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Induction of Heme Oxygenase-1 In Vivo Suppresses NADPH Oxidase Derived Oxidative Stress

Induction of Heme Oxygenase-1 In Vivo Suppresses NADPH Oxidase–Derived Oxidative Stress Srinivasa R. Datla ; Gregory J. Dusting ; Trevor A. Mori ; Caroline J. Taylor ; Kevin D. Croft ; Fan Jiang From the Bernard O’Brien Institute of Microsurgery (S.R.D., G.J.D., C.J.T., F.J.), University of Melbourn... Full description

Journal Title: Hypertension 2007-10-01, Vol.50 (4), p.636-642
Main Author: Datla, Srinivasa R
Other Authors: Dusting, Gregory J , Mori, Trevor A , Taylor, Caroline J , Croft, Kevin D , Jiang, Fan
Format: Electronic Article Electronic Article
Language: English
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Publisher: Philadelphia, PA: Am Heart Assoc
ID: ISSN: 0194-911X
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title: Induction of Heme Oxygenase-1 In Vivo Suppresses NADPH Oxidase Derived Oxidative Stress
format: Article
creator:
  • Datla, Srinivasa R
  • Dusting, Gregory J
  • Mori, Trevor A
  • Taylor, Caroline J
  • Croft, Kevin D
  • Jiang, Fan
subjects:
  • Angiotensin II - physiology
  • Animal infectious diseases
  • Animals
  • Apolipoproteins E - genetics
  • Apolipoproteins E - metabolism
  • Bilirubin - pharmacology
  • Biological and medical sciences
  • Blood vessels and receptors
  • Cell Line
  • Enzyme Induction
  • Enzyme Inhibitors - pharmacology
  • F2-Isoprostanes - blood
  • Fundamental and applied biological sciences. Psychology
  • General aspects
  • Heme Oxygenase-1 - antagonists & inhibitors
  • Heme Oxygenase-1 - drug effects
  • Heme Oxygenase-1 - metabolism
  • Hemin - pharmacology
  • HL-60 Cells
  • Humans
  • Infectious diseases
  • Male
  • Medical sciences
  • Metalloporphyrins - pharmacology
  • Mice
  • Mice, Mutant Strains
  • Muscle, Smooth, Vascular - cytology
  • Muscle, Smooth, Vascular - enzymology
  • NADPH Oxidases - antagonists & inhibitors
  • NADPH Oxidases - metabolism
  • Nitrates - metabolism
  • Nitrites - metabolism
  • Oxidative Stress - drug effects
  • Oxidative Stress - physiology
  • Phagocytes - cytology
  • Phagocytes - enzymology
  • Protoporphyrins - pharmacology
  • Rats
  • Superoxides - metabolism
  • Vertebrates: cardiovascular system
ispartof: Hypertension, 2007-10-01, Vol.50 (4), p.636-642
description: Induction of Heme Oxygenase-1 In Vivo Suppresses NADPH Oxidase–Derived Oxidative Stress Srinivasa R. Datla ; Gregory J. Dusting ; Trevor A. Mori ; Caroline J. Taylor ; Kevin D. Croft ; Fan Jiang From the Bernard O’Brien Institute of Microsurgery (S.R.D., G.J.D., C.J.T., F.J.), University of Melbourne, Victoria, Australia; and the School of Medicine and Pharmacology (T.A.M., K.D.C.), University of Western Australia, Western Australia, Australia. Correspondence to Fan Jiang, Bernard O’Brien Institute of Microsurgery, 42 Fitzroy St, Fitzroy, Victoria 3065, Australia. E-mail fjiang{at}unimelb.edu.au Our previous studies suggest that heme oxygenase (HO)-1 induction and/or subsequent bilirubin generation in endothelial cells may suppress superoxide generation of from reduced nicotinamide-adenine dinucleotide phosphate (NADPH) oxidase. In this study, we examined the consequence of HO-1 induction in vivo on NADPH oxidase activity. Three doses of hemin (25 mg · kg –1 , IP, every 48 hours), with or without cotreatment with the HO inhibitor tin protoporphyrin-IX (15 mg · kg –1 , IP), were given to apolipoprotein E–deficient mice, which display vascular oxidative stress. Hemin treatment increased HO-1 expression and activity in aorta (undetectable at baseline) and kidney (by 3-fold) and significantly reduced both NADPH oxidase activity (by 25% to 50%) and superoxide generation in situ. The increase in HO-1 activity and inhibition of NADPH oxidase activity by hemin were reversed by tin protoporphyrin-IX and were not associated with changes in Nox2 or Nox4 protein levels. Hemin also reduced plasma F 2 -isoprostane levels by 23%. The inhibition of NADPH oxidase activity by hemin in the aorta was mimicked by bilirubin in vitro (0.01 to 1 µmol/L). Bilirubin also concentration-dependently reduced NADPH oxidase–dependent superoxide production stimulated by angiotensin II in rat vascular smooth muscle cells and by phorbol 12-myristate 13-acetate in human neutrophil-like HL-60 cells. HO-1 overexpression by plasmid-mediated gene transfer in rat vascular smooth muscle cells decreased NADPH-stimulated superoxide production. Thus, systemic expression of HO-1 suppresses NADPH oxidase activity by mechanisms at least partly mediated by the bile pigment bilirubin, thereby reducing oxidative stress. Key Words: bilirubin • heme oxygenase-1 • NADPH oxidase • oxidative stress • reactive oxygen species
