메뉴 건너뛰기




Volumn 67, Issue 2, 1996, Pages 482-489

Expression of heme oxygenase isozyme mRNAs in the human brain and induction of heme oxygenase-1 by nitric oxide donors

Author keywords

Brain; Carbon monoxide; Glioblastoma; Heme oxygenase; Neuropeptide; Nitric oxide

Indexed keywords

8 BROMO CYCLIC GMP; CALCITONIN GENE RELATED PEPTIDE; CORTICOTROPIN RELEASING FACTOR; DACTINOMYCIN; ENDOTHELIN 1; HEAT SHOCK PROTEIN 70; HEME OXYGENASE; LINSIDOMINE; NEUROPEPTIDE; NITRIC OXIDE DONOR; NITROPRUSSIDE SODIUM; S NITROSOGLUTATHIONE; SODIUM NITRITE;

EID: 0030056221     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.67020482.x     Document Type: Article
Times cited : (94)

References (70)
  • 1
    • 0019948176 scopus 로고
    • Alternative RNA processing in calcitonin gene expression generates mRNAs encoding different polypeptide products
    • Amara S. G., Jonas V., Rosenfeld M. G., Ong E. S., and Evans R. M. (1982) Alternative RNA processing in calcitonin gene expression generates mRNAs encoding different polypeptide products. Nature 298, 240-244.
    • (1982) Nature , vol.298 , pp. 240-244
    • Amara, S.G.1    Jonas, V.2    Rosenfeld, M.G.3    Ong, E.S.4    Evans, R.M.5
  • 2
    • 0028798838 scopus 로고
    • Evidence for the involvement of hippocampal CO production in the acquisition and consolidation of inhibitory avoidance learning
    • Bernabeu R., Princ F., Levi de Stein M., Fin C., Juknat A. A., Batile A., Izquierdo I., and Medina J. H. (1995) Evidence for the involvement of hippocampal CO production in the acquisition and consolidation of inhibitory avoidance learning. Neuroreport 6, 516-518.
    • (1995) Neuroreport , vol.6 , pp. 516-518
    • Bernabeu, R.1    Princ, F.2    Levi De Stein, M.3    Fin, C.4    Juknat, A.A.5    Batile, A.6    Izquierdo, I.7    Medina, J.H.8
  • 3
    • 0029122409 scopus 로고
    • Modulation of carbon monoxide production and enhanced spatial learning by tin protoporphyrin
    • Bing O., Grundemar L., Ny L., Moller C., and Heilig M. (1995) Modulation of carbon monoxide production and enhanced spatial learning by tin protoporphyrin. Neuroreport 6, 1241-1244.
    • (1995) Neuroreport , vol.6 , pp. 1241-1244
    • Bing, O.1    Grundemar, L.2    Ny, L.3    Moller, C.4    Heilig, M.5
  • 4
    • 0026702955 scopus 로고
    • Microglial-produced nitric oxide and reactive nitrogen oxides mediate neuronal cell death
    • Boje K. M. and Arora P. K. (1992) Microglial-produced nitric oxide and reactive nitrogen oxides mediate neuronal cell death. Brain Res. 587, 250-256.
    • (1992) Brain Res. , vol.587 , pp. 250-256
    • Boje, K.M.1    Arora, P.K.2
  • 5
    • 0015914428 scopus 로고
    • Hypothalamic polypeptide that inhibits the secretion of immunoreactive pituitary growth hormone
    • Brazeau P., Vale W., Burgus R., Ling N., Butcher M., Rivier R., and Guillemin R. (1973) Hypothalamic polypeptide that inhibits the secretion of immunoreactive pituitary growth hormone. Science 179, 77-79.
    • (1973) Science , vol.179 , pp. 77-79
    • Brazeau, P.1    Vale, W.2    Burgus, R.3    Ling, N.4    Butcher, M.5    Rivier, R.6    Guillemin, R.7
  • 6
    • 0025011298 scopus 로고
    • Localization of nitric oxide synthase indicating a neural role for nitric oxide
    • Bredt D. S., Hwang P. M., and Snyder S. H. (1990) Localization of nitric oxide synthase indicating a neural role for nitric oxide. Nature 347, 768-770.
