Tumor necrosis factor-alpha convertase (ADAM17) mediates regulated ectodomain shedding of the severe-acute respiratory syndrome-coronavirus (SARS-CoV) receptor, angiotensin-converting enzyme-2 (ACE2).
Identifieur interne : 002668 ( PubMed/Corpus ); précédent : 002667; suivant : 002669Tumor necrosis factor-alpha convertase (ADAM17) mediates regulated ectodomain shedding of the severe-acute respiratory syndrome-coronavirus (SARS-CoV) receptor, angiotensin-converting enzyme-2 (ACE2).
Auteurs : Daniel W. Lambert ; Mike Yarski ; Fiona J. Warner ; Paul Thornhill ; Edward T. Parkin ; A Ian Smith ; Nigel M. Hooper ; Anthony J. TurnerSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2005.
English descriptors
- KwdEn :
- ADAM Proteins, ADAM17 Protein, Amyloid Precursor Protein Secretases, Aspartic Acid Endopeptidases (metabolism), Binding Sites, Carboxypeptidases (metabolism), Cell Line, Cytoplasm (metabolism), DNA, Complementary (metabolism), Disintegrins (metabolism), Electrophoresis, Polyacrylamide Gel, Endopeptidases, Humans, Immunoblotting, Membrane Proteins (metabolism), Metalloendopeptidases (chemistry), Metalloendopeptidases (metabolism), Metalloendopeptidases (physiology), Peptide Hydrolases (metabolism), Peptides (chemistry), Peptidyl-Dipeptidase A, Phorbol Esters, Plasmids (metabolism), Protein Binding, Protein Isoforms (chemistry), Protein Structure, Tertiary, RNA (chemistry), RNA, Double-Stranded (chemistry), RNA, Small Interfering (metabolism), SARS Virus (metabolism), Time Factors, Transfection.
- MESH :
- chemical , chemistry : Metalloendopeptidases, Peptides, Protein Isoforms, RNA, RNA, Double-Stranded.
- chemical , metabolism : Aspartic Acid Endopeptidases, Carboxypeptidases, DNA, Complementary, Disintegrins, Membrane Proteins, Metalloendopeptidases, Peptide Hydrolases, RNA, Small Interfering.
- chemical , physiology : Metalloendopeptidases.
- chemical : ADAM Proteins, ADAM17 Protein, Amyloid Precursor Protein Secretases, Endopeptidases, Peptidyl-Dipeptidase A, Phorbol Esters.
- metabolism : Cytoplasm, Plasmids, SARS Virus.
- Binding Sites, Cell Line, Electrophoresis, Polyacrylamide Gel, Humans, Immunoblotting, Protein Binding, Protein Structure, Tertiary, Time Factors, Transfection.
Abstract
Angiotensin-converting enzyme-2 (ACE2) is a critical regulator of heart function and a cellular receptor for the causative agent of severe-acute respiratory syndrome (SARS), SARS-CoV (coronavirus). ACE2 is a type I transmembrane protein, with an extracellular N-terminal domain containing the active site and a short intracellular C-terminal tail. A soluble form of ACE2, lacking its cytosolic and transmembrane domains, has been shown to block binding of the SARS-CoV spike protein to its receptor. In this study, we examined the ability of ACE2 to undergo proteolytic shedding and investigated the mechanisms responsible for this shedding event. We demonstrated that ACE2, heterologously expressed in HEK293 cells and endogenously expressed in Huh7 cells, undergoes metalloproteinase-mediated, phorbol ester-inducible ectodomain shedding. By using inhibitors with differing potency toward different members of the ADAM (a disintegrin and metalloproteinase) family of proteases, we identified ADAM17 as a candidate mediator of stimulated ACE2 shedding. Furthermore, ablation of ADAM17 expression using specific small interfering RNA duplexes reduced regulated ACE2 shedding, whereas overexpression of ADAM17 significantly increased shedding. Taken together, these data provided direct evidence for the involvement of ADAM17 in the regulated ectodomain shedding of ACE2. The identification of ADAM17 as the protease responsible for ACE2 shedding may provide new insight into the physiological roles of ACE2.
