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Articles in PresS, published online ahead of print February 21, 2002
Am J Physiol Heart Circ Physiol, 10.1152/ajpheart.01084.2001
Submitted on December 10, 2001
Accepted on February 18, 2002
1 Pharmacology & Toxicology, Queen's University, Kingston, Ontario, Canada
2 Pharmacology & Toxicology, Queen's University, Kingston, Ontario, Canada; Gynaecology & Obstetrics, Queen's University, Kingston, Ontario, Canada; Anatomy & Cell Biology, Queen's University, Kingston, Ontario, Canada
3 Anatomy & Cell Biology, Queen's University, Kingston, Ontario, Canada; Pharmacology & Toxicology, Queen's University, Kingston, Ontario, Canada
* To whom correspondence should be addressed. E-mail: 3sa31{at}qlink.queensu.ca.
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 since the catalytic activity of HO requires three molecules of oxygen for each molecule of CO formed from heme and HO activity may be limited by oxygen (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 placentae was determined following 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 non-infarcted areas of pre-eclamptic and normotensive placenta.
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