Hepatitis C virus core protein interacts with zinc finger E-box binding homeobox 2 to inhibit E-cadherin expression
Objective To investigate the molecular mechanism by which hepatitis C virus (HCV) core protein represses the expression of E-cadherin by interacting with zinc finger E-box binding homeobox 2 (ZEB2). Methods A HepG2 cell line stably expressing HCV core protein was constructed by transfecting the cell...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
LIU Chuanli [verfasserIn] MAO Jinju [verfasserIn] YE Yuanyuan [verfasserIn] HU Qin [verfasserIn] ZHANG Lijun [verfasserIn] CHEN Weixian [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Chinesisch |
| Erschienen: |
2019 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
In: Di-san junyi daxue xuebao - Editorial Office of Journal of Third Military Medical University, 2021, 41(2019), 18, Seite 1744-1749 |
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| Übergeordnetes Werk: |
volume:41 ; year:2019 ; number:18 ; pages:1744-1749 |
| Links: |
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| DOI / URN: |
10.16016/j.1000-5404.201904168 |
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| Katalog-ID: |
DOAJ068889216 |
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| 520 | |a Objective To investigate the molecular mechanism by which hepatitis C virus (HCV) core protein represses the expression of E-cadherin by interacting with zinc finger E-box binding homeobox 2 (ZEB2). Methods A HepG2 cell line stably expressing HCV core protein was constructed by transfecting the cells with pCore-3FLAG and G418 screening. The expression levels of ZEB2 and E-cadherin in the transfected cells were examined with RT-PCR and Western blotting, and the promoter activity of E-cadherin was assayed using a dual luciferase system. The interaction of HCV core protein with ZEB2 was detected by immunoprecipitation, and the binding of ZEB2 with E-cadherin promoter was determined by chromatin immuoprecipitation. Results Compared with the control cells, the cells transiently and stably expressing HCV core protein both showed significantly decreased expression of E-cadherin (P < 0.01) and increased ZEB2 expression (P < 0.05) at both the protein and mRNA levels. HepG2 cells transfected with HCV core protein exhibited obviously lowered luciferase activity driven by E-cadherin promoter (P < 0.01), while ZEB2 knockdown by RNA interference partly recovered the luciferase activity (P < 0.05). Immunoprecipitation results demonstrated that HCV core protein could bind directly to ZEB2. Chromatin immunoprecipitation assay showed that the presence of HCV core protein obviously enhanced the binding of ZEB2 to E-cadherin promoter. Conclusion HCV core protein increases the expression of ZEB2 and enhances its binding to E-cadherin promoter, and thus inhibits the expression of E-cadherin. | ||
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10.16016/j.1000-5404.201904168 doi (DE-627)DOAJ068889216 (DE-599)DOAJ752c11cb46684119888ca1d1b0e73a18 DE-627 ger DE-627 rakwb chi R5-920 LIU Chuanli verfasserin aut Hepatitis C virus core protein interacts with zinc finger E-box binding homeobox 2 to inhibit E-cadherin expression 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Objective To investigate the molecular mechanism by which hepatitis C virus (HCV) core protein represses the expression of E-cadherin by interacting with zinc finger E-box binding homeobox 2 (ZEB2). Methods A HepG2 cell line stably expressing HCV core protein was constructed by transfecting the cells with pCore-3FLAG and G418 screening. The expression levels of ZEB2 and E-cadherin in the transfected cells were examined with RT-PCR and Western blotting, and the promoter activity of E-cadherin was assayed using a dual luciferase system. The interaction of HCV core protein with ZEB2 was detected by immunoprecipitation, and the binding of ZEB2 with E-cadherin promoter was determined by chromatin immuoprecipitation. Results Compared with the control cells, the cells transiently and stably expressing HCV core protein both showed significantly decreased expression of E-cadherin (P < 0.01) and increased ZEB2 expression (P < 0.05) at both the protein and mRNA levels. HepG2 cells transfected with HCV core protein exhibited obviously lowered luciferase activity driven by E-cadherin promoter (P < 0.01), while ZEB2 knockdown by RNA interference partly recovered the luciferase activity (P < 0.05). Immunoprecipitation results demonstrated that HCV core protein could bind directly to ZEB2. Chromatin immunoprecipitation assay showed that the presence of HCV core protein obviously