SARS coronavirus papain-like protease induces Egr-1-dependent up-regulation of TGF-β1 via ROS/p38 MAPK/STAT3 pathway.
Identifieur interne : 000C52 ( PubMed/Corpus ); précédent : 000C51; suivant : 000C53SARS coronavirus papain-like protease induces Egr-1-dependent up-regulation of TGF-β1 via ROS/p38 MAPK/STAT3 pathway.
Auteurs : Shih-Wein Li ; Ching-Ying Wang ; Yu-Jen Jou ; Tsuey-Ching Yang ; Su-Hua Huang ; Lei Wan ; Ying-Ju Lin ; Cheng-Wen LinSource :
- Scientific reports [ 2045-2322 ] ; 2016.
English descriptors
- KwdEn :
- A549 Cells, Animals, Disease Models, Animal, Early Growth Response Protein 1 (metabolism), Epithelial Cells (metabolism), Fibrosis, Gene Silencing (drug effects), Glial Fibrillary Acidic Protein (metabolism), Humans, Lung (cytology), Mice, Inbred BALB C, Models, Biological, NF-kappa B (metabolism), Papain (pharmacology), Promoter Regions, Genetic (genetics), RNA, Messenger (genetics), RNA, Messenger (metabolism), RNA, Small Interfering (metabolism), Reactive Oxygen Species (metabolism), SARS Virus (enzymology), STAT3 Transcription Factor (metabolism), Signal Transduction (drug effects), Sp1 Transcription Factor (metabolism), Thrombospondin 1 (metabolism), Transforming Growth Factor beta1 (biosynthesis), Transforming Growth Factor beta1 (genetics), Transforming Growth Factor beta1 (metabolism), Up-Regulation (drug effects), Vimentin (metabolism), p38 Mitogen-Activated Protein Kinases (metabolism).
- MESH :
- chemical , biosynthesis : Transforming Growth Factor beta1.
- chemical , genetics : RNA, Messenger, Transforming Growth Factor beta1.
- chemical , metabolism : Early Growth Response Protein 1, Glial Fibrillary Acidic Protein, NF-kappa B, RNA, Messenger, RNA, Small Interfering, Reactive Oxygen Species, STAT3 Transcription Factor, Sp1 Transcription Factor, Thrombospondin 1, Transforming Growth Factor beta1, Vimentin, p38 Mitogen-Activated Protein Kinases.
- cytology : Lung.
- drug effects : Gene Silencing, Signal Transduction, Up-Regulation.
- enzymology : SARS Virus.
- genetics : Promoter Regions, Genetic.
- metabolism : Epithelial Cells.
- chemical , pharmacology : Papain.
- A549 Cells, Animals, Disease Models, Animal, Fibrosis, Humans, Mice, Inbred BALB C, Models, Biological.
Abstract
SARS coronavirus (SARS-CoV) papain-like protease (PLpro) has been identified in TGF-β1 up-regulation in human promonocytes (Proteomics 2012, 12: 3193-205). This study investigates the mechanisms of SARS-CoV PLpro-induced TGF-β1 promoter activation in human lung epithelial cells and mouse models. SARS-CoV PLpro dose- and time-dependently up-regulates TGF-β1 and vimentin in A549 cells. Dual luciferase reporter assays with TGF-β1 promoter plasmids indicated that TGF-β1 promoter region between -175 to -60, the Egr-1 binding site, was responsible for TGF-β1 promoter activation induced by SARS-CoV PLpro. Subcellular localization analysis of transcription factors showed PLpro triggering nuclear translocation of Egr-1, but not NF-κB and Sp-1. Meanwhile, Egr-1 silencing by siRNA significantly reduced PLpro-induced up-regulation of TGF-β1, TSP-1 and pro-fibrotic genes. Furthermore, the inhibitors for ROS (YCG063), p38 MAPK (SB203580), and STAT3 (Stattic) revealed ROS/p38 MAPK/STAT3 pathway involving in Egr-1 dependent activation of TGF-β1 promoter induced by PLpro. In a mouse model with a direct pulmonary injection, PLpro stimulated macrophage infiltration into lung, up-regulating Egr-1, TSP-1, TGF-β1 and vimentin expression in lung tissues. The results revealed that SARS-CoV PLpro significantly triggered Egr-1 dependent activation of TGF-β1 promoter via ROS/p38 MAPK/STAT3 pathway, correlating with up-regulation of pro-fibrotic responses in vitro and in vivo.