    • (1990) Nature , vol.347 , pp. 768-770
    • Bredt, D.S.1    Hwang, P.M.2    Snyder, S.H.3
  • 7
    • 0023490534 scopus 로고
    • Inhibition of platelet aggregation by carbon monoxide is mediated by activation of guanylate cyclase
    • Brune B. and Ullrich V. (1987) Inhibition of platelet aggregation by carbon monoxide is mediated by activation of guanylate cyclase. Mol. Pharmacol. 32, 497-504.
    • (1987) Mol. Pharmacol. , vol.32 , pp. 497-504
    • Brune, B.1    Ullrich, V.2
  • 8
    • 0027471457 scopus 로고
    • Nitric oxide modulates the release of corticotropin-releasing hormone from the rat hypothalamus in vitro
    • Costa A., Trainer P., Besser M., and Grossman A. (1993) Nitric oxide modulates the release of corticotropin-releasing hormone from the rat hypothalamus in vitro. Brain Res. 605, 187-192.
    • (1993) Brain Res. , vol.605 , pp. 187-192
    • Costa, A.1    Trainer, P.2    Besser, M.3    Grossman, A.4
  • 9
    • 0023854047 scopus 로고
    • Evidence suggesting that the two forms of heme oxygenase are products of different genes
    • Cruse I. and Maines M. D. (1988) Evidence suggesting that the two forms of heme oxygenase are products of different genes. J. Biol. Chem. 263, 3348-3353.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3348-3353
    • Cruse, I.1    Maines, M.D.2
  • 11
    • 0004559340 scopus 로고
    • Pressor effects of circulating endothelin are limited by its removal in the pulmonary circulation and by the release of prostacyclin and endothelium-derived relaxing factor
    • DeNucci G., Thomas R., D'Orleans-Juste P., Antunes E., Walder C., Warner T. D., and Vane J. R. (1988) Pressor effects of circulating endothelin are limited by its removal in the pulmonary circulation and by the release of prostacyclin and endothelium-derived relaxing factor. Proc. Natl. Acad. Sci. USA 85, 9797-9800.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9797-9800
    • DeNucci, G.1    Thomas, R.2    D'Orleans-Juste, P.3    Antunes, E.4    Walder, C.5    Warner, T.D.6    Vane, J.R.7
  • 12
    • 0028929896 scopus 로고
    • Differential expression of heme oxygenase-1 in cultured cortical neurons and astrocytes determined by the aid of a new heme oxygenase antibody. Response to oxidative stress
    • Dwyer B. E., Nishimura R. N., and Lu S.-Y. (1995) Differential expression of heme oxygenase-1 in cultured cortical neurons and astrocytes determined by the aid of a new heme oxygenase antibody. Response to oxidative stress. Mol. Brain Res. 30, 37-47.
    • (1995) Mol. Brain Res. , vol.30 , pp. 37-47
    • Dwyer, B.E.1    Nishimura, R.N.2    Lu, S.-Y.3
  • 13
    • 0026012324 scopus 로고
    • Rapid induction of heme oxygenase 1 mRNA and protein by hyperthermia in rat brain: Heme oxygenase 2 is not a heat shock protein
    • Ewing J. F. and Maines M. D. (1991) Rapid induction of heme oxygenase 1 mRNA and protein by hyperthermia in rat brain: heme oxygenase 2 is not a heat shock protein. Proc. Natl. Acad. Sci. USA 88, 5364-5368.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5364-5368
    • Ewing, J.F.1    Maines, M.D.2
  • 14
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg A. P. and Vogelstein B. (1983) A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132, 6-13.
    • (1983) Anal. Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 15
    • 0027996042 scopus 로고
    • Intrahippocampal, but not intra-amygdala, infusion of an inhibitor of heme oxygenase causes retrograde amnesia in the rat
    • Fin C., Schmitz P. K., Da Silva R. C., Bernabeu R., Medina J. H., and Izquierdo I. (1994) Intrahippocampal, but not intra-amygdala, infusion of an inhibitor of heme oxygenase causes retrograde amnesia in the rat. Eur. J. Pharmacol. 271, 227-229.
