protein and mRNA are discretely localized in neuronal populations of the mammalian CNS together with NADPH diaphorase. Neuron. 7:1991;615-624.
    • (1991) Neuron , vol.7 , pp. 615-624
    • Bredt, D.S.1    Glatt, C.E.2    Hwang, P.M.3    Fotuhi, M.4    Dawson, T.M.5    Snyder, S.H.6
  • 9
    • 0034646558 scopus 로고    scopus 로고
    • PKC-zeta-associated CK2 participates in the turnover of free IkappaBalpha
    • Bren G.D., Pennington K.N., Paya C.V. PKC-zeta-associated CK2 participates in the turnover of free IkappaBalpha. J. Mol. Biol. 297:2000;1245-1258.
    • (2000) J. Mol. Biol. , vol.297 , pp. 1245-1258
    • Bren, G.D.1    Pennington, K.N.2    Paya, C.V.3
  • 10
    • 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. 35:1993;567-576.
    • (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
  • 11
    • 0035012930 scopus 로고    scopus 로고
    • The case of CO signaling: Why the jury is still out
    • Cary S.P., Marletta M.A. The case of CO signaling. why the jury is still out J. Clin. Invest. 107:2001;1071-1073.
    • (2001) J. Clin. Invest. , vol.107 , pp. 1071-1073
    • Cary, S.P.1    Marletta, M.A.2
  • 13
    • 0026049663 scopus 로고
    • Benzimidazole nucleoside analogues as inhibitors of plant (maize seedling) casein kinases
    • Dobrowolska G., Muszynska G., Shugar D. Benzimidazole nucleoside analogues as inhibitors of plant (maize seedling) casein kinases. Biochim. Biophys. Acta. 1080:1991;221-226.
    • (1991) Biochim. Biophys. Acta , vol.1080 , pp. 221-226
    • Dobrowolska, G.1    Muszynska, G.2    Shugar, D.3
  • 14
    • 0030902595 scopus 로고    scopus 로고
    • Insulin-like growth factor I protects and rescues hippocampal neurons against beta-amyloid- and human amylin-induced toxicity
    • Dore S., Kar S., Quirion R. Insulin-like growth factor I protects and rescues hippocampal neurons against beta-amyloid- and human amylin-induced toxicity. Proc. Natl. Acad. Sci. USA. 94:1997;4772-4777.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4772-4777
    • Dore, S.1    Kar, S.2    Quirion, R.3
  • 16
    • 0026035590 scopus 로고
    • Inositol 1,4,5-trisphosphate receptor is phosphorylated by cyclic AMP-dependent protein kinase at serines 1755 and 1589
    • Ferris C.D., Cameron A.M., Bredt D.S., Huganir R.L., Snyder S.H. Inositol 1,4,5-trisphosphate receptor is phosphorylated by cyclic AMP-dependent protein kinase at serines 1755 and 1589. Biochem. Biophys. Res. Commun. 175:1991;192-198.
    • (1991) Biochem. Biophys. Res. Commun. , vol.175 , pp. 192-198
    • Ferris, C.D.1    Cameron, A.M.2    Bredt, D.S.3    Huganir, R.L.4    Snyder, S.H.5
  • 18
    • 0033985947 scopus 로고    scopus 로고
    • Nitric oxide and carbon monoxide modulate oscillations of olfactory interneurons in a terrestrial mollusk
    • Gelperin A., Flores J., Raccuia-Behling F., Cooke I.R. Nitric oxide and carbon monoxide modulate oscillations of olfactory interneurons in a terrestrial mollusk. J. Neurophysiol. 83:2000;116-127.
    • (2000) J. Neurophysiol. , vol.83 , pp. 116-127
    • Gelperin, A.1    Flores, J.2    Raccuia-Behling, F.3    Cooke, I.R.4
  • 19
    • 0029590042 scopus 로고
    • Direct demonstration of a physiological role for carbon monoxide in olfactory receptor neurons
    • Ingi T., Ronnett G.V. Direct demonstration of a physiological role for carbon monoxide in olfactory receptor neurons. J. Neurosci. 15:1995;8214-8222.
