A SARS-CoV protein, ORF-6, induces caspase-3 mediated, ER stress and JNK-dependent apoptosis.
Identifieur interne : 001A83 ( PubMed/Curation ); précédent : 001A82; suivant : 001A84A SARS-CoV protein, ORF-6, induces caspase-3 mediated, ER stress and JNK-dependent apoptosis.
Auteurs : Zhongde Ye [République populaire de Chine] ; Chung Kai Wong ; Peng Li ; Yong XieSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2008.
Descripteurs français
- KwdFr :
- Activation enzymatique, Animaux, Apoptose, Caspase-3 (physiologie), Chaperons moléculaires (biosynthèse), Humains, JNK Mitogen-Activated Protein Kinases (antagonistes et inhibiteurs), JNK Mitogen-Activated Protein Kinases (physiologie), Oligopeptides (pharmacologie), Protéines de la matrice virale (antagonistes et inhibiteurs), Protéines de la matrice virale (physiologie), Protéines du choc thermique HSP70 (biosynthèse), Protéines membranaires (biosynthèse), Protéines virales (antagonistes et inhibiteurs), Protéines virales (biosynthèse), Régulation positive, Réticulum endoplasmique (métabolisme).
- MESH :
- antagonistes et inhibiteurs : JNK Mitogen-Activated Protein Kinases, Protéines de la matrice virale, Protéines virales.
- biosynthèse : Chaperons moléculaires, Protéines du choc thermique HSP70, Protéines membranaires, Protéines virales.
- métabolisme : Réticulum endoplasmique.
- pharmacologie : Oligopeptides.
- physiologie : Caspase-3, JNK Mitogen-Activated Protein Kinases, Protéines de la matrice virale.
- Activation enzymatique, Animaux, Apoptose, Humains, Régulation positive.
English descriptors
- KwdEn :
- Animals, Apoptosis, Caspase 3 (physiology), Chlorocebus aethiops, Endoplasmic Reticulum (metabolism), Enzyme Activation, HSP70 Heat-Shock Proteins (biosynthesis), Humans, JNK Mitogen-Activated Protein Kinases (antagonists & inhibitors), JNK Mitogen-Activated Protein Kinases (physiology), Membrane Proteins (biosynthesis), Molecular Chaperones (biosynthesis), Oligopeptides (pharmacology), Up-Regulation, Viral Matrix Proteins (antagonists & inhibitors), Viral Matrix Proteins (physiology), Viral Proteins (antagonists & inhibitors), Viral Proteins (biosynthesis).
- MESH :
- chemical , antagonists & inhibitors : JNK Mitogen-Activated Protein Kinases, Viral Matrix Proteins, Viral Proteins.
- chemical , biosynthesis : HSP70 Heat-Shock Proteins, Membrane Proteins, Molecular Chaperones, Viral Proteins.
- chemical , pharmacology : Oligopeptides.
- chemical , physiology : Caspase 3, JNK Mitogen-Activated Protein Kinases, Viral Matrix Proteins.
- metabolism : Endoplasmic Reticulum.
- Animals, Apoptosis, Chlorocebus aethiops, Enzyme Activation, Humans, Up-Regulation.
Abstract
Severe acute respiratory syndrome (SARS) coronavirus (CoV) spread from China to more than 30 countries, causing severe outbreaks of atypical pneumonia and over 800 deaths worldwide. CoV primarily infects the upper respiratory and gastrointestinal tract; however, SARS-CoV has a unique pathogenesis because it infects both the upper and lower respiratory tracts and leads to human respiratory diseases. SARS-CoV genome has shown containing 14 open reading frames (ORFs) and 8 of them encode novel proteins. Previous reports show that overexpression of ORF-3a, ORF-3b and ORF-7a induce apoptosis. In this report, we demonstrate that overexpression of ORF-6 also induces apoptosis and that Caspase-3 inhibitor and JNK inhibitor block ORF-6 induced apoptosis. Importantly, the protein level of ER chaperon protein, GRP94, was up-regulated when ORF-6 was overexpressed. All these data suggest that ORF-6 induces apoptosis via Caspase-3 mediated, ER stress and JNK-dependent pathways.
