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Volumn 39, Issue 1, 2005, Pages 1-25

Heme oxygenase and the cardiovascular-renal system

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLSALICYLIC ACID; BILIRUBIN; CARBON MONOXIDE; CYTOCHROME P450; HEME OXYGENASE; HEME OXYGENASE 1; HEME OXYGENASE 2; N(G) NITROARGININE METHYL ESTER; NITRIC OXIDE DONOR; PENTAESITHRITYL TETRANITRATE; PROSTAGLANDIN SYNTHASE; UNCLASSIFIED DRUG;

EID: 19544370917     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2005.03.010     Document Type: Review
Times cited : (330)

References (227)
  • 2
    • 0023854047 scopus 로고
    • Evidence suggesting that the two forms of heme oxygenase are products of different genes
    • I. Cruse, and M.D. 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.D.2
  • 3
    • 0034871085 scopus 로고    scopus 로고
    • Heme oxygenase-2 interaction with metalloporphyrins: Function of heme regulatory motifs
    • T.J. Huang, W.K. McCoubrey Jr., and M.D. Maines Heme oxygenase-2 interaction with metalloporphyrins: function of heme regulatory motifs Antioxid. Redox. Signal. 3 2001 685 696
    • (2001) Antioxid. Redox. Signal. , vol.3 , pp. 685-696
    • Huang, T.J.1    McCoubrey Jr., W.K.2    Maines, M.D.3
  • 10
    • 2542434044 scopus 로고    scopus 로고
    • Heme oxygenase-1 gene expression modulates angiotensin II-induced increase in blood pressure
    • L. Yang, S. Quan, A. Nasjletti, M. Laniado-Schwartzman, and N.G. Abraham Heme oxygenase-1 gene expression modulates angiotensin II-induced increase in blood pressure Hypertension 43 2004 1221 1226
    • (2004) Hypertension , vol.43 , pp. 1221-1226
    • Yang, L.1    Quan, S.2    Nasjletti, A.3    Laniado-Schwartzman, M.4    Abraham, N.G.5
  • 11
    • 0141953982 scopus 로고    scopus 로고
    • Therapeutic applications of human heme oxygenase gene transfer and gene therapy
    • N.G. Abraham Therapeutic applications of human heme oxygenase gene transfer and gene therapy Curr. Pharm. Des. 9 2003 2513 2524
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 2513-2524
    • Abraham, N.G.1
  • 13
    • 0022553242 scopus 로고
    • Control of heme metabolism with synthetic metalloporphyrins
    • A. Kappas, and G. Drummond Control of heme metabolism with synthetic metalloporphyrins J. Clin. Invest. 77 1986 335 339
    • (1986) J. Clin. Invest. , vol.77 , pp. 335-339
    • Kappas, A.1    Drummond, G.2
  • 14
    • 0020074064 scopus 로고
    • The cytochrome P-450-depleted animal: An experimental model for in vivo studies in chemical biology
    • G.S. Drummond, and A. Kappas The cytochrome P-450-depleted animal: an experimental model for in vivo studies in chemical biology Proc. Natl. Acad. Sci. USA 79 1982 2384 2388
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2384-2388
    • Drummond, G.S.1    Kappas, A.2
  • 15
    • 0346340056 scopus 로고    scopus 로고
    • A method for interdicting the development of severe jaundice in newborns by inhibiting the production of bilirubin
    • A. Kappas A method for interdicting the development of severe jaundice in newborns by inhibiting the production of bilirubin Pediatrics 113 2004 119 123
    • (2004) Pediatrics , vol.113 , pp. 119-123
    • Kappas, A.1
  • 16
    • 0028300334 scopus 로고
    • Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts
    • G.F. Vile, S. Basu-Modak, C. Wlatner, and R.M. Tyrrell Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts Proc. Natl. Acad. Sci. USA 91 1994 2607 2610
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2607-2610
    • Vile, G.F.1    Basu-Modak, S.2    Wlatner, C.3    Tyrrell, R.M.4
  • 17
    • 0032881831 scopus 로고    scopus 로고
    • Differential effects of heme oxygenase isoforms on heme mediation of endothelial intracellular adhesion molecule 1 expression
    • F.A. Wagener, J.L. da Silva, T. Farley, T. de Witte, A. Kappas, and N.G. Abraham Differential effects of heme oxygenase isoforms on heme mediation of endothelial intracellular adhesion molecule 1 expression J. Pharmacol. Exp. Ther. 291 1999 416 423
    • (1999) J. Pharmacol. Exp. Ther. , vol.291 , pp. 416-423
    • Wagener, F.A.1    Da Silva, J.L.2    Farley, T.3    De Witte, T.4    Kappas, A.5    Abraham, N.G.6
  • 20
    • 0031758561 scopus 로고    scopus 로고
    • Heme oxygenase: Protective gene or Trojan horse
    • J.L. Platt, and K.A. Nath Heme oxygenase: protective gene or Trojan horse Nat. Med. 4 1998 1364 1365
    • (1998) Nat. Med. , vol.4 , pp. 1364-1365
    • Platt, J.L.1    Nath, K.A.2
  • 21
    • 0033847184 scopus 로고    scopus 로고
    • The indispensability of heme oxygenase-1 in protecting against acute heme protein-induced toxicity in vivo
    • K.A. Nath, J.J. Haggard, A.J. Croatt, J.P. Grande, K.D. Poss, and J. Alam The indispensability of heme oxygenase-1 in protecting against acute heme protein-induced toxicity in vivo Am. J. Pathol. 156 2000 1527 1535
    • (2000) Am. J. Pathol. , vol.156 , pp. 1527-1535
    • Nath, K.A.1    Haggard, J.J.2    Croatt, A.J.3    Grande, J.P.4    Poss, K.D.5    Alam, J.6
  • 22
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological importance
    • R. Stocker, Y. Yamamoto, A.F. McDonagh, A.N. Glazer, and B.N. Ames Bilirubin is an antioxidant of possible physiological importance Science 235 1987 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
  • 23
    • 0025150585 scopus 로고
    • Antioxidant activities of bile pigments: Biliverdin and bilirubin
    • R. Stocker, A.F. McDonagh, A.N. Glazer, and B.N. Ames Antioxidant activities of bile pigments: biliverdin and bilirubin Methods Enzymol. 186 1990 301 309
    • (1990) Methods Enzymol. , vol.186 , pp. 301-309
    • Stocker, R.1    McDonagh, A.F.2    Glazer, A.N.3    Ames, B.N.4
  • 25
    • 0141608946 scopus 로고    scopus 로고
    • Heme oxygenase-1 attenuates glucose-mediated cell growth arrest and apoptosis in human microvessel endothelial cells
    • N.G. Abraham, T. Kushida, J. McClung, M. Weiss, S. Quan, R. Lafaro, Z. Darzynkiewicz, and M. Wolin Heme oxygenase-1 attenuates glucose-mediated cell growth arrest and apoptosis in human microvessel endothelial cells Circ. Res. 93 2003 507 514
    • (2003) Circ. Res. , vol.93 , pp. 507-514
    • Abraham, N.G.1    Kushida, T.2    McClung, J.3    Weiss, M.4    Quan, S.5    Lafaro, R.6    Darzynkiewicz, Z.7    Wolin, M.8
  • 27
    • 2342447943 scopus 로고    scopus 로고
    • Expression of human heme oxygenase-1 in the thick ascending limb attenuates angiotensin II-mediated increase in oxidative injury
    • S. Quan, L. Yang, S. Shenouda, M.L. Schwartzman, A. Nasjletti, A.I. Goodman, and N.G. Abraham Expression of human heme oxygenase-1 in the thick ascending limb attenuates angiotensin II-mediated increase in oxidative injury Kidney Int. 65 2004 1628 1639
    • (2004) Kidney Int. , vol.65 , pp. 1628-1639
    • Quan, S.1    Yang, L.2    Shenouda, S.3    Schwartzman, M.L.4    Nasjletti, A.5    Goodman, A.I.6    Abraham, N.G.7
  • 28
    • 0032900940 scopus 로고    scopus 로고
    • Exogenous administration of heme oxygenase-1 by gene transfer provides protection against hyperoxia-induced lung injury
    • L.E. Otterbein, J.K. Kolls, L.L. Mantell, J.L. Cook, J. Alam, and A.M. Choi Exogenous administration of heme oxygenase-1 by gene transfer provides protection against hyperoxia-induced lung injury J. Clin. Invest. 103 1999 1047 1054
    • (1999) J. Clin. Invest. , vol.103 , pp. 1047-1054
    • Otterbein, L.E.1    Kolls, J.K.2    Mantell, L.L.3    Cook, J.L.4    Alam, J.5    Choi, A.M.6
  • 30
    • 0035007161 scopus 로고    scopus 로고
    • Contributions of prostacyclin and nitric oxide to carbon monoxide-induced cerebrovascular dilation in piglets
    • C.W. Leffler, A. Nasjletti, R.A. Johnson, and A.L. Fedinec Contributions of prostacyclin and nitric oxide to carbon monoxide-induced cerebrovascular dilation in piglets Am. J. Physiol. Heart Circ. Physiol. 280 2001 H1490 H1495
    • (2001) Am. J. Physiol. Heart Circ. Physiol. , vol.280
    • Leffler, C.W.1    Nasjletti, A.2    Johnson, R.A.3    Fedinec, A.L.4
  • 35
    • 0141919542 scopus 로고    scopus 로고
    • Role of heme oxygenase-1 in cardiovascular function
    • M.A. Perrella, and S.F. Yet Role of heme oxygenase-1 in cardiovascular function Curr. Pharm. Des. 9 2003 2479 2487
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 2479-2487
    • Perrella, M.A.1    Yet, S.F.2
  • 37
    • 0028917018 scopus 로고
    • A closed eye contact lens model of corneal inflammation. Part 2. Inhibition of cytochrome P450 arachidonic acid metabolism alleviates inflammatory sequelae
    • M.S. Conners, R.A. Stoltz, K.L. Davis, M.W. Dunn, N.G. Abraham, and R.D. Levere A closed eye contact lens model of corneal inflammation. Part 2. Inhibition of cytochrome P450 arachidonic acid metabolism alleviates inflammatory sequelae Invest. Ophthalmol. Vis. Sci. 36 1995 841 850
    • (1995) Invest. Ophthalmol. Vis. Sci. , vol.36 , pp. 841-850
    • Conners, M.S.1    Stoltz, R.A.2    Davis, K.L.3    Dunn, M.W.4    Abraham, N.G.5    Levere, R.D.6
  • 38
    • 0030045835 scopus 로고    scopus 로고
    • Heme oxygenase: A novel target for the modulation of the inflammatory response
    • D. Willis, A.R. Moore, R. Frederick, and D.A. Willoughby Heme oxygenase: a novel target for the modulation of the inflammatory response Nat. Med. 2 1996 87 90
    • (1996) Nat. Med. , vol.2 , pp. 87-90
    • Willis, D.1    Moore, A.R.2    Frederick, R.3    Willoughby, D.A.4
  • 40
    • 0035949615 scopus 로고    scopus 로고
    • Adenovirus-mediated heme oxygenase-1 gene transfer inhibits the development of atherosclerosis in apolipoprotein E-deficient mice
    • S.H. Juan, T.S. Lee, K.W. Tseng, J.Y. Liou, S.K. Shyue, K.K. Wu, and L.Y. Chau Adenovirus-mediated heme oxygenase-1 gene transfer inhibits the development of atherosclerosis in apolipoprotein E-deficient mice Circulation 104 2001 1519 1525