    • (1994) Eur. J. Pharmacol. , vol.271 , pp. 227-229
    • Fin, C.1    Schmitz, P.K.2    Da Silva, R.C.3    Bernabeu, R.4    Medina, J.H.5    Izquierdo, I.6
  • 16
    • 0028200313 scopus 로고
    • Expression of two types of nitric oxide synthase mRNA in human neuroblastoma cell lines
    • Fujisawa H., Ogura T., Kurashima Y., Yokoyama T., Yamashita J., and Esumi H. (1994) Expression of two types of nitric oxide synthase mRNA in human neuroblastoma cell lines. J. Neurochem. 63, 140-145.
    • (1994) J. Neurochem. , vol.63 , pp. 140-145
    • Fujisawa, H.1    Ogura, T.2    Kurashima, Y.3    Yokoyama, T.4    Yamashita, J.5    Esumi, H.6
  • 17
    • 0026034934 scopus 로고
    • Endothelium-dependent and -independent vasodilation involving cyclic GMP: Relaxation induced by nitric oxide, carbon monoxide and light
    • Furchgott R. F. and Jothianandan D. (1991) Endothelium-dependent and -independent vasodilation involving cyclic GMP: relaxation induced by nitric oxide, carbon monoxide and light. Blood Vessels 28, 52-61.
    • (1991) Blood Vessels , vol.28 , pp. 52-61
    • Furchgott, R.F.1    Jothianandan, D.2
  • 18
    • 0028814999 scopus 로고
    • A heme oxygenase product, presumably carbon monoxide, mediates a vasodepressor function in rats
    • Johnson R. A., Lavesa M., Askari B., Abraham N. G., and Nasjletti A. (1995) A heme oxygenase product, presumably carbon monoxide, mediates a vasodepressor function in rats. Hypertension 25, 166-169.
    • (1995) Hypertension , vol.25 , pp. 166-169
    • Johnson, R.A.1    Lavesa, M.2    Askari, B.3    Abraham, N.G.4    Nasjletti, A.5
  • 19
    • 0020643565 scopus 로고
    • Characterization of melanin-concentrating hormone in chum salmon pituitaries
    • Kawauchi H., Kawazoe I., Tsubokawa M., Kishida M., and Baker B. L. (1983) Characterization of melanin-concentrating hormone in chum salmon pituitaries. Nature 305, 321-323.
    • (1983) Nature , vol.305 , pp. 321-323
    • Kawauchi, H.1    Kawazoe, I.2    Tsubokawa, M.3    Kishida, M.4    Baker, B.L.5
  • 20
    • 0024497521 scopus 로고
    • Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite
    • Keyse S. M. and Tyrrell R. M. (1989) Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite. Proc. Natl. Acad. Sci. USA 86, 99-103.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 99-103
    • Keyse, S.M.1    Tyrrell, R.M.2
  • 22
    • 0025952267 scopus 로고
    • Natriuretic peptides inhibit rat astroglial proliferation: Mediation by C receptor
    • Levin E. R. and Frank H. J. L. (1991) Natriuretic peptides inhibit rat astroglial proliferation: mediation by C receptor. Am. J. Physiol. 261, R453-R457.
    • (1991) Am. J. Physiol. , vol.261
    • Levin, E.R.1    Frank, H.J.L.2
  • 23
    • 0027194540 scopus 로고
    • A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compound
    • Lipton S. A., Choi Y.-B., Pan Z.-H., Lei S. Z., Chen H.-S. V., Sucher N. J., Loscalzo J., Singel D. J., and Stamler J. S. (1993) A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compound. Nature 364, 626-632.
    • (1993) Nature , vol.364 , pp. 626-632
    • Lipton, S.A.1    Choi, Y.-B.2    Pan, Z.-H.3    Lei, S.Z.4    Chen, H.-S.V.5    Sucher, N.J.6    Loscalzo, J.7    Singel, D.J.8    Stamler, J.S.9
  • 24
    • 0026688148 scopus 로고
    • Nitric oxide, a novel biologic messenger
    • Lowenstein C. J. and Snyder S. H. (1992) Nitric oxide, a novel biologic messenger. Cell 70, 705-707.
    • (1992) Cell , vol.70 , pp. 705-707
    • Lowenstein, C.J.1    Snyder, S.H.2
  • 25
    • 0026653813 scopus 로고
    • Human heme oxygenase-2: Characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal
    • McCoubrey W. K. Jr., Ewing J. F., and Maines M. D. (1992) Human heme oxygenase-2: characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal. Arch. Biochem. Biophys. 295, 13-20.
