Proteasomal degradation of p130 facilitate cell cycle deregulation and impairment of cellular differentiation in high-risk Human Papillomavirus 16 and 18 E7 transfected cells
The High-Risk Human Papillomaviruses (HR-HPVs) 16 and 18 are known to cause cervical cancer, which is primarily attributed to E6 and E7 oncoproteins. In addition, recent studies have focused on the vital role of the p130 pocket protein as an oncosuppressor to limit the expression of E2F transcriptio...
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| description | The High-Risk Human Papillomaviruses (HR-HPVs) 16 and 18 are known to cause cervical cancer, which is primarily attributed to E6 and E7 oncoproteins. In addition, recent studies have focused on the vital role of the p130 pocket protein as an oncosuppressor to limit the expression of E2F transcription factors required for cell cycle progression. In view of this, the current study was conducted to investigate the mechanism by which transfection with HPV16/18 E7 leads to the deregulation of the host cell cycle, altering the localisation of p130, and expression of differentiation genes in Human Keratinocytes (HaCaT) cells. Co-immunoprecipitation, Western blot analysis, immunofluorescence microscopy, flow cytometry, quantitative-Polymerase Chain Reaction (qPCR), and the inhibition of p130 by MG132 inhibitor were employed to investigate the loss of p130 and its disruption in HPV 16/18 E7-transfected HaCaT cells. The HPV16- and HPV18-transformed cells, known as CaSki and HeLa, respectively, were also used to complement the ectopic expressions of E7 in HaCaT cells. Normal keratinocytes displayed higher level of p130 expression than HPV-transformed cells. In addition, the immunofluorescence analysis revealed that both HPV 16/18 E7-transfected HaCaT and HPV-transformed cells exhibited higher level of cytoplasmic p130 compared to nuclear p130. A significant increase in the number of S/G2 phase cells in HPV-transformed cells was also recorded since E7 has been shown to stimulate proliferation through the deactivation of Retinoblastoma Protein (pRB)-dependent G1/S checkpoint. Furthermore, the findings recorded the down-regulation of keratinocyte differentiation markers, namely p130, keratin10, and involucrin. The proteasomal degradation of the exported p130 confirmed the cellular localisation pattern of p130, which was commonly observed in cancerous cells. The findings provide strong evidence that the localisation of nuclear p130 nuclear was disrupted by HPV16/18 E7 led to the deregulation of the cell cycle and the impairment of cellular differentiation ultimately lead to cellular transformation. |
| doi_str_mv | 10.1007/s11033-021-06509-4 |
| format | Article |
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In addition, recent studies have focused on the vital role of the p130 pocket protein as an oncosuppressor to limit the expression of E2F transcription factors required for cell cycle progression. In view of this, the current study was conducted to investigate the mechanism by which transfection with HPV16/18 E7 leads to the deregulation of the host cell cycle, altering the localisation of p130, and expression of differentiation genes in Human Keratinocytes (HaCaT) cells. Co-immunoprecipitation, Western blot analysis, immunofluorescence microscopy, flow cytometry, quantitative-Polymerase Chain Reaction (qPCR), and the inhibition of p130 by MG132 inhibitor were employed to investigate the loss of p130 and its disruption in HPV 16/18 E7-transfected HaCaT cells. The HPV16- and HPV18-transformed cells, known as CaSki and HeLa, respectively, were also used to complement the ectopic expressions of E7 in HaCaT cells. Normal keratinocytes displayed higher level of p130 expression than HPV-transformed cells. In addition, the immunofluorescence analysis revealed that both HPV 16/18 E7-transfected HaCaT and HPV-transformed cells exhibited higher level of cytoplasmic p130 compared to nuclear p130. A significant increase in the number of S/G2 phase cells in HPV-transformed cells was also recorded since E7 has been shown to stimulate proliferation through the deactivation of Retinoblastoma Protein (pRB)-dependent G1/S checkpoint. Furthermore, the findings recorded the down-regulation of keratinocyte differentiation markers, namely p130, keratin10, and involucrin. The proteasomal degradation of the exported p130 confirmed the cellular localisation pattern of p130, which was commonly observed in cancerous cells. The findings provide strong evidence that the localisation of nuclear p130 nuclear was disrupted by HPV16/18 E7 led to the deregulation of the cell cycle and the impairment of cellular differentiation ultimately lead to cellular transformation.