Heme oxygenase expression in selected regions of term human placenta

BE McLaughlin, GE Lash, GN Smith… - Experimental …, 2003 - journals.sagepub.com
BE McLaughlin, GE Lash, GN Smith, GS Marks, K Nakatsu, CH Graham, JF Brien
Experimental Biology and Medicine, 2003journals.sagepub.com
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 …
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.
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