Deficiency in ethanolamine plasmalogen leads to altered cholesterol transport
Plasmalogens are a major sub-class of ethanolamine and choline phospholipids in which the sn-1 position has a long chain fatty alcohol attached through a vinyl ether bond. These phospholipids are proposed to play a role in membrane fusion-mediated events. In this study, we investigated the role of t...
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Elsevier
2003-01-01
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Series: | Journal of Lipid Research |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520328340 |
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author | Natalie J. Munn Emily Arnio Dailan Liu Raphael A. Zoeller Laura Liscum |
author_facet | Natalie J. Munn Emily Arnio Dailan Liu Raphael A. Zoeller Laura Liscum |
author_sort | Natalie J. Munn |
collection | DOAJ |
description | Plasmalogens are a major sub-class of ethanolamine and choline phospholipids in which the sn-1 position has a long chain fatty alcohol attached through a vinyl ether bond. These phospholipids are proposed to play a role in membrane fusion-mediated events. In this study, we investigated the role of the ethanolamine plasmalogen plasmenylethanolamine (PlsE11167) in intracellular cholesterol transport in Chinese hamster ovary cell mutants NRel-4 and NZel-1, which have single gene defects in PlsEtn biosynthesis. We found that PlsEtn was essential for specific cholesterol transport pathways, those from the cell surface or endocytic compartments to acyl-CoA/cholesterol acyltransferase in the endoplasmic reticulum. The movement of cholesterol from the endoplasmic reticulum or endocytic compartments to the cell surface was normal in PlsEtn-deficient cells. Also, vesicle trafficking was normal in PlsEtn-deficient cells, as measured by fluid phase endocytosis and exocytosis, as was the movement of newly-synthesized proteins to the cell surface. The mutant cholesterol transport phenotype was due to the lack of PlsEtn, since it was corrected when NRel-4 cells were transfected with a cDNA encoding the missing enzyme or supplied with a metabolic intermediate that enters the PlsEtn biosynthetic pathway downstream of the defect.Future work must determine the precise role that plasmalogens have on cholesterol transport to the endoplasmic reticulum. |
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spelling | doaj.art-895bc851a469492b8b1d86419f72eb512022-12-21T21:30:19ZengElsevierJournal of Lipid Research0022-22752003-01-01441182192Deficiency in ethanolamine plasmalogen leads to altered cholesterol transportNatalie J. Munn0Emily Arnio1Dailan Liu2Raphael A. Zoeller3Laura Liscum4Department of Physiology, Tufts University School of Medicine, Boston, MA 02111; Department of Physiology and Structural Biology, Boston University School of Medicine, Boston, MA 02118Department of Physiology, Tufts University School of Medicine, Boston, MA 02111; Department of Physiology and Structural Biology, Boston University School of Medicine, Boston, MA 02118Department of Physiology, Tufts University School of Medicine, Boston, MA 02111; Department of Physiology and Structural Biology, Boston University School of Medicine, Boston, MA 02118Department of Physiology, Tufts University School of Medicine, Boston, MA 02111; Department of Physiology and Structural Biology, Boston University School of Medicine, Boston, MA 02118Department of Physiology, Tufts University School of Medicine, Boston, MA 02111; Department of Physiology and Structural Biology, Boston University School of Medicine, Boston, MA 02118Plasmalogens are a major sub-class of ethanolamine and choline phospholipids in which the sn-1 position has a long chain fatty alcohol attached through a vinyl ether bond. These phospholipids are proposed to play a role in membrane fusion-mediated events. In this study, we investigated the role of the ethanolamine plasmalogen plasmenylethanolamine (PlsE11167) in intracellular cholesterol transport in Chinese hamster ovary cell mutants NRel-4 and NZel-1, which have single gene defects in PlsEtn biosynthesis. We found that PlsEtn was essential for specific cholesterol transport pathways, those from the cell surface or endocytic compartments to acyl-CoA/cholesterol acyltransferase in the endoplasmic reticulum. The movement of cholesterol from the endoplasmic reticulum or endocytic compartments to the cell surface was normal in PlsEtn-deficient cells. Also, vesicle trafficking was normal in PlsEtn-deficient cells, as measured by fluid phase endocytosis and exocytosis, as was the movement of newly-synthesized proteins to the cell surface. The mutant cholesterol transport phenotype was due to the lack of PlsEtn, since it was corrected when NRel-4 cells were transfected with a cDNA encoding the missing enzyme or supplied with a metabolic intermediate that enters the PlsEtn biosynthetic pathway downstream of the defect.Future work must determine the precise role that plasmalogens have on cholesterol transport to the endoplasmic reticulum.http://www.sciencedirect.com/science/article/pii/S0022227520328340plasmalogenplasmenylethanolaminecholesterolsomatic cell mutant |
spellingShingle | Natalie J. Munn Emily Arnio Dailan Liu Raphael A. Zoeller Laura Liscum Deficiency in ethanolamine plasmalogen leads to altered cholesterol transport Journal of Lipid Research plasmalogen plasmenylethanolamine cholesterol somatic cell mutant |
title | Deficiency in ethanolamine plasmalogen leads to altered cholesterol transport |
title_full | Deficiency in ethanolamine plasmalogen leads to altered cholesterol transport |
title_fullStr | Deficiency in ethanolamine plasmalogen leads to altered cholesterol transport |
title_full_unstemmed | Deficiency in ethanolamine plasmalogen leads to altered cholesterol transport |
title_short | Deficiency in ethanolamine plasmalogen leads to altered cholesterol transport |
title_sort | deficiency in ethanolamine plasmalogen leads to altered cholesterol transport |
topic | plasmalogen plasmenylethanolamine cholesterol somatic cell mutant |
url | http://www.sciencedirect.com/science/article/pii/S0022227520328340 |
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