language: eng
source:
identifier: ISSN: 0194-911X
fulltext: no_fulltext
issn:
  • 0194-911X
  • 1524-4563
url: Link


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titleInduction of Heme Oxygenase-1 In Vivo Suppresses NADPH Oxidase Derived Oxidative Stress
creatorDatla, Srinivasa R ; Dusting, Gregory J ; Mori, Trevor A ; Taylor, Caroline J ; Croft, Kevin D ; Jiang, Fan
creatorcontribDatla, Srinivasa R ; Dusting, Gregory J ; Mori, Trevor A ; Taylor, Caroline J ; Croft, Kevin D ; Jiang, Fan
descriptionInduction of Heme Oxygenase-1 In Vivo Suppresses NADPH Oxidase–Derived Oxidative Stress Srinivasa R. Datla ; Gregory J. Dusting ; Trevor A. Mori ; Caroline J. Taylor ; Kevin D. Croft ; Fan Jiang From the Bernard O’Brien Institute of Microsurgery (S.R.D., G.J.D., C.J.T., F.J.), University of Melbourne, Victoria, Australia; and the School of Medicine and Pharmacology (T.A.M., K.D.C.), University of Western Australia, Western Australia, Australia. Correspondence to Fan Jiang, Bernard O’Brien Institute of Microsurgery, 42 Fitzroy St, Fitzroy, Victoria 3065, Australia. E-mail fjiang{at}unimelb.edu.au Our previous studies suggest that heme oxygenase (HO)-1 induction and/or subsequent bilirubin generation in endothelial cells may suppress superoxide generation of from reduced nicotinamide-adenine dinucleotide phosphate (NADPH) oxidase. In this study, we examined the consequence of HO-1 induction in vivo on NADPH oxidase activity. Three doses of hemin (25 mg · kg –1 , IP, every 48 hours), with or without cotreatment with the HO inhibitor tin protoporphyrin-IX (15 mg · kg –1 , IP), were given to apolipoprotein E–deficient mice, which display vascular oxidative stress. Hemin treatment increased HO-1 expression and activity in aorta (undetectable at baseline) and kidney (by 3-fold) and significantly reduced both NADPH oxidase activity (by 25% to 50%) and superoxide generation in situ. The increase in HO-1 activity and inhibition of NADPH oxidase activity by hemin were reversed by tin protoporphyrin-IX and were not associated with changes in Nox2 or Nox4 protein levels. Hemin also reduced plasma F 2 -isoprostane levels by 23%. The inhibition of NADPH oxidase activity by hemin in the aorta was mimicked by bilirubin in vitro (0.01 to 1 µmol/L). Bilirubin also concentration-dependently reduced NADPH oxidase–dependent superoxide production stimulated by angiotensin II in rat vascular smooth muscle cells and by phorbol 12-myristate 13-acetate in human neutrophil-like HL-60 cells. HO-1 overexpression by plasmid-mediated gene transfer in rat vascular smooth muscle cells decreased NADPH-stimulated superoxide production. Thus, systemic expression of HO-1 suppresses NADPH oxidase activity by mechanisms at least partly mediated by the bile pigment bilirubin, thereby reducing oxidative stress. Key Words: bilirubin • heme oxygenase-1 • NADPH oxidase • oxidative stress • reactive oxygen species
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0ISSN: 0194-911X
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languageeng
publisherPhiladelphia, PA: Am Heart Assoc