</description><identifier>ISSN: 0301-4851</identifier><identifier>EISSN: 1573-4978</identifier><identifier>DOI: 10.1007/s11033-021-06509-4</identifier><identifier>PMID: 34169395</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Alphapapillomavirus - genetics ; Alphapapillomavirus - pathogenicity ; Animal Anatomy ; Animal Biochemistry ; Biomedical and Life Sciences ; Cancer ; Cell cycle ; Cell Cycle - physiology ; Cell Differentiation - physiology ; Cell Division - physiology ; Cell Line ; Cell proliferation ; Cervical cancer ; Cervix ; Crk-Associated Substrate Protein - genetics ; Crk-Associated Substrate Protein - metabolism ; Deactivation ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; E2F protein ; Ectopic expression ; Female ; Flow cytometry ; G2 phase ; HeLa Cells ; Histology ; Human papillomavirus ; Human papillomavirus 16 - metabolism ; Human papillomavirus 16 - pathogenicity ; Human papillomavirus 18 - metabolism ; Human papillomavirus 18 - pathogenicity ; Humans ; Immunofluorescence ; Immunoprecipitation ; Keratinocytes ; Keratinocytes - metabolism ; Life Sciences ; Localization ; Morphology ; Oncogene Proteins, Viral - genetics ; Oncogene Proteins, Viral - metabolism ; Original Article ; Papillomaviridae - genetics ; Papillomavirus E7 Proteins - genetics ; Papillomavirus E7 Proteins - metabolism ; Papillomavirus Infections - genetics ; Polymerase chain reaction ; Proteasomes ; Repressor Proteins - genetics ; Retina ; Retinoblastoma ; Retinoblastoma protein ; Retinoblastoma-Like Protein p130 - genetics ; Transcription factors ; Transfection ; Transformed cells ; Uterine Cervical Neoplasms - metabolism</subject><ispartof>Molecular biology reports, 2021-06, Vol.48 (6), p.5121-5133</ispartof><rights>The Author(s), under exclusive licence to Springer Nature B.V. 2021</rights><rights>2021. The Author(s), under exclusive licence to Springer Nature B.V.</rights><rights>The Author(s), under exclusive licence to Springer Nature B.V. 2021.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-c7f814cee46d21dbe51aff6e83dd308eed1075d22dc0dee8c417d0fa6cccc3143</citedby><cites>FETCH-LOGICAL-c375t-c7f814cee46d21dbe51aff6e83dd308eed1075d22dc0dee8c417d0fa6cccc3143</cites><orcidid>0000-0002-5164-4362 ; 0000-0003-3439-9104 ; 0000-0001-6562-2247 ; 0000-0002-3951-8136</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11033-021-06509-4$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11033-021-06509-4$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34169395$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gandhi, Sivasangkary</creatorcontrib><creatorcontrib>Nor Rashid, Nurshamimi</creatorcontrib><creatorcontrib>Mohamad Razif, Muhammad Fazril</creatorcontrib><creatorcontrib>Othman, Shatrah</creatorcontrib><title>Proteasomal degradation of p130 facilitate cell cycle deregulation and impairment of cellular differentiation in high-risk Human Papillomavirus 16 and 18 E7 transfected cells</title><title>Molecular biology reports</title><addtitle>Mol Biol Rep</addtitle><addtitle>Mol Biol Rep</addtitle><description>The High-Risk Human Papillomaviruses (HR-HPVs) 16 and 18 are known to cause cervical cancer, which is primarily attributed to E6 and E7 oncoproteins. In addition, recent studies have focused on the vital role of the p130 pocket protein as an oncosuppressor to limit the expression of E2F transcription factors required for cell cycle progression. In view of this, the current study was conducted to investigate the mechanism by which transfection with HPV16/18 E7 leads to the deregulation of the host cell cycle, altering the localisation of p130, and expression of differentiation genes in Human Keratinocytes (HaCaT) cells. Co-immunoprecipitation, Western blot analysis, immunofluorescence microscopy, flow cytometry, quantitative-Polymerase Chain Reaction (qPCR), and the inhibition of p130 by MG132 inhibitor were employed to investigate the loss of p130 and its disruption in HPV 16/18 E7-transfected HaCaT cells. The