DOI: 10.1038/srep25754
PubMed: 27173006
Links to Exploration step
pubmed:27173006Le document en format XML
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China Medical University, Taichung, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, Tsuey Ching" sort="Yang, Tsuey Ching" uniqKey="Yang T" first="Tsuey-Ching" last="Yang">Tsuey-Ching Yang</name><affiliation><nlm:affiliation>Department of Biotechnology and Laboratory Science in Medicine, National Yang Ming University, Taipei, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Huang, Su Hua" sort="Huang, Su Hua" uniqKey="Huang S" first="Su-Hua" last="Huang">Su-Hua Huang</name><affiliation><nlm:affiliation>Department of Biotechnology, Asia University, Wufeng, Taichung, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Wan, Lei" sort="Wan, Lei" uniqKey="Wan L" first="Lei" last="Wan">Lei Wan</name><affiliation><nlm:affiliation>Department of Medical Genetics and Medical Research, China Medical University Hospital, Taichung, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Lin, Ying Ju" sort="Lin, Ying Ju" uniqKey="Lin Y" first="Ying-Ju" last="Lin">Ying-Ju Lin</name><affiliation><nlm:affiliation>Department of Medical Genetics and Medical Research, China Medical University Hospital, Taichung, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Lin, Cheng Wen" sort="Lin, Cheng Wen" uniqKey="Lin C" first="Cheng-Wen" last="Lin">Cheng-Wen Lin</name><affiliation><nlm:affiliation>Department of Medical Laboratory Science and Biotechnology, China Medical University, Taichung, Taiwan.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2016">2016</date><idno type="RBID">pubmed:27173006</idno><idno type="pmid">27173006</idno><idno type="doi">10.1038/srep25754</idno><idno type="wicri:Area/PubMed/Corpus">000C52</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000C52</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">SARS coronavirus papain-like protease induces Egr-1-dependent up-regulation of TGF-β1 via ROS/p38 MAPK/STAT3 pathway.</title><author><name sortKey="Li, Shih Wein" sort="Li, Shih Wein" uniqKey="Li S" first="Shih-Wein" last="Li">Shih-Wein Li</name><affiliation><nlm:affiliation>Department of Medical Laboratory Science and Biotechnology, China Medical University, Taichung, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Wang, Ching Ying" sort="Wang, Ching Ying" uniqKey="Wang C" first="Ching-Ying" last="Wang">Ching-Ying Wang</name><affiliation><nlm:affiliation>Department of Medical Laboratory Science and Biotechnology, China Medical University, Taichung, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Jou, Yu Jen" sort="Jou, Yu Jen" uniqKey="Jou Y" first="Yu-Jen" last="Jou">Yu-Jen Jou</name><affiliation><nlm:affiliation>Department of Medical Laboratory Science and Biotechnology, China Medical University, Taichung, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, Tsuey Ching" sort="Yang, Tsuey Ching" uniqKey="Yang T" first="Tsuey-Ching" last="Yang">Tsuey-Ching Yang</name><affiliation><nlm:affiliation>Department of Biotechnology and Laboratory Science in Medicine, National Yang Ming University, Taipei, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Huang, Su Hua" sort="Huang, Su Hua" uniqKey="Huang S" first="Su-Hua" last="Huang">Su-Hua Huang</name><affiliation><nlm:affiliation>Department of Biotechnology, Asia University, Wufeng, Taichung, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Wan, Lei" sort="Wan, Lei" uniqKey="Wan L" first="Lei" last="Wan">Lei Wan</name><affiliation><nlm:affiliation>Department of Medical Genetics and Medical Research, China Medical University Hospital, Taichung, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Lin, Ying Ju" sort="Lin, Ying Ju" uniqKey="Lin Y" first="Ying-Ju" last="Lin">Ying-Ju Lin</name><affiliation><nlm:affiliation>Department of Medical Genetics and Medical Research, China Medical University Hospital, Taichung, Taiwan.</nlm:affiliation></affiliation></author><author><name sortKey="Lin, Cheng Wen" sort="Lin, Cheng Wen" uniqKey="Lin C" first="Cheng-Wen" last="Lin">Cheng-Wen Lin</name><affiliation><nlm:affiliation>Department of Medical Laboratory Science and Biotechnology, China Medical University, Taichung, Taiwan.