Post-transcriptional regulation of MMP2 mRNA by its interaction with miR-20a and Nucleolin in breast cancer cell lines
Matrix-metalloproteinase-2 (MMP2) is a foremost MMP, governing invasion of breast cancer cells during metastasis. miR-20a was reported to induce mesenchymal to epithelial transition in MDA-MB-231 cells and its endogenous expression varies directly with invasiveness of breast cancer cells. The invers...
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| Veröffentlicht in: | Molecular biology reports 2021-03, Vol.48 (3), p.2315-2324 |
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| description | Matrix-metalloproteinase-2 (MMP2) is a foremost MMP, governing invasion of breast cancer cells during metastasis. miR-20a was reported to induce mesenchymal to epithelial transition in MDA-MB-231 cells and its endogenous expression varies directly with invasiveness of breast cancer cells. The inverse and direct correlation of invasiveness with miR-20a and Nucleolin respectively led us to study the post-transcriptional regulation of MMP2 by miR-20a and mRNA stabilizing protein, Nucleolin. Thus, understanding the mechanism of its regulation will enable modification of the invasion potential. MMP2 was found to be higher in MDA-MB-231 than MCF-7 cells both at RNA and protein levels. RNA–protein co-immunoprecipitation assay with Argonaute 2 revealed that
MMP2
undergoes miRNA-mediated post-transcriptional regulation. miR-20a decreased MMP2 expression as well as its enzymatic activity as found by zymogram assay. Reporter assay showed that miR-20a directly binds to its putative binding site in
MMP2
3′-UTR as per in silico prediction. miR-20a additionally impeded
MMP2
mRNA stability, and binding of stabilizing trans-factor Nucleolin to its 3′-UTR was confirmed by RNA–protein co-immunoprecipitation assay. Partial down-regulation of Nucleolin by Si-RNA resulted in the downregulation of MMP2 and Nucleolin over-expression rescued the inhibitory effect of miR-20a on MMP2 expression. Delineating the mechanism of post-transcriptional regulation of MMP2, two of its potent regulators, miR-20a and Nucleolin were identified. It was established for the first time that MMP2 is a direct target of miR-20a. The results also elucidated that Nucleolin binds to
MMP2
3′ UTR and its abundance affects MMP2 expression. |
| doi_str_mv | 10.1007/s11033-021-06261-9 |
| format | Article |
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MMP2
undergoes miRNA-mediated post-transcriptional regulation. miR-20a decreased MMP2 expression as well as its enzymatic activity as found by zymogram assay. Reporter assay showed that miR-20a directly binds to its putative binding site in
MMP2
3′-UTR as per in silico prediction. miR-20a additionally impeded
MMP2
mRNA stability, and binding of stabilizing trans-factor Nucleolin to its 3′-UTR was confirmed by RNA–protein co-immunoprecipitation assay. Partial down-regulation of Nucleolin by Si-RNA resulted in the downregulation of MMP2 and Nucleolin over-expression rescued the inhibitory effect of miR-20a on MMP2 expression. Delineating the mechanism of post-transcriptional regulation of MMP2, two of its potent regulators, miR-20a and Nucleolin were identified. It was established for the first time that MMP2 is a direct target of miR-20a. The results also elucidated that Nucleolin binds to
MMP2
3′ UTR and its abundance affects MMP2 expression.</description><identifier>ISSN: 0301-4851</identifier><identifier>EISSN: 1573-4978</identifier><identifier>DOI: 10.1007/s11033-021-06261-9</identifier><identifier>PMID: 33788053</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>3' Untranslated regions ; 3' Untranslated Regions - genetics ; Animal Anatomy ; Animal Biochemistry ; Argonaute 2 protein ; Base Sequence ; Binding sites ; Binding Sites - genetics ; Biomedical and Life Sciences ; Breast cancer ; Breast Neoplasms - enzymology ; Breast Neoplasms - genetics ; Cell Line, Tumor ; Computer Simulation ; Down-regulation ; Down-Regulation - genetics ; Enzymatic activity ; Female ; Gelatinase A ; Gene Expression Regulation, Neoplastic ; Gene regulation ; Histology ; Humans ; Immunoprecipitation ; Invasiveness ; Life Sciences ; Matrix metalloproteinase ; Matrix Metalloproteinase 2 - genetics ; Matrix Metalloproteinase 2 - metabolism ; Mesenchyme ; Metalloproteinase ; Metastases ; MicroRNAs - genetics ; MicroRNAs - metabolism ; miRNA ; Morphology ; mRNA stability ; Nucleolin ; Original Article ; Overexpression ; Phosphoproteins - metabolism ; Post-transcription ; Protein Binding ; Proteins ; RNA Stability - genetics ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; RNA-Binding Proteins - metabolism ; Tumor cell lines</subject><ispartof>Molecular biology reports, 2021-03, Vol.48 (3), p.2315-2324</ispartof><rights>The Author(s), under exclusive licence to Springer Nature B.V. 2021</rights><rights>The Author(s), under exclusive licence to Springer Nature B.V. 2021.