DOI: 10.1016/j.bbagen.2008.07.009
PubMed: 18708124
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xml:lang="en"><term>Animals</term><term>Apoptosis</term><term>Caspase 3 (physiology)</term><term>Chlorocebus aethiops</term><term>Endoplasmic Reticulum (metabolism)</term><term>Enzyme Activation</term><term>HSP70 Heat-Shock Proteins (biosynthesis)</term><term>Humans</term><term>JNK Mitogen-Activated Protein Kinases (antagonists & inhibitors)</term><term>JNK Mitogen-Activated Protein Kinases (physiology)</term><term>Membrane Proteins (biosynthesis)</term><term>Molecular Chaperones (biosynthesis)</term><term>Oligopeptides (pharmacology)</term><term>Up-Regulation</term><term>Viral Matrix Proteins (antagonists & inhibitors)</term><term>Viral Matrix Proteins (physiology)</term><term>Viral Proteins (antagonists & inhibitors)</term><term>Viral Proteins (biosynthesis)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique</term><term>Animaux</term><term>Apoptose</term><term>Caspase-3 (physiologie)</term><term>Chaperons moléculaires (biosynthèse)</term><term>Humains</term><term>JNK Mitogen-Activated Protein Kinases (antagonistes et inhibiteurs)</term><term>JNK Mitogen-Activated Protein Kinases (physiologie)</term><term>Oligopeptides (pharmacologie)</term><term>Protéines de la matrice virale (antagonistes et inhibiteurs)</term><term>Protéines de la matrice virale (physiologie)</term><term>Protéines du choc thermique HSP70 (biosynthèse)</term><term>Protéines membranaires (biosynthèse)</term><term>Protéines virales (antagonistes et inhibiteurs)</term><term>Protéines virales (biosynthèse)</term><term>Régulation positive</term><term>Réticulum endoplasmique (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>JNK Mitogen-Activated Protein Kinases</term><term>Viral Matrix Proteins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>HSP70 Heat-Shock Proteins</term><term>Membrane Proteins</term><term>Molecular Chaperones</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Oligopeptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Caspase 3</term><term>JNK Mitogen-Activated Protein Kinases</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>JNK Mitogen-Activated Protein Kinases</term><term>Protéines de la matrice virale</term><term>Protéines virales</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Chaperons moléculaires</term><term>Protéines du choc thermique HSP70</term><term>Protéines membranaires</term><term>Protéines virales</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Endoplasmic Reticulum</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Réticulum endoplasmique</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Oligopeptides</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Caspase-3</term><term>JNK Mitogen-Activated Protein Kinases</term><term>Protéines de la matrice virale</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Apoptosis</term><term>Chlorocebus aethiops</term><term>Enzyme Activation</term><term>Humans</term><term>Up-Regulation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term><term>Animaux</term><term>Apoptose</term><term>Humains</term><term>Régulation positive</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome (SARS) coronavirus (CoV) spread from China to more than 30 countries, causing severe outbreaks of atypical pneumonia and over 800 deaths worldwide. CoV primarily infects the upper respiratory and gastrointestinal tract; however, SARS-CoV has a unique pathogenesis because it infects both the upper and lower respiratory tracts and leads to human respiratory diseases. SARS-CoV genome has shown containing 14 open reading frames (ORFs) and 8 of them encode novel proteins. Previous reports show that overexpression of ORF-3a, ORF-3b and ORF-7a induce apoptosis. In this report, we demonstrate that overexpression of ORF-6 also induces apoptosis and that Caspase-3 inhibitor and JNK inhibitor block ORF-6 induced apoptosis. Importantly, the protein level of ER chaperon protein, GRP94, was up-regulated when ORF-6 was overexpressed. All these data suggest that ORF-6 induces apoptosis via Caspase-3 mediated, ER stress and JNK-dependent pathways.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18708124</PMID><DateCompleted><Year>2009</Year><Month>01</Month><Day>05</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1780</Volume><Issue>12</Issue><PubDate><Year>2008</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim. Biophys. 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In this report, we demonstrate that overexpression of ORF-6 also induces apoptosis and that Caspase-3 inhibitor and JNK inhibitor block ORF-6 induced apoptosis. Importantly, the protein level of ER chaperon protein, GRP94, was up-regulated when ORF-6 was overexpressed. All these data suggest that ORF-6 induces apoptosis via Caspase-3 mediated, ER stress and JNK-dependent pathways.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ye</LastName><ForeName>Zhongde</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>Department of Biology, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong SAR, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wong</LastName><ForeName>Chung Kai</ForeName><Initials>CK</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Peng</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Xie</LastName><ForeName>Yong</ForeName><Initials>Y</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>2008</Year><Month>07</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018840">HSP70 Heat-Shock Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008565">Membrane Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018832">Molecular Chaperones</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009842">Oligopeptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014763">Viral Matrix Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral 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| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |