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Volumn 273, Issue 1 42-1, 1997, Pages

cAMP induces heme oxygenase-1 gene expression and carbon monoxide production in vascular smooth muscle

Author keywords

Cyclic nucleotides; Gene regulation; Soluble guanylate cyclase

Indexed keywords

CARBON MONOXIDE; CYCLIC AMP; GUANYLATE CYCLASE; HEME OXYGENASE; MESSENGER RNA;

EID: 33751264914     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.1997.273.1.h317     Document Type: Article
Times cited : (86)

References (41)
  • 1
    • 0029156942 scopus 로고
    • Transfection of the human heme oxygenase gene into rabbit coronary microvessel endothelial cells: Protective effect against heme and hemoglobin toxicity
    • Abraham, N. G., Y. Lavrovsky, M. L. Schwartzman, R. A. Stoltz, R. D. Levere, M. E. Gerritsen, S. Shibahara, and A. Kappas. Transfection of the human heme oxygenase gene into rabbit coronary microvessel endothelial cells: protective effect against heme and hemoglobin toxicity. Proc. Natl. Acad. Sci. USA 92: 6798-6802, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6798-6802
    • Abraham, N.G.1    Lavrovsky, Y.2    Schwartzman, M.L.3    Stoltz, R.A.4    Levere, R.D.5    Gerritsen, M.E.6    Shibahara, S.7    Kappas, A.8
  • 2
    • 0015309594 scopus 로고
    • Metabolic regulation of heme catabolism and bilirubin production: Hormonal control of hepatic heme oxygenase activity
    • Bakken, A. F., M. M. Thaler, and R. Schmid. Metabolic regulation of heme catabolism and bilirubin production: hormonal control of hepatic heme oxygenase activity. J. Clin. Invest. 51: 530-536, 1971.
    • (1971) J. Clin. Invest. , vol.51 , pp. 530-536
    • Bakken, A.F.1    Thaler, M.M.2    Schmid, R.3
  • 3
    • 0025181994 scopus 로고
    • Activation of soluble guanylate cyclase by carbon monoxide and inhibition by superoxide anion
    • Brune, B., K. U. Schmidt, and V. Ullrich. Activation of soluble guanylate cyclase by carbon monoxide and inhibition by superoxide anion. Eur. J. Biochem. 192: 683-688, 1990.
    • (1990) Eur. J. Biochem. , vol.192 , pp. 683-688
    • Brune, B.1    Schmidt, K.U.2    Ullrich, V.3
  • 4
    • 0023490534 scopus 로고
    • Inhibition of platelet aggregation by carbon monoxide is mediated by the activation of guanylate cyclase
    • Brune, B., and V. Ullrich. Inhibition of platelet aggregation by carbon monoxide is mediated by the activation of guanylate cyclase. Mol. Pharmacol. 32: 497-504, 1987.
    • (1987) Mol. Pharmacol. , vol.32 , pp. 497-504
    • Brune, B.1    Ullrich, V.2
  • 5
    • 0028945134 scopus 로고
    • Vascular smooth muscle cell heme oxygenases generate guanylyl cyclase-stimulatory carbon monoxide
    • Christodoulides, N., W. Durante, M. H. Kroll, and A. I. Schafer. 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
  • 7
    • 0028303697 scopus 로고
    • Cyclic nucleotide regulation of interleukin-1β induced nitric oxide synthase expression in vascular smooth muscle cells
    • Durante, W., K. Cheng, and A. I. Schafer. Cyclic nucleotide regulation of interleukin-1β induced nitric oxide synthase expression in vascular smooth muscle cells. Thromb. Res. 75: 63-71, 1994.
    • (1994) Thromb. Res. , vol.75 , pp. 63-71
    • Durante, W.1    Cheng, K.2    Schafer, A.I.3
  • 8
    • 0029961654 scopus 로고    scopus 로고
    • Hemostatic proteins regulate interleukin-1β stimulated inducible nitric oxide synthase expression in cultured vascular smooth muscle cells
    • Durante, W., M. H. Kroll, G. J. Orloff, J. M. Cunningham, T. Scott-Burden, P. M. Vanhoutte, and A. I. Schafer. Hemostatic proteins regulate interleukin-1β stimulated inducible nitric oxide synthase expression in cultured vascular smooth muscle cells. Biochem. Pharmacol. 51: 847-853, 1996.
    • (1996) Biochem. Pharmacol. , vol.51 , pp. 847-853
    • Durante, W.1    Kroll, M.H.2    Orloff, G.J.3    Cunningham, J.M.4    Scott-Burden, T.5    Vanhoutte, P.M.6    Schafer, A.I.7
