메뉴 건너뛰기




Volumn 283, Issue 5 27-5, 2002, Pages

Modulation of cGMP by human HO-1 retrovirus gene transfer in pulmonary microvessel endothelial cells

Author keywords

Guanosine 3 ,5 cyclic monophosphate; Heme oxygenase; Retroviral vector; Soluble guanylate cyclase

Indexed keywords

CYCLIC GMP; HEME OXYGENASE 1; N(G) NITROARGININE METHYL ESTER; NITRIC OXIDE SYNTHASE; RETROVIRUS VECTOR;

EID: 0036838926     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.00365.2001     Document Type: Article
Times cited : (43)

References (42)
  • 4
    • 0034054249 scopus 로고    scopus 로고
    • Adenoviral vector-mediated transfer of human heme oxygenase in rats decreases renal heme-dependent arachidonic acid epoxygenase activity
    • Abraham NG, Jiang S, Yang L, Zand BA, Marji J, Drummond GS, and Kappas A. Adenoviral vector-mediated transfer of human heme oxygenase in rats decreases renal heme-dependent arachidonic acid epoxygenase activity. J Pharmacol Exp Ther 293: 494-500, 2000.
    • (2000) J Pharmacol Exp Ther , vol.293 , pp. 494-500
    • Abraham, N.G.1    Jiang, S.2    Yang, L.3    Zand, B.A.4    Marji, J.5    Drummond, G.S.6    Kappas, A.7
  • 6
    • 0023490534 scopus 로고
    • Inhibition of platelet aggregation by carbon monoxide is mediated by activation of guanylate cyclase
    • Brune B and Ullrich V. Inhibition of platelet aggregation by carbon monoxide is mediated by activation of guanylate cyclase. Mol Pharmacol 32: 497-504, 1987.
    • (1987) Mol Pharmacol , vol.32 , pp. 497-504
    • Brune, B.1    Ullrich, V.2
  • 7
    • 0027246357 scopus 로고
    • The hematopoietic stromal microenvironment promotes retrovirus-mediated gene transfer into hematopoietic stem cells
    • Chertkov JL, Jiang S, Lutton JD, Harrison J, Levere RD, Tiefenthaler M, and Abraham NG. The hematopoietic stromal microenvironment promotes retrovirus-mediated gene transfer into hematopoietic stem cells. Stem Cells 11: 218-227, 1993.
    • (1993) Stem Cells , vol.11 , pp. 218-227
    • Chertkov, J.L.1    Jiang, S.2    Lutton, J.D.3    Harrison, J.4    Levere, R.D.5    Tiefenthaler, M.6    Abraham, N.G.7
  • 8
    • 0030188587 scopus 로고    scopus 로고
    • Heme oxygenase-1: Function, regulation, and implication of a novel stress-inducible protein in oxidant-induced lung injury
    • Choi AMK and Alam J. Heme oxygenase-1: Function, regulation, and implication of a novel stress-inducible protein in oxidant-induced lung injury. Am J Respir Cell Mol Biol 15: 9-19, 1996.
    • (1996) Am J Respir Cell Mol Biol , vol.15 , pp. 9-19
    • Choi, A.M.K.1    Alam, J.2
  • 9
    • 0028945134 scopus 로고
    • Vascular smooth muscle cell heme oxygenases generate guanylyl cyclase-stimulatory carbon monoxide
    • Christodoulides N, Durante W, Kroll MH, and Schafer AI. Vascular smooth muscle cell heme oxygenases generate guanylyl cyclase-stimulatory carbon monoxide. Circulation 91: 2306-2309, 1995
    • (1995) Circulation , vol.91 , pp. 2306-2309
    • Christodoulides, N.1    Durante, W.2    Kroll, M.H.3    Schafer, A.I.4
  • 11
    • 0018216365 scopus 로고
    • Restoration of the responsiveness of purified guanylate cyclase to nitrosoguanidine, nitric oxide, and related activators by heme and hemeproteins. Evidence for involvement of the paramagnetic nitrosyl-heme complex in enzyme activation
    • Craven PA and DeRubertis FR. Restoration of the responsiveness of purified guanylate cyclase to nitrosoguanidine, nitric oxide, and related activators by heme and hemeproteins. Evidence for involvement of the paramagnetic nitrosyl-heme complex in enzyme activation. J Biol Chem 253: 8433-8443, 1978.
    • (1978) J Biol Chem , vol.253 , pp. 8433-8443
    • Craven, P.A.1    DeRubertis, F.R.2
  • 12
    • 0000647710 scopus 로고    scopus 로고
    • Carbon monoxide and vascular cell function
    • Durante W and Schafer AI. Carbon monoxide and vascular cell function. Int J Mol Med 2: 255-262, 1998.
