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Am J Physiol Heart Circ Physiol 282: H2055-H2059, 2002. First published February 21, 2002; doi:10.1152/ajpheart.01084.2001
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Vol. 282, Issue 6, H2055-H2059, June 2002

Heme oxygenase activity in placenta: direct dependence on oxygen availability

Scott D. Appleton1, Gerald S. Marks1, Kanji Nakatsu1, James F. Brien1, Graeme N. Smith1,2,3, and Charles H. Graham1,2

1 Departments of Pharmacology and Toxicology, 2 Anatomy and Cell Biology, and 3 Obstetrics and Gynaecology, Queen's University, Kingston, Ontario, Canada K7L 3N6

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 O2 concentration and the dependence of HO activity on O2 concentration is similar in chorionic villi from noninfarcted areas of preeclamptic and normotensive placenta.

heme oxygenase-1 expression; carbon monoxide; hypoxia


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