subjectAngiotensin II - physiology ; Animal infectious diseases ; Animals ; Apolipoproteins E - genetics ; Apolipoproteins E - metabolism ; Bilirubin - pharmacology ; Biological and medical sciences ; Blood vessels and receptors ; Cell Line ; Enzyme Induction ; Enzyme Inhibitors - pharmacology ; F2-Isoprostanes - blood ; Fundamental and applied biological sciences. Psychology ; General aspects ; Heme Oxygenase-1 - antagonists & inhibitors ; Heme Oxygenase-1 - drug effects ; Heme Oxygenase-1 - metabolism ; Hemin - pharmacology ; HL-60 Cells ; Humans ; Infectious diseases ; Male ; Medical sciences ; Metalloporphyrins - pharmacology ; Mice ; Mice, Mutant Strains ; Muscle, Smooth, Vascular - cytology ; Muscle, Smooth, Vascular - enzymology ; NADPH Oxidases - antagonists & inhibitors ; NADPH Oxidases - metabolism ; Nitrates - metabolism ; Nitrites - metabolism ; Oxidative Stress - drug effects ; Oxidative Stress - physiology ; Phagocytes - cytology ; Phagocytes - enzymology ; Protoporphyrins - pharmacology ; Rats ; Superoxides - metabolism ; Vertebrates: cardiovascular system
ispartofHypertension, 2007-10-01, Vol.50 (4), p.636-642
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2Mori, Trevor A
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0Induction of Heme Oxygenase-1 In Vivo Suppresses NADPH Oxidase Derived Oxidative Stress
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descriptionInduction of Heme Oxygenase-1 In Vivo Suppresses NADPH Oxidase–Derived Oxidative Stress Srinivasa R. Datla ; Gregory J. Dusting ; Trevor A. Mori ; Caroline J. Taylor ; Kevin D. Croft ; Fan Jiang From the Bernard O’Brien Institute of Microsurgery (S.R.D., G.J.D., C.J.T., F.J.), University of Melbourne, Victoria, Australia; and the School of Medicine and Pharmacology (T.A.M., K.D.C.), University of Western Australia, Western Australia, Australia. Correspondence to Fan Jiang, Bernard O’Brien Institute of Microsurgery, 42 Fitzroy St, Fitzroy, Victoria 3065, Australia. E-mail fjiang{at}unimelb.edu.au Our previous studies suggest that heme oxygenase (HO)-1 induction and/or subsequent bilirubin generation in endothelial cells may suppress superoxide generation of from reduced nicotinamide-adenine dinucleotide phosphate (NADPH) oxidase. In this study, we examined the consequence of HO-1 induction in vivo on NADPH oxidase activity. Three doses of hemin (25 mg · kg –1 , IP, every 48 hours), with or without cotreatment with the HO inhibitor tin protoporphyrin-IX (15 mg · kg –1 , IP), were given to apolipoprotein E–deficient mice, which display vascular oxidative stress. Hemin treatment increased HO-1 expression and activity in aorta (undetectable at baseline) and kidney (by 3-fold) and significantly reduced both NADPH oxidase activity (by 25% to 50%) and superoxide generation in situ. The increase in HO-1 activity and inhibition of NADPH oxidase activity by hemin were reversed by tin protoporphyrin-IX and were not associated with changes in Nox2 or Nox4 protein levels. Hemin also reduced plasma F 2 -isoprostane levels by 23%. The inhibition of NADPH oxidase activity by hemin in the aorta was mimicked by bilirubin in vitro (0.01 to 1 µmol/L). Bilirubin also concentration-dependently reduced NADPH oxidase–dependent superoxide production stimulated by angiotensin II in rat vascular smooth muscle cells and by phorbol 12-myristate 13-acetate in human neutrophil-like HL-60 cells. HO-1 overexpression by plasmid-mediated gene transfer in rat vascular smooth muscle cells decreased NADPH-stimulated superoxide production. Thus, systemic expression of HO-1 suppresses NADPH oxidase activity by mechanisms at least partly mediated by the bile pigment bilirubin, thereby reducing oxidative stress. Key Words: bilirubin • heme oxygenase-1 • NADPH oxidase • oxidative stress • reactive oxygen species
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0Angiotensin II - physiology
1Animal infectious diseases
2Animals
3Apolipoproteins E - genetics
4Apolipoproteins E - metabolism
5Bilirubin - pharmacology
6Biological and medical sciences
7Blood vessels and receptors
8Cell Line
9Enzyme Induction
10Enzyme Inhibitors - pharmacology
11F2-Isoprostanes - blood
12Fundamental and applied biological sciences. Psychology
13General aspects
14Heme Oxygenase-1 - antagonists & inhibitors
15Heme Oxygenase-1 - drug effects
16Heme Oxygenase-1 - metabolism
17Hemin - pharmacology
18HL-60 Cells
19Humans
20Infectious diseases
21Male
22Medical sciences
23Metalloporphyrins - pharmacology
24Mice
25Mice, Mutant Strains
26Muscle, Smooth, Vascular - cytology
27Muscle, Smooth, Vascular - enzymology
28NADPH Oxidases - antagonists & inhibitors
29NADPH Oxidases - metabolism
30Nitrates - metabolism
31Nitrites - metabolism
