Endothelin-converting enzyme : Ultrastructural localization and its recycling from the cell surface
Identifieur interne : 002849 ( Main/Exploration ); précédent : 002848; suivant : 002850Endothelin-converting enzyme : Ultrastructural localization and its recycling from the cell surface
Auteurs : K. Barnes [Royaume-Uni] ; C. Brown [Royaume-Uni] ; A. J. Turner [Royaume-Uni]Source :
- Hypertension : (Dallas, Tex. 1979) [ 0194-911X ] ; 1998.
Descripteurs français
- KwdFr :
- Animaux, Appareil de Golgi, Aspartic acid endopeptidases (analyse), Aspartic acid endopeptidases (métabolisme), Chloroquine, Endothéline-1 (analyse), Endothéline-1 (métabolisme), Endothélium (), Endothélium (enzymologie), Endothélium vasculaire (), Endothélium vasculaire (enzymologie), Enzymes de conversion de l'endothéline, Glycoprotéines, Glycoprotéines membranaires, Humains, Lignée cellulaire, Metalloendopeptidases (analyse), Metalloendopeptidases (métabolisme), Microscopie immunoélectronique, Peptidyl-Dipeptidase A (analyse), Poumon (), Poumon (enzymologie), Protéines membranaires, Rats, Suidae.
- MESH :
- analyse : Aspartic acid endopeptidases, Endothéline-1, Metalloendopeptidases, Peptidyl-Dipeptidase A.
- enzymologie : Endothélium, Endothélium vasculaire, Poumon.
- métabolisme : Aspartic acid endopeptidases, Endothéline-1, Metalloendopeptidases.
- Pascal (Inist)
- Animaux, Appareil de Golgi, Chloroquine, Endothelin-converting enzyme 1, Endothélium, Endothélium vasculaire, Enzymes de conversion de l'endothéline, Glycoprotéines, Glycoprotéines membranaires, Humains, Lignée cellulaire, Localisation, Activité enzymatique, Microscopie immunoélectronique, Poumon, Protéines membranaires, Rats, Suidae, Ultrastructure, Surface cellulaire, Cellule endothéliale, Poumon, Membrane plasmique, In vitro, Culture cellulaire.
English descriptors
- KwdEn :
- Animals, Aspartic Acid Endopeptidases (analysis), Aspartic Acid Endopeptidases (metabolism), Cell Line, Cell culture, Cell surface, Chloroquine, Endothelial cell, Endothelin-1 (analysis), Endothelin-1 (metabolism), Endothelin-Converting Enzymes, Endothelin-converting enzyme 1, Endothelium (chemistry), Endothelium (enzymology), Endothelium, Vascular (chemistry), Endothelium, Vascular (enzymology), Enzymatic activity, Glycoproteins, Golgi Apparatus, Humans, In vitro, Localization, Lung, Lung (chemistry), Lung (enzymology), Membrane Glycoproteins, Membrane Proteins, Metalloendopeptidases (analysis), Metalloendopeptidases (metabolism), Microscopy, Immunoelectron, Peptidyl-Dipeptidase A (analysis), Plasma membrane, Rats, Swine, Ultrastructure.
- MESH :
- chemical , analysis : Aspartic Acid Endopeptidases, Endothelin-1, Metalloendopeptidases, Peptidyl-Dipeptidase A.
- chemical , metabolism : Aspartic Acid Endopeptidases, Endothelin-1, Metalloendopeptidases.
- chemistry : Endothelium, Endothelium, Vascular, Lung.
- enzymology : Endothelium, Endothelium, Vascular, Lung.
- Animals, Cell Line, Chloroquine, Endothelin-Converting Enzymes, Glycoproteins, Golgi Apparatus, Humans, Membrane Glycoproteins, Membrane Proteins, Microscopy, Immunoelectron, Rats, Swine.