    • (1998) Int J Mol Med , vol.2 , pp. 255-262
    • Durante, W.1    Schafer, A.I.2
  • 13
    • 0002263294 scopus 로고
    • Hemes: Determination as pyridine hemochromes
    • edited by Smith KM. New York: Elsevier Scientific
    • Fuhrop JH and Smith KM. Hemes: determination as pyridine hemochromes In: Porphyrins and Metalloporphyrins, edited by Smith KM. New York: Elsevier Scientific, 1975, p. 804-807.
    • (1975) Porphyrins and Metalloporphyrins , pp. 804-807
    • Fuhrop, J.H.1    Smith, K.M.2
  • 14
    • 0019879880 scopus 로고
    • Soluble guanylate cyclase purified from bovine lung contains heme and copper
    • Gerzer R, Bohme E, Hofmann F, and Schultz G. Soluble guanylate cyclase purified from bovine lung contains heme and copper. FEBS Lett 132: 71-74, 1981.
    • (1981) FEBS Lett , vol.132 , pp. 71-74
    • Gerzer, R.1    Bohme, E.2    Hofmann, F.3    Schultz, G.4
  • 15
    • 0021306536 scopus 로고
    • Regulation of purified soluble guanylate cyclase by porphyrins and metalloporphyrins: A unifying concept
    • Ignarro LJ, Wood KS, and Wolin MS. Regulation of purified soluble guanylate cyclase by porphyrins and metalloporphyrins: a unifying concept. Adv Cyclic Nucleotide Protein Phosphorylation Res 17: 267-274, 1984.
    • (1984) Adv Cyclic Nucleotide Protein Phosphorylation Res , vol.17 , pp. 267-274
    • Ignarro, L.J.1    Wood, K.S.2    Wolin, M.S.3
  • 16
    • 0028814999 scopus 로고
    • A heme oxygenase product, presumably carbon monoxide, mediates a vasodepressor function in rats
    • Johnson RA, Lavesa M, Askari B, Abraham NG, and Nasjletti A. A heme oxygenase product, presumably carbon monoxide, mediates a vasodepressor function in rats. Hypertension 25: 166-169, 1995.
    • (1995) Hypertension , vol.25 , pp. 166-169
    • Johnson, R.A.1    Lavesa, M.2    Askari, B.3    Abraham, N.G.4    Nasjletti, A.5
  • 20
    • 0025332748 scopus 로고
    • Effect of heme arginate administration on blood pressure in spontaneously hypertensive rats
    • Levere RD, Martasek P, Escalante B, Schwartzman ML, and Abraham NG. Effect of heme arginate administration on blood pressure in spontaneously hypertensive rats. J Clin Invest 86: 213-219, 1990.
    • (1990) J Clin Invest , vol.86 , pp. 213-219
    • Levere, R.D.1    Martasek, P.2    Escalante, B.3    Schwartzman, M.L.4    Abraham, N.G.5
  • 21
    • 0026769706 scopus 로고
    • Differential induction of heme oxygenase in the hepatocarcinoma cell line (Hep3b) by environmental agents
    • Lutton JD, da Silva JL, Moqattash S, Brown AC, Levere RD, and Abraham NG. Differential induction of heme oxygenase in the hepatocarcinoma cell line (Hep3b) by environmental agents. J Cell Biochem 49: 259-265, 1992.
    • (1992) J Cell Biochem , vol.49 , pp. 259-265
    • Lutton, J.D.1    Da Silva, J.L.2    Moqattash, S.3    Brown, A.C.4    Levere, R.D.5    Abraham, N.G.6
  • 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: 517-554, 1997.
    • (1997) Annu Rev Pharmacol Toxicol , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 23
    • 0006476631 scopus 로고
    • Cobalt induction of hepatic heme oxygenase with evidence that cytochrome P-450 is not essential for this enzyme activity
    • Maines MD and Kappas A. Cobalt induction of hepatic heme oxygenase with evidence that cytochrome P-450 is not essential for this enzyme activity. Proc Natl Acad Sci USA 71: 4293-4297, 1974.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 4293-4297
    • Maines, M.D.1    Kappas, A.2
  • 24
    • 0027483676 scopus 로고
    • Heme oxygenase, a likely regulator of cGMP production in the brain: Inductin of in vivo HO-1 compensates for depression in NO synthase activity
    • Maines MD, Mark JA, and Ewing JF. Heme oxygenase, a likely regulator of cGMP production in the brain: Inductin of in vivo HO-1 compensates for depression in NO synthase activity. Mol Cen Neurosci 4: 398-405, 1993.
