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Experimental Biology and Medicine 228:564-567 (2003)
© 2003 Society for Experimental Biology and Medicine


HEME OXYGENASE

Heme Oxygenase Expression in Selected Regions of Term Human Placenta

Brian E. McLaughlin*, Gendie E. Lash*,{dagger}, Graeme N. Smith*,{dagger},{ddagger}, Gerald S. Marks*, Kanji Nakatsu*, Charles H. Graham*,{dagger} and James F. Brien*,1

* Departments of Pharmacology and Toxicology,
{dagger} Anatomy and Cell Biology, and
{ddagger} Obstetrics and Gynaecology, Faculty of Health Sciences, Queen’s University, Kingston, Ontario, Canada K7L 3N6

Abstract

Carbon monoxide (CO), formed during heme oxygenase (HO)-catalyzed oxidation of heme, has been proposed to play a complementary role with nitric oxide in the regulation of placental hemodynamics. The objective of this study was to elucidate HO enzymatic activity and HO-1 (inducible) and HO-2 (constitutive) protein content in the microsomal subcellular fraction of homogenate of selected regions of placenta from normotensive and mild pre-eclamptic pregnancies. HO enzymatic activity was measured under optimized conditions by gas chromatography using CO formation as an index of activity, and HO-1 and HO-2 protein content were determined by Western immunoblot analysis. Microsomal HO activity in each of the four placental regions was not different between normotensive and mild pre-eclamptic pregnancies. Microsomal HO-2 protein content was not different between normotensive and mild pre-eclamptic pregnancies, whereas there was increased expression of microsomal HO-1 protein in chorionic villi and fetal membranes from pre-eclamptic pregnancy compared with normotensive pregnancy. Microsomal HO enzymatic activity correlated with HO-2, but not HO-1, protein content.

Key Words: heme oxygenase activity • carbon monoxide formation • heme oxygenase protein • term human placenta • pre-eclampsia




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