    • (2001) Circulation , vol.104 , pp. 1519-1525
    • Juan, S.H.1    Lee, T.S.2    Tseng, K.W.3    Liou, J.Y.4    Shyue, S.K.5    Wu, K.K.6    Chau, L.Y.7
  • 41
    • 0030930697 scopus 로고    scopus 로고
    • Induction of heme oxygenase-1 inhibits the monocyte transmigration induced by mildly oxidized LDL
    • K. Ishikawa, M. Navab, N. Leitinger, A.M. Fogelman, and A.J. Lusis Induction of heme oxygenase-1 inhibits the monocyte transmigration induced by mildly oxidized LDL J. Clin. Invest. 100 1997 1209 1216
    • (1997) J. Clin. Invest. , vol.100 , pp. 1209-1216
    • Ishikawa, K.1    Navab, M.2    Leitinger, N.3    Fogelman, A.M.4    Lusis, A.J.5
  • 42
    • 0031935208 scopus 로고    scopus 로고
    • Expression of heme oxygenase-1 in atherosclerotic lesions
    • L.J. Wang, T.S. Lee, F.Y. Lee, R.C. Pai, and L.Y. Chau Expression of heme oxygenase-1 in atherosclerotic lesions Am. J. Pathol. 152 1998 711 720
    • (1998) Am. J. Pathol. , vol.152 , pp. 711-720
    • Wang, L.J.1    Lee, T.S.2    Lee, F.Y.3    Pai, R.C.4    Chau, L.Y.5
  • 44
    • 0034782482 scopus 로고    scopus 로고
    • Adenovirus-mediated transfer of heme oxygenase-1 cDNA attenuates severe lung injury induced by the influenza virus in mice
    • T. Hashiba, M. Suzuki, Y. Nagashima, S. Suzuki, S. Inoue, T. Tsuburai, T. Matsuse, and Y. Ishigatubo Adenovirus-mediated transfer of heme oxygenase-1 cDNA attenuates severe lung injury induced by the influenza virus in mice Gene Ther. 8 2001 1499 1507
    • (2001) Gene Ther. , vol.8 , pp. 1499-1507
    • Hashiba, T.1    Suzuki, M.2    Nagashima, Y.3    Suzuki, S.4    Inoue, S.5    Tsuburai, T.6    Matsuse, T.7    Ishigatubo, Y.8
  • 48
    • 0020983340 scopus 로고
    • Heme metabolism in hepatic and erythroid cells
    • E. Brown Grune and Stratton New York
    • N.G. Abraham, M.L. Friedland, and R.D. Levere Heme metabolism in hepatic and erythroid cells E. Brown Progress in Hematology 1983 Grune and Stratton New York 75 130
    • (1983) Progress in Hematology , pp. 75-130
    • Abraham, N.G.1    Friedland, M.L.2    Levere, R.D.3
  • 49
    • 0024097799 scopus 로고
    • Heme catabolism by heme oxygenase: Physiology, regulation, and mechanism of action
    • B.A. Schacter Heme catabolism by heme oxygenase: physiology, regulation, and mechanism of action Semin. Hematol. 25 1988 349 369
    • (1988) Semin. Hematol. , vol.25 , pp. 349-369
    • Schacter, B.A.1
  • 50
    • 0036843934 scopus 로고    scopus 로고
    • TNF-alpha-mediated cell death is attenuated by retrovirus delivery of human heme oxygenase-1 gene into human microvessel endothelial cells
    • T. Kushida, G. LiVolti, A.I. Goodman, and N.G. Abraham TNF-alpha-mediated cell death is attenuated by retrovirus delivery of human heme oxygenase-1 gene into human microvessel endothelial cells Transplant. Proc. 34 2002 2973 2978
    • (2002) Transplant. Proc. , vol.34 , pp. 2973-2978
    • Kushida, T.1    Livolti, G.2    Goodman, A.I.3    Abraham, N.G.4
  • 51
    • 0036035001 scopus 로고    scopus 로고
    • Role of human heme oxygenase-1 in attenuating TNF-alpha-mediated inflammation injury in endothelial cells
    • T. Kushida, V.G. Li, S. Quan, A. Goodman, and N.G. Abraham Role of human heme oxygenase-1 in attenuating TNF-alpha-mediated inflammation injury in endothelial cells J. Cell. Biochem. 87 2002 377 385
    • (2002) J. Cell. Biochem. , vol.87 , pp. 377-385
    • Kushida, T.1    Li, V.G.2    Quan, S.3    Goodman, A.4    Abraham, N.G.5
  • 53
    • 0024239038 scopus 로고
    • Antioxidant defenses and lipid peroxidation in human blood plasma
    • B. Frei, R. Stocker, and B.N. Ames Antioxidant defenses and lipid peroxidation in human blood plasma Proc. Natl. Acad. Sci. USA 85 1988 9748 9752
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9748-9752
    • Frei, B.1    Stocker, R.2    Ames, B.N.3
  • 54
    • 0028239795 scopus 로고
    • Free and albumin-bound bilirubin are efficient co-antioxidants for alpha-tocopherol, inhibiting plasma and low density lipoprotein lipid peroxidation
    • J. Neuzil, 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 1994 16712 16719
    • (1994) J. Biol. Chem. , vol.269 , pp. 16712-16719
    • Neuzil, J.1    Stocker, R.2
  • 55
    • 0026235894 scopus 로고
    • Albumin-bound bilirubins protect human ventricular myocytes against oxyradical damage45
    • T.W. Wu, J. Wu, R.K. Li, D. Mickle, and D. Carey Albumin-bound bilirubins protect human ventricular myocytes against oxyradical damage45 Biochem. Cell Biol. 69 1991 683 688
    • (1991) Biochem. Cell Biol. , vol.69 , pp. 683-688
    • Wu, T.W.1    Wu, J.2    Li, R.K.3    Mickle, D.4    Carey, D.5
  • 57
    • 0027933447 scopus 로고
    • Evidence of involvement of bilirubin as physiological protector against oxidative damage
    • S.F. Lleusy, and M.L. Tomaro Evidence of involvement of bilirubin as physiological protector against oxidative damage Biochim. Biophys. Acta 1223 1994 9 14
    • (1994) Biochim. Biophys. Acta , vol.1223 , pp. 9-14
    • Lleusy, S.F.1    Tomaro, M.L.2
  • 58
    • 0029591458 scopus 로고
    • Heme oxygenase induction by cadmium chloride: Evidence for oxidative stress involvement
    • J.O. Ossola, and M.L. Tomaro Heme oxygenase induction by cadmium chloride: evidence for oxidative stress involvement Toxicology 104 1995 141 147
    • (1995) Toxicology , vol.104 , pp. 141-147
    • Ossola, J.O.1    Tomaro, M.L.2
  • 59
    • 0032571164 scopus 로고    scopus 로고
    • Heme oxygenase induction by UVA radiation. a response to oxidative stress in rat liver
    • J.O. Ossola, and M.L. Tomaro Heme oxygenase induction by UVA radiation. A response to oxidative stress in rat liver Int. J. Biochem. Cell Biol. 30 1998 285 292
    • (1998) Int. J. Biochem. Cell Biol. , vol.30 , pp. 285-292
    • Ossola, J.O.1    Tomaro, M.L.2
  • 60
    • 0034660185 scopus 로고    scopus 로고
    • Dynamics of haem oxygenase-1 expression and bilirubin production in cellular protection against oxidative stress
    • J.E. Clark, R. Foresti, C.J. Green, and R. Motterlini Dynamics of haem oxygenase-1 expression and bilirubin production in cellular protection against oxidative stress Biochem. J. 348 Pt 3 2000 615 619
    • (2000) Biochem. J. , vol.348 , Issue.PART 3 , pp. 615-619
    • Clark, J.E.1    Foresti, R.2    Green, C.J.3    Motterlini, R.4
  • 62
    • 0038206453 scopus 로고    scopus 로고
    • Heme oxygenase I gene expression attenuates angiotensin II-mediated DNA damage in endothelial cells
    • F. Mazza, A.I. Goodman, G. Lombardo, A. Vanella, and N.G. Abraham Heme oxygenase I gene expression attenuates angiotensin II-mediated DNA damage in endothelial cells Exp. Biol. Med. 228 2003 576 583
    • (2003) Exp. Biol. Med. , vol.228 , pp. 576-583
    • Mazza, F.1    Goodman, A.I.2    Lombardo, G.3    Vanella, A.4    Abraham, N.G.5
  • 63
    • 0042763565 scopus 로고    scopus 로고
    • Induction of heme oxygenase-1 in monocytes suppresses angiotensin II-elicited chemotactic activity through inhibition of CCR2: Role of bilirubin and carbon monoxide generated by the enzyme
    • T. Morita, T. Imai, T. Yamaguchi, T. Sugiyama, S. Katayama, and G. Yoshino Induction of heme oxygenase-1 in monocytes suppresses angiotensin II-elicited chemotactic activity through inhibition of CCR2: role of bilirubin and carbon monoxide generated by the enzyme Antioxid. Redox. Signal. 5 2003 439 447
    • (2003) Antioxid. Redox. Signal. , vol.5 , pp. 439-447
    • Morita, T.1    Imai, T.2    Yamaguchi, T.3    Sugiyama, T.4    Katayama, S.5    Yoshino, G.6
  • 64
    • 0026035905 scopus 로고
    • Bilirubin inhibits the activation of superoxide-producing NADPH oxidase in a neutrophil cell-free system
    • J.Y. Kwak, K. Takeshige, B.S. Cheung, and S. Minakami Bilirubin inhibits the activation of superoxide-producing NADPH oxidase in a neutrophil cell-free system Biochim. Biophys. Acta 1076 1991 369 373
    • (1991) Biochim. Biophys. Acta , vol.1076 , pp. 369-373
    • Kwak, J.Y.1    Takeshige, K.2    Cheung, B.S.3    Minakami, S.4
  • 65
    • 0021920319 scopus 로고
    • Mode of inhibitory action of bilirubin on protein kinase C
    • K. Sano, H. Nakamura, and T. Matsuo Mode of inhibitory action of bilirubin on protein kinase C Pediatr. Res. 19 1985 587 590
    • (1985) Pediatr. Res. , vol.19 , pp. 587-590
    • Sano, K.1    Nakamura, H.2    Matsuo, T.3
  • 66
    • 0030005713 scopus 로고    scopus 로고
    • Angiotensin II-mediated hypertension in the rat increases vascular superoxide production via membrane NADH/NADPH oxidase activation. Contribution to alterations of vasomotor tone
    • S. Rajagopalan, S. Kurz, T. Munzel, M. Tarpey, B.A. Freeman, K.K. Griendling, and D.G. Harrison Angiotensin II-mediated hypertension in the rat increases vascular superoxide production via membrane NADH/NADPH oxidase activation. Contribution to alterations of vasomotor tone J. Clin. Invest. 97 1996 1916 1923
    • (1996) J. Clin. Invest. , vol.97 , pp. 1916-1923
    • Rajagopalan, S.1    Kurz, S.2    Munzel, T.3    Tarpey, M.4    Freeman, B.A.5    Griendling, K.K.6    Harrison, D.G.7
  • 68
    • 2542577882 scopus 로고    scopus 로고
    • Bilirubin benefits: Cellular protection by a biliverdin reductase antioxidant cycle
    • T.W. Sedlak, and S.H. Snyder Bilirubin benefits: cellular protection by a biliverdin reductase antioxidant cycle Pediatrics 113 2004 1776 1782
    • (2004) Pediatrics , vol.113 , pp. 1776-1782
    • Sedlak, T.W.1    Snyder, S.H.2
  • 69
    • 23744508873 scopus 로고    scopus 로고
    • The antioxidant mechanism of heme oxygenase-1 involves an increase in superoxide dismutase and catalase in experimental diabetes
    • In Press;
    • S. Turkseven, A. Kruger, C.J. Mingone, P. Kaminski, M. Inaba, S. Ikehara, M.S. Wolin, N.G. Abraham, The antioxidant mechanism of heme oxygenase-1 involves an increase in superoxide dismutase and catalase in experimental diabetes. Am. J. Physiol. In Press; 2005.