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Scientific reports</title><idno type="eISSN">2045-2322</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>A549 Cells</term><term>Animals</term><term>Disease Models, Animal</term><term>Early Growth Response Protein 1 (metabolism)</term><term>Epithelial Cells (metabolism)</term><term>Fibrosis</term><term>Gene Silencing (drug effects)</term><term>Glial Fibrillary Acidic Protein (metabolism)</term><term>Humans</term><term>Lung (cytology)</term><term>Mice, Inbred BALB C</term><term>Models, Biological</term><term>NF-kappa B (metabolism)</term><term>Papain (pharmacology)</term><term>Promoter Regions, Genetic (genetics)</term><term>RNA, Messenger (genetics)</term><term>RNA, Messenger (metabolism)</term><term>RNA, Small Interfering (metabolism)</term><term>Reactive Oxygen Species (metabolism)</term><term>SARS Virus (enzymology)</term><term>STAT3 Transcription Factor (metabolism)</term><term>Signal Transduction (drug effects)</term><term>Sp1 Transcription Factor (metabolism)</term><term>Thrombospondin 1 (metabolism)</term><term>Transforming Growth Factor beta1 (biosynthesis)</term><term>Transforming Growth Factor beta1 (genetics)</term><term>Transforming Growth Factor beta1 (metabolism)</term><term>Up-Regulation (drug effects)</term><term>Vimentin (metabolism)</term><term>p38 Mitogen-Activated Protein Kinases (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Transforming Growth Factor beta1</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>RNA, Messenger</term><term>Transforming Growth Factor beta1</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Early Growth Response Protein 1</term><term>Glial Fibrillary Acidic Protein</term><term>NF-kappa B</term><term>RNA, Messenger</term><term>RNA, Small Interfering</term><term>Reactive Oxygen Species</term><term>STAT3 Transcription Factor</term><term>Sp1 Transcription Factor</term><term>Thrombospondin 1</term><term>Transforming Growth Factor beta1</term><term>Vimentin</term><term>p38 Mitogen-Activated Protein Kinases</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Lung</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Gene Silencing</term><term>Signal Transduction</term><term>Up-Regulation</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Promoter Regions, Genetic</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Epithelial Cells</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Papain</term></keywords><keywords scheme="MESH" xml:lang="en"><term>A549 Cells</term><term>Animals</term><term>Disease Models, Animal</term><term>Fibrosis</term><term>Humans</term><term>Mice, Inbred BALB C</term><term>Models, Biological</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">SARS coronavirus (SARS-CoV) papain-like protease (PLpro) has been identified in TGF-β1 up-regulation in human promonocytes (Proteomics 2012, 12: 3193-205). This study investigates the mechanisms of SARS-CoV PLpro-induced TGF-β1 promoter activation in human lung epithelial cells and mouse models. SARS-CoV PLpro dose- and time-dependently up-regulates TGF-β1 and vimentin in A549 cells. Dual luciferase reporter assays with TGF-β1 promoter plasmids indicated that TGF-β1 promoter region between -175 to -60, the Egr-1 binding site, was responsible for TGF-β1 promoter activation induced by SARS-CoV PLpro. Subcellular localization analysis of transcription factors showed PLpro triggering nuclear translocation of Egr-1, but not NF-κB and Sp-1. Meanwhile, Egr-1 silencing by siRNA significantly reduced PLpro-induced up-regulation of TGF-β1, TSP-1 and pro-fibrotic genes. Furthermore, the inhibitors for ROS (YCG063), p38 MAPK (SB203580), and STAT3 (Stattic) revealed ROS/p38 MAPK/STAT3 pathway involving in Egr-1 dependent activation of TGF-β1 promoter induced by PLpro. In a mouse model with a direct pulmonary injection, PLpro stimulated macrophage infiltration into lung, up-regulating Egr-1, TSP-1, TGF-β1 and vimentin expression in lung tissues. The results revealed that SARS-CoV PLpro significantly triggered Egr-1 dependent activation of TGF-β1 promoter via ROS/p38 MAPK/STAT3 pathway, correlating with up-regulation of pro-fibrotic responses in vitro and in vivo.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27173006</PMID><DateCompleted><Year>2018</Year><Month>03</Month><Day>26</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2045-2322</ISSN><JournalIssue CitedMedium="Internet"><Volume>6</Volume><PubDate><Year>2016</Year><Month>05</Month><Day>13</Day></PubDate></JournalIssue><Title>Scientific reports</Title><ISOAbbreviation>Sci Rep</ISOAbbreviation></Journal><ArticleTitle>SARS coronavirus papain-like protease induces Egr-1-dependent up-regulation of TGF-β1 via ROS/p38 MAPK/STAT3 pathway.</ArticleTitle><Pagination><MedlinePgn>25754</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/srep25754</ELocationID><Abstract><AbstractText>SARS coronavirus (SARS-CoV) papain-like protease (PLpro) has been identified in TGF-β1 up-regulation in human promonocytes (Proteomics 2012, 12: 3193-205). This study investigates the mechanisms of SARS-CoV PLpro-induced TGF-β1 promoter activation in human lung epithelial cells and mouse models. SARS-CoV PLpro dose- and time-dependently up-regulates TGF-β1 and vimentin in A549 cells. Dual luciferase reporter assays with TGF-β1 promoter plasmids indicated that TGF-β1 promoter region between -175 to -60, the Egr-1 binding site, was responsible for TGF-β1 promoter activation induced by SARS-CoV