    • (1995) J. Neurosci. , vol.15 , pp. 8214-8222
    • Ingi, T.1    Ronnett, G.V.2
  • 20
    • 0029990994 scopus 로고    scopus 로고
    • Carbon monoxide: An endogenous modulator of the nitric oxide-cyclic GMPsignaling system
    • a
    • Ingi T., Cheng J., Ronnett G.V. Carbon monoxide. an endogenous modulator of the nitric oxide-cyclic GMPsignaling system Neuron. 16:1996;835-842. a.
    • (1996) Neuron , vol.16 , pp. 835-842
    • Ingi, T.1    Cheng, J.2    Ronnett, G.V.3
  • 21
    • 0029830910 scopus 로고    scopus 로고
    • The regulation of heme turnover and carbon monoxide biosynthesis in cultured primary rat olfactory receptor neurons
    • b
    • Ingi T., Chiang G., Ronnett G.V. The regulation of heme turnover and carbon monoxide biosynthesis in cultured primary rat olfactory receptor neurons. J. Neurosci. 16:1996;5621-5628. b.
    • (1996) J. Neurosci. , vol.16 , pp. 5621-5628
    • Ingi, T.1    Chiang, G.2    Ronnett, G.V.3
  • 23
    • 0028884298 scopus 로고
    • Regulation of cyclic nucleotide-gated channels and membrane excitability in olfactory receptor cells by carbon monoxide
    • Leinders-Zufall T., Shepherd G.M., Zufall F. Regulation of cyclic nucleotide-gated channels and membrane excitability in olfactory receptor cells by carbon monoxide. J. Neurophysiol. 74:1995;1498-1508.
    • (1995) J. Neurophysiol. , vol.74 , pp. 1498-1508
    • Leinders-Zufall, T.1    Shepherd, G.M.2    Zufall, F.3
  • 25
    • 0028067882 scopus 로고
    • Inhibition of hippocampal heme oxygenase, nitric oxide synthase, and long-term potentiation by metalloporphyrins
    • Meffert M.K., Haley J.E., Schuman E.M., Schulman H., Madison D.V. Inhibition of hippocampal heme oxygenase, nitric oxide synthase, and long-term potentiation by metalloporphyrins. Neuron. 13:1994;1225-1233.
    • (1994) Neuron , vol.13 , pp. 1225-1233
    • Meffert, M.K.1    Haley, J.E.2    Schuman, E.M.3    Schulman, H.4    Madison, D.V.5
  • 26
    • 0025060131 scopus 로고
    • Ribofuranosyl-benzimidazole derivatives as inhibitors of casein kinase-2 and casein kinase-1
    • Meggio F., Shugar D., Pinna L.A. Ribofuranosyl-benzimidazole derivatives as inhibitors of casein kinase-2 and casein kinase-1. Eur. J. Biochem. 187:1990;89-94.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 89-94
    • Meggio, F.1    Shugar, D.2    Pinna, L.A.3
  • 27
    • 0032079821 scopus 로고    scopus 로고
    • Calcium-sensitive particulate guanylyl cyclase as a modulator of cAMP in olfactory receptor neurons
    • Moon C., Jaberi P., Otto-Bruc A., Baehr W., Palczewski K., Ronnett G.V. Calcium-sensitive particulate guanylyl cyclase as a modulator of cAMP in olfactory receptor neurons. J. Neurosci. 18:1998;3195-3205.
    • (1998) J. Neurosci. , vol.18 , pp. 3195-3205
    • Moon, C.1    Jaberi, P.2    Otto-Bruc, A.3    Baehr, W.4    Palczewski, K.5    Ronnett, G.V.6
  • 28
    • 0030010051 scopus 로고    scopus 로고
    • Localization and activity of haem oxygenase and functional effects of carbon monoxide in the feline lower oesophageal sphincter
    • Ny L., Alm P., Ekstrom P., Larsson B., Grundemar L., Andersson K.E. Localization and activity of haem oxygenase and functional effects of carbon monoxide in the feline lower oesophageal sphincter. Br. J. Pharmacol. 118:1996;392-399.
    • (1996) Br. J. Pharmacol. , vol.118 , pp. 392-399
    • Ny, L.1    Alm, P.2    Ekstrom, P.3    Larsson, B.4    Grundemar, L.5    Andersson, K.E.6
  • 29
    • 0343035632 scopus 로고    scopus 로고
    • Morphological relations between haem oxygenases, NO-synthase and VIP in the canine and feline gastrointestinal tracts
    • Ny L., Alm P., Larsson B., Andersson K.E. Morphological relations between haem oxygenases, NO-synthase and VIP in the canine and feline gastrointestinal tracts. J. Auton. Nerv. Syst. 65:1997;49-56.