DOI: 10.1074/jbc.M505111200
PubMed: 15983030
Links to Exploration step
pubmed:15983030Le document en format XML
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Warner</name></author><author><name sortKey="Thornhill, Paul" sort="Thornhill, Paul" uniqKey="Thornhill P" first="Paul" last="Thornhill">Paul Thornhill</name></author><author><name sortKey="Parkin, Edward T" sort="Parkin, Edward T" uniqKey="Parkin E" first="Edward T" last="Parkin">Edward T. Parkin</name></author><author><name sortKey="Smith, A Ian" sort="Smith, A Ian" uniqKey="Smith A" first="A Ian" last="Smith">A Ian Smith</name></author><author><name sortKey="Hooper, Nigel M" sort="Hooper, Nigel M" uniqKey="Hooper N" first="Nigel M" last="Hooper">Nigel M. Hooper</name></author><author><name sortKey="Turner, Anthony J" sort="Turner, Anthony J" uniqKey="Turner A" first="Anthony J" last="Turner">Anthony J. Turner</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:15983030</idno><idno type="pmid">15983030</idno><idno type="doi">10.1074/jbc.M505111200</idno><idno type="wicri:Area/PubMed/Corpus">002668</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002668</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Tumor necrosis factor-alpha convertase (ADAM17) mediates regulated ectodomain shedding of the severe-acute respiratory syndrome-coronavirus (SARS-CoV) receptor, angiotensin-converting enzyme-2 (ACE2).</title><author><name sortKey="Lambert, Daniel W" sort="Lambert, Daniel W" uniqKey="Lambert D" first="Daniel W" last="Lambert">Daniel W. Lambert</name><affiliation><nlm:affiliation>Proteolysis Research Group, School of Biochemistry and Microbiology, University of Leeds, Leeds LS2 9JT, United Kingdom. d.w.lambert@leeds.ac.uk</nlm:affiliation></affiliation></author><author><name sortKey="Yarski, Mike" sort="Yarski, Mike" uniqKey="Yarski M" first="Mike" last="Yarski">Mike Yarski</name></author><author><name sortKey="Warner, Fiona J" sort="Warner, Fiona J" uniqKey="Warner F" first="Fiona J" last="Warner">Fiona J. Warner</name></author><author><name sortKey="Thornhill, Paul" sort="Thornhill, Paul" uniqKey="Thornhill P" first="Paul" last="Thornhill">Paul Thornhill</name></author><author><name sortKey="Parkin, Edward T" sort="Parkin, Edward T" uniqKey="Parkin E" first="Edward T" last="Parkin">Edward T. Parkin</name></author><author><name sortKey="Smith, A Ian" sort="Smith, A Ian" uniqKey="Smith A" first="A Ian" last="Smith">A Ian Smith</name></author><author><name sortKey="Hooper, Nigel M" sort="Hooper, Nigel M" uniqKey="Hooper N" first="Nigel M" last="Hooper">Nigel M. Hooper</name></author><author><name sortKey="Turner, Anthony J" sort="Turner, Anthony J" uniqKey="Turner A" first="Anthony J" last="Turner">Anthony J. Turner</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>ADAM Proteins</term><term>ADAM17 Protein</term><term>Amyloid Precursor Protein Secretases</term><term>Aspartic Acid Endopeptidases (metabolism)</term><term>Binding Sites</term><term>Carboxypeptidases (metabolism)</term><term>Cell Line</term><term>Cytoplasm (metabolism)</term><term>DNA, Complementary (metabolism)</term><term>Disintegrins (metabolism)</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Endopeptidases</term><term>Humans</term><term>Immunoblotting</term><term>Membrane Proteins (metabolism)</term><term>Metalloendopeptidases (chemistry)</term><term>Metalloendopeptidases (metabolism)</term><term>Metalloendopeptidases (physiology)</term><term>Peptide Hydrolases (metabolism)</term><term>Peptides (chemistry)</term><term>Peptidyl-Dipeptidase A</term><term>Phorbol Esters</term><term>Plasmids (metabolism)</term><term>Protein Binding</term><term>Protein Isoforms (chemistry)</term><term>Protein Structure, Tertiary</term><term>RNA (chemistry)</term><term>RNA, Double-Stranded (chemistry)</term><term>RNA, Small Interfering (metabolism)</term><term>SARS Virus (metabolism)</term><term>Time Factors</term><term>Transfection</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Metalloendopeptidases</term><term>Peptides</term><term>Protein Isoforms</term><term>RNA</term><term>RNA, Double-Stranded</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Aspartic Acid Endopeptidases</term><term>Carboxypeptidases</term><term>DNA, Complementary</term><term>Disintegrins</term><term>Membrane Proteins</term><term>Metalloendopeptidases</term><term>Peptide Hydrolases</term><term>RNA, Small