  • 9
    • 0027468889 scopus 로고
    • Plasmin potentiates the induction of nitric oxide synthase by interleukin-1β in vascular smooth muscle
    • Heart Circ. Physiol. 33
    • Durante, W., V. B. Schini, S. Catovsky, M. H. Kroll, P. M. Vanhoutte, and A. I. Schafer. Plasmin potentiates the induction of nitric oxide synthase by interleukin-1β in vascular smooth muscle. Am. J. Physiol. 264 (Heart Circ. Physiol. 33): H617-H624, 1993.
    • (1993) Am. J. Physiol. , vol.264
    • Durante, W.1    Schini, V.B.2    Catovsky, S.3    Kroll, M.H.4    Vanhoutte, P.M.5    Schafer, A.I.6
  • 11
    • 0028149406 scopus 로고
    • Induction of heart heme oxygenase-1 (HSP32) by hyperthermia: Possible role in stress-mediated elevation of cyclic 3′-5′-guanosine monophosphate
    • Ewing, J. F., V. S. Raju, and M. D. Maines. Induction of heart heme oxygenase-1 (HSP32) by hyperthermia: possible role in stress-mediated elevation of cyclic 3′-5′-guanosine monophosphate. J. Pharmacol. Exp. Ther. 271: 408-411, 1994.
    • (1994) J. Pharmacol. Exp. Ther. , vol.271 , pp. 408-411
    • Ewing, J.F.1    Raju, V.S.2    Maines, M.D.3
  • 12
    • 0016434353 scopus 로고
    • Erythrophagocytosis by macrophages: Suppression of heme oxygenase by cyclic AMP
    • Gemsa, D., C. H. Woo, D. Webb, H. H. Fudenberg, and R. Schmid. Erythrophagocytosis by macrophages: suppression of heme oxygenase by cyclic AMP. Cell. Immunol. 15: 21-36, 1975.
    • (1975) Cell. Immunol. , vol.15 , pp. 21-36
    • Gemsa, D.1    Woo, C.H.2    Webb, D.3    Fudenberg, H.H.4    Schmid, R.5
  • 13
    • 0025153308 scopus 로고
    • Study on the mechanism of carbon monoxide induced endothelium-independent relaxation in porcine coronary artery and vein
    • Graser, T., Y. P. Vedernikov, and D. S. Li. Study on the mechanism of carbon monoxide induced endothelium-independent relaxation in porcine coronary artery and vein. Biomed. Biochim. Acta 4:293-296, 1990.
    • (1990) Biomed. Biochim. Acta , vol.4 , pp. 293-296
    • Graser, T.1    Vedernikov, Y.P.2    Li, D.S.3
  • 14
    • 0028903204 scopus 로고
    • Haem oxygenase activity in blood vessel homogenates as measured by carbon monoxide production
    • Grundemar, L., M. B. Johansson, M. Ekelund, and E. D. Hogestatt. Haem oxygenase activity in blood vessel homogenates as measured by carbon monoxide production. Acta Physiol. Scand. 153: 203-204, 1995.
    • (1995) Acta Physiol. Scand. , vol.153 , pp. 203-204
    • Grundemar, L.1    Johansson, M.B.2    Ekelund, M.3    Hogestatt, E.D.4
  • 15
    • 0030063426 scopus 로고    scopus 로고
    • Higher serum bilirubin is associated with decreased risk for early familial coronary artery disease
    • Hopkins, P. N., L. L. Wu, S. C. Hunt, G. M. Vincent, and R. R. Williams. Higher serum bilirubin is associated with decreased risk for early familial coronary artery disease. Arterioscler. Thromb. Vasc. Biol. 16: 250-255, 1996.
    • (1996) Arterioscler. Thromb. Vasc. Biol. , vol.16 , pp. 250-255
    • Hopkins, P.N.1    Wu, L.L.2    Hunt, S.C.3    Vincent, G.M.4    Williams, R.R.5
  • 16
    • 0028345042 scopus 로고
    • Induction of nitric oxide synthase by cyclic AMP in rat vascular smooth muscle cells
    • Imai, T., Y. Hirata, K. Kanno, and F. Marumo. Induction of nitric oxide synthase by cyclic AMP in rat vascular smooth muscle cells. J. Clin. Invest. 93: 543-549, 1994.
    • (1994) J. Clin. Invest. , vol.93 , pp. 543-549
    • Imai, T.1    Hirata, Y.2    Kanno, K.3    Marumo, F.4
  • 17
    • 0028814999 scopus 로고
    • Aheme oxygenase product, presumably carbon monoxide, mediates a vasodepressor function in rats
    • Johnson, R. A., M. Lavesa, B. Askari, N. G. Abraham, and A. Nasjletti. Aheme 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
  • 19
    • 0027496744 scopus 로고
    • Cyclic AMP-elevating agents induce an inducible type of nitric oxide synthase in cultured vascular smooth muscle cells: Synergism with the induction elicited by inflammatory cytokines