HPV16- and HPV18-transformed cells, known as CaSki and HeLa, respectively, were also used to complement the ectopic expressions of E7 in HaCaT cells. Normal keratinocytes displayed higher level of p130 expression than HPV-transformed cells. In addition, the immunofluorescence analysis revealed that both HPV 16/18 E7-transfected HaCaT and HPV-transformed cells exhibited higher level of cytoplasmic p130 compared to nuclear p130. A significant increase in the number of S/G2 phase cells in HPV-transformed cells was also recorded since E7 has been shown to stimulate proliferation through the deactivation of Retinoblastoma Protein (pRB)-dependent G1/S checkpoint. Furthermore, the findings recorded the down-regulation of keratinocyte differentiation markers, namely p130, keratin10, and involucrin. The proteasomal degradation of the exported p130 confirmed the cellular localisation pattern of p130, which was commonly observed in cancerous cells. The findings provide strong evidence that the localisation of nuclear p130 nuclear was disrupted by HPV16/18 E7 led to the deregulation of the cell cycle and the impairment of cellular differentiation ultimately lead to cellular transformation.</description><subject>Alphapapillomavirus - genetics</subject><subject>Alphapapillomavirus - pathogenicity</subject><subject>Animal Anatomy</subject><subject>Animal Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cancer</subject><subject>Cell cycle</subject><subject>Cell Cycle - physiology</subject><subject>Cell Differentiation - physiology</subject><subject>Cell Division - physiology</subject><subject>Cell Line</subject><subject>Cell proliferation</subject><subject>Cervical cancer</subject><subject>Cervix</subject><subject>Crk-Associated Substrate Protein - genetics</subject><subject>Crk-Associated Substrate Protein - metabolism</subject><subject>Deactivation</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>E2F protein</subject><subject>Ectopic expression</subject><subject>Female</subject><subject>Flow cytometry</subject><subject>G2 phase</subject><subject>HeLa Cells</subject><subject>Histology</subject><subject>Human papillomavirus</subject><subject>Human papillomavirus 16 - metabolism</subject><subject>Human papillomavirus 16 - pathogenicity</subject><subject>Human papillomavirus 18 - metabolism</subject><subject>Human papillomavirus 18 - pathogenicity</subject><subject>Humans</subject><subject>Immunofluorescence</subject><subject>Immunoprecipitation</subject><subject>Keratinocytes</subject><subject>Keratinocytes - metabolism</subject><subject>Life Sciences</subject><subject>Localization</subject><subject>Morphology</subject><subject>Oncogene Proteins, Viral - genetics</subject><subject>Oncogene Proteins, Viral - metabolism</subject><subject>Original Article</subject><subject>Papillomaviridae - genetics</subject><subject>Papillomavirus E7 Proteins - genetics</subject><subject>Papillomavirus E7 Proteins - metabolism</subject><subject>Papillomavirus Infections - genetics</subject><subject>Polymerase chain reaction</subject><subject>Proteasomes</subject><subject>Repressor Proteins - genetics</subject><subject>Retina</subject><subject>Retinoblastoma</subject><subject>Retinoblastoma protein</subject><subject>Retinoblastoma-Like Protein p130 - genetics</subject><subject>Transcription factors</subject><subject>Transfection</subject><subject>Transformed cells</subject><subject>Uterine Cervical Neoplasms - metabolism</subject><issn>0301-4851</issn><issn>1573-4978</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kcFu1TAQRS1ERR-FH2CBLLFhE-qJ7ThZoqpQpEp00a4j1x6_uiROsB2k_lS_EeelUIkFs5nFnLlzNZeQd8A-AWPqNAEwzitWQ8UaybpKvCA7kIpXolPtS7JjnEElWgnH5HVK94wxAUq-IsdcQNPxTu7I41WcMuo0jXqgFvdRW539FOjk6AycUaeNH3zWGanBYaDmwQxYyIj7ZdhQHSz146x9HDHkdXMlyzRS650raMh-Q32gd35_V0WfftCLZdSBXunZD0O5_8vHJVFoDnrQ0nNFc9QhOTQZ7UEzvSFHTg8J3z71E3Lz5fz67KK6_P7129nny8pwJXNllGtBGETR2BrsLUrQzjXYcms5axEtMCVtXVvDLGJryl8sc7oxpTgIfkI-brpznH4umHI_-rQ60AGnJfW1FFJ2ohZdQT_8g95PSwzFXaGUUkLwdqXqjTJxSimi6-foRx0femD9mma_pdmXNPtDmv3q4v2T9HI7ov278ie-AvANSGUU9hifb_9H9jcmba2Q</recordid><startdate>20210601</startdate><enddate>20210601</enddate><creator>Gandhi, Sivasangkary</creator><creator>Nor Rashid, Nurshamimi</creator><creator>Mohamad Razif, Muhammad