메뉴 건너뛰기




Volumn 50, Issue 1-2, 1997, Pages 267-276

Activation of heme oxygenase and consequent carbon monoxide formation inhibits the release of arginine vasopressin from rat hypothalamic explants. Molecular linkage between heme catabolism and neuroendocrine function

Author keywords

Biliverdin; Carbon monoxide; Heme oxygenase; Hemin; Hypothalamus; Vasopressin

Indexed keywords

ARGIPRESSIN; BILIVERDIN; CARBON MONOXIDE; HEME OXYGENASE; HEME OXYGENASE INHIBITOR; HEMIN; MESOPORPHYRIN TIN; POTASSIUM CHLORIDE; PROTOPORPHYRIN ZINC; VASOPRESSIN;

EID: 0030682163     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-328X(97)00197-6     Document Type: Article
Times cited : (58)

References (34)
  • 2
    • 0027471457 scopus 로고
    • Nitric oxide modulates the release of corticotropin-releasing hormone from the rat hypothalamus in vitro
    • A. Costa, P. Trainer, M. Besser, A. Grossman, Nitric oxide modulates the release of corticotropin-releasing hormone from the rat hypothalamus in vitro, Brain Res. 605 (1993) 187-192.
    • (1993) Brain Res. , vol.605 , pp. 187-192
    • Costa, A.1    Trainer, P.2    Besser, M.3    Grossman, A.4
  • 3
    • 0023854047 scopus 로고
    • Evidence suggesting that the two forms of heme oxygenase are products of different genes
    • I. Cruse, M. Maines, Evidence suggesting that the two forms of heme oxygenase are products of different genes, J. Biol. Chem. 263 (1988) 3348-3353.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3348-3353
    • Cruse, I.1    Maines, M.2
  • 4
    • 0026542512 scopus 로고
    • Normal and heat-induced pattern of expression of heme oxygenase-1 (HSP32) in rat brain: Hyperthermia causes rapid induction of mRNA and protein
    • J.F. Ewing, S.N. Haber, M.D. Maines, Normal and heat-induced pattern of expression of heme oxygenase-1 (HSP32) in rat brain: hyperthermia causes rapid induction of mRNA and protein, J. Neurochem. 58 (1992) 1140-1149.
    • (1992) J. Neurochem. , vol.58 , pp. 1140-1149
    • Ewing, J.F.1    Haber, S.N.2    Maines, M.D.3
  • 5
    • 0027054312 scopus 로고
    • In situ hybridization and immunohistochemical localization of heme oxygenase-2 mRNA and protein in normal rat brain: Differential distribution of isozyme 1 and 2
    • J.F. Ewing, M.D. Maines, In situ hybridization and immunohistochemical localization of heme oxygenase-2 mRNA and protein in normal rat brain: differential distribution of isozyme 1 and 2, Mol. Cell. Neurosci. 3 (1992) 559-570.
    • (1992) Mol. Cell. Neurosci. , vol.3 , pp. 559-570
    • Ewing, J.F.1    Maines, M.D.2
  • 6
    • 0027176344 scopus 로고
    • Biliverdin reductase is heat resistant and coexpressed with constitutive and heat shock forms of heme oxygenase in brain
    • J.F. Ewing, C.M. Weber, M.D. Maines, Biliverdin reductase is heat resistant and coexpressed with constitutive and heat shock forms of heme oxygenase in brain, J. Neurochem. 61 (1993) 1015-1023.
    • (1993) J. Neurochem. , vol.61 , pp. 1015-1023
    • Ewing, J.F.1    Weber, C.M.2    Maines, M.D.3
  • 7
    • 0343188694 scopus 로고
    • Pituitary and plasma vasopressin concentrations and fluid balance throughout the oestrous cycle in tha rat
    • M.L. Forsling, K. Peysner, Pituitary and plasma vasopressin concentrations and fluid balance throughout the oestrous cycle in tha rat. J. Endocrinol. 116 (1988) 335-341.
    • (1988) J. Endocrinol. , vol.116 , pp. 335-341
    • Forsling, M.L.1    Peysner, K.2
  • 9
    • 0018095311 scopus 로고
    • Destruction of heme and hemoproteins mediated by liver microsomal reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 reductase
