메뉴 건너뛰기




Volumn 21, Issue 4, 2000, Pages 337-344

Haem oxygenase activity in human umbilical cord and rat vascular tissues

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE; CHROMIUM; HEME; MESOPORPHYRIN; OXYGENASE; PROTEIN;

EID: 0034114951     PISSN: 01434004     EISSN: None     Source Type: Journal    
DOI: 10.1053/plac.1999.0495     Document Type: Article
Times cited : (20)

References (51)
  • 1
    • 0032032945 scopus 로고    scopus 로고
    • Hemeoxygenase-1 inhibits human myometrial contractility via carbon monoxide and is upregulated by progesterone during pregnancy
    • Acevedo CH, Ahmed A. Hemeoxygenase-1 inhibits human myometrial contractility via carbon monoxide and is upregulated by progesterone during pregnancy. J Clin Invest. 101:1998;949-955.
    • (1998) J Clin Invest , vol.101 , pp. 949-955
    • Acevedo, C.H.1    Ahmed, A.2
  • 6
  • 7
    • 0028217920 scopus 로고
    • Nitric-oxide synthase (NOS) in the human umbilical cord vessels: An immunohistochemical study
    • Dikranian K, Trosheva M, Nikolov S, Bodin P. Nitric-oxide synthase (NOS) in the human umbilical cord vessels: An immunohistochemical study. Acta Histochem. 96:1994;145-153.
    • (1994) Acta Histochem , vol.96 , pp. 145-153
    • Dikranian, K.1    Trosheva, M.2    Nikolov, S.3    Bodin, P.4
  • 8
    • 0021693485 scopus 로고
    • Methene bridge carbon atom elimination in oxidative heme degradation catalyzed by heme oxygenase and NADPH-cytochrome P-450 reductase
    • Docherty JC, Firneisz GD, Schacter BA. Methene bridge carbon atom elimination in oxidative heme degradation catalyzed by heme oxygenase and NADPH-cytochrome P-450 reductase. Arch Biochem Biophys. 235:1984;657-664.
    • (1984) Arch Biochem Biophys , vol.235 , pp. 657-664
    • Docherty, J.C.1    Firneisz, G.D.2    Schacter, B.A.3
  • 9
    • 0000647710 scopus 로고    scopus 로고
    • Carbon monoxide and vascular cell function (Review)
    • Durante W, Schafer AI. Carbon monoxide and vascular cell function (Review). Int J Molec Med. 2:1998;255-262.
    • (1998) Int J Molec Med , vol.2 , pp. 255-262
    • Durante, W.1    Schafer, A.I.2
  • 10
    • 0026034934 scopus 로고
    • Endothelium-dependent and -independent vasodilation involving cyclic GMP: Relaxation induced by nitric oxide, carbon monoxide and light
    • Furchgott RF, Jothianandan D. Endothelium-dependent and -independent vasodilation involving cyclic GMP: Relaxation induced by nitric oxide, carbon monoxide and light. Blood Vessels. 28:1991;52-61.
    • (1991) Blood Vessels , vol.28 , pp. 52-61
    • Furchgott, R.F.1    Jothianandan, D.2
  • 11
    • 0028903204 scopus 로고
    • Haem oxygenase activity in blood vessel homogenates as measured by carbon monoxide production
    • Grundemar L, Johansson MB, Ekelund M, Hogestatt ED. Haem oxygenase activity in blood vessel homogenates as measured by carbon monoxide production. Acta Physiol Scand. 153:1995;203-204.
    • (1995) Acta Physiol Scand , vol.153 , pp. 203-204
    • Grundemar, L.1    Johansson, M.B.2    Ekelund, M.3    Hogestatt, E.D.4
  • 12
    • 0021275463 scopus 로고
    • Regulation of soluble guanylate cyclase activity by porphyrins and metalloporphyrins
    • Ignarro LJ, Ballot B, Wood KS. 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
  • 14
    • 0032602310 scopus 로고    scopus 로고
    • Carbon monoxide: From toxin to endogenous modulator of cardiovascular functions
    • Johnson RA, Kozma F, Colombari E. Carbon monoxide: From toxin to endogenous modulator of cardiovascular functions. Braz J Med Biol Res. 32:1999;1-14.
