Modified endogenous carbon monoxide production through modulation of heme oxygenase activity alters some aspects of the cold restraint stress response in male albino rats

2012 ◽  
Vol 46 (04) ◽  
pp. 205-215 ◽  
Author(s):  
S. El-Sayed ◽  
M. Hassan ◽  
M. Ibrahim ◽  
E. Elbassuoni ◽  
N. Aziz
Keyword(s):  
Carbon Monoxide ◽  
Stress Response ◽  
Heme Oxygenase ◽  
Restraint Stress ◽  
Albino Rats ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity ◽  
Cold Restraint Stress ◽  
Cold Restraint

scholarly journals Heme Oxygenase Activity Correlates with Serum Indices of Iron Homeostasis in Healthy Nonsmokers

2016 ◽  
Vol 11 ◽  
pp. BMI.S36226 ◽  
Author(s):  
Andrew J. Ghio ◽  
Dina M. Schreinemachers
Keyword(s):  
Carbon Monoxide ◽  
Heme Oxygenase ◽  
Iron Homeostasis ◽  
Serum Levels ◽  
Iron Availability ◽  
Health And Nutrition ◽  
Iron Saturation ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity ◽  
Study Population

Heme oxygenase (HO) catalyzes the breakdown of heme to carbon monoxide, iron, and biliverdin. While the use of genetically altered animal models in investigation has established distinct associations between HO activity and systemic iron availability, studies have not yet confirmed such participation of HO in iron homeostasis of humans. Carbon monoxide produced through HO activity will bind to hemoglobin in circulating erythrocytes, and therefore, blood carboxyhemoglobin (COHb) can be used as an index of HO activity. Using the second National Health and Nutrition Examination Survey, we tested the postulate that HO activity correlates with serum indices of iron homeostasis in healthy nonsmokers. The investigation included 844 lifetime nonsmokers (586 females) 18 years of age and older in the study population. Significant correlations were demonstrated between COHb and several indices of iron homeostasis including serum levels of both ferritin and iron and percentage iron saturation of transferrin. There was no significant association between COHb and hemoglobin, the largest repository of heme in the human body, which functions as the substrate for HO. We conclude that HO activity contributes to human iron homeostasis with significant correlations between COHb and serum ferritin and iron levels and percentage iron saturation of transferrin.

scholarly journals Heme oxygenase activity in placenta: direct dependence on oxygen availability

2002 ◽  
Vol 282 (6) ◽  
pp. H2055-H2059 ◽  
Author(s):  
Scott D. Appleton ◽  
Gerald S. Marks ◽  
Kanji Nakatsu ◽  
James F. Brien ◽  
Graeme N. Smith ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Catalytic Activity ◽  
Protein Expression ◽  
Heme Oxygenase ◽  
Progressive Decrease ◽  
Vascular Control ◽  
Chorionic Villi ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity ◽  
Mrna And Protein Expression

Carbon monoxide (CO), which is formed endogenously from heme catalyzed by heme oxygenase (HO), is proposed to play a role in vascular control. The mRNA and protein expression of the inducible isoform of HO (HO-1) increases in response to hypoxia, and it has been assumed that HO activity also increases. This assumption requires evaluation because the catalytic activity of HO requires three molecules of O2 for each molecule of CO formed from heme, and HO activity may be limited by O2 availability. To test the hypothesis that low physiological O2 concentrations limit HO activity, heme-derived CO formation by microsomal fractions of homogenates of chorionic villi of human placentas was determined after exposure to 0, 1, 5, or 21% O2. Results revealed that HO activity was directly dependent on O2 concentration. Thus, although hypoxia may increase HO protein and mRNA expression, there is a progressive decrease in HO activity with decreasing O2concentration and the dependence of HO activity on O2concentration is similar in chorionic villi from noninfarcted areas of preeclamptic and normotensive placenta.

scholarly journals Carbon Monoxide Production and Upregulation of Heme Oxygenase Activity in Mice after Heme Administration

1999 ◽  
Vol 45 (4, Part 2 of 2) ◽  
pp. 231A-231A ◽  
Author(s):  
Hendrik J Vreman ◽  
Andrea R Zentner ◽  
Ronald J Wong ◽  
David K Stevenson
Keyword(s):  
Carbon Monoxide ◽  
Heme Oxygenase ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity

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.

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