    • (2005) Am. J. Physiol.
    • Turkseven, S.1    Kruger, A.2    Mingone, C.J.3    Kaminski, P.4    Inaba, M.5    Ikehara, S.6    Wolin, M.S.7    Abraham, N.G.8
  • 70
    • 19544370747 scopus 로고    scopus 로고
    • Heme oxygenase-1 prevents superoxide anion-associated vascular smooth muscle growth and decreases circulating endothelial cells in a rat model of balloon injury and restenosis in diabetes mellitus (abstract)
    • American Heart Association Scientific Session
    • J.A. McClung, T. Morita, L. Rodella, R. Rezzani, M.B. Weiss, and N.G. Abraham Heme oxygenase-1 prevents superoxide anion-associated vascular smooth muscle growth and decreases circulating endothelial cells in a rat model of balloon injury and restenosis in diabetes mellitus (abstract) Circulation 110 2004 American Heart Association Scientific Session
    • (2004) Circulation , vol.110
    • McClung, J.A.1    Morita, T.2    Rodella, L.3    Rezzani, R.4    Weiss, M.B.5    Abraham, N.G.6
  • 71
    • 19544380101 scopus 로고    scopus 로고
    • Heme oxygenase-1 upregulation attenuates glucose-mediated oxidative stress renal injury in HO-2 knockout mice (abstract)
    • R. Rezzani, S. Quan, L. Rodella, R. Bianchi, A. Goodman, and N.G. Abraham Heme oxygenase-1 upregulation attenuates glucose-mediated oxidative stress renal injury in HO-2 knockout mice (abstract) Hypertension 42 2003
    • (2003) Hypertension , vol.42
    • Rezzani, R.1    Quan, S.2    Rodella, L.3    Bianchi, R.4    Goodman, A.5    Abraham, N.G.6
  • 72
    • 0033527413 scopus 로고    scopus 로고
    • Oxidation of tetrahydrobiopterin by peroxynitrite: Implications for vascular endothelial function
    • S. Milstien, and Z. Katusic Oxidation of tetrahydrobiopterin by peroxynitrite: implications for vascular endothelial function Biochem. Biophys. Res. Commun. 263 1999 681 684
    • (1999) Biochem. Biophys. Res. Commun. , vol.263 , pp. 681-684
    • Milstien, S.1    Katusic, Z.2
  • 74
    • 0037127305 scopus 로고    scopus 로고
    • Glucose deprivation induces heme oxygenase-1 gene expression by a pathway independent of the unfolded protein response
    • S.H. Chang, I. Barbosa-Tessmann, C. Chen, M.S. Kilberg, and A. Agarwal Glucose deprivation induces heme oxygenase-1 gene expression by a pathway independent of the unfolded protein response J. Biol. Chem. 277 2002 1933 1940
    • (2002) J. Biol. Chem. , vol.277 , pp. 1933-1940
    • Chang, S.H.1    Barbosa-Tessmann, I.2    Chen, C.3    Kilberg, M.S.4    Agarwal, A.5
  • 75
    • 19544393950 scopus 로고    scopus 로고
    • Heme-oxygenase-1 modulates vascular responses in diabetic rats via guanylate cyclase activation:role of superoxide dismutase (abstract)
    • C.J. Mingone, S. Turkseven, M.S. Wolin, and N.G. Abraham Heme-oxygenase-1 modulates vascular responses in diabetic rats via guanylate cyclase activation:role of superoxide dismutase (abstract) FASEB 2005
    • (2005) FASEB
    • Mingone, C.J.1    Turkseven, S.2    Wolin, M.S.3    Abraham, N.G.4
  • 76
    • 68049097788 scopus 로고    scopus 로고
    • Down regulation of iNOS and in eNOS by overexpression of heme oxygenase-1 restore vascular response in diabetic rats (abstract)
    • A. Mansoor, C.J. Mingone, S. Turkseven, M.S. Wolin, and N.G. Abraham Down regulation of iNOS and in eNOS by overexpression of heme oxygenase-1 restore vascular response in diabetic rats (abstract) FASEB 2005
    • (2005) FASEB
    • Mansoor, A.1    Mingone, C.J.2    Turkseven, S.3    Wolin, M.S.4    Abraham, N.G.5
  • 79
    • 4043058702 scopus 로고    scopus 로고
    • Bilirubin inhibits iNOS expression and NO production in response to endotoxin in rats
    • W.W. Wang, D.L. Smith, and S.D. Zucker Bilirubin inhibits iNOS expression and NO production in response to endotoxin in rats Hepatology 40 2004 424 433
    • (2004) Hepatology , vol.40 , pp. 424-433
    • Wang, W.W.1    Smith, D.L.2    Zucker, S.D.3
  • 80
    • 0024587145 scopus 로고
    • Treatment with tin prevents the development of hypertension in spontaneously hypertensive rats
    • D. Sacerdoti, B. Escalante, N.G. Abraham, J.C. McGiff, R.D. Levere, and M.L. Schwartzman Treatment with tin prevents the development of hypertension in spontaneously hypertensive rats Science 243 1989 388 390
    • (1989) Science , vol.243 , pp. 388-390
    • Sacerdoti, D.1    Escalante, B.2    Abraham, N.G.3    McGiff, J.C.4    Levere, R.D.5    Schwartzman, M.L.6
  • 81
    • 0038335799 scopus 로고    scopus 로고
    • Expression of heme oxygenase-1 and endothelial nitric oxide synthase in the lung of newborns with congenital diaphragmatic hernia and persistent pulmonary hypertension
    • V. Solari, A.P. Piotrowska, and P. Puri Expression of heme oxygenase-1 and endothelial nitric oxide synthase in the lung of newborns with congenital diaphragmatic hernia and persistent pulmonary hypertension J. Pediatr. Surg. 38 2003 808 813
    • (2003) J. Pediatr. Surg. , vol.38 , pp. 808-813
    • Solari, V.1    Piotrowska, A.P.2    Puri, P.3
  • 82
    • 0034883783 scopus 로고    scopus 로고
    • Heme oxygenase: A font of multiple messengers
    • S.H. Snyder, and D.E. Baranano Heme oxygenase: a font of multiple messengers Neuropsychopharmacology 25 2001 294 298
    • (2001) Neuropsychopharmacology , vol.25 , pp. 294-298
    • Snyder, S.H.1    Baranano, D.E.2
  • 83
    • 0030065052 scopus 로고    scopus 로고
    • NO-mediated activation of heme oxgenase: Endogenous cytoprotection against oxidative stress to endothelium
    • R. Motterlini, R. Foresti, M. Intaglietta, and R.M. Winslow NO-mediated activation of heme oxgenase: endogenous cytoprotection against oxidative stress to endothelium Am. J. Physiol. 270 1996 H107 H114
    • (1996) Am. J. Physiol. , vol.270
    • Motterlini, R.1    Foresti, R.2    Intaglietta, M.3    Winslow, R.M.4
  • 86
    • 0038264420 scopus 로고    scopus 로고
    • Induction of heme oxygenase-1 and stimulation of cGMP production by hemin in aortic tissues from hypertensive rats
    • J.F. Ndisang, L. Wu, W. Zhao, and R. Wang Induction of heme oxygenase-1 and stimulation of cGMP production by hemin in aortic tissues from hypertensive rats Blood 101 2003 3893 3900
    • (2003) Blood , vol.101 , pp. 3893-3900
    • Ndisang, J.F.1    Wu, L.2    Zhao, W.3    Wang, R.4
  • 87
    • 0039966913 scopus 로고    scopus 로고
    • Role of endogenous carbon monoxide in the pathogenesis of hypotension during septic shock
    • H.S. Ou, J. Yang, L.W. Dong, Y.Z. Pang, J.Y. Su, C.S. Tang, and N.K. Liu Role of endogenous carbon monoxide in the pathogenesis of hypotension during septic shock Sheng Li Xue. Bao. 51 1999 1 6
    • (1999) Sheng Li Xue. Bao. , vol.51 , pp. 1-6
    • Ou, H.S.1    Yang, J.2    Dong, L.W.3    Pang, Y.Z.4    Su, J.Y.5    Tang, C.S.6    Liu, N.K.7
  • 88
    • 5444228527 scopus 로고    scopus 로고
    • [Heme oxygenase and carbon monoxide in the physiology and pathology of the cardiovascular system]
    • J. Beltowski, A. Jamroz, and E. Borkowska [Heme oxygenase and carbon monoxide in the physiology and pathology of the cardiovascular system] Postepy Hig. Med. Dosw. (Online) 58 2004 83 99
    • (2004) Postepy Hig. Med. Dosw. (Online) , vol.58 , pp. 83-99
    • Beltowski, J.1    Jamroz, A.2    Borkowska, E.3
  • 89
    • 0036347845 scopus 로고    scopus 로고
    • Carbon monoxide regulates blood pressure cooperatively with nitric oxide in hypertensive rats
    • M. Ushiyama, T. Morita, and S. Katayama Carbon monoxide regulates blood pressure cooperatively with nitric oxide in hypertensive rats Heart Vessels 16 2002 189 195
    • (2002) Heart Vessels , vol.16 , pp. 189-195
    • Ushiyama, M.1    Morita, T.2    Katayama, S.3
  • 92
    • 1842829881 scopus 로고    scopus 로고
    • [Cardioprotective effect of heme oxygenase-1 induction by hemin on the isolated rat heart during ischemia-reperfusion]
    • T.V. Kukoba, O.O. Moibenko, and A.V. Kotsioruba [Cardioprotective effect of heme oxygenase-1 induction by hemin on the isolated rat heart during ischemia-reperfusion] Fiziol. Zh. 49 2003 14 21
    • (2003) Fiziol. Zh. , vol.49 , pp. 14-21
    • Kukoba, T.V.1    Moibenko, O.O.2    Kotsioruba, A.V.3
  • 93
    • 0033925281 scopus 로고    scopus 로고
    • Microsatellite polymorphism in the heme oxygenase-1 gene promoter is associated with susceptibility to emphysema
    • N. Yamada, M. Yamaya, S. Okinaga, K. Nakayama, K. Sekizawa, S. Shibahara, and H. Sasaki Microsatellite polymorphism in the heme oxygenase-1 gene promoter is associated with susceptibility to emphysema Am. J. Hum. Genet. 66 2000 187 195
    • (2000) Am. J. Hum. Genet. , vol.66 , pp. 187-195
