Proteomic analysis of up-regulated proteins in human promonocyte cells expressing severe acute respiratory syndrome coronavirus 3C-like protease.
Identifieur interne : 001D28 ( PubMed/Checkpoint ); précédent : 001D27; suivant : 001D29Proteomic analysis of up-regulated proteins in human promonocyte cells expressing severe acute respiratory syndrome coronavirus 3C-like protease.
Auteurs : Chien-Chen Lai [Taïwan] ; Ming-Jia Jou ; Shiuan-Yi Huang ; Shih-Wein Li ; Lei Wan ; Fuu-Jen Tsai ; Cheng-Wen LinSource :
- Proteomics [ 1615-9853 ] ; 2007.
Descripteurs français
- KwdFr :
- MESH :
- biosynthèse : Cysteine endopeptidases, Facteur inducteur d'apoptose, Proteasome endopeptidase complex, Protéines virales.
- génétique : Virus du SRAS.
- métabolisme : Monocytes.
- Cellules cultivées, Humains, Protéome, Électrophorèse bidimensionnelle sur gel.
English descriptors
- KwdEn :
- MESH :
- chemical , biosynthesis : Apoptosis Inducing Factor, Cysteine Endopeptidases, Proteasome Endopeptidase Complex, Viral Proteins.
- chemical , chemistry : Proteome.
- genetics : SARS Virus.
- metabolism : Monocytes.
- Cells, Cultured, Electrophoresis, Gel, Two-Dimensional, Humans.
Abstract
The pathogenesis of severe acute respiratory syndrome coronavirus (SARS CoV) is an important issue for treatment and prevention of SARS. Previously, SARS CoV 3C-like protease (3CLpro) has been demonstrated to induce apoptosis via the activation of caspase-3 and caspase-9 (Lin, C. W., Lin, K. H., Hsieh, T. H., Shiu, S. Y. et al., FEMS Immunol. Med. Microbiol. 2006, 46, 375-380). In this study, proteome analysis of the human promonocyte HL-CZ cells expressing SARS CoV 3CLpro was performed using 2-DE and nanoscale capillary LC/ESI quadrupole-TOF MS. Functional classification of identified up-regulated proteins indicated that protein metabolism and modification, particularly in the ubiquitin proteasome pathway, was the main biological process occurring in SARS CoV 3CLpro-expressing cells. Thirty-six percent of identified up-regulated proteins were located in the mitochondria, including apoptosis-inducing factor, ATP synthase beta chain and cytochrome c oxidase. Interestingly, heat shock cognate 71-kDa protein (HSP70), which antagonizes apoptosis-inducing factor was shown to down-regulate and had a 5.29-fold decrease. In addition, confocal image analysis has shown release of mitochondrial apoptogenic apoptosis-inducing factor and cytochrome c into the cytosol. Our results revealed that SARS CoV 3CLpro could be considered to induce mitochondrial-mediated apoptosis. The study provides system-level insights into the interaction of SARS CoV 3CLpro with host cells, which will be helpful in elucidating the molecular basis of SARS CoV pathogenesis.
DOI: 10.1002/pmic.200600459
PubMed: 17407183
Affiliations:
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last="Huang">Shiuan-Yi Huang</name></author><author><name sortKey="Li, Shih Wein" sort="Li, Shih Wein" uniqKey="Li S" first="Shih-Wein" last="Li">Shih-Wein Li</name></author><author><name sortKey="Wan, Lei" sort="Wan, Lei" uniqKey="Wan L" first="Lei" last="Wan">Lei Wan</name></author><author><name sortKey="Tsai, Fuu Jen" sort="Tsai, Fuu Jen" uniqKey="Tsai F" first="Fuu-Jen" last="Tsai">Fuu-Jen Tsai</name></author><author><name sortKey="Lin, Cheng Wen" sort="Lin, Cheng Wen" uniqKey="Lin C" first="Cheng-Wen" last="Lin">Cheng-Wen Lin</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17407183</idno><idno type="pmid">17407183</idno><idno type="doi">10.1002/pmic.200600459</idno><idno type="wicri:Area/PubMed/Corpus">001E54</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001E54</idno><idno type="wicri:Area/PubMed/Curation">001E54</idno><idno 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sortKey="Jou, Ming Jia" sort="Jou, Ming Jia" uniqKey="Jou M" first="Ming-Jia" last="Jou">Ming-Jia Jou</name></author><author><name sortKey="Huang, Shiuan Yi" sort="Huang, Shiuan Yi" uniqKey="Huang S" first="Shiuan-Yi" last="Huang">Shiuan-Yi Huang</name></author><author><name sortKey="Li, Shih Wein" sort="Li, Shih Wein" uniqKey="Li S" first="Shih-Wein" last="Li">Shih-Wein Li</name></author><author><name sortKey="Wan, Lei" sort="Wan, Lei" uniqKey="Wan L" first="Lei" last="Wan">Lei Wan</name></author><author><name sortKey="Tsai, Fuu