ChloroquineV1, Main, Exploration, bibRecord, 003370

Synthesis and hydrolysis of cholesteryl esters by isolated rat-liver lysosomes and cell-free extracts of human lung fibroblasts

Identifieur interne : 003370 ( Main/Exploration ); précédent : 003369; suivant : 003371

Synthesis and hydrolysis of cholesteryl esters by isolated rat-liver lysosomes and cell-free extracts of human lung fibroblasts

Auteurs : J. Peter Slotte ; Stig Ekman

Source :

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism [ 0005-2760 ] ; 1986.

RBID : ISTEX:97108205839BFF5643B40DBBF4047FF230317C15

Descripteurs français

KwdFr :
- Animaux, Cholestérol ester (biosynthèse), Cholestérol ester (métabolisme), Fibroblastes (enzymologie), Foie (enzymologie), Humains, Hydrolyse, Lignées consanguines de rats, Lysosomes (enzymologie), Mâle, Poumon (enzymologie), Rats, Sterol Esterase (métabolisme), Système acellulaire, Techniques in vitro.
MESH :
- biosynthèse : Cholestérol ester.
- enzymologie : Fibroblastes, Foie, Lysosomes, Poumon.
- métabolisme : Cholestérol ester, Sterol Esterase.
- Animaux, Humains, Hydrolyse, Lignées consanguines de rats, Mâle, Rats, Système acellulaire, Techniques in vitro.

English descriptors

KwdEn :
- Animals, Cell-Free System, Cholesterol Esters (biosynthesis), Cholesterol Esters (metabolism), Fibroblasts (enzymology), Humans, Hydrolysis, In Vitro Techniques, Liver (enzymology), Lung (enzymology), Lysosomes (enzymology), Male, Rats, Rats, Inbred Strains, Sterol Esterase (metabolism).
MESH :
- chemical , biosynthesis : Cholesterol Esters.
- chemical , metabolism : Cholesterol Esters, Sterol Esterase.
- enzymology : Fibroblasts, Liver, Lung, Lysosomes.
Teeft :
- Acid cholesteryl ester hydrolase, Acta, Acyltransferase, Ammonium, Ammonium chloride, Animals, Biochim, Biophys, Cell-Free System, Chloroquine, Cholesteryl, Cholesteryl ester hydrolysis, Cholesteryl esters, Cholesteryl oleate, Cultured cells, Cultured fibroblasts, Ester, Esterification, Esterification activity, Esterification reaction, Esterified cholesterol, Fibroblast, Final concentration, Free cholesterol, Humans, Hydrolase, Hydrolysis, Hydrolytic activity, In Vitro Techniques, Incubation mixture, Inhibitor, Intact cells, Lipid, Lipid vesicles, Liver lysosomes, Lung fibroblasts, Lysosomal, Lysosomal acid cholesteryl ester hydrolase, Lysosomal compartment, Lysosome, Male, Microemulsion particles, Oleate, Other hand, Phosphatidylcholine, Potent inhibitor, Progesterone, Rats, Rats, Inbred Strains, Same enzyme, Sandoz, Sodium oleate, Vesicle.

Abstract

Abstract: The objective of this study was to examine and characterize the cholesteryl ester synthesizing [S] and hydrolyzing [H] properties of the acid cholesteryl ester hydrolase (acid cholesteryl ester hydrolase), both in isolated rat liver lysosomes and in cell-free extracts from cultured fibroblasts. For both liver lysosomes and fibroblasts extracts, the major synthesizing activity was found around pH 4 and did not require exogenous ATP. The rate of hydrolysis was measured at pH 4.5. Several different inhibitors were used in order to characterize the reactions. Ammonium chloride did not markedly affect the activity of acid cholesteryl ester hydrolase at pH 4 [S] or 4.5 [H], whereas chloroquine was a potent inhibitor of acid CEase in both liver lysosomes and fibroblast extracts. The [S] activity of the acid cholesteryl ester hydrolase in either material was not affected by the acylCoA:cholesterol acyltransferase inhibitor Compound 58-035 from Sandoz. Progesterone, on the other hand, which is an often used acylCoA:cholesterol acyltransferase inhibitor, markedly blocked both activities of the acid CEase. Our results indicate that the lysosomal compartment of both studied tissues, in addition to hydrolysis activity, also have a significant esterification activity. It appears that both activities are carried out by the same enzyme.