    • Koide, M., Y. Kawahara, I. Nakayama, T. Tsuda, and M. Yokoyama. Cyclic AMP-elevating agents induce an inducible type of nitric oxide synthase in cultured vascular smooth muscle cells: synergism with the induction elicited by inflammatory cytokines. J. Biol. Chem. 268: 24959-24966, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24959-24966
    • Koide, M.1    Kawahara, Y.2    Nakayama, I.3    Tsuda, T.4    Yokoyama, M.5
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0025332748 scopus 로고
    • Effect of heme arginate administration on blood pressure in spontaneously hypertensive rats
    • Levere, R. D., P. Martasek, B. Escalante, M. L. Schwartzman, and N. G. Abraham. 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
  • 22
    • 0025936245 scopus 로고
    • Cloning of the GATA-binding protein that regulates endothelin-1 gene expression in endothelial cells
    • Lee, M. E., D. H. Temizer, J. A. Clifford, and T. Quertermous. Cloning of the GATA-binding protein that regulates endothelin-1 gene expression in endothelial cells. J. Biol. Chem. 266: 16188-16192, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16188-16192
    • Lee, M.E.1    Temizer, D.H.2    Clifford, J.A.3    Quertermous, T.4
  • 23
    • 0023731036 scopus 로고
    • Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications
    • Maines, M. D. Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications. FASEB J. 2: 2557-2568, 1988.
    • (1988) FASEB J. , vol.2 , pp. 2557-2568
    • Maines, M.D.1
  • 24
    • 0022632224 scopus 로고
    • Characterization of two constitutive forms of heme oxygenase: Only one molecular species of the enzyme is inducible
    • Maines, M. D., G. M. Trakshel, and R. K. Kutty. Characterization of two constitutive forms of heme oxygenase: only one molecular species of the enzyme is inducible. J. Biol. Chem. 261: 411-419, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 411-419
    • Maines, M.D.1    Trakshel, G.M.2    Kutty, R.K.3
  • 25
    • 0024208276 scopus 로고
    • Macrophage oxidation of L-arginine to nitrite and nitrate: Nitric oxide is an intermediate
    • Marletta, M. A., P. S. Yoon, R. Iyengar, C. D. Leaf, and J. S. Wishnok. Macrophage oxidation of L-arginine to nitrite and nitrate: nitric oxide is an intermediate. Biochemistry 27: 8706-8711, 1988.
    • (1988) Biochemistry , vol.27 , pp. 8706-8711
    • Marletta, M.A.1    Yoon, P.S.2    Iyengar, R.3    Leaf, C.D.4    Wishnok, J.S.5
  • 26
    • 0028838293 scopus 로고
    • Endothelial cell expression of vasoconstrictors and growth factors is regulated by smooth muscle cell-derived carbon monoxide
    • Morita, T., and S. Kourembanas. Endothelial cell expression of vasoconstrictors and growth factors is regulated by smooth muscle cell-derived carbon monoxide. J. Clin. Invest. 96: 2676-2682, 1995.
    • (1995) J. Clin. Invest. , vol.96 , pp. 2676-2682
    • Morita, T.1    Kourembanas, S.2
  • 27
    • 0028928004 scopus 로고
    • Smooth muscle cell-derived carbon monoxide is a regulator of vascular cGMP
    • Morita, T., M. A. Perella, M. U. Lee, and S. Kourembanas. Smooth muscle cell-derived carbon monoxide is a regulator of vascular cGMP. Proc. Natl. Acad. Sci. USA 92: 1475-1479, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1475-1479
    • Morita, T.1    Perella, M.A.2    Lee, M.U.3    Kourembanas, S.4
  • 28
    • 0030065052 scopus 로고    scopus 로고
    • NO-mediated activation of heme oxygenase: Endogenous cytoprotection against oxidative stress to endothelium
    • Heart Circ. Physiol. 39
    • Motterlini, R., R. Foresti, M. Intaglietta, and R. M. Winslow. NO-mediated activation of heme oxygenase: endogenous cytoprotection against oxidative stress to endothelium. Am. J. Physiol. 270 (Heart Circ. Physiol. 39): H107-H114, 1996.
    • (1996) Am. J. Physiol. , vol.270
    • Motterlini, R.1    Foresti, R.2    Intaglietta, M.3    Winslow, R.M.4