    • Yamada, N.1    Yamaya, M.2    Okinaga, S.3    Nakayama, K.4    Sekizawa, K.5    Shibahara, S.6    Sasaki, H.7
  • 94
    • 0035960644 scopus 로고    scopus 로고
    • Adenovirus-mediated heme oxygenase-1 gene delivery inhibits injury-induced vascular neointima formation
    • D.A. Tulis, W. Durante, X. Liu, A.J. Evans, K.J. Peyton, and A.I. Schafer Adenovirus-mediated heme oxygenase-1 gene delivery inhibits injury-induced vascular neointima formation Circulation 104 2001 2710 2715
    • (2001) Circulation , vol.104 , pp. 2710-2715
    • Tulis, D.A.1    Durante, W.2    Liu, X.3    Evans, A.J.4    Peyton, K.J.5    Schafer, A.I.6
  • 96
    • 0036392112 scopus 로고    scopus 로고
    • Differential effect of heme oxygenase-1 in endothelial and smooth muscle cell cycle progression
    • G. Li Volti, J. Wang, F. Traganos, A. Kappas, and N.G. Abraham Differential effect of heme oxygenase-1 in endothelial and smooth muscle cell cycle progression Biochem. Biophys. Res. Commun. 296 2002 1077 1082
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 1077-1082
    • Li Volti, G.1    Wang, J.2    Traganos, F.3    Kappas, A.4    Abraham, N.G.5
  • 98
    • 0029130496 scopus 로고
    • Induction of heme oxygenase in toxic renal injury: A protective role in cisplatin nephrotoxicity in the rat
    • A. Agarwal, J. Balla, J. Alam, A.J. Croatt, and K.A. Nath Induction of heme oxygenase in toxic renal injury: a protective role in cisplatin nephrotoxicity in the rat Kidney Int. 48 1995 1298 1307
    • (1995) Kidney Int. , vol.48 , pp. 1298-1307
    • Agarwal, A.1    Balla, J.2    Alam, J.3    Croatt, A.J.4    Nath, K.A.5
  • 99
    • 0026769706 scopus 로고
    • Differential induction of heme oxygenase in the hepatocarcinoma cell line (Hep3b) by environmental agents
    • J.D. Lutton, J.-L. da Silva, S. Moqattash, A.C. Brown, R.D. Levere, and N.G. Abraham Differential induction of heme oxygenase in the hepatocarcinoma cell line (Hep3b) by environmental agents J. Cell. Biochem. 49 1992 259 265
    • (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
  • 100
    • 0028820196 scopus 로고
    • Growth imbalance and altered expression of cyclins B1, A, e and D3 in MOLT-4 cells synchronized in the cell cycle by inhibitors of DNA replication
    • J. Gong, and F.D.Z. Traganos Growth imbalance and altered expression of cyclins B1, A, E and D3 in MOLT-4 cells synchronized in the cell cycle by inhibitors of DNA replication Cell Growth Differ. 6 1995 1485 1493
    • (1995) Cell Growth Differ. , vol.6 , pp. 1485-1493
    • Gong, J.1    Traganos, F.D.Z.2
  • 101
    • 0030952477 scopus 로고    scopus 로고
    • Cytokine regulation of endothelial cell function: From molecular level to the bedside
    • A. Mantovani, F. Bussolino, and M. Introna Cytokine regulation of endothelial cell function: from molecular level to the bedside Immunol. Today 18 1997 231 240
    • (1997) Immunol. Today , vol.18 , pp. 231-240
    • Mantovani, A.1    Bussolino, F.2    Introna, M.3
  • 102
    • 0344011671 scopus 로고    scopus 로고
    • Human heme oxygenase: Cell cycle-dependent expression and DNA microarray identification of multiple gene responses after transduction of endothelial cells
    • N.G. Abraham, G. Scapagnini, and A. Kappas Human heme oxygenase: cell cycle-dependent expression and DNA microarray identification of multiple gene responses after transduction of endothelial cells J. Cell. Biochem. 90 2003 1098 1111
    • (2003) J. Cell. Biochem. , vol.90 , pp. 1098-1111
    • Abraham, N.G.1    Scapagnini, G.2    Kappas, A.3
  • 104
    • 0042171477 scopus 로고    scopus 로고
    • Neonatal hyperbilirubinemia in Japanese neonates: Analysis of the heme oxygenase-1 gene and fetal hemoglobin composition in cord blood
    • M. Kanai, K. Akaba, A. Sasaki, M. Sato, T. Harano, S. Shibahara, H. Kurachi, T. Yoshida, and K. Hayasaka Neonatal hyperbilirubinemia in Japanese neonates: analysis of the heme oxygenase-1 gene and fetal hemoglobin composition in cord blood Pediatr. Res. 54 2003 165 171
    • (2003) Pediatr. Res. , vol.54 , pp. 165-171
    • Kanai, M.1    Akaba, K.2    Sasaki, A.3    Sato, M.4    Harano, T.5    Shibahara, S.6    Kurachi, H.7    Yoshida, T.8    Hayasaka, K.9
  • 105
    • 0042655121 scopus 로고    scopus 로고
    • Association of a promoter variant of the haeme oxygenase-1 gene with hypertension in women
    • K. Ono, T. Mannami, and N. Iwai Association of a promoter variant of the haeme oxygenase-1 gene with hypertension in women J. Hypertens. 21 2003 1497 1503
    • (2003) J. Hypertens. , vol.21 , pp. 1497-1503
    • Ono, K.1    Mannami, T.2    Iwai, N.3
  • 106
    • 0141996321 scopus 로고    scopus 로고
    • Polymorphisms of heme oxygenase-1 and bilirubin UDP- glucuronosyltransferase genes are not associated with Kawasaki disease susceptibility
    • M. Kanai, S. Tanabe, M. Okada, H. Suzuki, T. Niki, M. Katsuura, T. Akiba, and K. Hayasaka Polymorphisms of heme oxygenase-1 and bilirubin UDP-glucuronosyltransferase genes are not associated with Kawasaki disease susceptibility J. Tohoku, Exp. Med. 200 2003 155 159
    • (2003) J. Tohoku, Exp. Med. , vol.200 , pp. 155-159
    • Kanai, M.1    Tanabe, S.2    Okada, M.3    Suzuki, H.4    Niki, T.5    Katsuura, M.6    Akiba, T.7    Hayasaka, K.8
  • 107
    • 7944222236 scopus 로고    scopus 로고
    • Polymorphism in heme oxygenase-1 (HO-1) promoter is related to the risk of oral squamous cell carcinoma occurring on male areca chewers
    • K.W. Chang, T.C. Lee, W.I. Yeh, M.Y. Chung, C.J. Liu, L.Y. Chi, and S.C. Lin Polymorphism in heme oxygenase-1 (HO-1) promoter is related to the risk of oral squamous cell carcinoma occurring on male areca chewers Br. J. Cancer 91 2004 1551 1555
    • (2004) Br. J. Cancer , vol.91 , pp. 1551-1555
    • Chang, K.W.1    Lee, T.C.2    Yeh, W.I.3    Chung, M.Y.4    Liu, C.J.5    Chi, L.Y.6    Lin, S.C.7
  • 108
    • 2342452451 scopus 로고    scopus 로고
    • The effect of a promoter polymorphism in the heme oxygenase-1 gene on the risk of ischaemic cerebrovascular events: The influence of other vascular risk factors
    • M. Funk, G. Endler, M. Schillinger, S. Mustafa, K. Hsieh, M. Exner, W. Lalouschek, C. Mannhalter, and O. Wagner The effect of a promoter polymorphism in the heme oxygenase-1 gene on the risk of ischaemic cerebrovascular events: the influence of other vascular risk factors Thromb. Res. 113 2004 217 223
    • (2004) Thromb. Res. , vol.113 , pp. 217-223
    • Funk, M.1    Endler, G.2    Schillinger, M.3    Mustafa, S.4    Hsieh, K.5    Exner, M.6    Lalouschek, W.7    Mannhalter, C.8    Wagner, O.9
  • 114
    • 19544387654 scopus 로고    scopus 로고
    • Mesenchymal stem cells protected with a hypoxia-regulated heme oxygenase-1 vector: A potential strategy to prevent graft cell death in the ischemic heart (abstract)
    • Y.L. Tang, Y. Tang, Y.C. Zhang, and M.I. Philips Mesenchymal stem cells protected with a hypoxia-regulated heme oxygenase-1 vector: A potential strategy to prevent graft cell death in the ischemic heart (abstract) Circulation 110 2004 17
    • (2004) Circulation , vol.110 , pp. 17
    • Tang, Y.L.1    Tang, Y.2    Zhang, Y.C.3    Philips, M.I.4
  • 116
    • 3042783328 scopus 로고    scopus 로고
    • Water-soluble carbon monoxide-releasing molecules: Helping to elucidate the vascular activity of the 'silent killer'
    • P.K. Chatterjee Water-soluble carbon monoxide-releasing molecules: helping to elucidate the vascular activity of the 'silent killer' Br. J. Pharmacol. 142 2004 391 393
    • (2004) Br. J. Pharmacol. , vol.142 , pp. 391-393
    • Chatterjee, P.K.1
  • 119
    • 0031010733 scopus 로고    scopus 로고
    • Carbon monoxide-induced vasorelaxation and the underlying mechanisms
    • R. Wang, Z. Wang, and L. Wu 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.2    Wu, L.3
  • 120
    • 0028928004 scopus 로고
    • Smooth muscle cell-derived carbon monoxide is a regulator of vascular cGMP
    • T. Morita, M.A. Perrella, M. Lee, and S. Kourembanas 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.3    Kourembanas, S.4
  • 121
    • 0038545203 scopus 로고    scopus 로고
    • Alterations in heme oxygenase/carbon monoxide system in pulmonary arteries in hypertension
    • J.F. Ndisang, and R. Wang Alterations in heme oxygenase/carbon monoxide system in pulmonary arteries in hypertension Exp. Biol. Med. (Maywood) 228 2003 557 563
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , pp. 557-563
    • Ndisang, J.F.1    Wang, R.2
  • 122
    • 0025332748 scopus 로고
    • Effect of heme arginate administration on blood pressure in spontaneously hypertensive rats