    • (1999) Braz J Med Biol Res , vol.32 , pp. 1-14
    • Johnson, R.A.1    Kozma, F.2    Colombari, E.3
  • 15
    • 0032960103 scopus 로고    scopus 로고
    • Contribution of endogenous carbon monoxide to regulation of diameter in resistance vessels
    • Kozma F, Johnson RA, Zhang F, Yu C, Tong X, Nasjletti A. Contribution of endogenous carbon monoxide to regulation of diameter in resistance vessels. Am J Physiol. 276:1999;R1087-1094.
    • (1999) Am J Physiol , vol.276 , pp. 1087-1094
    • Kozma, F.1    Johnson, R.A.2    Zhang, F.3    Yu, C.4    Tong, X.5    Nasjletti, A.6
  • 16
    • 0027992219 scopus 로고
    • Simulation of the diffusion and reaction of endogenously produced nitric oxide
    • Lancaster JR Jr. Simulation of the diffusion and reaction of endogenously produced nitric oxide. Proc Natl Acad Sci USA. 91:1994;8137-8141.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8137-8141
    • Lancaster J.R., Jr.1
  • 17
    • 0017850799 scopus 로고
    • The effect of phenobarbital and 3-methylcholanthrene treatment on carbon tetrachloride-stimulated heme degradation and carbon monoxide expiration in vivo
    • Lindstrom AD, Anders MW. The effect of phenobarbital and 3-methylcholanthrene treatment on carbon tetrachloride-stimulated heme degradation and carbon monoxide expiration in vivo. Toxicol Lett. 1:1978;307-314.
    • (1978) Toxicol Lett , vol.1 , pp. 307-314
    • Lindstrom, A.D.1    Anders, M.W.2
  • 19
    • 0019883606 scopus 로고
    • Zinc.protoporphyrin is a selective inhibitor of heme oxygenase activity in the neonatal rat
    • Maines MD. Zinc.protoporphyrin is a selective inhibitor of heme oxygenase activity in the neonatal rat. Biochim Biophys Acta. 673:1981;339-350.
    • (1981) Biochim Biophys Acta , vol.673 , pp. 339-350
    • Maines, M.D.1
  • 21
    • 0029799191 scopus 로고    scopus 로고
    • Carbon monoxide and nitric oxide homology: Differential modulation of heme oxygenases in brain and detection of protein and activity
    • Maines MD. Carbon monoxide and nitric oxide homology: Differential modulation of heme oxygenases in brain and detection of protein and activity. Methods Enzymol. 268:1996;473-488.
    • (1996) Methods Enzymol , vol.268 , pp. 473-488
    • Maines, M.D.1
  • 22
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system: A regulator of second messenger gases
    • Maines MD. The heme oxygenase system: A regulator of second messenger gases. Annu Rev Pharmacol Toxicol. 37:1997;517-554.
    • (1997) Annu Rev Pharmacol Toxicol , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 26
    • 8544246393 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3
    • McCoubrey WK Jr, Huang TJ, Maines MD. Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3. Eur J Biochem. 247:1997;725-732.
    • (1997) Eur J Biochem , vol.247 , pp. 725-732
    • McCoubrey W.K., Jr.1    Huang, T.J.2    Maines, M.D.3
  • 27
    • 0023784506 scopus 로고
    • Inhibition of human adult and fetal heme oxygenase by new synthetic heme analogues
    • Mitrione SM, Villalon P, Lutton JD, Levere RD, Abraham NG. Inhibition of human adult and fetal heme oxygenase by new synthetic heme analogues. Am J Med Sci. 296:1988;180-186.
