Endothelial and lipoprotein lipases in human and mouse placenta

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Endothelial and lipoprotein lipases in human and mouse placenta. / Lindegaard, Marie Louise Skakkebæk; Olivecrona, Gunilla; Christoffersen, Christina; Kratky, Dagmar; Hannibal, Jens; Petersen, Bodil L; Zechner, Rudolf; Damm, Peter; Nielsen, Lars B.

I: Journal of Lipid Research, Bind 46, Nr. 11, 01.11.2005, s. 2339-46.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskning

Harvard

Lindegaard, MLS, Olivecrona, G, Christoffersen, C, Kratky, D, Hannibal, J, Petersen, BL, Zechner, R, Damm, P & Nielsen, LB 2005, 'Endothelial and lipoprotein lipases in human and mouse placenta', Journal of Lipid Research, bind 46, nr. 11, s. 2339-46. https://doi.org/10.1194/jlr.M500277-JLR200

APA

Lindegaard, M. L. S., Olivecrona, G., Christoffersen, C., Kratky, D., Hannibal, J., Petersen, B. L., ... Nielsen, L. B. (2005). Endothelial and lipoprotein lipases in human and mouse placenta. Journal of Lipid Research, 46(11), 2339-46. https://doi.org/10.1194/jlr.M500277-JLR200

Vancouver

Lindegaard MLS, Olivecrona G, Christoffersen C, Kratky D, Hannibal J, Petersen BL o.a. Endothelial and lipoprotein lipases in human and mouse placenta. Journal of Lipid Research. 2005 nov 1;46(11):2339-46. https://doi.org/10.1194/jlr.M500277-JLR200

Author

Lindegaard, Marie Louise Skakkebæk ; Olivecrona, Gunilla ; Christoffersen, Christina ; Kratky, Dagmar ; Hannibal, Jens ; Petersen, Bodil L ; Zechner, Rudolf ; Damm, Peter ; Nielsen, Lars B. / Endothelial and lipoprotein lipases in human and mouse placenta. I: Journal of Lipid Research. 2005 ; Bind 46, Nr. 11. s. 2339-46.

Bibtex

@article{2306e6c9ae3e4b01bbcde4d4c980bce8,
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.",
author = "Lindegaard, {Marie Louise Skakkeb{\ae}k} and Gunilla Olivecrona and Christina Christoffersen and Dagmar Kratky and Jens Hannibal and Petersen, {Bodil L} and Rudolf Zechner and Peter Damm and Nielsen, {Lars B}",
year = "2005",
month = "11",
day = "1",
doi = "http://dx.doi.org/10.1194/jlr.M500277-JLR200",
language = "English",
volume = "46",
pages = "2339--46",
journal = "Journal of Lipid Research",
issn = "0022-2275",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "11",

}

RIS

TY - JOUR

T1 - Endothelial and lipoprotein lipases in human and mouse placenta

AU - Lindegaard, Marie Louise Skakkebæk

AU - Olivecrona, Gunilla

AU - Christoffersen, Christina

AU - Kratky, Dagmar

AU - Hannibal, Jens

AU - Petersen, Bodil L

AU - Zechner, Rudolf

AU - Damm, Peter

AU - Nielsen, Lars B

PY - 2005/11/1

Y1 - 2005/11/1

N2 - 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.

AB - 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.

U2 - http://dx.doi.org/10.1194/jlr.M500277-JLR200

DO - http://dx.doi.org/10.1194/jlr.M500277-JLR200

M3 - Journal article

VL - 46

SP - 2339

EP - 2346

JO - Journal of Lipid Research

JF - Journal of Lipid Research

SN - 0022-2275

IS - 11

ER -

ID: 34075710