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

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

Gas-chromatographic assay for heme oxygenase activity.

1982 ◽  
Vol 28 (10) ◽  
pp. 2026-2032 ◽  
Author(s):  
F W Sunderman ◽  
J R Downs ◽  
M C Reid ◽  
L M Bibeau
Keyword(s):  
Gas Chromatography ◽  
Detection Limit ◽  
Heme Oxygenase ◽  
Liver Microsomes ◽  
Microsomal Protein ◽  
Spectrophotometric Assay ◽  
Rat Tissues ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity ◽  
Kidney Microsomes

Abstract We have developed an improved assay for microsomal heme oxygenase activity, based on the enzymic release of CO from the alpha-methene bridge of hemin and the quantitation of CO by gas chromatography. The within-run coefficient of variation (CV) of heme oxygenase assays in microsomes from rat tissues (liver, kidney) averaged 8%; the between-run CV averaged 15%. The detection limit for heme oxygenase activity was approximately 1 nmol/h per milligram of microsomal protein. Gas-chromatographic assays of heme oxygenase activities in rat tissues correlated well (r = 0.94) with results by a spectrophotometric assay based on bilirubin production. In untreated rats, heme oxygenase activity averaged 7 +/- 3 nmol/h per milligram of protein (n = 36) in kidney microsomes and 14 +/- 5 nmol/h per milligram of protein (n = 17) in liver microsomes. Heme oxygenase activity was increased 10-fold in kidney microsomes and threefold in liver microsomes from rats killed 17 h after subcutaneous injection of NiCl2 (0.5 mmol/kg body wt). These findings illustrate the efficacy of the gas-chromatographic assay for measuring xenobiotic effects on heme oxygenase activity.

scholarly journals Heme oxygenase activity increases after exercise in healthy volunteers

2018 ◽  
Vol 52 (2) ◽  
pp. 267-272 ◽  
Author(s):  
Andrew J. Ghio ◽  
Martin W. Case ◽  
Joleen M. Soukup
Keyword(s):  
Healthy Volunteers ◽  
Heme Oxygenase ◽  
Heme Oxygenase Activity ◽  
Oxygenase Activity

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.

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