J. Lipid Res.
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Originally published In Press as doi:10.1194/jlr.M500277-JLR200 on September 8, 2005

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Journal of Lipid Research, Vol. 46, 2339-2346, November 2005
Copyright © 2005 by American Society for Biochemistry and Molecular Biology

Endothelial and lipoprotein lipases in human and mouse placenta

Marie L. S. Lindegaard*, Gunilla Olivecrona{dagger}, Christina Christoffersen*, Dagmar Kratky§, Jens Hannibal**, Bodil L. Petersen{dagger}{dagger}, Rudolf Zechner§§, Peter Damm*** and Lars B. Nielsen1,*

* Departments of Clinical Biochemistry, Bispebjerg Hospital, University of Copenhagen, Copenhagen, Denmark
{dagger}{dagger} Pathology, Bispebjerg Hospital, University of Copenhagen, Copenhagen, Denmark
*** Obstetrics, Bispebjerg Hospital, University of Copenhagen, Copenhagen, Denmark
** Rigshospitalet, and Department of Clinical Biochemistry, Bispebjerg Hospital, University of Copenhagen, Copenhagen, Denmark
{dagger} Department of Medical Biosciences, Physiological Chemistry, Umeå University, Umeå, Sweden
§§ Institute of Molecular Biosciences, University of Graz, Graz, Austria
§ Institute of Molecular Biology and Biochemistry, Center of Molecular Medicine, Medical University Graz, Graz, Austria

Published, JLR Papers in Press, September 8, 2005. DOI 10.1194/jlr.M500277-JLR200

1 To whom correspondence should be addressed. e-mail: 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 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 phospholipid or triglyceride (TG) 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 TG 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.

Abbreviations: DIG, digoxigenin; EL, endothelial lipase; TG, triglyceride

Supplementary key words lipid transport • in situ hybridization • immunohistochemistry • lipase activity • lipoprotein lipase deficiency


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