scholarly journals Comparative effects of curcuminoids on endothelial heme oxygenase-1 expression: ortho-methoxy groups are essential to enhance heme oxygenase activity and protection

2006 ◽  
Vol 38 (4) ◽  
pp. 393-400 ◽  
Author(s):  
Gil-Saeng Jeong ◽  
Gi-Su Oh ◽  
Hyun-Ock Pae ◽  
Sun-Oh Jeong ◽  
Youn-Chul Kim ◽  
...  
Keyword(s):  
Heme Oxygenase ◽  
Heme Oxygenase 1 ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity ◽  
Methoxy Groups

Role of heme oxygenase-1 in hypoxia-reoxygenation: requirement of substrate heme to promote cardioprotection

2001 ◽  
Vol 281 (5) ◽  
pp. H1976-H1984 ◽  
Author(s):  
Roberta Foresti ◽  
Helen Goatly ◽  
Colin J. Green ◽  
Roberto Motterlini
Keyword(s):  
Heme Oxygenase ◽  
Reactive Oxygen Species Generation ◽  
Free Radical Scavenger ◽  
Radical Scavenger ◽  
Heme Oxygenase 1 ◽  
Bile Pigment ◽  
Activity Levels ◽  
Low Oxygen ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity

Heme oxygenase-1 (HO-1) catalyzes the enzymatic degradation of heme to carbon monoxide, bilirubin, and iron. All three products possess biological functions; bilirubin, in particular, is a potent free radical scavenger of which its antioxidant property is enhanced at low oxygen tension. Here, we investigated the effect of severe hypoxia and reoxygenation on HO-1 expression in cardiomyocytes and determined whether HO-1 and its product, bilirubin, have a protective role against reoxygenation damage. Hypoxia caused a time-dependent increase in both HO-1 expression and heme oxygenase activity, which gradually declined during reoxygenation. Reoxygenation of hypoxic cardiomyocytes produced marked injury; however, incubation with hemin or bilirubin during hypoxia considerably reduced the damage at reoxygenation. The protective effect of hemin is attributable to increased availability of substrate for heme oxygenase activity, because hypoxic cardiomyocytes generated very little bilirubin when incubated with medium alone but produced substantial bile pigment in the presence of hemin. Interestingly, incubation with hemin also maintained high heme oxygenase activity levels during the reoxygenation period. Reactive oxygen species generation was enhanced after hypoxia, and hemin and bilirubin were capable once again to attenuate this effect. These results indicate that the HO-1-bilirubin pathway can effectively defend hypoxic cardiomyocytes against reoxygenation injury and highlight the issue of heme availability in the cytoprotective action afforded by HO-1.

Heme oxygenase-1 induction in skeletal muscle cells: hemin and sodium nitroprusside are regulators in vitro

1998 ◽  
Vol 275 (4) ◽  
pp. C1087-C1094 ◽  
Author(s):  
M. J. J. Vesely ◽  
D. J. Exon ◽  
J. E. Clark ◽  
R. Foresti ◽  
C. J. Green ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Sodium Nitroprusside ◽  
Heme Oxygenase ◽  
Muscle Tissue ◽  
Skeletal Muscle Tissue ◽  
Heme Oxygenase 1 ◽  
Skeletal Myoblast ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity ◽  
Myoblast Cells

The heat shock protein heme oxygenase-1 (HO-1) is regulated by a variety of physiological and pharmacological factors. In skeletal muscle tissue, HO-1 has been shown to be induced only by exercise and electrical stimulation in vivo. Both hemin and sodium nitroprusside (SNP) are potent inducers of HO-1 in other tissues. In this study, we examined the effects of these two agents on HO-1 induction in L6.G8 rat skeletal myoblast cells. Hemin and SNP increased cellular heme oxygenase activity in both a time- and concentration-dependent manner. Increases in the HO-1 mRNA level and protein expression accompanied changes in heme oxygenase activity. The ability of SNP to induce HO-1 in L6.G8 cells was reduced by coincubation with hydroxocobalamin, a known nitric oxide (NO) scavenger, suggesting that NO itself may be involved in HO-1 gene stimulation. These results indicate that HO-1 expression is sensitive to both hemin and SNP in skeletal myoblast cells and may indicate an important regulatory mechanism of heme catabolism in skeletal muscle tissue.

scholarly journals Heme oxygenase-1-derived bilirubin ameliorates postischemic myocardial dysfunction