Jen" sort="Tsai, Fuu Jen" uniqKey="Tsai F" first="Fuu-Jen" last="Tsai">Fuu-Jen Tsai</name></author><author><name sortKey="Lin, Cheng Wen" sort="Lin, Cheng Wen" uniqKey="Lin C" first="Cheng-Wen" last="Lin">Cheng-Wen Lin</name></author></analytic><series><title level="j">Proteomics</title><idno type="ISSN">1615-9853</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Apoptosis Inducing Factor (biosynthesis)</term><term>Cells, Cultured</term><term>Cysteine Endopeptidases (biosynthesis)</term><term>Electrophoresis, Gel, Two-Dimensional</term><term>Humans</term><term>Monocytes (metabolism)</term><term>Proteasome Endopeptidase Complex (biosynthesis)</term><term>Proteome (chemistry)</term><term>SARS Virus (genetics)</term><term>Viral Proteins (biosynthesis)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cellules cultivées</term><term>Cysteine endopeptidases (biosynthèse)</term><term>Facteur inducteur d'apoptose (biosynthèse)</term><term>Humains</term><term>Monocytes (métabolisme)</term><term>Proteasome endopeptidase complex (biosynthèse)</term><term>Protéines virales (biosynthèse)</term><term>Protéome ()</term><term>Virus du SRAS (génétique)</term><term>Électrophorèse bidimensionnelle sur gel</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Apoptosis Inducing Factor</term><term>Cysteine Endopeptidases</term><term>Proteasome Endopeptidase Complex</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Proteome</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Cysteine endopeptidases</term><term>Facteur inducteur d'apoptose</term><term>Proteasome endopeptidase complex</term><term>Protéines virales</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Monocytes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Monocytes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cells, Cultured</term><term>Electrophoresis, Gel, Two-Dimensional</term><term>Humans</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules cultivées</term><term>Humains</term><term>Protéome</term><term>Électrophorèse bidimensionnelle sur gel</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The pathogenesis of severe acute respiratory syndrome coronavirus (SARS CoV) is an important issue for treatment and prevention of SARS. Previously, SARS CoV 3C-like protease (3CLpro) has been demonstrated to induce apoptosis via the activation of caspase-3 and caspase-9 (Lin, C. W., Lin, K. H., Hsieh, T. H., Shiu, S. Y. et al., FEMS Immunol. Med. Microbiol. 2006, 46, 375-380). In this study, proteome analysis of the human promonocyte HL-CZ cells expressing SARS CoV 3CLpro was performed using 2-DE and nanoscale capillary LC/ESI quadrupole-TOF MS. Functional classification of identified up-regulated proteins indicated that protein metabolism and modification, particularly in the ubiquitin proteasome pathway, was the main biological process occurring in SARS CoV 3CLpro-expressing cells. Thirty-six percent of identified up-regulated proteins were located in the mitochondria, including apoptosis-inducing factor, ATP synthase beta chain and cytochrome c oxidase. Interestingly, heat shock cognate 71-kDa protein (HSP70), which antagonizes apoptosis-inducing factor was shown to down-regulate and had a 5.29-fold decrease. In addition, confocal image analysis has shown release of mitochondrial apoptogenic apoptosis-inducing factor and cytochrome c into the cytosol. Our results revealed that SARS CoV 3CLpro could be considered to induce mitochondrial-mediated apoptosis. The study provides system-level insights into the interaction of SARS CoV 3CLpro with host cells, which will be helpful in elucidating the molecular basis of SARS CoV pathogenesis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17407183</PMID><DateCompleted><Year>2007</Year><Month>07</Month><Day>25</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>25</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1615-9853</ISSN><JournalIssue CitedMedium="Print"><Volume>7</Volume><Issue>9</Issue><PubDate><Year>2007</Year><Month>May</Month></PubDate></JournalIssue><Title>Proteomics</Title><ISOAbbreviation>Proteomics</ISOAbbreviation></Journal><ArticleTitle>Proteomic analysis of up-regulated proteins in human promonocyte cells expressing severe acute respiratory syndrome coronavirus 3C-like protease.