    • (1993) Mol Cen Neurosci , vol.4 , pp. 398-405
    • Maines, M.D.1    Mark, J.A.2    Ewing, J.F.3
  • 26
    • 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 WK Jr, Ewing JF, and Maines MD. 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.
    • (1992) Arch Biochem Biophys , vol.295 , pp. 13-20
    • McCoubrey W.K., Jr.1    Ewing, J.F.2    Maines, M.D.3
  • 27
    • 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, and Maines MD. Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3. Eur J Biochem 247: 725-732, 1997.
    • (1997) Eur J Biochem , vol.247 , pp. 725-732
    • McCoubrey W.K., Jr.1    Huang, T.J.2    Maines, M.D.3
  • 29
    • 0024372743 scopus 로고
    • Heat shock induction of heme oxygenase mRNA in human Hep3B hepatoma cells
    • Mitani K, Fujita H, Sassa S, and Kappas A. Heat shock induction of heme oxygenase mRNA in human Hep3B hepatoma cells. Biochem Biophys Res Commun 165: 437-441, 1989.
    • (1989) Biochem Biophys Res Commun , vol.165 , pp. 437-441
    • Mitani, K.1    Fujita, H.2    Sassa, S.3    Kappas, A.4
  • 32
  • 34
    • 0023665016 scopus 로고
    • Transcriptional control of rat heme oxygenase by heat shock
    • Shibahara S, Muller M, and Taguchi H. Transcriptional control of rat heme oxygenase by heat shock. J Biol Chem 262: 12889-12892, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 12889-12892
    • Shibahara, S.1    Muller, M.2    Taguchi, H.3
  • 35
    • 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. Functional analysis of cDNAs for two types of human heme oxygenase and evidence for their separate regulation. J Biochem (Tokyo) 113: 214-218, 1993.
    • (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
  • 36
    • 0028228808 scopus 로고
    • Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states
    • Stone JR and Marletta MA. Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states. Biochemistry 33: 5636-5640, 1994.
    • (1994) Biochemistry , vol.33 , pp. 5636-5640
    • Stone, J.R.1    Marletta, M.A.2
  • 37
    • 0030734872 scopus 로고    scopus 로고
    • Heme induces the expression of adhesion molecules ICAM-1, VCAM-1, and E selectin in vascular endothelial cells
    • Wagener FADTG, Feldman E, de Witte T, and Abraham NG. Heme induces the expression of adhesion molecules ICAM-1, VCAM-1, and E selectin in vascular endothelial cells. Proc Soc Exp Biol Med 216: 456-463, 1997.
    • (1997) Proc Soc Exp Biol Med , vol.216 , pp. 456-463
    • Wagener, F.A.D.T.G.1    Feldman, E.2    De Witte, T.3    Abraham, N.G.4
  • 38
    • 0030856625 scopus 로고    scopus 로고
    • Hemodynaic forces induce the expression of heme oxygenase in cultured vascular smooth muscle cells
    • Wagner CT, Durante W, Christodoulides N, Hellums JD, and Schafer AI. Hemodynaic forces induce the expression of heme oxygenase in cultured vascular smooth muscle cells. J Clin Invest 100: 589-596, 1997.
    • (1997) J Clin Invest , vol.100 , pp. 589-596
    • Wagner, C.T.1    Durante, W.2    Christodoulides, N.3    Hellums, J.D.4    Schafer, A.I.5
  • 39
    • 0031010733 scopus 로고    scopus 로고
    • Carbon monoxide-induced vasorelaxation and the underlying mechanisms
    • Wang R, Wang Z, and Wu L. Carbon monoxide-induced vasorelaxation and the underlying mechanisms. Br J Pharmacol 121: 927-934, 1997.
    • (1997) Br J Pharmacol , vol.121 , pp. 927-934
    • Wang, R.1    Wang, Z.2    Wu, L.3
  • 40
    • 0032765028 scopus 로고    scopus 로고
    • Retrovirus-mediated HO gene transfer into endothelial cells protects against oxidant-induced injury
    • Yang L, Quan S, and Abraham NG. Retrovirus-mediated HO gene transfer into endothelial cells protects against oxidant-induced injury. Am J Physiol Lung Cell Mol Physiol 277: L127-L133, 1999.
    • (1999) Am J Physiol Lung Cell Mol Physiol , vol.277
    • Yang, L.1    Quan, S.2    Abraham, N.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.