    • (1988) Am J Med Sci , vol.296 , pp. 180-186
    • Mitrione, S.M.1    Villalon, P.2    Lutton, J.D.3    Levere, R.D.4    Abraham, N.G.5
  • 28
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology, and pharmacology
    • Moncada S, Palmer RM, Higgs EA. Nitric oxide: Physiology, pathophysiology, and pharmacology. Pharmacol Rev. 43:1991;109-142.
    • (1991) Pharmacol Rev , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.2    Higgs, E.A.3
  • 29
    • 0028928004 scopus 로고
    • Smooth muscle cell-derived carbon monoxide is a regulator of vascular cGMP
    • Morita T, Perrella MA, Lee ME, Kourembanas S. Smooth muscle cell-derived carbon monoxide is a regulator of vascular cGMP. Proc Natl Acad Sci USA. 92:1995;1475-1479.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1475-1479
    • Morita, T.1    Perrella, M.A.2    Lee, M.E.3    Kourembanas, S.4
  • 30
    • 0025971084 scopus 로고
    • The action of nitric oxide in the perfused human fetal-placental circulation
    • Myatt L, Brewer A, Brockman DE. The action of nitric oxide in the perfused human fetal-placental circulation. Am J Obstet Gynecol. 164:1991;687-692.
    • (1991) Am J Obstet Gynecol , vol.164 , pp. 687-692
    • Myatt, L.1    Brewer, A.2    Brockman, D.E.3
  • 31
    • 0027508202 scopus 로고
    • Immunohistochemical localization of nitric oxide synthase in the human placenta
    • Myatt L, Brockman DE, Eis AL, Pollock JS. Immunohistochemical localization of nitric oxide synthase in the human placenta. Placenta. 14:1993;487-495.
    • (1993) Placenta , vol.14 , pp. 487-495
    • Myatt, L.1    Brockman, D.E.2    Eis, A.L.3    Pollock, J.S.4
  • 33
    • 0032509237 scopus 로고    scopus 로고
    • Identification of enzymes responsible for the metabolism of heme in human platelets
    • 342-33 346
    • Nowell SA, Leakey JEA, Warren JF, Lang NP, Frame LT. Identification of enzymes responsible for the metabolism of heme in human platelets. J Biol Chem. 273:1998;33 342-33 346.
    • (1998) J Biol Chem , vol.273 , pp. 33
    • Nowell, S.A.1    Leakey, J.E.A.2    Warren, J.F.3    Lang, N.P.4    Frame, L.T.5
  • 35
    • 0022647459 scopus 로고
    • Suppression of carbon monoxide excretion rate by tin protoporphyrin
    • Posselt AM, Kwong LK, Vreman HJ, Stevenson DK. Suppression of carbon monoxide excretion rate by tin protoporphyrin. Am J Dis Child. 140:1986;147-150.
    • (1986) Am J Dis Child , vol.140 , pp. 147-150
    • Posselt, A.M.1    Kwong, L.K.2    Vreman, H.J.3    Stevenson, D.K.4
  • 37
    • 0032212183 scopus 로고    scopus 로고
    • Effect of heme oxygenase inhibitors on soluble guanylyl cyclase activity
    • Serfass L, Burstyn JN. Effect of heme oxygenase inhibitors on soluble guanylyl cyclase activity. Arch Biochem Biophys. 359:1998;8-16.
    • (1998) Arch Biochem Biophys , vol.359 , pp. 8-16
    • Serfass, L.1    Burstyn, J.N.2
  • 38
    • 0026669125 scopus 로고
    • Nitric oxide: First in a new class of neurotransmitters
    • Snyder SH. Nitric oxide: First in a new class of neurotransmitters. Science. 257:1992;494-496.
    • (1992) Science , vol.257 , pp. 494-496
    • Snyder, S.H.1
  • 39
  • 40
    • 0014670945 scopus 로고
    • Microsomal heme oxygenase. Characterization of the enzyme
    • Tenhunen R, Marver HS, Schmid R. 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
  • 41
    • 0027407240 scopus 로고
    • Selection of metalloporphyrin heme oxygenase inhibitors based on potency and photoreactivity
    • Vreman HJ, Ekstrand BC, Stevenson DK. Selection of metalloporphyrin heme oxygenase inhibitors based on potency and photoreactivity. Pediatr Res. 33:1993;195-200.
