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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Main Authors: Natalie J. Munn, Emily Arnio, Dailan Liu, Raphael A. Zoeller, Laura Liscum
Format: Article
Language:English
Published: Elsevier 2003-01-01
Series:Journal of Lipid Research
Subjects:
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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AT raphaelazoeller deficiencyinethanolamineplasmalogenleadstoalteredcholesteroltransport
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