2000 ◽  
Vol 278 (2) ◽  
pp. H643-H651 ◽  
Author(s):  
James E. Clark ◽  
Roberta Foresti ◽  
Padmini Sarathchandra ◽  
Harparkash Kaur ◽  
Colin J. Green ◽  
...  
Keyword(s):  
Infarct Size ◽  
Heme Oxygenase ◽  
Myocardial Function ◽  
Myocardial Dysfunction ◽  
Protoporphyrin Ix ◽  
Heme Oxygenase 1 ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity ◽  
Tin Protoporphyrin

Bilirubin is a potent antioxidant generated intracellularly during the degradation of heme by the enzyme heme oxygenase. The purpose of this study was to determine the role of increased cardiac bilirubin in protection against postischemic myocardial dysfunction. Rat hearts were isolated and perfused according to the Langendorff technique to evaluate the recovery of myocardial function after 30 min of global ischemia and 60 min of reperfusion. We found that upregulation of the inducible isoform of heme oxygenase (HO-1) by treatment of animals with hemin 24 h before ischemia ameliorated myocardial function and reduced infarct size (tetrazolium staining) on reperfusion of isolated hearts. Tin protoporphyrin IX, an inhibitor of heme oxygenase activity, completely abolished the improved postischemic myocardial performance observed after hemin-mediated HO-1 induction. Likewise, cardiac tissue injury was exacerbated by treatment with tin protoporphyrin IX. Increased cardiac HO-1 expression and heme oxygenase activity were associated with enhanced tissue bilirubin content and an increased rate of bilirubin release into the perfusion buffer. Furthermore, exogenously administered bilirubin at concentrations as low as 100 nanomolar significantly restored myocardial function and minimized both infarct size and mitochondrial damage on reperfusion. Our data provide strong evidence for a primary role of HO-1-derived bilirubin in cardioprotection against reperfusion injury.

scholarly journals Suppression of hyperbilirubinemia in the rat neonate by chromium-protoporphyrin. Interactions of metalloporphyrins with microsomal heme oxygenase of human spleen.

1982 ◽  
Vol 156 (6) ◽  
pp. 1878-1883 ◽  
Author(s):  
G S Drummond ◽  
A Kappas
Keyword(s):  
Single Dose ◽  
Heme Oxygenase ◽  
Competitive Inhibitor ◽  
Bile Pigment ◽  
Human Spleen ◽  
Oxidation Activity ◽  
Heme Oxygenase Activity ◽  
Heme Degradation ◽  
Oxygenase Activity ◽  
Liver And Kidney

The synthetic metalloporphyrin, Cr-protoporphyrin, as a potent competitive inhibitor of heme oxygenase activity in rat spleen, liver, and kidney. When administered to neonatal animals in a single dose immediately after birth, Cr-protoporphyrin suppresses postnatal hyperbilirubinemia and produces a marked and sustained lowering of heme oxidation activity in liver, spleen, and kidney. The metalloporphyrin also potently inhibited the rate of heme degradation to bile pigment in human spleen.

Heme oxygenase activity causes transient hypersensitivity to oxidative ultraviolet a radiation that depends on release of iron from heme

2000 ◽  
Vol 28 (8) ◽  
pp. 1191-1196 ◽  
Author(s):  
Egil Kvam ◽  
Vidya Hejmadi ◽  
Stefan Ryter ◽  
Charareh Pourzand ◽  
Rex M Tyrrell
Keyword(s):  
Heme Oxygenase ◽  
Ultraviolet A ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity

scholarly journals Heme oxygenase activity and hemoglobin neurotoxicity are attenuated by inhibitors of the MEK/ERK pathway

2009 ◽  
Vol 56 (5) ◽  
pp. 922-928 ◽  
Author(s):  
Jing Chen-Roetling ◽  
Zhi Li ◽  
Mai Chen ◽  
Olatilewa O. Awe ◽  
Raymond F. Regan
Keyword(s):  
Heme Oxygenase ◽  
Erk Pathway ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity

281 HEME OXYGENASE ACTIVITY IN THE MOUSE PLACENTA DURING FETAL DEVELOPMENT.:

2006 ◽  
Vol 54 (1) ◽  
pp. S128.3-S128
Author(s):  
H. Zhao ◽  
R. J. Wong ◽  
I. Morioka ◽  
F. A. Kalish ◽  
D. K. Stevenson
Keyword(s):  
Heme Oxygenase ◽  
Fetal Development ◽  
Heme Oxygenase Activity ◽  
Mouse Placenta ◽  
Oxygenase Activity
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