title: Endothelial and lipoprotein lipases in human and mouse placenta.
abstract: 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.
authors.affiliation: Department of Clinical Biochemistry, Rigshospitalet, Bispebjerg Hospital, University of Copenhagen, Copenhagen, Denmark.
authors.forename: Marie L S
authors.initials: ML
authors.lastname: Lindegaard
authors.forename: Gunilla
authors.initials: G
authors.lastname: Olivecrona
authors.forename: Christina
authors.initials: C
authors.lastname: Christoffersen
authors.forename: Dagmar
authors.initials: D
authors.lastname: Kratky
authors.forename: Jens
authors.initials: J
authors.lastname: Hannibal
authors.forename: Bodil L
authors.initials: BL
authors.lastname: Petersen
authors.forename: Rudolf
authors.initials: R
authors.lastname: Zechner
authors.forename: Peter
authors.initials: P
authors.lastname: Damm
authors.forename: Lars B
authors.initials: LB
authors.lastname: Nielsen
mesh_terms: D000818:Animals; D001706:Biopsy; D015153:Blotting, Western; D002846:Chromatography, Affinity; D019281:Dimerization; D004727:Endothelium / Q000201:enzymology*; D006493:Heparin / Q000737:chemistry; D006801:Humans; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D008071:Lipoprotein Lipase / Q000737:chemistry*; D051379:Mice; D008822:Mice, Transgenic; D010743:Phospholipids / Q000737:chemistry; D010920:Placenta / Q000201:enzymology*; D012333:RNA, Messenger / Q000378:metabolism; D012685:Sepharose / Q000737:chemistry / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology; D013045:Species Specificity; D014280:Triglycerides / Q000737:chemistry; D014327:Trophoblasts / Q000378:metabolism
chemical_list: D010743:Phospholipids; D012333:RNA, Messenger; D014280:Triglycerides; D012965:Sodium Chloride; D006493:Heparin; D012685:Sepharose; D008071:Lipoprotein Lipase