    • (1992) Arch. Biochem. Biophys. , vol.295 , pp. 13-20
    • McCoubrey Jr., W.K.1    Ewing, J.F.2    Maines, M.D.3
  • 26
    • 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., and Madison D. V. (1994) Inhibition of hippocampal heme oxygenase, nitric oxide synthase, and long-term potentiation by metalloporphyrins. Neuron 13, 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
  • 28
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology and pharmacology
    • Moncada S., Palmer R. M. J., and Higgs E. A. (1991) Nitric oxide: physiology, pathophysiology and pharmacology. Pharmacol. Rev. 43, 109-142.
    • (1991) Pharmacol. Rev. , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.J.2    Higgs, E.A.3
  • 29
    • 0027428648 scopus 로고
    • Nitric oxide regulates luteininzing hormone-releasing hormone secretion
    • Moretto M., Lopez F. J., and Negro-Vilar A. (1993) Nitric oxide regulates luteininzing hormone-releasing hormone secretion. Endocrinology 133, 2399-2402.
    • (1993) Endocrinology , vol.133 , pp. 2399-2402
    • Moretto, M.1    Lopez, F.J.2    Negro-Vilar, A.3
  • 30
    • 0026629902 scopus 로고
    • Nitric oxide as a secretory product of mammalian cells
    • Nathan C. (1992) Nitric oxide as a secretory product of mammalian cells. FASEB J. 6, 3051-3064.
    • (1992) FASEB J. , vol.6 , pp. 3051-3064
    • Nathan, C.1
  • 31
    • 0028941685 scopus 로고
    • + pump as a site of action for carbon monoxide and glutamate: A mechanism for long-term modulation of cellular activity
    • + pump as a site of action for carbon monoxide and glutamate: a mechanism for long-term modulation of cellular activity. Neuron 14, 781-794.
    • (1995) Neuron , vol.14 , pp. 781-794
    • Nathanson, J.A.1    Scavone, C.2    Scanlon, C.3    McKee, M.4
  • 33
    • 0028300814 scopus 로고
    • Carbon monoxide modulates secretion of corticotropin-releasing factor from rat hypothalamic cell cultures
    • Parkes D., Kasckow J., and Vale W. (1994) Carbon monoxide modulates secretion of corticotropin-releasing factor from rat hypothalamic cell cultures. Brain Res. 646, 315-318.
    • (1994) Brain Res. , vol.646 , pp. 315-318
    • Parkes, D.1    Kasckow, J.2    Vale, W.3
  • 34
    • 0028880959 scopus 로고
    • Hippocampal long-term potentiation is normal in heme oxygenase-2 mutant mice
    • Poss K. D., Thomas M. J., Ebralidze A. K., O'Dell T. J., and Tonegawa S. (1995) Hippocampal long-term potentiation is normal in heme oxygenase-2 mutant mice. Neuron 15, 867-873.
    • (1995) Neuron , vol.15 , pp. 867-873
    • Poss, K.D.1    Thomas, M.J.2    Ebralidze, A.K.3    O'Dell, T.J.4    Tonegawa, S.5
  • 35
    • 0028090560 scopus 로고
    • Carbon monoxide as a novel neuroendocrine modulator: Inhibition of stimulated corticotropin-releasing hormone release from acute rat hypothalamic explants
    • Pozzoli G., Mancuso C., Mirtella A., Preziosi P., Grossman A. B., and Navarra P. (1994) Carbon monoxide as a novel neuroendocrine modulator: inhibition of stimulated corticotropin-releasing hormone release from acute rat hypothalamic explants. Endocrinology 135, 2314-2317.
    • (1994) Endocrinology , vol.135 , pp. 2314-2317
    • Pozzoli, G.1    Mancuso, C.2    Mirtella, A.3    Preziosi, P.4    Grossman, A.B.5    Navarra, P.6
  • 38
    • 0027428932 scopus 로고
    • Inhibitory effect of CO on internal anal sphincter: Heme oxygenase inhibitor inhibits NANC relaxation
    • Rattan S. and Chakder S. (1993) Inhibitory effect of CO on internal anal sphincter: heme oxygenase inhibitor inhibits NANC relaxation. Am. J. Physiol. 265, G799-G804.