    • F.P. Guengerich, Destruction of heme and hemoproteins mediated by liver microsomal reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 reductase, Biochemistry 17 (1978) 3633-3639.
    • (1978) Biochemistry , vol.17 , pp. 3633-3639
    • Guengerich, F.P.1
  • 10
    • 0021275463 scopus 로고
    • Regulation of soluble guanylate cyclase activity by porphyrins and metalloporphyrins
    • L.J. Ignarro, B. Ballot, K.S. Wood, Regulation of soluble guanylate cyclase activity by porphyrins and metalloporphyrins, J. Biol. Chem. 259 (1984) 6201-6207.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6201-6207
    • Ignarro, L.J.1    Ballot, B.2    Wood, K.S.3
  • 11
    • 0029990994 scopus 로고    scopus 로고
    • Carbon monoxide: An endogenous modulator of the nitric oxide-cyclic GMP signaling system
    • T. Ingi, J. Cheng, G.V. Ronnett, Carbon monoxide: an endogenous modulator of the nitric oxide-cyclic GMP signaling system, Neuron 16 (1996) 835-842.
    • (1996) Neuron , vol.16 , pp. 835-842
    • Ingi, T.1    Cheng, J.2    Ronnett, G.V.3
  • 12
    • 0007559982 scopus 로고
    • The porphyrias
    • J.B. Stanbury, J.B. Wingaarden, D.S. Frederickson, J.L. Goldstein, M.S. Brown (Eds.), McGraw-Hill, New York
    • A. Kappas, S. Sassa, K.E. Anderson, The porphyrias, in: J.B. Stanbury, J.B. Wingaarden, D.S. Frederickson, J.L. Goldstein, M.S. Brown (Eds.), Metabolic Bases of Inherited Disease, 5th edn., McGraw-Hill, New York, 1982, pp. 1301-1384.
    • (1982) Metabolic Bases of Inherited Disease, 5th Edn. , pp. 1301-1384
    • Kappas, A.1    Sassa, S.2    Anderson, K.E.3
  • 13
  • 14
    • 0019887888 scopus 로고
    • Purification and characterization of biliverdin reductase from the rat liver
    • R.K. Kutty, M.D. Maines, Purification and characterization of biliverdin reductase from the rat liver, J. Biol. Chem. 256 (1981) 3956-3962.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3956-3962
    • Kutty, R.K.1    Maines, M.D.2
  • 15
    • 0029133298 scopus 로고
    • A sensitive microassay reveals marked regional differences in the capacity of rat brain to generate carbon monoxide
    • J.T. Laitinen, R.O. Juvonen, A sensitive microassay reveals marked regional differences in the capacity of rat brain to generate carbon monoxide, Brain Res. 694 (1995) 246-252.
    • (1995) Brain Res. , vol.694 , pp. 246-252
    • Laitinen, J.T.1    Juvonen, R.O.2
  • 16
    • 1042263983 scopus 로고    scopus 로고
    • Regulation of gonadotropin-releasing hormone (GnRH) secretion by heme molecules: A regulatory role for carbon monoxide?
    • C.A. Lamar, V.B. Mahesh, D.W. Brann, Regulation of gonadotropin-releasing hormone (GnRH) secretion by heme molecules: a regulatory role for carbon monoxide?. Endocrinology 137 (1996) 790-793.
    • (1996) Endocrinology , vol.137 , pp. 790-793
    • Lamar, C.A.1    Mahesh, V.B.2    Brann, D.W.3
  • 17
    • 0022632224 scopus 로고
    • Characterization of two constitutive forms of rat liver microsomal heme oxygenase: Only one molecular species of the enzyme is inducible
    • M.D. Maines, G. M. Trakshel, R.K. Kutty, Characterization of two constitutive forms of rat liver microsomal heme oxygenase: only one molecular species of the enzyme is inducible, J. Biol. Chem. 261 (1986) 411-419.
    • (1986) J. Biol. Chem. , vol.261 , pp. 411-419
    • Maines, M.D.1    Trakshel, G.M.2    Kutty, R.K.3
  • 18
    • 0028067882 scopus 로고
    • Inhibition of hippocampal heme oxygenase, nitric oxide synthase, and long-term potentiation by metalloporphyrins
    • M.K. Meffert, J.E. Haley, E.M. Schuman, H. Schulman, D.V. Madison, 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
