Evidence that a neutral cholesteryl ester hydrolase is responsible for the extralysosomal hydrolysis of high‐density lipoprotein cholesteryl ester in rat hepatoma cells (Fu5AH)
Identifieur interne : 002D99 ( Main/Exploration ); précédent : 002D98; suivant : 002E00Evidence that a neutral cholesteryl ester hydrolase is responsible for the extralysosomal hydrolysis of high‐density lipoprotein cholesteryl ester in rat hepatoma cells (Fu5AH)
Auteurs : John G. Delamatre [États-Unis] ; Robert M. Carter [États-Unis] ; Conrad A. Hornick [États-Unis]Source :
- Journal of Cellular Physiology [ 0021-9541 ] ; 1993-10.
English descriptors
- Teeft :
- Atherosclerosis, Biol, Cholesterol delivery, Cholesteryl, Cholesteryl ester, Delamatre, Density marker beads, Diethylumbelliferyl phosphate, Direct transfer, Endosomes, Ester, Free cholesterol, Fu5ah, Hepatic lipase, Hepatoma, Hepatoma cells, High density lipoproteins, Hydrolase, Hydrolysis, Isotope, Isotope ratio, Lipid, Lipoprotein, Lysosome, Nceh, Neutral cholesteryl ester hydrolase, Open circles, Open triangles, Other groups, Percoll, Percoll gradient, Percoll gradient fractions, Plasma membrane.
Abstract
Diethylumbelliferyl phosphate (UBP) has been shown to inhibit the neutral cholesteryl ester hydrolase activity responsible for hydrolysis of cellular lipid droplet cholesteryl ester (Harrison et al., 1990). The potential for (UBP) to inhibit uptake and hydrolysis of high density lipoprotein (HDL) cholestryl ester was studied in Fu5AH hepatoma cells, a model for HDL cholesterol delivery. Coincubation of 3H‐cholesteryl ester labeled HDL with UBP resulted in a 72% decrease in the cellular free cholesterol/cholesterl ester (FC/CE) isotope ratio, indicating an inhibition in the conversion of cholesteryl ester to free cholesterol. Total cellular 3H‐CE uptake was modestly (27%) but significantly decreased by UBP. Pulsechase experiments (15 min. pulse and 7 min. chase) were used to study the hydrolysis of HDL 3H‐CE in subcellular fractions separated by percoll gradients. The conversion of 3H‐CE to 3H‐FC could be demonstrated in fractions that comigrated with the plasma membrane/endosome fractions but were well separated from lysosomes. Neutral cholesteryl ester hydrolase activity was detected in those same fractions. These results suggest that an extralysosomal pathway is operating in the metabolism of HDL cholesterol and its delivery to hepatoma cells. © 1993 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/jcp.1041570121
Affiliations:
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Delamatre</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Louisiane</region></placeName><wicri:cityArea>Department of Physiology, Division of Lipoprotein Metabolism and Pathophysiology, Louisiana State University Medical Center, New Orleans</wicri:cityArea></affiliation><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Louisiane</region></placeName><wicri:cityArea>Correspondence address: Department of Physiology, Division of Lipoprotein Metabolism and Pathophysiology, Louisiana State University Medical Center, New Orleans</wicri:cityArea></affiliation></author><author><name sortKey="Carter, Robert M" sort="Carter, Robert M" uniqKey="Carter R" first="Robert M." last="Carter">Robert M. Carter</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Louisiane</region></placeName><wicri:cityArea>Department of Physiology, Division of Lipoprotein Metabolism and Pathophysiology, Louisiana State University Medical Center, New Orleans</wicri:cityArea></affiliation></author><author><name sortKey="Hornick, Conrad A" sort="Hornick, Conrad A" uniqKey="Hornick C" first="Conrad A." last="Hornick">Conrad A. Hornick</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Louisiane</region></placeName><wicri:cityArea>Department of Physiology, Division of Lipoprotein Metabolism and Pathophysiology, Louisiana State University Medical Center, New Orleans</wicri:cityArea></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Journal of Cellular Physiology</title><title level="j" type="alt">JOURNAL OF CELLULAR PHYSIOLOGY</title><idno type="ISSN">0021-9541</idno><idno type="eISSN">1097-4652</idno><imprint><biblScope unit="vol">157</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="164">164</biblScope><biblScope unit="page" to="168">168</biblScope><biblScope unit="page-count">5</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="1993-10">1993-10</date></imprint><idno type="ISSN">0021-9541</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0021-9541</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Atherosclerosis</term><term>Biol</term><term>Cholesterol delivery</term><term>Cholesteryl</term><term>Cholesteryl ester</term><term>Delamatre</term><term>Density marker beads</term><term>Diethylumbelliferyl phosphate</term><term>Direct transfer</term><term>Endosomes</term><term>Ester</term><term>Free cholesterol</term><term>Fu5ah</term><term>Hepatic lipase</term><term>Hepatoma</term><term>Hepatoma cells</term><term>High density lipoproteins</term><term>Hydrolase</term><term>Hydrolysis</term><term>Isotope</term><term>Isotope ratio</term><term>Lipid</term><term>Lipoprotein</term><term>Lysosome</term><term>Nceh</term><term>Neutral cholesteryl ester hydrolase</term><term>Open circles</term><term>Open triangles</term><term>Other groups</term><term>Percoll</term><term>Percoll gradient</term><term>Percoll gradient fractions</term><term>Plasma membrane</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="fr">Diethylumbelliferyl phosphate (UBP) has been shown to inhibit the neutral cholesteryl ester hydrolase activity responsible for hydrolysis of cellular lipid droplet cholesteryl ester (Harrison et al., 1990). The potential for (UBP) to inhibit uptake and hydrolysis of high density lipoprotein (HDL) cholestryl ester was studied in Fu5AH hepatoma cells, a model for HDL cholesterol delivery. Coincubation of 3H‐cholesteryl ester labeled HDL with UBP resulted in a 72% decrease in the cellular free cholesterol/cholesterl ester (FC/CE) isotope ratio, indicating an inhibition in the conversion of cholesteryl ester to free cholesterol. Total cellular 3H‐CE uptake was modestly (27%) but significantly decreased by UBP. Pulsechase experiments (15 min. pulse and 7 min. chase) were used to study the hydrolysis of HDL 3H‐CE in subcellular fractions separated by percoll gradients. The conversion of 3H‐CE to 3H‐FC could be demonstrated in fractions that comigrated with the plasma membrane/endosome fractions but were well separated from lysosomes. Neutral cholesteryl ester hydrolase activity was detected in those same fractions. These results suggest that an extralysosomal pathway is operating in the metabolism of HDL cholesterol and its delivery to hepatoma cells. © 1993 Wiley‐Liss, Inc.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Louisiane</li></region></list><tree><country name="États-Unis"><region name="Louisiane"><name sortKey="Delamatre, John G" sort="Delamatre, John G" uniqKey="Delamatre J" first="John G." last="Delamatre">John G. Delamatre</name></region><name sortKey="Carter, Robert M" sort="Carter, Robert M" uniqKey="Carter R" first="Robert M." last="Carter">Robert M. Carter</name><name sortKey="Delamatre, John G" sort="Delamatre, John G" uniqKey="Delamatre J" first="John G." last="Delamatre">John G. Delamatre</name><name sortKey="Hornick, Conrad A" sort="Hornick, Conrad A" uniqKey="Hornick C" first="Conrad A." last="Hornick">Conrad A. Hornick</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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