    • (1993) Am. J. Physiol. , vol.265
    • Rattan, S.1    Chakder, S.2
  • 39
    • 0028300689 scopus 로고
    • Expression of pituitary adenylate cyclase activating polypeptide (PACAP) receptors in human glial cell tumors
    • Robberecht P., Woussen-Colle M.-C., Vertongen P., De Neef P., Hou X., Salmon I., and Brotchi J. (1994) Expression of pituitary adenylate cyclase activating polypeptide (PACAP) receptors in human glial cell tumors. Peptides 15, 661-665.
    • (1994) Peptides , vol.15 , pp. 661-665
    • Robberecht, P.1    Woussen-Colle, M.-C.2    Vertongen, P.3    De Neef, P.4    Hou, X.5    Salmon, I.6    Brotchi, J.7
  • 41
    • 0029032632 scopus 로고
    • Expression of heme oxygenase-1 in the senescent and Alzheimer-diseased brain
    • Schipper H. M., Cisse S., and Stopa E. G. (1995) Expression of heme oxygenase-1 in the senescent and Alzheimer-diseased brain. Ann. Neurol. 37, 758-768.
    • (1995) Ann. Neurol. , vol.37 , pp. 758-768
    • Schipper, H.M.1    Cisse, S.2    Stopa, E.G.3
  • 42
    • 0024100201 scopus 로고
    • Regulation of heme oxygenase gene expression. Semin
    • Shibahara S. (1988) Regulation of heme oxygenase gene expression. Semin. Hematol. 25, 370-376.
    • (1988) Hematol. , vol.25 , pp. 370-376
    • Shibahara, S.1
  • 43
    • 0000916150 scopus 로고
    • Heme oxygenase - Regulation of and physiological implication in heme catabolism
    • (Fujita H., ed), AlphaMed Press, Medina, Ohio
    • Shibahara S. (1994) Heme oxygenase - regulation of and physiological implication in heme catabolism, in Regulation of Heme Protein Synthesis (Fujita H., ed), pp. 103-116. AlphaMed Press, Medina, Ohio.
    • (1994) Regulation of Heme Protein Synthesis , pp. 103-116
    • Shibahara, S.1
  • 44
    • 0023665016 scopus 로고
    • Transcriptional control of rat heme oxygenase by heat shock
    • Shibahara S., Muller R. M., and Taguchi H. (1987) Transcriptional control of rat heme oxygenase by heat shock. J. Biol. Chem. 262, 12889-12892.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12889-12892
    • Shibahara, S.1    Muller, R.M.2    Taguchi, H.3
  • 45
    • 0027532668 scopus 로고
    • Functional analysis of cDNAs for two types of human heme oxygenase and evidence for their separate regulation
    • Shibahara S., Yoshizawa M., Suzuki H., Takeda K., Meguro K., and Endo K. (1993) Functional analysis of cDNAs for two types of human heme oxygenase and evidence for their separate regulation. J. Biochem. (Tokyo) 113, 214-218.
    • (1993) J. Biochem. (Tokyo) , vol.113 , pp. 214-218
    • Shibahara, S.1    Yoshizawa, M.2    Suzuki, H.3    Takeda, K.4    Meguro, K.5    Endo, K.6
  • 46
    • 0027296209 scopus 로고
    • Reversal of long-term potentiation by inhibitors of haem oxygenase
    • Stevens C. F. and Wang Y. (1993) Reversal of long-term potentiation by inhibitors of haem oxygenase. Nature 364, 147-149.
    • (1993) Nature , vol.364 , pp. 147-149
    • Stevens, C.F.1    Wang, Y.2
  • 48
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological importance
    • Stocker R., Yamamoto Y., McDonagh A. F., Glazer A. N., and Ames B. N. (1987b) Bilirubin is an antioxidant of possible physiological importance. Science 235, 1043-1046.
    • (1987) Science , vol.235 , pp. 1043-1046
    • Stocker, R.1    Yamamoto, Y.2    McDonagh, A.F.3    Glazer, A.N.4    Ames, B.N.5
  • 49
    • 0026703832 scopus 로고
    • Atrial natriuretic peptide receptor subtypes in rat neuronal and astrocyte glial cultures
    • Sumners C. and Tang W. (1992) Atrial natriuretic peptide receptor subtypes in rat neuronal and astrocyte glial cultures. Am. J. Physiol. 262, C1134-C1143.