    • R.D. Levere, 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 1990 213 219
    • (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
  • 128
    • 0037370554 scopus 로고    scopus 로고
    • Characterization of heme oxygenase 1 (heat shock protein 32) induction by atrial natriuretic peptide in human endothelial cells
    • A.K. Kiemer, N. Bildner, N.C. Weber, and A.M. Vollmar Characterization of heme oxygenase 1 (heat shock protein 32) induction by atrial natriuretic peptide in human endothelial cells Endocrinology 144 2003 802 812
    • (2003) Endocrinology , vol.144 , pp. 802-812
    • Kiemer, A.K.1    Bildner, N.2    Weber, N.C.3    Vollmar, A.M.4
  • 129
    • 0036139813 scopus 로고    scopus 로고
    • Atrial natriuretic peptide reduces cyclosporin toxicity in renal cells: Role of cGMP and heme oxygenase-1
    • T. Polte, A. Hemmerle, G. Berndt, N. Grosser, A. Abate, and H. Schroder Atrial natriuretic peptide reduces cyclosporin toxicity in renal cells: role of cGMP and heme oxygenase-1 Free Radic. Biol. Med. 32 2002 56 63
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 56-63
    • Polte, T.1    Hemmerle, A.2    Berndt, G.3    Grosser, N.4    Abate, A.5    Schroder, H.6
  • 130
    • 0037448802 scopus 로고    scopus 로고
    • Rapamycin induces heme oxygenase-1 in human pulmonary vascular cells: Implications in the antiproliferative response to rapamycin
    • G.A. Visner, F. Lu, H. Zhou, J. Liu, K. Kazemfar, and A. Agarwal Rapamycin induces heme oxygenase-1 in human pulmonary vascular cells: implications in the antiproliferative response to rapamycin Circulation 107 2003 911 916
    • (2003) Circulation , vol.107 , pp. 911-916
    • Visner, G.A.1    Lu, F.2    Zhou, H.3    Liu, J.4    Kazemfar, K.5    Agarwal, A.6
  • 131
    • 0034063564 scopus 로고    scopus 로고
    • Heme oxygenase-1 is a cGMP-inducible endothelial protein and mediates the cytoprotective action of nitric oxide
    • T. Polte, A. Abate, P.A. Dennery, and H. Schroder Heme oxygenase-1 is a cGMP-inducible endothelial protein and mediates the cytoprotective action of nitric oxide Arterioscler. Thromb. Vasc. Biol. 20 2000 1209 1215
    • (2000) Arterioscler. Thromb. Vasc. Biol. , vol.20 , pp. 1209-1215
    • Polte, T.1    Abate, A.2    Dennery, P.A.3    Schroder, H.4
  • 132
    • 0032960103 scopus 로고    scopus 로고
    • Contribution of endogenous carbon monoxide to regulation of diameter in resistance vessels
    • F. Kozma, R.A. Johnson, F. Zhang, C. Yu, X. Tong, and A. Nasjletti Contribution of endogenous carbon monoxide to regulation of diameter in resistance vessels Am. J. Physiol. 276 1999 R1087 R1094
    • (1999) Am. J. Physiol. , vol.276
    • Kozma, F.1    Johnson, R.A.2    Zhang, F.3    Yu, C.4    Tong, X.5    Nasjletti, A.6
  • 135
    • 3042584685 scopus 로고    scopus 로고
    • Persistent lowering of pressure by transplanting kidneys from adult spontaneously hypertensive rats treated with brief antihypertensive therapy
    • C. Smallegange, T.M. Hale, T.L. Bushfield, and M.A. Adams Persistent lowering of pressure by transplanting kidneys from adult spontaneously hypertensive rats treated with brief antihypertensive therapy Hypertension 44 2004 89 94
    • (2004) Hypertension , vol.44 , pp. 89-94
    • Smallegange, C.1    Hale, T.M.2    Bushfield, T.L.3    Adams, M.A.4
  • 137
    • 0031914416 scopus 로고    scopus 로고
    • Heme oxygenase is induced in nephrotoxic nephritis and hemin, a stimulator of heme oxygenase synthesis, ameliorates disease
    • K. Mosley, D.E. Wembridge, V. Cattell, and H.T. Cook Heme oxygenase is induced in nephrotoxic nephritis and hemin, a stimulator of heme oxygenase synthesis, ameliorates disease Kidney Int. 53 1998 672 678
    • (1998) Kidney Int. , vol.53 , pp. 672-678
    • Mosley, K.1    Wembridge, D.E.2    Cattell, V.3    Cook, H.T.4
  • 138
    • 1642520796 scopus 로고    scopus 로고
    • Acute renal hemodynamic effects of dimanganese decacarbonyl and cobalt protoporphyrin
    • B. Arregui, B. Lopez, S.M. Garcia, F. Valero, C. Navarro, and F.J. Fenoy Acute renal hemodynamic effects of dimanganese decacarbonyl and cobalt protoporphyrin Kidney Int. 65 2004 564 574
    • (2004) Kidney Int. , vol.65 , pp. 564-574
    • Arregui, B.1    Lopez, B.2    Garcia, S.M.3    Valero, F.4    Navarro, C.5    Fenoy, F.J.6
  • 139
    • 0035019739 scopus 로고    scopus 로고
    • The role of haem oxygenase in renal vascular reactivity in normotensive and hypertensive rats
    • M.R. Mustafa, and E.J. Johns The role of haem oxygenase in renal vascular reactivity in normotensive and hypertensive rats J. Hypertens. 19 2001 1105 1111
    • (2001) J. Hypertens. , vol.19 , pp. 1105-1111
    • Mustafa, M.R.1    Johns, E.J.2
  • 140
    • 0141928185 scopus 로고    scopus 로고
    • Effects of exogenous heme on renal function. Role of heme oxygenase and cyclooxygenase
    • F. Rodriguez, R. Kemp, M. Balazy, and A. Nasjletti Effects of exogenous heme on renal function. Role of heme oxygenase and cyclooxygenase Hypertension 42 2003 680 684
    • (2003) Hypertension , vol.42 , pp. 680-684
    • Rodriguez, F.1    Kemp, R.2    Balazy, M.3    Nasjletti, A.4
  • 141
    • 0034034173 scopus 로고    scopus 로고
    • Targeting of the renin-angiotensin system by antisense gene therapy: A possible strategy for the long-term control of hypertension
    • M.K. Raizada, S.C. Francis, H. Wang, C.H. Gelband, P.Y. Reaves, and M.J. Katovich Targeting of the renin-angiotensin system by antisense gene therapy: a possible strategy for the long-term control of hypertension J. Hypertens. 18 2000 353 362
    • (2000) J. Hypertens. , vol.18 , pp. 353-362
    • Raizada, M.K.1    Francis, S.C.2    Wang, H.3    Gelband, C.H.4    Reaves, P.Y.5    Katovich, M.J.6
  • 143
    • 0033922326 scopus 로고    scopus 로고
    • Angiotensin II induces renal oxidant stress in vivo and heme oxygenase- 1 in vivo and in vitro
    • E.N. Haugen, A.J. Croatt, and K.A. Nath Angiotensin II induces renal oxidant stress in vivo and heme oxygenase- 1 in vivo and in vitro Kidney Int. 58 2000 144 152
    • (2000) Kidney Int. , vol.58 , pp. 144-152
    • Haugen, E.N.1    Croatt, A.J.2    Nath, K.A.3
  • 144
    • 0034065989 scopus 로고    scopus 로고
    • Heme oxygenase-1 is upregulated in the kidney of angiotensin II-induced hypertensive rats: Possible role in renoprotection
    • T. Aizawa, N. Ishizaka, J. Taguchi, R. Nagai, I. Mori, S.S. Tang, J.R. Ingelfinger, and M. Ohno Heme oxygenase-1 is upregulated in the kidney of angiotensin II-induced hypertensive rats: possible role in renoprotection Hypertension 35 2000 800 806
    • (2000) Hypertension , vol.35 , pp. 800-806
    • Aizawa, T.1    Ishizaka, N.2    Taguchi, J.3    Nagai, R.4    Mori, I.5    Tang, S.S.6    Ingelfinger, J.R.7    Ohno, M.8
  • 145
    • 0036839125 scopus 로고    scopus 로고
    • Superoxide stimulates NaCl absorption by the thick ascending limb
    • P.A. Ortiz, and J.L. Garvin Superoxide stimulates NaCl absorption by the thick ascending limb Am. J. Physiol. Renal Physiol. 283 2002 F957 F962
    • (2002) Am. J. Physiol. Renal Physiol. , vol.283
    • Ortiz, P.A.1    Garvin, J.L.2
  • 146
    • 0035002888 scopus 로고    scopus 로고
    • Induction of heme oxygenase 1 in radiation nephropathy: Role of angiotensin II
    • P.K. Datta, J.E. Moulder, B.L. Fish, E.P. Cohen, and E.A. Lianos Induction of heme oxygenase 1 in radiation nephropathy: role of angiotensin II Radiat. Res. 155 2001 734 739
    • (2001) Radiat. Res. , vol.155 , pp. 734-739
    • Datta, P.K.1    Moulder, J.E.2    Fish, B.L.3    Cohen, E.P.4    Lianos, E.A.5
  • 147
    • 0031026658 scopus 로고    scopus 로고
    • Heme oxygenase-1 is regulated by angiotensin II in rat vascular smooth muscle cells
    • N. Ishizaka, and K.K. Griendling Heme oxygenase-1 is regulated by angiotensin II in rat vascular smooth muscle cells Hypertension 29 1997 790 795
    • (1997) Hypertension , vol.29 , pp. 790-795
    • Ishizaka, N.1    Griendling, K.K.2
  • 148
    • 0030886381 scopus 로고    scopus 로고
    • Heme oxygenase 1 is required for mammalian iron reutilization
    • K.D. Poss, and S. Tonegawa Heme oxygenase 1 is required for mammalian iron reutilization Proc. Natl. Acad. Sci. USA 94 1997 10919 10924
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10919-10924
    • Poss, K.D.1    Tonegawa, S.2
  • 152
    • 16444380220 scopus 로고    scopus 로고
    • NAD(P)H oxidase inhibition attenuates neuronal chronotropic actions of angiotensin II
    • C. Sun, K.W. Sellers, C. Sumners, and M.K. Raizada NAD(P)H oxidase inhibition attenuates neuronal chronotropic actions of angiotensin II Circ. Res. 2005
    • (2005) Circ. Res.