enhanced the binding of ZEB2 to E-cadherin promoter. Conclusion HCV core protein increases the expression of ZEB2 and enhances its binding to E-cadherin promoter, and thus inhibits the expression of E-cadherin. hepatitis c virus core protein hepatocellular carcinoma Medicine (General) MAO Jinju verfasserin aut YE Yuanyuan verfasserin aut HU Qin verfasserin aut ZHANG Lijun verfasserin aut CHEN Weixian verfasserin aut In Di-san junyi daxue xuebao Editorial Office of Journal of Third Military Medical University, 2021 41(2019), 18, Seite 1744-1749 (DE-627)1760645346 10005404 nnns volume:41 year:2019 number:18 pages:1744-1749 https://doi.org/10.16016/j.1000-5404.201904168 kostenfrei https://doaj.org/article/752c11cb46684119888ca1d1b0e73a18 kostenfrei http://aammt.tmmu.edu.cn/Upload/rhtml/201904168.htm kostenfrei https://doaj.org/toc/1000-5404 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ AR 41 2019 18 1744-1749 |
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10.16016/j.1000-5404.201904168 doi (DE-627)DOAJ068889216 (DE-599)DOAJ752c11cb46684119888ca1d1b0e73a18 DE-627 ger DE-627 rakwb chi R5-920 LIU Chuanli verfasserin aut Hepatitis C virus core protein interacts with zinc finger E-box binding homeobox 2 to inhibit E-cadherin expression 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Objective To investigate the molecular mechanism by which hepatitis C virus (HCV) core protein represses the expression of E-cadherin by interacting with zinc finger E-box binding homeobox 2 (ZEB2). Methods A HepG2 cell line stably expressing HCV core protein was constructed by transfecting the cells with pCore-3FLAG and G418 screening. The expression levels of ZEB2 and E-cadherin in the transfected cells were examined with RT-PCR and Western blotting, and the promoter activity of E-cadherin was assayed using a dual luciferase system. The interaction of HCV core protein with ZEB2 was detected by immunoprecipitation, and the binding of ZEB2 with E-cadherin promoter was determined by chromatin immuoprecipitation. Results Compared with the control cells, the cells transiently and stably expressing HCV core protein both showed significantly decreased expression of E-cadherin (P < 0.01) and increased ZEB2 expression (P < 0.05) at both the protein and mRNA levels. HepG2 cells transfected with HCV core protein exhibited obviously lowered luciferase activity driven by E-cadherin promoter (P < 0.01), while ZEB2 knockdown by RNA interference partly recovered the luciferase activity (P < 0.05). Immunoprecipitation results demonstrated that HCV core protein could bind directly to ZEB2. Chromatin immunoprecipitation assay showed that the presence of HCV core protein obviously enhanced the binding of ZEB2 to E-cadherin promoter. Conclusion HCV core protein increases the expression of ZEB2 and enhances its binding to E-cadherin promoter, and thus inhibits the expression of E-cadherin. hepatitis c virus core protein hepatocellular carcinoma Medicine (General) MAO Jinju verfasserin aut YE Yuanyuan verfasserin aut HU Qin verfasserin aut ZHANG Lijun verfasserin aut CHEN Weixian verfasserin aut In Di-san junyi daxue xuebao Editorial Office of Journal of Third Military Medical University, 2021 41(2019), 18, Seite 1744-1749 (DE-627)1760645346 10005404 nnns volume:41 year:2019 number:18 pages:1744-1749 https://doi.org/10.16016/j.1000-5404.201904168 kostenfrei https://doaj.org/article/752c11cb46684119888ca1d1b0e73a18 kostenfrei http://aammt.tmmu.edu.cn/Upload/rhtml/201904168.htm kostenfrei https://doaj.org/toc/1000-5404 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ AR 41 2019 18 1744-1749 |
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10.16016/j.1000-5404.201904168 doi (DE-627)DOAJ068889216 (DE-599)DOAJ752c11cb46684119888ca1d1b0e73a18 DE-627 ger DE-627 rakwb chi R5-920 LIU Chuanli verfasserin aut Hepatitis C virus core protein interacts with zinc finger E-box binding homeobox 2 to inhibit E-cadherin expression 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Objective To investigate the molecular mechanism by which hepatitis C virus (HCV) core protein represses the expression of E-cadherin by interacting with zinc finger E-box binding homeobox 2 (ZEB2). Methods A HepG2 cell line stably expressing HCV core protein was constructed by transfecting the cells with pCore-3FLAG and G418 screening. The expression levels of ZEB2 and E-cadherin in the transfected cells were examined with RT-PCR and Western blotting, and the promoter activity of E-cadherin was assayed using a dual luciferase system. The interaction of HCV core protein with ZEB2 was detected by immunoprecipitation, and the binding of