Url:

https://api.istex.fr/ark:/67375/6H6-7GBX2RCG-7/fulltext.pdf

DOI: 10.1016/0005-2760(86)90106-2

Affiliations:

Le document en format XML

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<term>Fibroblasts (enzymology)</term>
<term>Humans</term>
<term>Hydrolysis</term>
<term>In Vitro Techniques</term>
<term>Liver (enzymology)</term>
<term>Lung (enzymology)</term>
<term>Lysosomes (enzymology)</term>
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<term>Rats, Inbred Strains</term>
<term>Sterol Esterase (metabolism)</term>
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<term>Foie (enzymologie)</term>
<term>Humains</term>
<term>Hydrolyse</term>
<term>Lignées consanguines de rats</term>
<term>Lysosomes (enzymologie)</term>
<term>Mâle</term>
<term>Poumon (enzymologie)</term>
<term>Rats</term>
<term>Sterol Esterase (métabolisme)</term>
<term>Système acellulaire</term>
<term>Techniques in vitro</term>
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<term>Ammonium chloride</term>
<term>Animals</term>
<term>Biochim</term>
<term>Biophys</term>
<term>Cell-Free System</term>
<term>Chloroquine</term>
<term>Cholesteryl</term>
<term>Cholesteryl ester hydrolysis</term>
<term>Cholesteryl esters</term>
<term>Cholesteryl oleate</term>
<term>Cultured cells</term>
<term>Cultured fibroblasts</term>
<term>Ester</term>
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<term>Hydrolase</term>
<term>Hydrolysis</term>
<term>Hydrolytic activity</term>
<term>In Vitro Techniques</term>
<term>Incubation mixture</term>
<term>Inhibitor</term>
<term>Intact cells</term>
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<term>Lipid vesicles</term>
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<term>Lung fibroblasts</term>
<term>Lysosomal</term>
<term>Lysosomal acid cholesteryl ester hydrolase</term>
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<term>Lysosome</term>
<term>Male</term>
<term>Microemulsion particles</term>
<term>Oleate</term>
<term>Other hand</term>
<term>Phosphatidylcholine</term>
<term>Potent inhibitor</term>
<term>Progesterone</term>
<term>Rats</term>
<term>Rats, Inbred Strains</term>
<term>Same enzyme</term>
<term>Sandoz</term>
<term>Sodium oleate</term>
<term>Vesicle</term>
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<term>Humains</term>
<term>Hydrolyse</term>
<term>Lignées consanguines de rats</term>
<term>Mâle</term>
<term>Rats</term>
<term>Système acellulaire</term>
<term>Techniques in vitro</term>
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<front><div type="abstract" xml:lang="en">Abstract: The objective of this study was to examine and characterize the cholesteryl ester synthesizing [S] and hydrolyzing [H] properties of the acid cholesteryl ester hydrolase (acid cholesteryl ester hydrolase), both in isolated rat liver lysosomes and in cell-free extracts from cultured fibroblasts. For both liver lysosomes and fibroblasts extracts, the major synthesizing activity was found around pH 4 and did not require exogenous ATP. The rate of hydrolysis was measured at pH 4.5. Several different inhibitors were used in order to characterize the reactions. Ammonium chloride did not markedly affect the activity of acid cholesteryl ester hydrolase at pH 4 [S] or 4.5 [H], whereas chloroquine was a potent inhibitor of acid CEase in both liver lysosomes and fibroblast extracts. The [S] activity of the acid cholesteryl ester hydrolase in either material was not affected by the acylCoA:cholesterol acyltransferase inhibitor Compound 58-035 from Sandoz. Progesterone, on the other hand, which is an often used acylCoA:cholesterol acyltransferase inhibitor, markedly blocked both activities of the acid CEase. Our results indicate that the lysosomal compartment of both studied tissues, in addition to hydrolysis activity, also have a significant esterification activity. It appears that both activities are carried out by the same enzyme.</div>
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Serveur d'exploration Chloroquine

Synthesis and hydrolysis of cholesteryl esters by isolated rat-liver lysosomes and cell-free extracts of human lung fibroblasts

Synthesis and hydrolysis of cholesteryl esters by isolated rat-liver lysosomes and cell-free extracts of human lung fibroblasts

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

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