    • Sun, C.1    Sellers, K.W.2    Sumners, C.3    Raizada, M.K.4
  • 153
    • 0034167908 scopus 로고    scopus 로고
    • Free radical production and angiotensin
    • G. Wolf Free radical production and angiotensin Curr. Hypertens. Rep. 2 2000 167 173
    • (2000) Curr. Hypertens. Rep. , vol.2 , pp. 167-173
    • Wolf, G.1
  • 154
    • 0036182341 scopus 로고    scopus 로고
    • Regulation of cyclooxygenase- and cytochrome p450-derived eicosanoids by heme oxygenase in the rat kidney
    • F.T. Botros, M. Laniado-Schwartzman, and N.G. Abraham Regulation of cyclooxygenase- and cytochrome p450-derived eicosanoids by heme oxygenase in the rat kidney Hypertension 39 2002 639 644
    • (2002) Hypertension , vol.39 , pp. 639-644
    • Botros, F.T.1    Laniado-Schwartzman, M.2    Abraham, N.G.3
  • 155
    • 0037340031 scopus 로고    scopus 로고
    • Heme oxygenase attenuates angiotensin II-mediated increase in cyclooxygenase-2 activity in human femoral endothelial cells
    • G. Li Volti, F. Seta, M.L. Schwartzman, A. Nasjletti, and N.G. Abraham Heme oxygenase attenuates angiotensin II-mediated increase in cyclooxygenase-2 activity in human femoral endothelial cells Hypertension 41 2003 715 719
    • (2003) Hypertension , vol.41 , pp. 715-719
    • Li Volti, G.1    Seta, F.2    Schwartzman, M.L.3    Nasjletti, A.4    Abraham, N.G.5
  • 157
    • 0028087299 scopus 로고
    • Effects of 17-octadecynoic acid, a suicide-substrate inhibitor of cytochrome P450 fatty acid omega-hydroxylase, on renal function in rats
    • A.P. Zou, Y.H. Ma, Z.H. Sui, P.R. Ortiz-de-Montellano, J.E. Clark, B.S. Masters, and R.J. Roman Effects of 17-octadecynoic acid, a suicide-substrate inhibitor of cytochrome P450 fatty acid omega-hydroxylase, on renal function in rats J. Pharmacol. Exp. Ther. 268 1994 474 481
    • (1994) J. Pharmacol. Exp. Ther. , vol.268 , pp. 474-481
    • Zou, A.P.1    Ma, Y.H.2    Sui, Z.H.3    Ortiz-De-Montellano, P.R.4    Clark, J.E.5    Masters, B.S.6    Roman, R.J.7
  • 158
    • 0025345277 scopus 로고
    • Thromboxane mediation of the pressor response to infused angiotensin II
    • C.S. Wilcox, and W.J. Welch Thromboxane mediation of the pressor response to infused angiotensin II Am. J. Hypertens. 3 1990 242 249
    • (1990) Am. J. Hypertens. , vol.3 , pp. 242-249
    • Wilcox, C.S.1    Welch, W.J.2
  • 159
    • 0028179292 scopus 로고
    • Expression of prostaglandin H2-mediated mechanism of vascular contraction in hypertensive rats. Relation to lipoxygenase and prostacyclin synthase activities
    • L. Lin, M. Balazy, P.J. Pagano, and A. Nasjletti Expression of prostaglandin H2-mediated mechanism of vascular contraction in hypertensive rats. Relation to lipoxygenase and prostacyclin synthase activities Circ. Res. 74 1994 197 205
    • (1994) Circ. Res. , vol.74 , pp. 197-205
    • Lin, L.1    Balazy, M.2    Pagano, P.J.3    Nasjletti, A.4
  • 160
    • 0024582076 scopus 로고
    • Manipulation of cytochrome P-450 dependent renal thromboxane synthase activity in spontaneously hypertensive rats
    • W.C. Sessa, N.G. Abraham, B. Escalante, and M.L. Schwartzman Manipulation of cytochrome P-450 dependent renal thromboxane synthase activity in spontaneously hypertensive rats J. Hypertens. 7 1989 37 42
    • (1989) J. Hypertens. , vol.7 , pp. 37-42
    • Sessa, W.C.1    Abraham, N.G.2    Escalante, B.3    Schwartzman, M.L.4
  • 162
    • 0028326284 scopus 로고
    • Tin-mediated heme oxygenase gene activation and cytochrome P450 arachidonate hydroxylase inhibition in spontaneously hypertensive rats [published erratum appears in Am. J. Med. Sci. 308(2):138; 1994]
    • J.L. da-Silva, M. Tiefenthaler, E. Park, B. Escalante, M.L. Schwartzman, R.D. Levere, and N.G. Abraham Tin-mediated heme oxygenase gene activation and cytochrome P450 arachidonate hydroxylase inhibition in spontaneously hypertensive rats [published erratum appears in Am. J. Med. Sci. 308(2):138; 1994] Am. J. Med. Sci. 307 1994 173 181
    • (1994) Am. J. Med. Sci. , vol.307 , pp. 173-181
    • Da-Silva, J.L.1    Tiefenthaler, M.2    Park, E.3    Escalante, B.4    Schwartzman, M.L.5    Levere, R.D.6    Abraham, N.G.7
  • 163
    • 0023839318 scopus 로고
    • Renal cytochrome P450-dependent metabolism of arachidonic acid in spontaneously hypertensive rats
    • D. Sacerdoti, N.G. Abraham, J.C. McGiff, and M.L. Schwartzman Renal cytochrome P450-dependent metabolism of arachidonic acid in spontaneously hypertensive rats Biochem. Pharmacol. 37 1988 521 527
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 521-527
    • Sacerdoti, D.1    Abraham, N.G.2    McGiff, J.C.3    Schwartzman, M.L.4
  • 164
    • 0025780578 scopus 로고
    • Cytochrome P-450 metabolism of arachidonic acid
    • J.C. McGiff Cytochrome P-450 metabolism of arachidonic acid Annu. Rev. Pharmacol. Toxicol. 31 1991 339 369
    • (1991) Annu. Rev. Pharmacol. Toxicol. , vol.31 , pp. 339-369
    • McGiff, J.C.1
  • 165
    • 0023671325 scopus 로고
    • Eicosanoids and hypertension
    • J.C. McGiff Eicosanoids and hypertension Rev. Port. Cardiol. 7 1988 59 61
    • (1988) Rev. Port. Cardiol. , vol.7 , pp. 59-61
    • McGiff, J.C.1
  • 166
    • 0024381618 scopus 로고
    • Metabolism of 20-hydroxyeicosatetraenoic acid by cyclooxygenase. Formation and identification of novel endothelium-dependent vasoconstrictor metabolites
    • M.L. Schwartzman, J.R. Falck, P. Yadagiri, and B. Escalante Metabolism of 20-hydroxyeicosatetraenoic acid by cyclooxygenase. Formation and identification of novel endothelium-dependent vasoconstrictor metabolites J. Biol. Chem. 264 1989 11658 11662
    • (1989) J. Biol. Chem. , vol.264 , pp. 11658-11662
    • Schwartzman, M.L.1    Falck, J.R.2    Yadagiri, P.3    Escalante, B.4
  • 167
    • 0026567720 scopus 로고
    • Cyclooxygenase dependency of the renovascular actions of cytochrome P450-derived arachidonate metabolites
    • M.A. Carroll, M.P. Garcia, J.R. Falck, and J.C. McGiff Cyclooxygenase dependency of the renovascular actions of cytochrome P450-derived arachidonate metabolites J. Pharmacol. Exp. Ther. 260 1992 104 109
    • (1992) J. Pharmacol. Exp. Ther. , vol.260 , pp. 104-109
    • Carroll, M.A.1    Garcia, M.P.2    Falck, J.R.3    McGiff, J.C.4
  • 169
    • 0021813222 scopus 로고
    • Renal cytochrome P450-related arachidonate metabolite inhibits (Na+ + K+)ATPase
    • M. Schwartzman, N.R. Ferreri, M.A. Carroll, E. Songu-Mize, and J.C. McGiff Renal cytochrome P450-related arachidonate metabolite inhibits (Na+ + K+)ATPase Nature 314 1985 620 622
    • (1985) Nature , vol.314 , pp. 620-622
    • Schwartzman, M.1    Ferreri, N.R.2    Carroll, M.A.3    Songu-Mize, E.4    McGiff, J.C.5
  • 171
    • 0029976078 scopus 로고    scopus 로고
    • Role of 20-HETE in elevating loop chloride reabsorption in Dahl SS/Jr rats
    • A.P. Zou, H.A. Drummond, and R.J. Roman Role of 20-HETE in elevating loop chloride reabsorption in Dahl SS/Jr rats Hypertension 27 1996 631 635
    • (1996) Hypertension , vol.27 , pp. 631-635
    • Zou, A.P.1    Drummond, H.A.2    Roman, R.J.3
  • 172
    • 0028807418 scopus 로고
    • Effect of arachidonic acid on activity of the apical K+ channel in the thick ascending limb of the rat kidney
    • W. Wang, and M. Lu Effect of arachidonic acid on activity of the apical K+ channel in the thick ascending limb of the rat kidney J. Gen. Physiol. 106 1995 727 743
    • (1995) J. Gen. Physiol. , vol.106 , pp. 727-743
    • Wang, W.1    Lu, M.2
  • 174
    • 0029177711 scopus 로고
    • 20-Hydroxyeicosatetraenoic acid is formed in response to EGF and is a mitogen in rat proximal tubule