PLpro. Subcellular localization analysis of transcription factors showed PLpro triggering nuclear translocation of Egr-1, but not NF-κB and Sp-1. Meanwhile, Egr-1 silencing by siRNA significantly reduced PLpro-induced up-regulation of TGF-β1, TSP-1 and pro-fibrotic genes. Furthermore, the inhibitors for ROS (YCG063), p38 MAPK (SB203580), and STAT3 (Stattic) revealed ROS/p38 MAPK/STAT3 pathway involving in Egr-1 dependent activation of TGF-β1 promoter induced by PLpro. In a mouse model with a direct pulmonary injection, PLpro stimulated macrophage infiltration into lung, up-regulating Egr-1, TSP-1, TGF-β1 and vimentin expression in lung tissues. The results revealed that SARS-CoV PLpro significantly triggered Egr-1 dependent activation of TGF-β1 promoter via ROS/p38 MAPK/STAT3 pathway, correlating with up-regulation of pro-fibrotic responses in vitro and in vivo.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Shih-Wein</ForeName><Initials>SW</Initials><AffiliationInfo><Affiliation>Department of Medical Laboratory Science and Biotechnology, China Medical University, Taichung, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Ching-Ying</ForeName><Initials>CY</Initials><AffiliationInfo><Affiliation>Department of Medical Laboratory Science and Biotechnology, China Medical University, Taichung, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jou</LastName><ForeName>Yu-Jen</ForeName><Initials>YJ</Initials><AffiliationInfo><Affiliation>Department of Medical Laboratory Science and Biotechnology, China Medical University, Taichung, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Tsuey-Ching</ForeName><Initials>TC</Initials><AffiliationInfo><Affiliation>Department of Biotechnology and Laboratory Science in Medicine, National Yang Ming University, Taipei, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Huang</LastName><ForeName>Su-Hua</ForeName><Initials>SH</Initials><AffiliationInfo><Affiliation>Department of Biotechnology, Asia University, Wufeng, Taichung, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wan</LastName><ForeName>Lei</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Medical Genetics and Medical Research, China Medical University Hospital, Taichung, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>Ying-Ju</ForeName><Initials>YJ</Initials><AffiliationInfo><Affiliation>Department of Medical Genetics and Medical Research, China Medical University Hospital, Taichung, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>Cheng-Wen</ForeName><Initials>CW</Initials><AffiliationInfo><Affiliation>Department of Medical Laboratory Science and Biotechnology, China Medical University, Taichung, Taiwan.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Biotechnology, Asia University, Wufeng, Taichung, Taiwan.</Affiliation></AffiliationInfo></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>2016</Year><Month>05</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Sci Rep</MedlineTA><NlmUniqueID>101563288</NlmUniqueID><ISSNLinking>2045-2322</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C497325">EGR1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051766">Early Growth Response Protein 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005904">Glial Fibrillary Acidic Protein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016328">NF-kappa B</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012333">RNA, Messenger</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D034741">RNA, Small Interfering</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017382">Reactive Oxygen Species</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050796">STAT3 Transcription Factor</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016329">Sp1 Transcription Factor</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019700">Thrombospondin 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D053773">Transforming Growth Factor beta1</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014746">Vimentin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.24</RegistryNumber><NameOfSubstance UI="D048051">p38 Mitogen-Activated Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.2</RegistryNumber><NameOfSubstance UI="D010206">Papain</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000072283" MajorTopicYN="N">A549 Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004195" MajorTopicYN="N">Disease Models, Animal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051766" MajorTopicYN="N">Early Growth Response Protein 1</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004847" MajorTopicYN="N">Epithelial Cells</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005355" MajorTopicYN="N">Fibrosis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020868" MajorTopicYN="N">Gene 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