    • (1997) J. Auton. Nerv. Syst. , vol.65 , pp. 49-56
    • Ny, L.1    Alm, P.2    Larsson, B.3    Andersson, K.E.4
  • 30
    • 0027232056 scopus 로고
    • Nerve mediated relaxation of the human internal anal sphincter: The role of nitric oxide
    • O'Kelly T., Brading A., Mortensen N. Nerve mediated relaxation of the human internal anal sphincter. the role of nitric oxide Gut. 34:1993;689-693.
    • (1993) Gut , vol.34 , pp. 689-693
    • O'Kelly, T.1    Brading, A.2    Mortensen, N.3
  • 31
    • 0037107552 scopus 로고    scopus 로고
    • Protein kinase CK2: A challenge to canons
    • Pinna L.A. Protein kinase CK2. a challenge to canons J. Cell Sci. 115:2002;3873-3878.
    • (2002) J. Cell Sci. , vol.115 , pp. 3873-3878
    • Pinna, L.A.1
  • 32
    • 0027428932 scopus 로고
    • Inhibitory effect of CO on internal anal sphincter: Heme oxygenase inhibitor inhibits NANC relaxation
    • Rattan S., Chakder S. Inhibitory effect of CO on internal anal sphincter. heme oxygenase inhibitor inhibits NANC relaxation Am. J. Physiol. 265:1993;G799-G804.
    • (1993) Am. J. Physiol. , vol.265
    • Rattan, S.1    Chakder, S.2
  • 33
    • 0033842260 scopus 로고    scopus 로고
    • Influence of heme oxygenase inhibitors on the basal tissue enzymatic activity and smooth muscle relaxation of internal anal sphincter
    • Rattan S., Chakder S. Influence of heme oxygenase inhibitors on the basal tissue enzymatic activity and smooth muscle relaxation of internal anal sphincter. J. Pharmacol. Exp. Ther. 294:2000;1009-1016.
    • (2000) J. Pharmacol. Exp. Ther. , vol.294 , pp. 1009-1016
    • Rattan, S.1    Chakder, S.2
  • 34
    • 0025934770 scopus 로고
    • Primary culture of neonatal rat olfactory neurons
    • Ronnett G.V., Hester L.D., Snyder S.H. Primary culture of neonatal rat olfactory neurons. J. Neurosci. 11:1991;1243-1255.
    • (1991) J. Neurosci. , vol.11 , pp. 1243-1255
    • Ronnett, G.V.1    Hester, L.D.2    Snyder, S.H.3
  • 35
    • 0026605405 scopus 로고
    • Purification and characterization of echinoderm casein kinase II. Regulation by protein kinase C
    • Sanghera J.S., Charlton L.A., Paddon H.B., Pelech S.L. Purification and characterization of echinoderm casein kinase II. Regulation by protein kinase C. Biochem. J. 283:1992;829-837.
    • (1992) Biochem. J. , vol.283 , pp. 829-837
    • Sanghera, J.S.1    Charlton, L.A.2    Paddon, H.B.3    Pelech, S.L.4
  • 36
    • 0035805108 scopus 로고    scopus 로고
    • Selectivity of 4,5,6,7-tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 ("casein kinase-2")
    • Sarno S., Reddy H., Meggio F., Ruzzene M., Davies S.P., Donella-Deana A., Shugar D., Pinna L.A. Selectivity of 4,5,6,7-tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 ("casein kinase-2"). FEBS Lett. 496:2001;44-48.
    • (2001) FEBS Lett. , vol.496 , pp. 44-48
    • Sarno, S.1    Reddy, H.2    Meggio, F.3    Ruzzene, M.4    Davies, S.P.5    Donella-Deana, A.6    Shugar, D.7    Pinna, L.A.8
  • 37
    • 0036079617 scopus 로고    scopus 로고
    • Platelet-activating factor (PAF) activates casein kinase 2 in the protozoan parasite Herpetomonas muscarum muscarum
    • Silva-Neto M.A., Carneiro A.B., Vieira D.P., Mesquita R.D., Lopes A.H. Platelet-activating factor (PAF) activates casein kinase 2 in the protozoan parasite Herpetomonas muscarum muscarum. Biochem. Biophys. Res. Commun. 293:2002;1358-1363.