Interfering</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Metalloendopeptidases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>ADAM Proteins</term><term>ADAM17 Protein</term><term>Amyloid Precursor Protein Secretases</term><term>Endopeptidases</term><term>Peptidyl-Dipeptidase A</term><term>Phorbol Esters</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cytoplasm</term><term>Plasmids</term><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Cell Line</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Humans</term><term>Immunoblotting</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Time Factors</term><term>Transfection</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Angiotensin-converting enzyme-2 (ACE2) is a critical regulator of heart function and a cellular receptor for the causative agent of severe-acute respiratory syndrome (SARS), SARS-CoV (coronavirus). ACE2 is a type I transmembrane protein, with an extracellular N-terminal domain containing the active site and a short intracellular C-terminal tail. A soluble form of ACE2, lacking its cytosolic and transmembrane domains, has been shown to block binding of the SARS-CoV spike protein to its receptor. In this study, we examined the ability of ACE2 to undergo proteolytic shedding and investigated the mechanisms responsible for this shedding event. We demonstrated that ACE2, heterologously expressed in HEK293 cells and endogenously expressed in Huh7 cells, undergoes metalloproteinase-mediated, phorbol ester-inducible ectodomain shedding. By using inhibitors with differing potency toward different members of the ADAM (a disintegrin and metalloproteinase) family of proteases, we identified ADAM17 as a candidate mediator of stimulated ACE2 shedding. Furthermore, ablation of ADAM17 expression using specific small interfering RNA duplexes reduced regulated ACE2 shedding, whereas overexpression of ADAM17 significantly increased shedding. Taken together, these data provided direct evidence for the involvement of ADAM17 in the regulated ectodomain shedding of ACE2. The identification of ADAM17 as the protease responsible for ACE2 shedding may provide new insight into the physiological roles of ACE2.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15983030</PMID><DateCompleted><Year>2005</Year><Month>10</Month><Day>03</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>24</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>280</Volume><Issue>34</Issue><PubDate><Year>2005</Year><Month>Aug</Month><Day>26</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>Tumor necrosis factor-alpha convertase (ADAM17) mediates regulated ectodomain shedding of the severe-acute respiratory syndrome-coronavirus (SARS-CoV) receptor, angiotensin-converting enzyme-2 (ACE2).</ArticleTitle><Pagination><MedlinePgn>30113-9</MedlinePgn></Pagination><Abstract><AbstractText>Angiotensin-converting enzyme-2 (ACE2) is a critical regulator of heart function and a cellular receptor for the causative agent of severe-acute respiratory syndrome (SARS), SARS-CoV (coronavirus). ACE2 is a type I transmembrane protein, with an extracellular N-terminal domain containing the active site and a short intracellular C-terminal tail. A soluble form of ACE2, lacking its cytosolic and transmembrane domains, has been shown to block binding of the SARS-CoV spike protein to its receptor. In this study, we examined the ability of ACE2 to undergo proteolytic shedding and investigated the mechanisms responsible for this shedding event. We demonstrated that ACE2, heterologously expressed in HEK293 cells and endogenously expressed in Huh7 cells, undergoes metalloproteinase-mediated, phorbol ester-inducible ectodomain shedding. By using inhibitors with differing potency toward different members of the ADAM (a disintegrin and metalloproteinase) family of proteases, we identified ADAM17 as a candidate mediator of stimulated ACE2 shedding. Furthermore, ablation of ADAM17 expression using specific small interfering RNA duplexes reduced regulated ACE2 shedding, whereas overexpression of ADAM17 significantly increased shedding. Taken together, these data provided direct evidence for the involvement of ADAM17 in the regulated ectodomain shedding of ACE2. The identification of ADAM17 as the protease responsible for ACE2 shedding may provide new insight into the physiological roles of ACE2.