  • 19
    • 0028902346 scopus 로고
    • Secondary alcohol metabolites mediate iron delocalization in cytosolic fractions of myocardial biopsies exposed to anticancer anthracyclines, novel linkage between anthracyclin metabolism and iron-induced cardiotoxicity
    • G. Minotti, A.F. Cavaliere, A. Mordente, M. Rossi, R. Schiavello, R. Zamparelli, G.F. Possati, Secondary alcohol metabolites mediate iron delocalization in cytosolic fractions of myocardial biopsies exposed to anticancer anthracyclines, Novel linkage between anthracyclin metabolism and iron-induced cardiotoxicity, J. Clin, Invest. 95 (1995) 1595-1605.
    • (1995) J. Clin. Invest. , vol.95 , pp. 1595-1605
    • Minotti, G.1    Cavaliere, A.F.2    Mordente, A.3    Rossi, M.4    Schiavello, R.5    Zamparelli, R.6    Possati, G.F.7
  • 20
    • 0028300814 scopus 로고
    • Carbon moxide modulates secretion of corticotropin-releasing factor from rat hypothalamic cell cultures
    • D. Parkes, J. Kasckow, W. Vale, Carbon moxide modulates secretion of corticotropin-releasing factor from rat hypothalamic cell cultures, Brain Res. 646 (1994) 315-318.
    • (1994) Brain Res. , vol.646 , pp. 315-318
    • Parkes, D.1    Kasckow, J.2    Vale, W.3
  • 21
    • 0018596222 scopus 로고
    • Studies on heme biosynthesis in the rat brain
    • V.A. Percy, B.C. Shanley, Studies on heme biosynthesis in the rat brain, J. Neurochem. 33 (1979) 1267.
    • (1979) J. Neurochem. , vol.33 , pp. 1267
    • Percy, V.A.1    Shanley, B.C.2
  • 22
    • 0028090560 scopus 로고
    • Carbon monoxide as a novel neuroendocrine modulator: Inhibition of stimulated crh release from acute rat hypoyhalamic explants
    • G. Pozzoli, C. Mancuso, A. Mirtella, P. Preziosi, A. Grossman, P. Navarra, Carbon monoxide as a novel neuroendocrine modulator: inhibition of stimulated CRH release from acute rat hypoyhalamic explants, Endocrinology 136 (1994) 2314-2317.
    • (1994) Endocrinology , vol.136 , pp. 2314-2317
    • Pozzoli, G.1    Mancuso, C.2    Mirtella, A.3    Preziosi, P.4    Grossman, A.5    Navarra, P.6
  • 23
    • 0018906431 scopus 로고
    • High performance liquid chromatographic separation and quantification of the four biliverdin dimethyl ester isomers of the IX series
    • R.D. Rasmussen, W.H. Yokoyama, S.G. Blumenthal, D.E. Bergstrom, B. Ruebner, High performance liquid chromatographic separation and quantification of the four biliverdin dimethyl ester isomers of the IX series, Anal. Biochem. 101 (1988) 66-74.
    • (1988) Anal. Biochem. , vol.101 , pp. 66-74
    • Rasmussen, R.D.1    Yokoyama, W.H.2    Blumenthal, S.G.3    Bergstrom, D.E.4    Ruebner, B.5
  • 24
    • 0028278727 scopus 로고
    • In the rat, endogenous nitric oxide modulates the response of the hypothalamic-pituitary-adrenal axis to interleukin-lβ, vasopressin, and oxytocin
    • C. Rivier, G.H. Shen, In the rat, endogenous nitric oxide modulates the response of the hypothalamic-pituitary-adrenal axis to interleukin-lβ, vasopressin, and oxytocin, J. Neurosci. 14 (1994) 1985-1993.
    • (1994) J. Neurosci. , vol.14 , pp. 1985-1993
    • Rivier, C.1    Shen, G.H.2
  • 25
    • 0021833801 scopus 로고
    • Characterization of the enzymatic and nonenzymatic peroxidative degradation of iron porphyrins and cytochrome P-450 heme
    • S.H. Schaefer, T.M. Harris, F.P. Guengerich, Characterization of the enzymatic and nonenzymatic peroxidative degradation of iron porphyrins and cytochrome P-450 heme, Biochemistry 24 (1985) 3254-3263.
    • (1985) Biochemistry , vol.24 , pp. 3254-3263