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 1358-1363
    • Silva-Neto, M.A.1    Carneiro, A.B.2    Vieira, D.P.3    Mesquita, R.D.4    Lopes, A.H.5
  • 38
    • 0034604726 scopus 로고    scopus 로고
    • Endogenous protein kinase CK2 participates in Wnt signaling in mammary epithelial cells
    • Song D.H., Sussman D.J., Seldin D.C. Endogenous protein kinase CK2 participates in Wnt signaling in mammary epithelial cells. J. Biol. Chem. 275:2000;23790-23797.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23790-23797
    • Song, D.H.1    Sussman, D.J.2    Seldin, D.C.3
  • 39
    • 0028939610 scopus 로고
    • Halogenated benzimidazoles and benzotriazoles as selective inhibitors of protein kinases CK I and CK II from Saccharomyces cerevisiae and other sources
    • Szyszka R., Grankowski N., Felczak K., Shugar D. Halogenated benzimidazoles and benzotriazoles as selective inhibitors of protein kinases CK I and CK II from Saccharomyces cerevisiae and other sources. Biochem. Biophys. Res. Commun. 208:1995;418-424.
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 418-424
    • Szyszka, R.1    Grankowski, N.2    Felczak, K.3    Shugar, D.4
  • 41
    • 0031040997 scopus 로고    scopus 로고
    • Conventional PKC-alpha, novel PKC-epsilon and PKC-theta, but not atypical PKC-lambda are MARCKS kinases in intact NIH 3T3 fibroblasts
    • Uberall F., Giselbrecht S., Hellbert K., Fresser F., Bauer B., Gschwendt M., Grunicke H.H., Baier G. Conventional PKC-alpha, novel PKC-epsilon and PKC-theta, but not atypical PKC-lambda are MARCKS kinases in intact NIH 3T3 fibroblasts. J. Biol. Chem. 272:1997;4072-4078.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4072-4078
    • Uberall, F.1    Giselbrecht, S.2    Hellbert, K.3    Fresser, F.4    Bauer, B.5    Gschwendt, M.6    Grunicke, H.H.7    Baier, G.8
  • 43
    • 0031016768 scopus 로고    scopus 로고
    • Carbon monoxide-induced relaxation and distribution of haem oxygenase isoenzymes in the pig urethra and lower oesophagogastric junction
    • Werkstrom V., Ny L., Persson K., Andersson K.E. Carbon monoxide-induced relaxation and distribution of haem oxygenase isoenzymes in the pig urethra and lower oesophagogastric junction. Br. J. Pharmacol. 120:1997;312-318.
    • (1997) Br. J. Pharmacol. , vol.120 , pp. 312-318
    • Werkstrom, V.1    Ny, L.2    Persson, K.3    Andersson, K.E.4
  • 44
    • 0034652357 scopus 로고    scopus 로고
    • Carbon monoxide and nitric oxide as coneurotransmitters in the enteric nervous system: Evidence from genomic deletion of biosynthetic enzymes
    • Xue L., Farrugia G., Miller S.M., Ferris C.D., Snyder S.H., Szurszewski J.H. Carbon monoxide and nitric oxide as coneurotransmitters in the enteric nervous system. evidence from genomic deletion of biosynthetic enzymes Proc. Natl. Acad. Sci. USA. 97:2000;1851-1855.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1851-1855
    • Xue, L.1    Farrugia, G.2    Miller, S.M.3    Ferris, C.D.4    Snyder, S.H.5    Szurszewski, J.H.6
  • 47
    • 0030960783 scopus 로고    scopus 로고
    • Identification of a long-lasting form of odor adaptation that depends on the carbon monoxide/cGMP second-messenger system
    • Zufall F., Leinders-Zufall T. Identification of a long-lasting form of odor adaptation that depends on the carbon monoxide/cGMP second-messenger system. J. Neurosci. 17:1997;2703-2712.
    • (1997) J. Neurosci. , vol.17 , pp. 2703-2712
    • Zufall, F.1    Leinders-Zufall, T.2


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