32Oxidative Stress - drug effects
33Oxidative Stress - physiology
34Phagocytes - cytology
35Phagocytes - enzymology
36Protoporphyrins - pharmacology
37Rats
38Superoxides - metabolism
39Vertebrates: cardiovascular system
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titleInduction of Heme Oxygenase-1 In Vivo Suppresses NADPH Oxidase Derived Oxidative Stress
authorDatla, Srinivasa R ; Dusting, Gregory J ; Mori, Trevor A ; Taylor, Caroline J ; Croft, Kevin D ; Jiang, Fan
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0Angiotensin II - physiology
1Animal infectious diseases
2Animals
3Apolipoproteins E - genetics
4Apolipoproteins E - metabolism
5Bilirubin - pharmacology
6Biological and medical sciences
7Blood vessels and receptors
8Cell Line
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10Enzyme Inhibitors - pharmacology
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15Heme Oxygenase-1 - drug effects
16Heme Oxygenase-1 - metabolism
17Hemin - pharmacology
18HL-60 Cells
19Humans
20Infectious diseases
21Male
22Medical sciences
23Metalloporphyrins - pharmacology
24Mice
25Mice, Mutant Strains
26Muscle, Smooth, Vascular - cytology
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28NADPH Oxidases - antagonists & inhibitors
29NADPH Oxidases - metabolism
30Nitrates - metabolism
31Nitrites - metabolism
32Oxidative Stress - drug effects
33Oxidative Stress - physiology
34Phagocytes - cytology
35Phagocytes - enzymology
36Protoporphyrins - pharmacology
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38Superoxides - metabolism
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abstractInduction of Heme Oxygenase-1 In Vivo Suppresses NADPH Oxidase–Derived Oxidative Stress Srinivasa R. Datla ; Gregory J. Dusting ; Trevor A. Mori ; Caroline J. Taylor ; Kevin D. Croft ; Fan Jiang From the Bernard O’Brien Institute of Microsurgery (S.R.D., G.J.D., C.J.T., F.J.), University of Melbourne, Victoria, Australia; and the School of Medicine and Pharmacology (T.A.M., K.D.C.), University of Western Australia, Western Australia, Australia. Correspondence to Fan Jiang, Bernard O’Brien Institute of Microsurgery, 42 Fitzroy St, Fitzroy, Victoria 3065, Australia. E-mail fjiang{at}unimelb.edu.au Our previous studies suggest that heme oxygenase (HO)-1 induction and/or subsequent bilirubin generation in endothelial cells may suppress superoxide generation of from reduced nicotinamide-adenine dinucleotide phosphate (NADPH) oxidase. In this study, we examined the consequence of HO-1 induction in vivo on NADPH oxidase activity. Three doses of hemin (25 mg · kg –1 , IP, every 48 hours), with or without cotreatment with the HO inhibitor tin protoporphyrin-IX (15 mg · kg –1 , IP), were given to apolipoprotein E–deficient mice, which display vascular oxidative stress. Hemin treatment increased HO-1 expression and activity in aorta (undetectable at baseline) and kidney (by 3-fold) and significantly reduced both NADPH oxidase activity (by 25% to 50%) and superoxide generation in situ. The increase in HO-1 activity and inhibition of NADPH oxidase activity by hemin were reversed by tin protoporphyrin-IX and were not associated with changes in Nox2 or Nox4 protein levels. Hemin also reduced plasma F 2 -isoprostane levels by 23%. The inhibition of NADPH oxidase activity by hemin in the aorta was mimicked by bilirubin in vitro (0.01 to 1 µmol/L). Bilirubin also concentration-dependently reduced NADPH oxidase–dependent superoxide production stimulated by angiotensin II in rat vascular smooth muscle cells and by phorbol 12-myristate 13-acetate in human neutrophil-like HL-60 cells. HO-1 overexpression by plasmid-mediated gene transfer in rat vascular smooth muscle cells decreased NADPH-stimulated superoxide production. Thus, systemic expression of HO-1 suppresses NADPH oxidase activity by mechanisms at least partly mediated by the bile pigment bilirubin, thereby reducing oxidative stress. Key Words: bilirubin • heme oxygenase-1 • NADPH oxidase • oxidative stress • reactive oxygen species
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pmid17679649
doi10.1161/HYPERTENSIONAHA.107.092296
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