Abstract
The potent vasoconstrictor endothelin-1 (ET-1) is secreted constitutively by endothelial cells and has been implicated in the pathophysiology ofseveral cardiovascular diseases. It is generated from its inactive intermediate, big ET-1, through the action of endothelin-converting enzyme (ECE). Using several complementary techniques, we have demonstrated that ECE is present at the cell surface and on intracellular vesicles and that it recycles from the cell surface in endothelial cells. This is the first ultrastructural localization of ECE in lung and the first time big ET-1 and ECE have been colocalized by immunogold in a vesicular population, 50 to 100 nm in diameter. In addition, by double immunogold staining of ultrathin cryosections, we have localized ECE together with angiotensin-converting enzyme on the luminal membrane of endothelial cells. With cell surface biotinylation of a transformed rat endothelial cell line and of human umbilical vein endothelial cells, we have confirmed the presence of ECE on the plasma membrane. After treatment of endothelial cells with chloroquine, ECE and trans-Golgi network 38 protein were shown by immunofluorescence staining to localize to the same intracellular compartment.
Affiliations:
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Le document en format XML
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Barnes</name><affiliation wicri:level="4"><inist:fA14 i1="01"><s1>Department of Biochemistry and Molecular Biology, University of Leeds</s1><s3>GBR</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ></inist:fA14><country>Royaume-Uni</country><placeName><settlement type="city">Leeds</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Yorkshire-et-Humber</region></placeName><orgName type="university">Université de Leeds</orgName></affiliation></author><author><name sortKey="Brown, C" sort="Brown, C" uniqKey="Brown C" first="C." last="Brown">C. Brown</name><affiliation wicri:level="4"><inist:fA14 i1="01"><s1>Department of Biochemistry and Molecular Biology, University of Leeds</s1><s3>GBR</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ></inist:fA14><country>Royaume-Uni</country><placeName><settlement type="city">Leeds</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Yorkshire-et-Humber</region></placeName><orgName type="university">Université de Leeds</orgName></affiliation></author><author><name sortKey="Turner, A J" sort="Turner, A J" uniqKey="Turner A" first="A. J." last="Turner">A. J. Turner</name><affiliation wicri:level="4"><inist:fA14 i1="01"><s1>Department of Biochemistry and Molecular Biology, University of Leeds</s1><s3>GBR</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ></inist:fA14><country>Royaume-Uni</country><placeName><settlement type="city">Leeds</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Yorkshire-et-Humber</region></placeName><orgName type="university">Université de Leeds</orgName></affiliation></author></analytic><series><title level="j" type="main">Hypertension : (Dallas, Tex. 1979)</title><title level="j" type="abbreviated">Hypertension : (Dallas Tex., 1979)</title><idno type="ISSN">0194-911X</idno><imprint><date when="1998">1998</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Hypertension : (Dallas, Tex. 1979)</title><title level="j" type="abbreviated">Hypertension : (Dallas Tex., 1979)</title><idno type="ISSN">0194-911X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Aspartic Acid Endopeptidases (analysis)</term><term>Aspartic Acid Endopeptidases (metabolism)</term><term>Cell Line</term><term>Cell culture</term><term>Cell surface</term><term>Chloroquine</term><term>Endothelial cell</term><term>Endothelin-1 (analysis)</term><term>Endothelin-1 (metabolism)</term><term>Endothelin-Converting Enzymes</term><term>Endothelin-converting enzyme 1</term><term>Endothelium (chemistry)</term><term>Endothelium (enzymology)</term><term>Endothelium, Vascular (chemistry)</term><term>Endothelium, Vascular (enzymology)</term><term>Enzymatic activity</term><term>Glycoproteins</term><term>Golgi Apparatus</term><term>Humans</term><term>In vitro</term><term>Localization</term><term>Lung</term><term>Lung (chemistry)</term><term>Lung (enzymology)</term><term>Membrane Glycoproteins</term><term>Membrane Proteins</term><term>Metalloendopeptidases (analysis)</term><term>Metalloendopeptidases (metabolism)</term><term>Microscopy, Immunoelectron</term><term>Peptidyl-Dipeptidase A (analysis)</term><term>Plasma membrane</term><term>Rats</term><term>Swine</term><term>Ultrastructure</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Appareil de Golgi</term><term>Aspartic acid endopeptidases (analyse)</term><term>Aspartic acid endopeptidases (métabolisme)</term><term>Chloroquine</term><term>Endothéline-1 (analyse)</term><term>Endothéline-1 (métabolisme)</term><term>Endothélium ()</term><term>Endothélium (enzymologie)</term><term>Endothélium vasculaire ()</term><term>Endothélium vasculaire (enzymologie)</term><term>Enzymes de conversion de l'endothéline</term><term>Glycoprotéines</term><term>Glycoprotéines membranaires</term><term>Humains</term><term>Lignée cellulaire</term><term>Metalloendopeptidases (analyse)</term><term>Metalloendopeptidases (métabolisme)</term><term>Microscopie immunoélectronique</term><term>Peptidyl-Dipeptidase A (analyse)</term><term>Poumon ()</term><term>Poumon (enzymologie)</term><term>Protéines membranaires</term><term>Rats</term><term>Suidae</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Aspartic Acid Endopeptidases</term><term>Endothelin-1</term><term>Metalloendopeptidases</term><term>Peptidyl-Dipeptidase A</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Aspartic Acid Endopeptidases</term><term>Endothelin-1</term><term>Metalloendopeptidases</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Aspartic acid endopeptidases</term><term>Endothéline-1</term><term>Metalloendopeptidases</term><term>Peptidyl-Dipeptidase A</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Endothelium</term><term>Endothelium, Vascular</term><term>Lung</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Endothélium</term><term>Endothélium vasculaire</term><term>Poumon</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Endothelium</term><term>Endothelium, Vascular</term><term>Lung</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Aspartic acid endopeptidases</term><term>Endothéline-1</term><term>Metalloendopeptidases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Chloroquine</term><term>Endothelin-Converting Enzymes</term><term>Glycoproteins</term><term>Golgi Apparatus</term><term>Humans</term><term>Membrane Glycoproteins</term><term>Membrane Proteins</term><term>Microscopy, Immunoelectron</term><term>Rats</term><term>Swine</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Animaux</term><term>Appareil de Golgi</term><term>Chloroquine</term><term>Endothelin-converting enzyme 1</term><term>Endothélium</term><term>Endothélium vasculaire</term><term>Enzymes de conversion de l'endothéline</term><term>Glycoprotéines</term><term>Glycoprotéines membranaires</term><term>Humains</term><term>Lignée cellulaire</term><term>Localisation</term><term>Activité enzymatique</term><term>Microscopie immunoélectronique</term><term>Poumon</term><term>Protéines membranaires</term><term>Rats</term><term>Suidae</term><term>Ultrastructure</term><term>Surface cellulaire</term><term>Cellule endothéliale</term><term>Poumon</term><term>Membrane plasmique</term><term>In vitro</term><term>Culture cellulaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The potent vasoconstrictor endothelin-1 (ET-1) is secreted constitutively by endothelial cells and has been implicated in the pathophysiology ofseveral cardiovascular diseases. It is generated from its inactive intermediate, big ET-1, through the action of endothelin-converting enzyme (ECE). Using several complementary techniques, we have demonstrated that ECE is present at the cell surface and on intracellular vesicles and that it recycles from the cell surface in endothelial cells. This is the first ultrastructural localization of ECE in lung and the first time big ET-1 and ECE have been colocalized by immunogold in a vesicular population, 50 to 100 nm in diameter. In addition, by double immunogold staining of ultrathin cryosections, we have localized ECE together with angiotensin-converting enzyme on the luminal membrane of endothelial cells. With cell surface biotinylation of a transformed rat endothelial cell line and of human umbilical vein endothelial cells, we have confirmed the presence of ECE on the plasma membrane. After treatment of endothelial cells with chloroquine, ECE and trans-Golgi network 38 protein were shown by immunofluorescence staining to localize to the same intracellular compartment.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Yorkshire-et-Humber</li></region><settlement><li>Leeds</li></settlement><orgName><li>Université de Leeds</li></orgName></list><tree><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Barnes, K" sort="Barnes, K" uniqKey="Barnes K" first="K." last="Barnes">K. Barnes</name></region><name sortKey="Brown, C" sort="Brown, C" uniqKey="Brown C" first="C." last="Brown">C. Brown</name><name sortKey="Turner, A J" sort="Turner, A J" uniqKey="Turner A" first="A. J." last="Turner">A. J. Turner</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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