ZEB2 with E-cadherin promoter was determined by chromatin immuoprecipitation. Results Compared with the control cells, the cells transiently and stably expressing HCV core protein both showed significantly decreased expression of E-cadherin (P < 0.01) and increased ZEB2 expression (P < 0.05) at both the protein and mRNA levels. HepG2 cells transfected with HCV core protein exhibited obviously lowered luciferase activity driven by E-cadherin promoter (P < 0.01), while ZEB2 knockdown by RNA interference partly recovered the luciferase activity (P < 0.05). Immunoprecipitation results demonstrated that HCV core protein could bind directly to ZEB2. Chromatin immunoprecipitation assay showed that the presence of HCV core protein obviously enhanced the binding of ZEB2 to E-cadherin promoter. Conclusion HCV core protein increases the expression of ZEB2 and enhances its binding to E-cadherin promoter, and thus inhibits the expression of E-cadherin. hepatitis c virus core protein hepatocellular carcinoma Medicine (General) MAO Jinju verfasserin aut YE Yuanyuan verfasserin aut HU Qin verfasserin aut ZHANG Lijun verfasserin aut CHEN Weixian verfasserin aut In Di-san junyi daxue xuebao Editorial Office of Journal of Third Military Medical University, 2021 41(2019), 18, Seite 1744-1749 (DE-627)1760645346 10005404 nnns volume:41 year:2019 number:18 pages:1744-1749 https://doi.org/10.16016/j.1000-5404.201904168 kostenfrei https://doaj.org/article/752c11cb46684119888ca1d1b0e73a18 kostenfrei http://aammt.tmmu.edu.cn/Upload/rhtml/201904168.htm kostenfrei https://doaj.org/toc/1000-5404 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ AR 41 2019 18 1744-1749 |
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10.16016/j.1000-5404.201904168 doi (DE-627)DOAJ068889216 (DE-599)DOAJ752c11cb46684119888ca1d1b0e73a18 DE-627 ger DE-627 rakwb chi R5-920 LIU Chuanli verfasserin aut Hepatitis C virus core protein interacts with zinc finger E-box binding homeobox 2 to inhibit E-cadherin expression 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Objective To investigate the molecular mechanism by which hepatitis C virus (HCV) core protein represses the expression of E-cadherin by interacting with zinc finger E-box binding homeobox 2 (ZEB2). Methods A HepG2 cell line stably expressing HCV core protein was constructed by transfecting the cells with pCore-3FLAG and G418 screening. The expression levels of ZEB2 and E-cadherin in the transfected cells were examined with RT-PCR and Western blotting, and the promoter activity of E-cadherin was assayed using a dual luciferase system. The interaction of HCV core protein with ZEB2 was detected by immunoprecipitation, and the binding of ZEB2 with E-cadherin promoter was determined by chromatin immuoprecipitation. Results Compared with the control cells, the cells transiently and stably expressing HCV core protein both showed significantly decreased expression of E-cadherin (P < 0.01) and increased ZEB2 expression (P < 0.05) at both the protein and mRNA levels. HepG2 cells transfected with HCV core protein exhibited obviously lowered luciferase activity driven by E-cadherin promoter (P < 0.01), while ZEB2 knockdown by RNA interference partly recovered the luciferase activity (P < 0.05). Immunoprecipitation results demonstrated that HCV core protein could bind directly to ZEB2. Chromatin immunoprecipitation assay showed that the presence of HCV core protein obviously enhanced the binding of ZEB2 to E-cadherin promoter. Conclusion HCV core protein increases the expression of ZEB2 and enhances its binding to E-cadherin promoter, and thus inhibits the expression of E-cadherin. hepatitis c virus core protein hepatocellular carcinoma Medicine (General) MAO Jinju verfasserin aut YE Yuanyuan verfasserin aut HU Qin verfasserin aut ZHANG Lijun verfasserin aut CHEN Weixian verfasserin aut In Di-san junyi daxue xuebao Editorial Office of Journal of Third Military Medical University, 2021 41(2019), 18, Seite 1744-1749 (DE-627)1760645346 10005404 nnns volume:41 year:2019 number:18 pages:1744-1749 https://doi.org/10.16016/j.1000-5404.201904168 kostenfrei https://doaj.org/article/752c11cb46684119888ca1d1b0e73a18 kostenfrei http://aammt.tmmu.edu.cn/Upload/rhtml/201904168.htm kostenfrei https://doaj.org/toc/1000-5404 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ AR 41 2019 18 1744-1749 |