Fazril</creator><creator>Othman, Shatrah</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-5164-4362</orcidid><orcidid>https://orcid.org/0000-0003-3439-9104</orcidid><orcidid>https://orcid.org/0000-0001-6562-2247</orcidid><orcidid>https://orcid.org/0000-0002-3951-8136</orcidid></search><sort><creationdate>20210601</creationdate><title>Proteasomal degradation of p130 facilitate cell cycle deregulation and impairment of cellular differentiation in high-risk Human Papillomavirus 16 and 18 E7 transfected cells</title><author>Gandhi, Sivasangkary ; Nor Rashid, Nurshamimi ; Mohamad Razif, Muhammad Fazril ; Othman, Shatrah</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-c7f814cee46d21dbe51aff6e83dd308eed1075d22dc0dee8c417d0fa6cccc3143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Alphapapillomavirus - genetics</topic><topic>Alphapapillomavirus - pathogenicity</topic><topic>Animal Anatomy</topic><topic>Animal Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Cancer</topic><topic>Cell cycle</topic><topic>Cell Cycle - physiology</topic><topic>Cell Differentiation - physiology</topic><topic>Cell Division - physiology</topic><topic>Cell Line</topic><topic>Cell proliferation</topic><topic>Cervical cancer</topic><topic>Cervix</topic><topic>Crk-Associated Substrate Protein - genetics</topic><topic>Crk-Associated Substrate Protein - metabolism</topic><topic>Deactivation</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>E2F protein</topic><topic>Ectopic expression</topic><topic>Female</topic><topic>Flow cytometry</topic><topic>G2 phase</topic><topic>HeLa Cells</topic><topic>Histology</topic><topic>Human papillomavirus</topic><topic>Human papillomavirus 16 - metabolism</topic><topic>Human papillomavirus 16 - pathogenicity</topic><topic>Human papillomavirus 18 - metabolism</topic><topic>Human papillomavirus 18 - pathogenicity</topic><topic>Humans</topic><topic>Immunofluorescence</topic><topic>Immunoprecipitation</topic><topic>Keratinocytes</topic><topic>Keratinocytes - metabolism</topic><topic>Life Sciences</topic><topic>Localization</topic><topic>Morphology</topic><topic>Oncogene Proteins, Viral - genetics</topic><topic>Oncogene Proteins, Viral - metabolism</topic><topic>Original Article</topic><topic>Papillomaviridae - genetics</topic><topic>Papillomavirus E7 Proteins - genetics</topic><topic>Papillomavirus E7 Proteins - metabolism</topic><topic>Papillomavirus Infections - genetics</topic><topic>Polymerase chain reaction</topic><topic>Proteasomes</topic><topic>Repressor Proteins - genetics</topic><topic>Retina</topic><topic>Retinoblastoma</topic><topic>Retinoblastoma protein</topic><topic>Retinoblastoma-Like Protein p130 - genetics</topic><topic>Transcription factors</topic><topic>Transfection</topic><topic>Transformed cells</topic><topic>Uterine Cervical Neoplasms - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gandhi, Sivasangkary</creatorcontrib><creatorcontrib>Nor Rashid, Nurshamimi</creatorcontrib><creatorcontrib>Mohamad Razif, Muhammad Fazril</creatorcontrib><creatorcontrib>Othman, Shatrah</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular biology reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gandhi, Sivasangkary</au><au>Nor Rashid, Nurshamimi</au><au>Mohamad Razif, Muhammad Fazril</au><au>Othman, Shatrah</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteasomal degradation of p130 facilitate cell cycle deregulation and impairment of cellular differentiation in high-risk Human Papillomavirus 16 and 18 E7 transfected cells</atitle><jtitle>Molecular biology reports</jtitle><stitle>Mol Biol Rep</stitle><addtitle>Mol Biol Rep</addtitle><date>2021-06-01</date><risdate>2021</risdate><volume>48</volume><issue>6</issue><spage>5121</spage><epage>5133</epage><pages>5121-5133</pages><issn>0301-4851</issn><eissn>1573-4978</eissn><abstract>The High-Risk Human Papillomaviruses (HR-HPVs) 16 and 18 are known to cause cervical cancer, which is primarily attributed to E6 and E7 oncoproteins. In addition, recent studies have focused on the vital role of the p130 pocket protein as an oncosuppressor to limit the expression of E2F transcription factors required for cell cycle progression. In view of this, the current study was conducted to investigate the mechanism by which transfection with HPV16/18 E7 leads to the deregulation of the host cell cycle, altering the localisation of p130, and expression of differentiation genes in Human Keratinocytes (HaCaT) cells. Co-immunoprecipitation, Western blot