  • 29
    • 0023654799 scopus 로고
    • Nucleotide sequence and organization of the rat heme oxygenase gene
    • Muller, R. M., H. Taguchi, and S. Shibahara. Nucleotide sequence and organization of the rat heme oxygenase gene. J. Biol. Chem. 262: 6795-6802, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6795-6802
    • Muller, R.M.1    Taguchi, H.2    Shibahara, S.3
  • 30
    • 0028239795 scopus 로고
    • Free and albumin-bound bilirubin are efficient co-antioxidants for alpha-tocopherol, inhibiting plasma and low density lipoprotein lipid peroxidation
    • Neuzil, J., and R. Stocker. Free and albumin-bound bilirubin are efficient co-antioxidants for alpha-tocopherol, inhibiting plasma and low density lipoprotein lipid peroxidation. J. Biol. Chem. 269: 16712-16719, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16712-16719
    • Neuzil, J.1    Stocker, R.2
  • 31
    • 0025321850 scopus 로고
    • Isolation, characterization, and expression of cDNA for rat heme oxygenase
    • Rotenberg, M. O., and M. D. Maines. Isolation, characterization, and expression of cDNA for rat heme oxygenase. J. Biol. Chem. 265: 7501-7506, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7501-7506
    • Rotenberg, M.O.1    Maines, M.D.2
  • 32
    • 0343999803 scopus 로고    scopus 로고
    • Carbon monoxide mediates the coronary vasodilator effect of heme in isolated rat hearts
    • Scholer, M. J., R. A. Johnson, and A. Nasjletti. Carbon monoxide mediates the coronary vasodilator effect of heme in isolated rat hearts (Abstract). FASEB J. 10: 341, 1996.
    • (1996) FASEB J. , vol.10 , pp. 341
    • Scholer, M.J.1    Johnson, R.A.2    Nasjletti, A.3
  • 34
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological importance
    • Stocker, R., Y. Yamamoto, A. N. McDonagh, A. N. Glazer, and B. N. Ames. Bilirubin is an antioxidant of possible physiological importance. Science 235: 1043-1046, 1987.
    • (1987) Science , vol.235 , pp. 1043-1046
    • Stocker, R.1    Yamamoto, Y.2    McDonagh, A.N.3    Glazer, A.N.4    Ames, B.N.5
  • 35
    • 0014348401 scopus 로고
    • The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase
    • Tenhunen, R., H. S. Marver, and R. Schmidt. The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase. Proc. Natl. Acad. Sci. USA 61: 748-755, 1968.
    • (1968) Proc. Natl. Acad. Sci. USA , vol.61 , pp. 748-755
    • Tenhunen, R.1    Marver, H.S.2    Schmidt, R.3
  • 36
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76: 4350-4354, 1979.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 37
    • 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 M. D. Maines. 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.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1323-1328
    • Trakshel, G.M.1    Maines, M.D.2
  • 39
    • 0029162242 scopus 로고
    • Bilirubin is oxidized in rats treated with endotoxin and acts as a physiological antioxidant synergystically with ascorbic acid in vivo
    • Yamaguchi, T., F. Horio, T. Hashizume, M. Tanaka, S. Ikeda, A. Kakinuma, and H. Nakajima. Bilirubin is oxidized in rats treated with endotoxin and acts as a physiological antioxidant synergystically with ascorbic acid in vivo. Biochem. Biophys. Res. Commun. 214: 11-19, 1995.
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 11-19
    • Yamaguchi, T.1    Horio, F.2    Hashizume, T.3    Tanaka, M.4    Ikeda, S.5    Kakinuma, A.6    Nakajima, H.7
  • 40
    • 0023712739 scopus 로고
    • Phosphorylation-induced binding and transcriptional efficacy of nuclear CREB
    • Yamamoto, K. K., G. A. Gonzalez, W. H. Biggs, and M. R. Montminy. Phosphorylation-induced binding and transcriptional efficacy of nuclear CREB. Nature 334: 494-498, 1988.
    • (1988) Nature , vol.334 , pp. 494-498
    • Yamamoto, K.K.1    Gonzalez, G.A.2    Biggs, W.H.3    Montminy, M.R.4


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