    • Schaefer, S.H.1    Harris, T.M.2    Guengerich, F.P.3
  • 26
    • 0026527808 scopus 로고
    • A microassay for heme oxygenase activity using thin-layer chromatography
    • E.E. Sierra, L.M. Nutter, A microassay for heme oxygenase activity using thin-layer chromatography, Anal. Biochem. 200 (1992) 27-30.
    • (1992) Anal. Biochem. , vol.200 , pp. 27-30
    • Sierra, E.E.1    Nutter, L.M.2
  • 27
    • 0026588683 scopus 로고
    • Elevated lead levels in a patient with sickle cell disease and inappropriate secretion of antidiuretic hormone
    • C.R. Suarez, L.E. Black III. R. Morrison Hurley, Elevated lead levels in a patient with sickle cell disease and inappropriate secretion of antidiuretic hormone, Pediatr. Emerg. Care 8 (1992) 88-90.
    • (1992) Pediatr. Emerg. Care , vol.8 , pp. 88-90
    • Suarez, C.R.1    Black L.E. III2    Hurley, R.M.3
  • 28
    • 0025303671 scopus 로고
    • Developmental expression of heme oxygenase isozymes in rat brain. Two HO-2 mRNAs are detected
    • Y. Sun, M.O. Rotenberg, M.D. Maines, Developmental expression of heme oxygenase isozymes in rat brain. Two HO-2 mRNAs are detected, J. Biol. Chem. 265 (1990) 8212-8217.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8212-8217
    • Sun, Y.1    Rotenberg, M.O.2    Maines, M.D.3
  • 29
    • 0014670945 scopus 로고
    • Microsomal heme oxygenase characterization of the enzyme
    • R. Tenhunen, H.S. Marver, R. Schmid, Microsomal heme oxygenase characterization of the enzyme, J. Biol. Chem. 244 (1969) 6388-6394.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6388-6394
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 30
    • 0025275376 scopus 로고
    • Opiate receptor subtype regulation of CRF 41 release from the rat hypothalamus in vitro
    • S. Tsagarakis, L.H. Rees, G. M. Besser, A. Grossman, Opiate receptor subtype regulation of CRF 41 release from the rat hypothalamus in vitro. Neuroendocrinology 51 (1990) 599-605.
    • (1990) Neuroendocrinology , vol.51 , pp. 599-605
    • Tsagarakis, S.1    Rees, L.H.2    Besser, G.M.3    Grossman, A.4
  • 32
    • 0027522767 scopus 로고
    • Melatonin and its analogues inhibit the basal and stimulated release of hypothalamic vasopressin and oxytocin in vitro
    • S.A. Yasin, A. Costa, G.M. Besser, D. Hucks, A. Grossman, M.L. Forsling, Melatonin and its analogues inhibit the basal and stimulated release of hypothalamic vasopressin and oxytocin in vitro, Endocrinology 132 (1993) 1329-1336.
    • (1993) Endocrinology , vol.132 , pp. 1329-1336
    • Yasin, S.A.1    Costa, A.2    Besser, G.M.3    Hucks, D.4    Grossman, A.5    Forsling, M.L.6
  • 33
    • 0020479234 scopus 로고
    • A comparative study of heme degradation by NADPH-cytochrome c reductase alone and by complete heme oxygenase system: Distinctive aspects of heme degradation by NADPH-cytochrome c reductase
    • T. Yoshinaga, S. Sassa, A. Kappas, A comparative study of heme degradation by NADPH-cytochrome c reductase alone and by complete heme oxygenase system: distinctive aspects of heme degradation by NADPH-cytochrome c reductase, J. Biol. Chem. 257 (1982) 7794-7802.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7794-7802
    • Yoshinaga, T.1    Sassa, S.2    Kappas, A.3
  • 34
    • 0027267817 scopus 로고
    • Nitric oxide and carbon monoxide produce activity-dependent long-term synaptic enhancement in hippocampus
    • M. Zhuo, S.A. Small, E.R. Kandel, R.D. Hawkins, Nitric oxide and carbon monoxide produce activity-dependent long-term synaptic enhancement in hippocampus. Science 260 (1993) 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.