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lambert</LastName><ForeName>Daniel W</ForeName><Initials>DW</Initials><AffiliationInfo><Affiliation>Proteolysis Research Group, School of Biochemistry and Microbiology, University of Leeds, Leeds LS2 9JT, United Kingdom. d.w.lambert@leeds.ac.uk</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yarski</LastName><ForeName>Mike</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Warner</LastName><ForeName>Fiona J</ForeName><Initials>FJ</Initials></Author><Author ValidYN="Y"><LastName>Thornhill</LastName><ForeName>Paul</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Parkin</LastName><ForeName>Edward T</ForeName><Initials>ET</Initials></Author><Author ValidYN="Y"><LastName>Smith</LastName><ForeName>A Ian</ForeName><Initials>AI</Initials></Author><Author ValidYN="Y"><LastName>Hooper</LastName><ForeName>Nigel M</ForeName><Initials>NM</Initials></Author><Author ValidYN="Y"><LastName>Turner</LastName><ForeName>Anthony 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><ArticleDate DateType="Electronic"><Year>2005</Year><Month>06</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019483">Disintegrins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008565">Membrane Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010703">Phorbol Esters</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020033">Protein Isoforms</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012330">RNA, Double-Stranded</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D034741">RNA, Small Interfering</NameOfSubstance></Chemical><Chemical><RegistryNumber>63231-63-0</RegistryNumber><NameOfSubstance UI="D012313">RNA</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D053829">Amyloid Precursor Protein Secretases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D002268">Carboxypeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D010450">Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D010447">Peptide Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.15.1</RegistryNumber><NameOfSubstance UI="D007703">Peptidyl-Dipeptidase A</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.17.-</RegistryNumber><NameOfSubstance UI="C413524">angiotensin converting enzyme 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.23.-</RegistryNumber><NameOfSubstance UI="D016282">Aspartic Acid Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.23.46</RegistryNumber><NameOfSubstance UI="C509280">BACE1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.24.-</RegistryNumber><NameOfSubstance UI="D051722">ADAM Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.24.-</RegistryNumber><NameOfSubstance UI="C098339">ADAM9 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.24.-</RegistryNumber><NameOfSubstance UI="D008666">Metalloendopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.24.86</RegistryNumber><NameOfSubstance UI="D000072198">ADAM17 Protein</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.24.86</RegistryNumber><NameOfSubstance UI="C000606462">ADAM17 protein, human</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D051722" MajorTopicYN="N">ADAM Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000072198" MajorTopicYN="N">ADAM17 Protein</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053829" MajorTopicYN="N">Amyloid Precursor Protein 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MajorTopicYN="N">Disintegrins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010450" MajorTopicYN="N">Endopeptidases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015151" MajorTopicYN="N">Immunoblotting</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008565" MajorTopicYN="N">Membrane Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008666" MajorTopicYN="N">Metalloendopeptidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName 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Isoforms</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012313" MajorTopicYN="N">RNA</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012330" MajorTopicYN="N">RNA, Double-Stranded</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D034741" MajorTopicYN="N">RNA, Small Interfering</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013997" MajorTopicYN="N">Time 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