</ArticleTitle><Pagination><MedlinePgn>1446-60</MedlinePgn></Pagination><Abstract><AbstractText>The pathogenesis of severe acute respiratory syndrome coronavirus (SARS CoV) is an important issue for treatment and prevention of SARS. Previously, SARS CoV 3C-like protease (3CLpro) has been demonstrated to induce apoptosis via the activation of caspase-3 and caspase-9 (Lin, C. W., Lin, K. H., Hsieh, T. H., Shiu, S. Y. et al., FEMS Immunol. Med. Microbiol. 2006, 46, 375-380). In this study, proteome analysis of the human promonocyte HL-CZ cells expressing SARS CoV 3CLpro was performed using 2-DE and nanoscale capillary LC/ESI quadrupole-TOF MS. Functional classification of identified up-regulated proteins indicated that protein metabolism and modification, particularly in the ubiquitin proteasome pathway, was the main biological process occurring in SARS CoV 3CLpro-expressing cells. Thirty-six percent of identified up-regulated proteins were located in the mitochondria, including apoptosis-inducing factor, ATP synthase beta chain and cytochrome c oxidase. Interestingly, heat shock cognate 71-kDa protein (HSP70), which antagonizes apoptosis-inducing factor was shown to down-regulate and had a 5.29-fold decrease. In addition, confocal image analysis has shown release of mitochondrial apoptogenic apoptosis-inducing factor and cytochrome c into the cytosol. Our results revealed that SARS CoV 3CLpro could be considered to induce mitochondrial-mediated apoptosis. The study provides system-level insights into the interaction of SARS CoV 3CLpro with host cells, which will be helpful in elucidating the molecular basis of SARS CoV pathogenesis.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lai</LastName><ForeName>Chien-Chen</ForeName><Initials>CC</Initials><AffiliationInfo><Affiliation>Department of Medical Genetics and Medical Research, China Medical University Hospital, Taichung, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jou</LastName><ForeName>Ming-Jia</ForeName><Initials>MJ</Initials></Author><Author ValidYN="Y"><LastName>Huang</LastName><ForeName>Shiuan-Yi</ForeName><Initials>SY</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Shih-Wein</ForeName><Initials>SW</Initials></Author><Author ValidYN="Y"><LastName>Wan</LastName><ForeName>Lei</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Tsai</LastName><ForeName>Fuu-Jen</ForeName><Initials>FJ</Initials></Author><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>Cheng-Wen</ForeName><Initials>CW</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>Germany</Country><MedlineTA>Proteomics</MedlineTA><NlmUniqueID>101092707</NlmUniqueID><ISSNLinking>1615-9853</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051033">Apoptosis Inducing Factor</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020543">Proteome</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral 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Virus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>4</Month><Day>5</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>7</Month><Day>26</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>4</Month><Day>5</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17407183</ArticleId><ArticleId IdType="doi">10.1002/pmic.200600459</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Taïwan</li></country></list><tree><noCountry><name sortKey="Huang, Shiuan Yi" sort="Huang, Shiuan Yi" uniqKey="Huang S" first="Shiuan-Yi" last="Huang">Shiuan-Yi Huang</name><name sortKey="Jou, Ming Jia" sort="Jou, Ming Jia" uniqKey="Jou M" first="Ming-Jia" last="Jou">Ming-Jia Jou</name><name sortKey="Li, Shih Wein" sort="Li, Shih Wein" uniqKey="Li S" first="Shih-Wein" last="Li">Shih-Wein Li</name><name sortKey="Lin, Cheng Wen" sort="Lin, Cheng Wen" uniqKey="Lin C" first="Cheng-Wen" last="Lin">Cheng-Wen Lin</name><name sortKey="Tsai, Fuu Jen" sort="Tsai, Fuu Jen" uniqKey="Tsai F" first="Fuu-Jen" last="Tsai">Fuu-Jen Tsai</name><name sortKey="Wan, Lei" sort="Wan, Lei" uniqKey="Wan L" first="Lei" last="Wan">Lei Wan</name></noCountry><country name="Taïwan"><noRegion><name sortKey="Lai, Chien Chen" sort="Lai, Chien Chen" uniqKey="Lai C" first="Chien-Chen" last="Lai">Chien-Chen Lai</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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