Endothelin-converting enzyme: ultrastructural localization and its recycling from the cell surface.
Identifieur interne : 000503 ( PubMed/Curation ); précédent : 000502; suivant : 000504Endothelin-converting enzyme: ultrastructural localization and its recycling from the cell surface.
Auteurs : K. Barnes [Royaume-Uni] ; C. Brown ; A J TurnerSource :
- 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.
- Animaux, Appareil de Golgi, Chloroquine, Endothélium, Endothélium vasculaire, Enzymes de conversion de l'endothéline, Glycoprotéines, Glycoprotéines membranaires, Humains, Lignée cellulaire, Microscopie immunoélectronique, Poumon, Protéines membranaires, Rats, Suidae.
English descriptors
- KwdEn :
- Animals, Aspartic Acid Endopeptidases (analysis), Aspartic Acid Endopeptidases (metabolism), Cell Line, Chloroquine, Endothelin-1 (analysis), Endothelin-1 (metabolism), Endothelin-Converting Enzymes, Endothelium (chemistry), Endothelium (enzymology), Endothelium, Vascular (chemistry), Endothelium, Vascular (enzymology), Glycoproteins, Golgi Apparatus, Humans, Lung (chemistry), Lung (enzymology), Membrane Glycoproteins, Membrane Proteins, Metalloendopeptidases (analysis), Metalloendopeptidases (metabolism), Microscopy, Immunoelectron, Peptidyl-Dipeptidase A (analysis), Rats, Swine.
- 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 of several 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.
DOI: 10.1161/01.hyp.31.1.3
PubMed: 9449382
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000503
Links to Exploration step
pubmed:9449382Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Endothelin-converting enzyme: ultrastructural localization and its recycling from the cell surface.</title><author><name sortKey="Barnes, K" sort="Barnes, K" uniqKey="Barnes K" first="K" last="Barnes">K. Barnes</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, University of Leeds, UK. k.barnes@leeds.ac.uk</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, University of Leeds</wicri:regionArea></affiliation></author><author><name sortKey="Brown, C" sort="Brown, C" uniqKey="Brown C" first="C" last="Brown">C. Brown</name></author><author><name sortKey="Turner, A J" sort="Turner, A J" uniqKey="Turner A" first="A J" last="Turner">A J Turner</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1998">1998</date><idno type="RBID">pubmed:9449382</idno><idno type="pmid">9449382</idno><idno type="doi">10.1161/01.hyp.31.1.3</idno><idno type="wicri:Area/PubMed/Corpus">000503</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000503</idno><idno type="wicri:Area/PubMed/Curation">000503</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000503</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Endothelin-converting enzyme: ultrastructural localization and its recycling from the cell surface.</title><author><name sortKey="Barnes, K" sort="Barnes, K" uniqKey="Barnes K" first="K" last="Barnes">K. Barnes</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, University of Leeds, UK. k.barnes@leeds.ac.uk</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, University of Leeds</wicri:regionArea></affiliation></author><author><name sortKey="Brown, C" sort="Brown, C" uniqKey="Brown C" first="C" last="Brown">C. Brown</name></author><author><name sortKey="Turner, A J" sort="Turner, A J" uniqKey="Turner A" first="A J" last="Turner">A J Turner</name></author></analytic><series><title level="j">Hypertension (Dallas, Tex. : 1979)</title><idno type="ISSN">0194-911X</idno><imprint><date when="1998" type="published">1998</date></imprint></series></biblStruct></sourceDesc></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>Chloroquine</term><term>Endothelin-1 (analysis)</term><term>Endothelin-1 (metabolism)</term><term>Endothelin-Converting Enzymes</term><term>Endothelium (chemistry)</term><term>Endothelium (enzymology)</term><term>Endothelium, Vascular (chemistry)</term><term>Endothelium, Vascular (enzymology)</term><term>Glycoproteins</term><term>Golgi Apparatus</term><term>Humans</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>Rats</term><term>Swine</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="MESH" xml:lang="fr"><term>Animaux</term><term>Appareil de Golgi</term><term>Chloroquine</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>Microscopie immunoélectronique</term><term>Poumon</term><term>Protéines membranaires</term><term>Rats</term><term>Suidae</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 of several 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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9449382</PMID><DateCompleted><Year>1998</Year><Month>02</Month><Day>03</Day></DateCompleted><DateRevised><Year>2019</Year><Month>07</Month><Day>22</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0194-911X</ISSN><JournalIssue CitedMedium="Print"><Volume>31</Volume><Issue>1</Issue><PubDate><Year>1998</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Hypertension (Dallas, Tex. : 1979)</Title><ISOAbbreviation>Hypertension</ISOAbbreviation></Journal><ArticleTitle>Endothelin-converting enzyme: ultrastructural localization and its recycling from the cell surface.