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10.16016/j.1000-5404.201904168 doi (DE-627)DOAJ068889216 (DE-599)DOAJ752c11cb46684119888ca1d1b0e73a18 DE-627 ger DE-627 rakwb chi R5-920 LIU Chuanli verfasserin aut Hepatitis C virus core protein interacts with zinc finger E-box binding homeobox 2 to inhibit E-cadherin expression 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Objective To investigate the molecular mechanism by which hepatitis C virus (HCV) core protein represses the expression of E-cadherin by interacting with zinc finger E-box binding homeobox 2 (ZEB2). Methods A HepG2 cell line stably expressing HCV core protein was constructed by transfecting the cells with pCore-3FLAG and G418 screening. The expression levels of ZEB2 and E-cadherin in the transfected cells were examined with RT-PCR and Western blotting, and the promoter activity of E-cadherin was assayed using a dual luciferase system. The interaction of HCV core protein with ZEB2 was detected by immunoprecipitation, and the binding of ZEB2 with E-cadherin promoter was determined by chromatin immuoprecipitation. Results Compared with the control cells, the cells transiently and stably expressing HCV core protein both showed significantly decreased expression of E-cadherin (P < 0.01) and increased ZEB2 expression (P < 0.05) at both the protein and mRNA levels. HepG2 cells transfected with HCV core protein exhibited obviously lowered luciferase activity driven by E-cadherin promoter (P < 0.01), while ZEB2 knockdown by RNA interference partly recovered the luciferase activity (P < 0.05). Immunoprecipitation results demonstrated that HCV core protein could bind directly to ZEB2. Chromatin immunoprecipitation assay showed that the presence of HCV core protein obviously enhanced the binding of ZEB2 to E-cadherin promoter. Conclusion HCV core protein increases the expression of ZEB2 and enhances its binding to E-cadherin promoter, and thus inhibits the expression of E-cadherin. hepatitis c virus core protein hepatocellular carcinoma Medicine (General) MAO Jinju verfasserin aut YE Yuanyuan verfasserin aut HU Qin verfasserin aut ZHANG Lijun verfasserin aut CHEN Weixian verfasserin aut In Di-san junyi daxue xuebao Editorial Office of Journal of Third Military Medical University, 2021 41(2019), 18, Seite 1744-1749 (DE-627)1760645346 10005404 nnns volume:41 year:2019 number:18 pages:1744-1749 https://doi.org/10.16016/j.1000-5404.201904168 kostenfrei https://doaj.org/article/752c11cb46684119888ca1d1b0e73a18 kostenfrei http://aammt.tmmu.edu.cn/Upload/rhtml/201904168.htm kostenfrei https://doaj.org/toc/1000-5404 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ AR 41 2019 18 1744-1749 |
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Methods A HepG2 cell line stably expressing HCV core protein was constructed by transfecting the cells with pCore-3FLAG and G418 screening. The expression levels of ZEB2 and E-cadherin in the transfected cells were examined with RT-PCR and Western blotting, and the promoter activity of E-cadherin was assayed using a dual luciferase system. The interaction of HCV core protein with ZEB2 was detected by immunoprecipitation, and the binding of ZEB2 with E-cadherin promoter was determined by chromatin immuoprecipitation. Results Compared with the control cells, the cells transiently and stably expressing HCV core protein both showed significantly decreased expression of E-cadherin (P < 0.01) and increased ZEB2 expression (P < 0.05) at both the protein and mRNA levels. 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Hepatitis C virus core protein interacts with zinc finger E-box binding homeobox 2 to inhibit E-cadherin expression |
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Hepatitis C virus core protein interacts with zinc finger E-box binding homeobox 2 to inhibit E-cadherin expression |
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LIU Chuanli |
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LIU Chuanli MAO Jinju YE Yuanyuan HU Qin ZHANG Lijun CHEN Weixian |
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10.16016/j.1000-5404.201904168 |
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hepatitis c virus core protein interacts with zinc finger e-box binding homeobox 2 to inhibit e-cadherin expression |
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Hepatitis C virus core protein interacts with zinc finger E-box binding homeobox 2 to inhibit E-cadherin expression |
| abstract |