analysis, immunofluorescence microscopy, flow cytometry, quantitative-Polymerase Chain Reaction (qPCR), and the inhibition of p130 by MG132 inhibitor were employed to investigate the loss of p130 and its disruption in HPV 16/18 E7-transfected HaCaT cells. The HPV16- and HPV18-transformed cells, known as CaSki and HeLa, respectively, were also used to complement the ectopic expressions of E7 in HaCaT cells. Normal keratinocytes displayed higher level of p130 expression than HPV-transformed cells. In addition, the immunofluorescence analysis revealed that both HPV 16/18 E7-transfected HaCaT and HPV-transformed cells exhibited higher level of cytoplasmic p130 compared to nuclear p130. A significant increase in the number of S/G2 phase cells in HPV-transformed cells was also recorded since E7 has been shown to stimulate proliferation through the deactivation of Retinoblastoma Protein (pRB)-dependent G1/S checkpoint. Furthermore, the findings recorded the down-regulation of keratinocyte differentiation markers, namely p130, keratin10, and involucrin. The proteasomal degradation of the exported p130 confirmed the cellular localisation pattern of p130, which was commonly observed in cancerous cells. The findings provide strong evidence that the localisation of nuclear p130 nuclear was disrupted by HPV16/18 E7 led to the deregulation of the cell cycle and the impairment of cellular differentiation ultimately lead to cellular transformation.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>34169395</pmid><doi>10.1007/s11033-021-06509-4</doi><tpages>13</tpages><orcidid>https://orcid.org/0000-0002-5164-4362</orcidid><orcidid>https://orcid.org/0000-0003-3439-9104</orcidid><orcidid>https://orcid.org/0000-0001-6562-2247</orcidid><orcidid>https://orcid.org/0000-0002-3951-8136</orcidid></addata></record> |
| fulltext | fulltext |
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| ispartof | Molecular biology reports, 2021-06, Vol.48 (6), p.5121-5133 |
| issn | 0301-4851 1573-4978 |
| language | eng |
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| source | MEDLINE; SpringerNature Journals |
| subjects | Alphapapillomavirus - genetics Alphapapillomavirus - pathogenicity Animal Anatomy Animal Biochemistry Biomedical and Life Sciences Cancer Cell cycle Cell Cycle - physiology Cell Differentiation - physiology Cell Division - physiology Cell Line Cell proliferation Cervical cancer Cervix Crk-Associated Substrate Protein - genetics Crk-Associated Substrate Protein - metabolism Deactivation DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism E2F protein Ectopic expression Female Flow cytometry G2 phase HeLa Cells Histology Human papillomavirus Human papillomavirus 16 - metabolism Human papillomavirus 16 - pathogenicity Human papillomavirus 18 - metabolism Human papillomavirus 18 - pathogenicity Humans Immunofluorescence Immunoprecipitation Keratinocytes Keratinocytes - metabolism Life Sciences Localization Morphology Oncogene Proteins, Viral - genetics Oncogene Proteins, Viral - metabolism Original Article Papillomaviridae - genetics Papillomavirus E7 Proteins - genetics Papillomavirus E7 Proteins - metabolism Papillomavirus Infections - genetics Polymerase chain reaction Proteasomes Repressor Proteins - genetics Retina Retinoblastoma Retinoblastoma protein Retinoblastoma-Like Protein p130 - genetics Transcription factors Transfection Transformed cells Uterine Cervical Neoplasms - metabolism |
| title | Proteasomal degradation of p130 facilitate cell cycle deregulation and impairment of cellular differentiation in high-risk Human Papillomavirus 16 and 18 E7 transfected cells |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-27T12%3A29%3A31IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Proteasomal%20degradation%20of%20p130%20facilitate%20cell%20cycle%20deregulation%20and%20impairment%20of%20cellular%20differentiation%20in%20high-risk%20Human%20Papillomavirus%2016%20and%2018%20E7%20transfected%20cells&rft.jtitle=Molecular%20biology%20reports&rft.au=Gandhi,%20Sivasangkary&rft.date=2021-06-01&rft.volume=48&rft.issue=6&rft.spage=5121&rft.epage=5133&rft.pages=5121-5133&rft.issn=0301-4851&rft.eissn=1573-4978&rft_id=info:doi/10.1007/s11033-021-06509-4&rft_dat=%3Cproquest_cross%3E2577744389%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2577744389&rft_id=info:pmid/34169395&rfr_iscdi=true |