</ArticleTitle><Pagination><MedlinePgn>3-9</MedlinePgn></Pagination><Abstract><AbstractText>The potent vasoconstrictor endothelin-1 (ET-1) is secreted constitutively by endothelial cells and has been implicated in the pathophysiology of several 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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Barnes</LastName><ForeName>K</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, University of Leeds, UK. k.barnes@leeds.ac.uk</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Brown</LastName><ForeName>C</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Turner</LastName><ForeName>A J</ForeName><Initials>AJ</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Hypertension</MedlineTA><NlmUniqueID>7906255</NlmUniqueID><ISSNLinking>0194-911X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019332">Endothelin-1</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006023">Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008565">Membrane Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C072237">TGOLN2 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C513045">Tgoln2 protein, rat</NameOfSubstance></Chemical><Chemical><RegistryNumber>886U3H6UFF</RegistryNumber><NameOfSubstance UI="D002738">Chloroquine</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.15.1</RegistryNumber><NameOfSubstance UI="D007703">Peptidyl-Dipeptidase A</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.23.-</RegistryNumber><NameOfSubstance UI="D016282">Aspartic Acid Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.24.-</RegistryNumber><NameOfSubstance UI="D008666">Metalloendopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.24.71</RegistryNumber><NameOfSubstance UI="D000072396">Endothelin-Converting Enzymes</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016282" MajorTopicYN="N">Aspartic Acid Endopeptidases</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002738" MajorTopicYN="N">Chloroquine</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019332" MajorTopicYN="N">Endothelin-1</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000072396" MajorTopicYN="N">Endothelin-Converting Enzymes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004727" MajorTopicYN="N">Endothelium</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004730" MajorTopicYN="N">Endothelium, Vascular</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006023" MajorTopicYN="Y">Glycoproteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006056" MajorTopicYN="N">Golgi Apparatus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008168" MajorTopicYN="N">Lung</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008565" MajorTopicYN="Y">Membrane Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008666" MajorTopicYN="N">Metalloendopeptidases</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016253" MajorTopicYN="N">Microscopy, Immunoelectron</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007703" MajorTopicYN="N">Peptidyl-Dipeptidase A</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013552" MajorTopicYN="N">Swine</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1998</Year><Month>2</Month><Day>4</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1998</Year><Month>2</Month><Day>4</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1998</Year><Month>2</Month><Day>4</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9449382</ArticleId><ArticleId IdType="doi">10.1161/01.hyp.31.1.3</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/ChloroquineV1/Data/PubMed/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000503 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd -nk 000503 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= ChloroquineV1
|flux= PubMed
|étape= Curation
|type= RBID
|clé= pubmed:9449382
|texte= Endothelin-converting enzyme: ultrastructural localization and its recycling from the cell surface.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Curation/RBID.i -Sk "pubmed:9449382" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd \
| NlmPubMed2Wicri -a ChloroquineV1
| This area was generated with Dilib version V0.6.33. |  |