    • (1992) Am. J. Physiol. , vol.262
    • Sumners, C.1    Tang, W.2
  • 50
    • 0025303671 scopus 로고
    • Developmental expression of heme oxygenase isozymes in rat brain. Two HO-2 mRNAs are detected
    • Sun Y., Rotenberg M. O., and Maines M. D. (1990) Developmental expression of heme oxygenase isozymes in rat brain. Two HO-2 mRNAs are detected. J. Biol. Chem. 265, 8212-8217.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8212-8217
    • Sun, Y.1    Rotenberg, M.O.2    Maines, M.D.3
  • 51
    • 0024842995 scopus 로고
    • Free calcium rise and mitogenesis in glial cells caused by endothelin
    • Supattapone S., Simpson A. W. M., and Ashley C. C. (1989) Free calcium rise and mitogenesis in glial cells caused by endothelin. Biochem. Biophys. Res. Commun. 165, 1115-1122.
    • (1989) Biochem. Biophys. Res. Commun. , vol.165 , pp. 1115-1122
    • Supattapone, S.1    Simpson, A.W.M.2    Ashley, C.C.3
  • 52
    • 0026333880 scopus 로고
    • Brain tumors predominantly express the neurofibromatosis type 1 gene transcripts containing the 63 base insert in the region coding for GTPase activating protein-related domain
    • Suzuki Y., Suzuki H., Kayama T., Yoshimoto T., and Shibahara S. (1991) Brain tumors predominantly express the neurofibromatosis type 1 gene transcripts containing the 63 base insert in the region coding for GTPase activating protein-related domain. Biochem. Biophys. Res. Commun. 181, 955-961.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 955-961
    • Suzuki, Y.1    Suzuki, H.2    Kayama, T.3    Yoshimoto, T.4    Shibahara, S.5
  • 53
    • 0028116747 scopus 로고
    • Increased expression of heme oxygenase mRNA in rat brain following transient ischemia
    • Takeda A., Onodera H., Sugimoto A., Itoyama Y., Kogure K., and Shibahara S. (1994) Increased expression of heme oxygenase mRNA in rat brain following transient ischemia. Brain Res. 666, 120-124.
    • (1994) Brain Res. , vol.666 , pp. 120-124
    • Takeda, A.1    Onodera, H.2    Sugimoto, A.3    Itoyama, Y.4    Kogure, K.5    Shibahara, S.6
  • 54
    • 0028133168 scopus 로고
    • Identification of a cis-acting element that is responsible for cadmium-mediated induction of the human heme oxygenase gene
    • Takeda K., Ishizawa S., Sato M., Yoshida T., and Shibahara S. (1994) Identification of a cis-acting element that is responsible for cadmium-mediated induction of the human heme oxygenase gene. J. Biol. Chem. 269, 22858-22867.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22858-22867
    • Takeda, K.1    Ishizawa, S.2    Sato, M.3    Yoshida, T.4    Shibahara, S.5
  • 55
    • 0019944850 scopus 로고
    • Neuropeptide Y: A novel brain peptide with structural similarities to peptide YY and pancreatic polypeptide
    • Tatemoto K., Carlquist M., and Mutt V. (1982) Neuropeptide Y: a novel brain peptide with structural similarities to peptide YY and pancreatic polypeptide. Nature 296, 659-660.
    • (1982) Nature , vol.296 , pp. 659-660
    • Tatemoto, K.1    Carlquist, M.2    Mutt, V.3
  • 56
    • 0025356772 scopus 로고
    • Demonstration of specific binding sites for pituitary adenylate cyclase activating polypeptide (PACAP) in rat astrocytes
    • Tatsuno I., Gottschall P. E., Koves K., and Arimura A. (1990) Demonstration of specific binding sites for pituitary adenylate cyclase activating polypeptide (PACAP) in rat astrocytes. Biochem. Biophys. Res. Commun. 168, 1027-1033.
    • (1990) Biochem. Biophys. Res. Commun. , vol.168 , pp. 1027-1033
    • Tatsuno, I.1    Gottschall, P.E.2    Koves, K.3    Arimura, A.4
  • 57
    • 0014348401 scopus 로고
    • The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase
    • Tenhunen R., Marver H. S., and Schmid R. (1968) The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase. Proc. Natl. Acad. Sci. USA 61, 748-755.