    • (1993) Pediatr Res , vol.33 , pp. 195-200
    • Vreman, H.J.1    Ekstrand, B.C.2    Stevenson, D.K.3
  • 42
    • 0023837193 scopus 로고
    • Heme oxygenase activity as measured by carbon monoxide production
    • Vreman HJ, Stevenson DK. Heme oxygenase activity as measured by carbon monoxide production. Anal Biochem. 168:1988;31-38.
    • (1988) Anal Biochem , vol.168 , pp. 31-38
    • Vreman, H.J.1    Stevenson, D.K.2
  • 43
    • 0000064519 scopus 로고    scopus 로고
    • Detection of heme oxygenase activity by measurement of CO
    • M.D. Maines, L.G. Costa, D.J. Reed, S. Sassa, & I.G. Sipes. New York: John Wiley & Sons, Inc
    • Vreman HJ, Stevenson DK. Detection of heme oxygenase activity by measurement of CO. Maines MD, Costa LG, Reed DJ, Sassa S, Sipes IG. Current Protocols in Toxicology. 1999;9.2.1-9.2.10 John Wiley & Sons, Inc, New York.
    • (1999) Current Protocols in Toxicology , pp. 921-9210
    • Vreman, H.J.1    Stevenson, D.K.2
  • 44
    • 0023945020 scopus 로고
    • Correlation of carbon monoxide and bilirubin production by tissue homogenates
    • Vreman HJ, Stevenson DK, Henton D, Rosenthal P. Correlation of carbon monoxide and bilirubin production by tissue homogenates. J Chromatogr. 427:1988;315-319.
    • (1988) J Chromatogr , vol.427 , pp. 315-319
    • Vreman, H.J.1    Stevenson, D.K.2    Henton, D.3    Rosenthal, P.4
  • 45
  • 46
    • 0001073933 scopus 로고    scopus 로고
    • In vitro heme oxygenase isozyme activity inhibition by metalloporphyrins
    • Vreman HJ, Wong RJ, Williams SA, Stevenson DK. In vitro heme oxygenase isozyme activity inhibition by metalloporphyrins. Pediatr Res. 43:1998b;202A.
    • (1998) Pediatr Res , vol.43
    • Vreman, H.J.1    Wong, R.J.2    Williams, S.A.3    Stevenson, D.K.4
  • 47
    • 0031892220 scopus 로고    scopus 로고
    • Resurgence of carbon-monoxide: An endogenous gaseous vasorelaxing factor
    • Wang R. Resurgence of carbon-monoxide: An endogenous gaseous vasorelaxing factor. Can J Physiol Pharmacol. 76:1998;1-15.
    • (1998) Can J Physiol Pharmacol , vol.76 , pp. 1-15
    • Wang, R.1
  • 48
    • 0031010733 scopus 로고    scopus 로고
    • Carbon monoxide-induced vasorelaxation and the underlying mechanisms
    • Wang R, Wang ZZ, Wu LY. Carbon monoxide-induced vasorelaxation and the underlying mechanisms. Br J Pharmacol. 121:1997;927-934.
    • (1997) Br J Pharmacol , vol.121 , pp. 927-934
    • Wang, R.1    Wang, Z.Z.2    Wu, L.Y.3
  • 49
    • 0017057687 scopus 로고
    • The formation of carbon monoxide during peroxidation of microsomal lipids
    • Wolff DG, Bidlack WK. The formation of carbon monoxide during peroxidation of microsomal lipids. Biochem Biophys Res Commun. 73:1976;850-857.
    • (1976) Biochem Biophys Res Commun , vol.73 , pp. 850-857
    • Wolff, D.G.1    Bidlack, W.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.