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Papers In Press, published online ahead of print September 8, 2005
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Department of Clinical Biochemistry, University of Copenhagen, Copenhagen 2100
Corresponding Author: larsbo{at}rh.dk
Placenta expresses various lipase activities. However, a detailed characterization of the involved genes and proteins is lacking. In this study we compared the expression of endothelial lipase (EL) and lipoprotein lipase (LPL) in human term placenta. When placental protein extracts were separated by heparin-sepharose affinity chromatography, the EL protein eluted as a single peak without detectable phospho- or triglyceride lipase activity. The major portion of LPL protein eluted slightly after EL. This peak also had no lipase activity and most likely contained monomeric LPL. Fractions eluting at a higher NaCl concentration contained small amounts of LPL protein (most likely dimeric LPL), and had substantial triglyceride lipase activity. In situ hybridization studies showed EL mRNA expression in syncytiotrophoblasts and endothelial cells and LPL mRNA in syncytiotrophoblasts. In contrast, immunohistochemistry showed EL and LPL protein associated with both cell types. In mouse placentas, lack of LPL expression resulted in increased EL mRNA expression. These results suggest that the cellular expression of EL and LPL in human placenta is different. Nevertheless, the two lipases might have overlapping functions in the mouse placenta. Our data also suggest that the major portions of both proteins are stored in an inactive form in human term placenta.
Revised on August 18, 2005
Accepted on August 18, 2005
Endothelial and lipoprotein lipases in human and mouse placenta
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