    • F. Lin, A. Rios, J.R. Falck, Y. Belosludtsev, and M.L. Schwartzman 20-Hydroxyeicosatetraenoic acid is formed in response to EGF and is a mitogen in rat proximal tubule Am. J. Physiol. 269 1995 F806 F816
    • (1995) Am. J. Physiol. , vol.269
    • Lin, F.1    Rios, A.2    Falck, J.R.3    Belosludtsev, Y.4    Schwartzman, M.L.5
  • 175
    • 0036080081 scopus 로고    scopus 로고
    • P-450 metabolites of arachidonic acid in the control of cardiovascular function
    • R.J. Roman P-450 metabolites of arachidonic acid in the control of cardiovascular function Physiol. Rev. 82 2002 131 185
    • (2002) Physiol. Rev. , vol.82 , pp. 131-185
    • Roman, R.J.1
  • 178
    • 0024412950 scopus 로고
    • Sensitivity of human tissue heme oxygenase to a new synthetic metalloporphyrin
    • R.J. Chernick, P. Martasek, R.D. Levere, R. Margreiter, and N.G. Abraham Sensitivity of human tissue heme oxygenase to a new synthetic metalloporphyrin Hepatology 10 1989 365 369
    • (1989) Hepatology , vol.10 , pp. 365-369
    • Chernick, R.J.1    Martasek, P.2    Levere, R.D.3    Margreiter, R.4    Abraham, N.G.5
  • 179
    • 0842333051 scopus 로고    scopus 로고
    • Nitric oxide synthesis inhibition promotes renal production of carbon monoxide
    • F. Rodriguez, B.D. Lamon, W. Gong, R. Kemp, and A. Nasjletti Nitric oxide synthesis inhibition promotes renal production of carbon monoxide Hypertension 43 2004 347 351
    • (2004) Hypertension , vol.43 , pp. 347-351
    • Rodriguez, F.1    Lamon, B.D.2    Gong, W.3    Kemp, R.4    Nasjletti, A.5
  • 182
    • 0141543088 scopus 로고    scopus 로고
    • Regulation of cyclooxygenase- and cytochrome P450-derived eicosanoids by heme oxygenase isoforms in rat kidney (abstract)
    • F.T. Botros, M.L. Schwartzman, and N.G. Abraham Regulation of cyclooxygenase- and cytochrome P450-derived eicosanoids by heme oxygenase isoforms in rat kidney (abstract) Hypertension 38 3 2001
    • (2001) Hypertension , vol.38 , Issue.3
    • Botros, F.T.1    Schwartzman, M.L.2    Abraham, N.G.3
  • 183
    • 0142165026 scopus 로고    scopus 로고
    • Heme oxygenase attenuated angiotensin II-mediated increase in cyclooxygenase activity and decreased isoprostane F2alpha in endothelial cells
    • N.G. Abraham Heme oxygenase attenuated angiotensin II-mediated increase in cyclooxygenase activity and decreased isoprostane F2alpha in endothelial cells Thromb. Res. 110 2003 305 309
    • (2003) Thromb. Res. , vol.110 , pp. 305-309
    • Abraham, N.G.1
  • 185
    • 0141792612 scopus 로고    scopus 로고
    • Functional expression of human heme oxygenase-1 gene in renal structure of spontaneously hypertensive rats
    • A.I. Goodman, S. Quan, L. Yang, A. Synghal, and N.G. Abraham Functional expression of human heme oxygenase-1 gene in renal structure of spontaneously hypertensive rats Exp. Biol. Med. (Maywood) 228 2003 454 458
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , pp. 454-458
    • Goodman, A.I.1    Quan, S.2    Yang, L.3    Synghal, A.4    Abraham, N.G.5
  • 186
    • 0018033563 scopus 로고
    • Immunohistochemical localization of the prostaglandin-forming cyclooxygenase in renal cortex
    • W.L. Smith, and T.G. Bell Immunohistochemical localization of the prostaglandin-forming cyclooxygenase in renal cortex Am. J. Physiol. 235 1978 F451 F457
    • (1978) Am. J. Physiol. , vol.235
    • Smith, W.L.1    Bell, T.G.2
  • 187
    • 0028034970 scopus 로고
    • Cyclooxygenase-2 is associated with the macula densa of rat kidney and increases with salt restriction
    • R.C. Harris, J.A. McKanna, Y. Akai, H.R. Jacobson, R.N. DuBois, and M.D. Breyer Cyclooxygenase-2 is associated with the macula densa of rat kidney and increases with salt restriction J. Clin. Invest. 94 1994 2504 2510
    • (1994) J. Clin. Invest. , vol.94 , pp. 2504-2510
    • Harris, R.C.1    McKanna, J.A.2    Akai, Y.3    Jacobson, H.R.4    Dubois, R.N.5    Breyer, M.D.6
  • 188
    • 0030860640 scopus 로고    scopus 로고
    • Renal identification of cyclooxygenase-2 in a subset of thick ascending limb cells
    • C.P. Vio, C. Cespedes, P. Gallardo, and J.L. Masferrer Renal identification of cyclooxygenase-2 in a subset of thick ascending limb cells Hypertension 30 1997 687 692
    • (1997) Hypertension , vol.30 , pp. 687-692
    • Vio, C.P.1    Cespedes, C.2    Gallardo, P.3    Masferrer, J.L.4
  • 189
    • 0032739363 scopus 로고    scopus 로고
    • Inhibition of macula densa-stimulated renin secretion by pharmacological blockade of cyclooxygenase-2
    • T.R. Traynor, A. Smart, J.P. Briggs, and J. Schnermann Inhibition of macula densa-stimulated renin secretion by pharmacological blockade of cyclooxygenase-2 Am. J. Physiol. 277 1999 F706 F710
    • (1999) Am. J. Physiol. , vol.277
    • Traynor, T.R.1    Smart, A.2    Briggs, J.P.3    Schnermann, J.4
  • 190
    • 0021913684 scopus 로고
    • Prostaglandins in the sodium excretory response to altered renal arterial pressure in dogs
    • P.K. Carmines, P.D. Bell, R.J. Roman, J. Work, and L.G. Navar Prostaglandins in the sodium excretory response to altered renal arterial pressure in dogs Am. J. Physiol. 248 1985 F8 F14
    • (1985) Am. J. Physiol. , vol.248
    • Carmines, P.K.1    Bell, P.D.2    Roman, R.J.3    Work, J.4    Navar, L.G.5
  • 194
    • 0029119740 scopus 로고
    • Cell cycle control in mammalian cells: Role of cyclins, cyclin dependent kinases (CDKs), growth suppressor genes and cyclin-dependent kinase inhibitors (CKIs)
    • X. Grana, and E.P. Reddy Cell cycle control in mammalian cells: role of cyclins, cyclin dependent kinases (CDKs), growth suppressor genes and cyclin-dependent kinase inhibitors (CKIs) Oncogene 11 1995 211 219
    • (1995) Oncogene , vol.11 , pp. 211-219
    • Grana, X.1    Reddy, E.P.2
  • 195
    • 0028072520 scopus 로고
    • Joining the complex: Cyclin-dependent kinase inhibitory proteins and the cell cycle
    • M. Peter, and I. Herskowitz Joining the complex: cyclin-dependent kinase inhibitory proteins and the cell cycle Cell 79 1994 181 184
    • (1994) Cell , vol.79 , pp. 181-184
    • Peter, M.1    Herskowitz, I.2
  • 196
    • 0028179669 scopus 로고
    • P27Kip1, a cyclin-Cdk inhibitor, links transforming growth factor-beta and contact inhibition to cell cycle arrest
    • K. Polyak, J.Y. Kato, M.J. Solomon, C.J. Sherr, J. Massague, J.M. Roberts, and A. Koff p27Kip1, a cyclin-Cdk inhibitor, links transforming growth factor-beta and contact inhibition to cell cycle arrest Genes Dev. 8 1994 9 22
    • (1994) Genes Dev. , vol.8 , pp. 9-22
    • Polyak, K.1    Kato, J.Y.2    Solomon, M.J.3    Sherr, C.J.4    Massague, J.5    Roberts, J.M.6    Koff, A.7
  • 197
    • 0031596225 scopus 로고    scopus 로고
    • G1 arrest of U937 cells by onconase is associated with suppression of cyclin D3 expression, induction of p16INK4A, p21WAF1/CIP1 and p27KIP and decreased pRb phosphorylation
    • G. Juan, B. Ardelt, X. Li, S.M. Mikulski, K. Shogen, W. Ardelt, A. Mittelman, and Z. Darzynkiewicz G1 arrest of U937 cells by onconase is associated with suppression of cyclin D3 expression, induction of p16INK4A, p21WAF1/CIP1 and p27KIP and decreased pRb phosphorylation Leukemia 12 1998 1241 1248
    • (1998) Leukemia , vol.12 , pp. 1241-1248
    • Juan, G.1    Ardelt, B.2    Li, X.3    Mikulski, S.M.4    Shogen, K.5    Ardelt, W.6    Mittelman, A.7    Darzynkiewicz, Z.8
  • 199
    • 0026474521 scopus 로고
    • An oxidative mechanism is involved in high glucose-induced serum protein modification causing inhibition of endothelial cell proliferation
    • J. Nakao-Hayashi, H. Ito, and S. Kawashima An oxidative mechanism is involved in high glucose-induced serum protein modification causing inhibition of endothelial cell proliferation Atherosclerosis 97 1992 89 95
    • (1992) Atherosclerosis , vol.97 , pp. 89-95