    • (1968) Proc. Natl. Acad. Sci. USA , vol.61 , pp. 748-755
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 58
    • 0014670945 scopus 로고
    • Microsomal heme oxygenase. Characterization of the enzyme
    • Tenhunen R., Marver H. S., and Schmid R. (1969) Microsomal heme oxygenase. Characterization of the enzyme. J. Biol. Chem. 244, 6388-6394.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6388-6394
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 59
    • 0024494769 scopus 로고
    • Multiplicity of heme oxygenase isozymes-HO-1 and HO-2 are different molecular species in rat and rabbit
    • Trakshel G. M. and Maines M. D. (1989) Multiplicity of heme oxygenase isozymes-HO-1 and HO-2 are different molecular species in rat and rabbit. J. Biol. Chem. 264, 1323-1328.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1323-1328
    • Trakshel, G.M.1    Maines, M.D.2
  • 60
    • 0022977615 scopus 로고
    • Purification and characterization of the major constitutive form of testicular heme oxygenase. The noninducible isoform
    • Trakshel G. M., Kutty R. K., and Maines M. D. (1986) Purification and characterization of the major constitutive form of testicular heme oxygenase. The noninducible isoform. J. Biol. Chem. 261, 11131-11137.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11131-11137
    • Trakshel, G.M.1    Kutty, R.K.2    Maines, M.D.3
  • 61
    • 0023831291 scopus 로고
    • Resolution of the rat brain heme oxygenase activity: Absence of a detectable amount of the inducible form (HO-1)
    • Trakshel G. M., Kutty R. K., and Maines M. D. (1988) Resolution of the rat brain heme oxygenase activity: absence of a detectable amount of the inducible form (HO-1). Arch. Biochem. Biophys. 260, 732-739.
    • (1988) Arch. Biochem. Biophys. , vol.260 , pp. 732-739
    • Trakshel, G.M.1    Kutty, R.K.2    Maines, M.D.3
  • 63
    • 0028073463 scopus 로고
    • Brain heme oxygenase isozymes and nitric oxide synthase are co-localized in select neurons
    • Vincent S. R., Das S., and Maines M. D. (1994) Brain heme oxygenase isozymes and nitric oxide synthase are co-localized in select neurons. Neuroscience 63, 223-231.
    • (1994) Neuroscience , vol.63 , pp. 223-231
    • Vincent, S.R.1    Das, S.2    Maines, M.D.3
  • 64
    • 0026735580 scopus 로고
    • Nitric oxide synthase is a cytochrome P-450 type hemoprotein
    • White K. A. and Marletta M. A. (1992) Nitric oxide synthase is a cytochrome P-450 type hemoprotein. Biochemistry 31, 6627-6631.
    • (1992) Biochemistry , vol.31 , pp. 6627-6631
    • White, K.A.1    Marletta, M.A.2
  • 66
    • 0022002022 scopus 로고
    • Structure and expression of the human gene encoding major heat shock protein HSP70
    • Wu B., Hunt C., and Morimoto R. (1985) Structure and expression of the human gene encoding major heat shock protein HSP70. Mol. Cell. Biol. 5, 330-341.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 330-341
    • Wu, B.1    Hunt, C.2    Morimoto, R.3
  • 68
    • 0027213518 scopus 로고
    • Nitric oxide modulates the release of vasopressin from rat hypothalamic explants
    • Yasin S., Costa A., Trainer P., Windle R., Forsling M. L., and Grossman A. (1993) Nitric oxide modulates the release of vasopressin from rat hypothalamic explants. Endocrinology 133, 1466-1469.
    • (1993) Endocrinology , vol.133 , pp. 1466-1469
    • Yasin, S.1    Costa, A.2    Trainer, P.3    Windle, R.4    Forsling, M.L.5    Grossman, A.6
  • 70
    • 0027267817 scopus 로고
    • Nitric oxide and carbon monoxide produce activity-dependent long-term synaptic enhancement in hippocampus
    • Zhuo M., Small S. A., Kandel E. R., and Hawkins R. D. (1993) Nitric oxide and carbon monoxide produce activity-dependent long-term synaptic enhancement in hippocampus. Science 260, 1946-1950.
    • (1993) Science , vol.260 , pp. 1946-1950
    • Zhuo, M.1    Small, S.A.2    Kandel, E.R.3    Hawkins, R.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.