Objective To investigate the molecular mechanism by which hepatitis C virus (HCV) core protein represses the expression of E-cadherin by interacting with zinc finger E-box binding homeobox 2 (ZEB2). Methods A HepG2 cell line stably expressing HCV core protein was constructed by transfecting the cells with pCore-3FLAG and G418 screening. The expression levels of ZEB2 and E-cadherin in the transfected cells were examined with RT-PCR and Western blotting, and the promoter activity of E-cadherin was assayed using a dual luciferase system. The interaction of HCV core protein with ZEB2 was detected by immunoprecipitation, and the binding of ZEB2 with E-cadherin promoter was determined by chromatin immuoprecipitation. Results Compared with the control cells, the cells transiently and stably expressing HCV core protein both showed significantly decreased expression of E-cadherin (P < 0.01) and increased ZEB2 expression (P < 0.05) at both the protein and mRNA levels. HepG2 cells transfected with HCV core protein exhibited obviously lowered luciferase activity driven by E-cadherin promoter (P < 0.01), while ZEB2 knockdown by RNA interference partly recovered the luciferase activity (P < 0.05). Immunoprecipitation results demonstrated that HCV core protein could bind directly to ZEB2. Chromatin immunoprecipitation assay showed that the presence of HCV core protein obviously enhanced the binding of ZEB2 to E-cadherin promoter. Conclusion HCV core protein increases the expression of ZEB2 and enhances its binding to E-cadherin promoter, and thus inhibits the expression of E-cadherin. |
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Objective To investigate the molecular mechanism by which hepatitis C virus (HCV) core protein represses the expression of E-cadherin by interacting with zinc finger E-box binding homeobox 2 (ZEB2). Methods A HepG2 cell line stably expressing HCV core protein was constructed by transfecting the cells with pCore-3FLAG and G418 screening. The expression levels of ZEB2 and E-cadherin in the transfected cells were examined with RT-PCR and Western blotting, and the promoter activity of E-cadherin was assayed using a dual luciferase system. The interaction of HCV core protein with ZEB2 was detected by immunoprecipitation, and the binding of ZEB2 with E-cadherin promoter was determined by chromatin immuoprecipitation. Results Compared with the control cells, the cells transiently and stably expressing HCV core protein both showed significantly decreased expression of E-cadherin (P < 0.01) and increased ZEB2 expression (P < 0.05) at both the protein and mRNA levels. HepG2 cells transfected with HCV core protein exhibited obviously lowered luciferase activity driven by E-cadherin promoter (P < 0.01), while ZEB2 knockdown by RNA interference partly recovered the luciferase activity (P < 0.05). Immunoprecipitation results demonstrated that HCV core protein could bind directly to ZEB2. Chromatin immunoprecipitation assay showed that the presence of HCV core protein obviously enhanced the binding of ZEB2 to E-cadherin promoter. Conclusion HCV core protein increases the expression of ZEB2 and enhances its binding to E-cadherin promoter, and thus inhibits the expression of E-cadherin. |
| abstract_unstemmed |
Objective To investigate the molecular mechanism by which hepatitis C virus (HCV) core protein represses the expression of E-cadherin by interacting with zinc finger E-box binding homeobox 2 (ZEB2). Methods A HepG2 cell line stably expressing HCV core protein was constructed by transfecting the cells with pCore-3FLAG and G418 screening. The expression levels of ZEB2 and E-cadherin in the transfected cells were examined with RT-PCR and Western blotting, and the promoter activity of E-cadherin was assayed using a dual luciferase system. The interaction of HCV core protein with ZEB2 was detected by immunoprecipitation, and the binding of ZEB2 with E-cadherin promoter was determined by chromatin immuoprecipitation. Results Compared with the control cells, the cells transiently and stably expressing HCV core protein both showed significantly decreased expression of E-cadherin (P < 0.01) and increased ZEB2 expression (P < 0.05) at both the protein and mRNA levels. HepG2 cells transfected with HCV core protein exhibited obviously lowered luciferase activity driven by E-cadherin promoter (P < 0.01), while ZEB2 knockdown by RNA interference partly recovered the luciferase activity (P < 0.05). Immunoprecipitation results demonstrated that HCV core protein could bind directly to ZEB2. Chromatin immunoprecipitation assay showed that the presence of HCV core protein obviously enhanced the binding of ZEB2 to E-cadherin promoter. Conclusion HCV core protein increases the expression of ZEB2 and enhances its binding to E-cadherin promoter, and thus inhibits the expression of E-cadherin. |
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Hepatitis C virus core protein interacts with zinc finger E-box binding homeobox 2 to inhibit E-cadherin expression |
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