    • Nakao-Hayashi, J.1    Ito, H.2    Kawashima, S.3
  • 201
    • 0037428458 scopus 로고    scopus 로고
    • Carbon monoxide inhibition of apoptosis during ischemia-reperfusion lung injury is dependent on the p38 mitogen-activated protein kinase pathway and involves caspase 3
    • X. Zhang, P. Shan, L.E. Otterbein, J. Alam, R.A. Flavell, R.J. Davis, A.M. Choi, and P.J. Lee Carbon monoxide inhibition of apoptosis during ischemia-reperfusion lung injury is dependent on the p38 mitogen-activated protein kinase pathway and involves caspase 3 J. Biol. Chem. 278 2003 1248 1258
    • (2003) J. Biol. Chem. , vol.278 , pp. 1248-1258
    • Zhang, X.1    Shan, P.2    Otterbein, L.E.3    Alam, J.4    Flavell, R.A.5    Davis, R.J.6    Choi, A.M.7    Lee, P.J.8
  • 204
    • 0034677947 scopus 로고    scopus 로고
    • NAD(P)H oxidase: Role in cardiovascular biology and disease
    • K.K. Griendling, D. Sorescu, and M. Ushio-Fukai NAD(P)H oxidase: role in cardiovascular biology and disease Circ. Res. 86 2000 494 501
    • (2000) Circ. Res. , vol.86 , pp. 494-501
    • Griendling, K.K.1    Sorescu, D.2    Ushio-Fukai, M.3
  • 205
    • 0029942652 scopus 로고    scopus 로고
    • Superoxide anion and endothelial regulation of arterial tone
    • Z.S. Katusic Superoxide anion and endothelial regulation of arterial tone Free Radic. Biol. Med. 20 1996 443 448
    • (1996) Free Radic. Biol. Med. , vol.20 , pp. 443-448
    • Katusic, Z.S.1
  • 206
    • 0042867404 scopus 로고    scopus 로고
    • Effects of antioxidants in diabetes-induced oxidative stress in the glomeruli of diabetic rats
    • D. Koya, K. Hayashi, M. Kitada, A. Kashiwagi, R. Kikkawa, and M. Haneda Effects of antioxidants in diabetes-induced oxidative stress in the glomeruli of diabetic rats J. Am. Soc. Nephrol. 14 2003 S250 S253
    • (2003) J. Am. Soc. Nephrol. , vol.14
    • Koya, D.1    Hayashi, K.2    Kitada, M.3    Kashiwagi, A.4    Kikkawa, R.5    Haneda, M.6
  • 210
    • 0031443801 scopus 로고    scopus 로고
    • The nitric oxide donor SIN-1 protects endothelial cells from tumor necrosis factor-alpha-mediated cytotoxicity: Possible role for cyclic GMP and heme oxygenase
    • T. Polte, S. Oberle, and H. Schroder The nitric oxide donor SIN-1 protects endothelial cells from tumor necrosis factor-alpha-mediated cytotoxicity: possible role for cyclic GMP and heme oxygenase J. Mol. Cell. Cardiol. 29 1997 3305 3310
    • (1997) J. Mol. Cell. Cardiol. , vol.29 , pp. 3305-3310
    • Polte, T.1    Oberle, S.2    Schroder, H.3
  • 212
    • 4444369432 scopus 로고    scopus 로고
    • Simvastatin induces heme oxygenase-1: A novel mechanism of vessel protection
    • T.S. Lee, C.C. Chang, Y. Zhu, and J.Y. Shyy Simvastatin induces heme oxygenase-1: a novel mechanism of vessel protection Circulation 110 2004 1296 1302
    • (2004) Circulation , vol.110 , pp. 1296-1302
    • Lee, T.S.1    Chang, C.C.2    Zhu, Y.3    Shyy, J.Y.4
  • 215
    • 1642460715 scopus 로고    scopus 로고
    • Smart gene therapy for the heart
    • D.E. Stec Smart gene therapy for the heart Hypertension 43 2004 720 721
    • (2004) Hypertension , vol.43 , pp. 720-721
    • Stec, D.E.1
  • 217
    • 0037099359 scopus 로고    scopus 로고
    • Heme oxygenase-1 gene transfer inhibits inducible nitric oxide synthase expression and protects genetically fat Zucker rat livers from ischemia- reperfusion injury
    • A.J. Coito, R. Buelow, X.D. Shen, F. Amersi, C. Moore, H.D. Volk, R.W. Busuttil, and J.W. Kupiec-Weglinski Heme oxygenase-1 gene transfer inhibits inducible nitric oxide synthase expression and protects genetically fat Zucker rat livers from ischemia- reperfusion injury Transplantation 74 2002 96 102
    • (2002) Transplantation , vol.74 , pp. 96-102
    • Coito, A.J.1    Buelow, R.2    Shen, X.D.3    Amersi, F.4    Moore, C.5    Volk, H.D.6    Busuttil, R.W.7    Kupiec-Weglinski, J.W.8
  • 218
  • 220
    • 1642501642 scopus 로고    scopus 로고
    • Protection from ischemic heart injury by a vigilant heme oxygenase-1 plasmid system
    • Y.L. Tang, Y. Tang, Y.C. Zhang, K. Qian, L. Shen, and M.I. Phillips Protection from ischemic heart injury by a vigilant heme oxygenase-1 plasmid system Hypertension 43 2004 746 751
    • (2004) Hypertension , vol.43 , pp. 746-751
    • Tang, Y.L.1    Tang, Y.2    Zhang, Y.C.3    Qian, K.4    Shen, L.5    Phillips, M.I.6
  • 221
    • 0028946357 scopus 로고
    • Targeted vectors for gene therapy
    • N. Miller, and R. Vile Targeted vectors for gene therapy FASEB 9 1995 190 199
    • (1995) FASEB , vol.9 , pp. 190-199
    • Miller, N.1    Vile, R.2
  • 222
    • 0030883521 scopus 로고    scopus 로고
    • Transcriptional targeting of replication-defective adenovirus transgene expression to smooth muscle cells in vivo
    • S. Kim, H. Lin, E. Barr, L. Chu, J.M. Leiden, and M.S. Parmacek Transcriptional targeting of replication-defective adenovirus transgene expression to smooth muscle cells in vivo J. Clin. Invest. 100 1997 1006 1014
    • (1997) J. Clin. Invest. , vol.100 , pp. 1006-1014
    • Kim, S.1    Lin, H.2    Barr, E.3    Chu, L.4    Leiden, J.M.5    Parmacek, M.S.6
  • 223
    • 0030985971 scopus 로고    scopus 로고
    • A 346-base pair region of the mouse γ-glutamyl transpeptidase type II promoter contains sufficient cis-acting elements for kidney-restricted expression in transgenic mice
    • A.R. Sepulveda, S.L. Huang, R.M. Lebovitz, and M.W. Lieberman A 346-base pair region of the mouse γ-glutamyl transpeptidase type II promoter contains sufficient cis-acting elements for kidney-restricted expression in transgenic mice J. Biol. Chem. 272 1997 11959 11967
    • (1997) J. Biol. Chem. , vol.272 , pp. 11959-11967
    • Sepulveda, A.R.1    Huang, S.L.2    Lebovitz, R.M.3    Lieberman, M.W.4
  • 224
    • 0030736087 scopus 로고    scopus 로고
    • The kidney androgen-regulated protein promoter confers renal proximal tubule cell-specific and highly androgen-responsive expression on the human angiotensinogen gene in transgeneic mice
    • Y. Ding, R.L. Davisson, D.O. Hardy, L.-J. Zhu, D.C. Merrill, J.F. Catterall, and C.D. Sigmund The kidney androgen-regulated protein promoter confers renal proximal tubule cell-specific and highly androgen-responsive expression on the human angiotensinogen gene in transgeneic mice J. Biol. Chem. 272 1997 28142 28148
    • (1997) J. Biol. Chem. , vol.272 , pp. 28142-28148
    • Ding, Y.1    Davisson, R.L.2    Hardy, D.O.3    Zhu, L.-J.4    Merrill, D.C.5    Catterall, J.F.6    Sigmund, C.D.7
  • 226
    • 0029919180 scopus 로고    scopus 로고
    • Cloning and kidney cell-specific activity of the promoter of the murine renal Na-K-Cl cotransporter gene
    • P. Igarashi, D.A. Whyte, K. Li, and G.T. Nagami Cloning and kidney cell-specific activity of the promoter of the murine renal Na-K-Cl cotransporter gene J. Biol. Chem. 271 1997 9666 9674
    • (1997) J. Biol. Chem. , vol.271 , pp. 9666-9674
    • Igarashi, P.1    Whyte, D.A.2    Li, K.3    Nagami, G.T.4
  • 227
    • 3142581994 scopus 로고    scopus 로고
    • Induction of heme oxygenase-1 inhibits NAD(P)H oxidase activity by down-regulating cytochrome b558 expression via the reduction of heme availability
    • C. Taille, J. El Benna, S. Lanone, M.C. Dang, E. Ogier-Denis, M. Aubier, and J. Boczkowski Induction of heme oxygenase-1 inhibits NAD(P)H oxidase activity by down-regulating cytochrome b558 expression via the reduction of heme availability J. Biol. Chem. 279 2004 28681 28688
    • (2004) J. Biol. Chem. , vol.279 , pp. 28681-28688
    • Taille, C.1    El Benna, J.2    Lanone, S.3    Dang, M.C.4    Ogier-Denis, E.5    Aubier, M.6    Boczkowski, J.7


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