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c326t-ee643e882ddbc7d832ea119654d5c8e9f60327c5409d23e42dfc54516259dffb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11033-021-06261-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11033-021-06261-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33788053$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Das, Sayantani</creatorcontrib><creatorcontrib>De, Soumasree</creatorcontrib><creatorcontrib>Sengupta, Sumita</creatorcontrib><title>Post-transcriptional regulation of MMP2 mRNA by its interaction with miR-20a and Nucleolin in breast cancer cell lines</title><title>Molecular biology reports</title><addtitle>Mol Biol Rep</addtitle><addtitle>Mol Biol Rep</addtitle><description>Matrix-metalloproteinase-2 (MMP2) is a foremost MMP, governing invasion of breast cancer cells during metastasis. miR-20a was reported to induce mesenchymal to epithelial transition in MDA-MB-231 cells and its endogenous expression varies directly with invasiveness of breast cancer cells. The inverse and direct correlation of invasiveness with miR-20a and Nucleolin respectively led us to study the post-transcriptional regulation of MMP2 by miR-20a and mRNA stabilizing protein, Nucleolin. Thus, understanding the mechanism of its regulation will enable modification of the invasion potential. MMP2 was found to be higher in MDA-MB-231 than MCF-7 cells both at RNA and protein levels. RNA–protein co-immunoprecipitation assay with Argonaute 2 revealed that
MMP2
undergoes miRNA-mediated post-transcriptional regulation. miR-20a decreased MMP2 expression as well as its enzymatic activity as found by zymogram assay. Reporter assay showed that miR-20a directly binds to its putative binding site in
MMP2
3′-UTR as per in silico prediction. miR-20a additionally impeded
MMP2
mRNA stability, and binding of stabilizing trans-factor Nucleolin to its 3′-UTR was confirmed by RNA–protein co-immunoprecipitation assay. Partial down-regulation of Nucleolin by Si-RNA resulted in the downregulation of MMP2 and Nucleolin over-expression rescued the inhibitory effect of miR-20a on MMP2 expression. Delineating the mechanism of post-transcriptional regulation of MMP2, two of its potent regulators, miR-20a and Nucleolin were identified. It was established for the first time that MMP2 is a direct target of miR-20a. The results also elucidated that Nucleolin binds to
MMP2
3′ UTR and its abundance affects MMP2 expression.</description><subject>3' Untranslated regions</subject><subject>3' Untranslated Regions - genetics</subject><subject>Animal Anatomy</subject><subject>Animal Biochemistry</subject><subject>Argonaute 2 protein</subject><subject>Base Sequence</subject><subject>Binding sites</subject><subject>Binding Sites - genetics</subject><subject>Biomedical and Life Sciences</subject><subject>Breast cancer</subject><subject>Breast Neoplasms - enzymology</subject><subject>Breast Neoplasms - genetics</subject><subject>Cell Line, Tumor</subject><subject>Computer Simulation</subject><subject>Down-regulation</subject><subject>Down-Regulation - genetics</subject><subject>Enzymatic activity</subject><subject>Female</subject><subject>Gelatinase A</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>Gene regulation</subject><subject>Histology</subject><subject>Humans</subject><subject>Immunoprecipitation</subject><subject>Invasiveness</subject><subject>Life Sciences</subject><subject>Matrix metalloproteinase</subject><subject>Matrix Metalloproteinase 2 - genetics</subject><subject>Matrix Metalloproteinase 2 - metabolism</subject><subject>Mesenchyme</subject><subject>Metalloproteinase</subject><subject>Metastases</subject><subject>MicroRNAs - genetics</subject><subject>MicroRNAs - metabolism</subject><subject>miRNA</subject><subject>Morphology</subject><subject>mRNA stability</subject><subject>Nucleolin</subject><subject>Original Article</subject><subject>Overexpression</subject><subject>Phosphoproteins - metabolism</subject><subject>Post-transcription</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>RNA Stability - genetics</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>Tumor cell lines</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>BENPR</sourceid><recordid>eNp9kUtLHjEUhoO01K-2f8CFBLrpJm2uk8xSxF5ArUi7DpnkjEbm8plkFP99M37WQhddhcP7nDchD0KHjH5ilOrPmTEqBKGcEdrwhpF2D22Y0oLIVptXaEMFZUQaxfbR25xvKaWSafUG7QuhjaFKbND95ZwLKclN2ae4LXGe3IATXC-DWwc89_j8_JLj8eriGHePOJaM41QgOf-UP8Ryg8d4RTh12E0BXyx-gHmIU8Vwl8Dlgr2bPCTsYRhwTSC_Q697N2R4_3weoF9fTn-efCNnP75-Pzk-I17wphCARgowhofQeR2M4OAYaxslg_IG2r6hgmuvJG0DFyB56OugWMNVG_q-Ewfo4653m-a7BXKxY8zrM9wE85ItV1RrLg0zFf3wD3o7L6n-xkpprWWjRVspvqN8mnNO0NttiqNLj5ZRu1qxOyu2WrFPVuy6dPRcvXQjhJeVPxoqIHZArtF0Denv3f-p_Q2__JcG</recordid><startdate>20210301</startdate><enddate>20210301</enddate><creator>Das, Sayantani</creator><creator>De, Soumasree</creator><creator>Sengupta, Sumita</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>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20210301</creationdate><title>Post-transcriptional regulation of MMP2 mRNA by its interaction with miR-20a and Nucleolin in breast cancer cell lines</title><author>Das, Sayantani ; De, Soumasree ; Sengupta, Sumita</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c326t-ee643e882ddbc7d832ea119654d5c8e9f60327c5409d23e42dfc54516259dffb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>3' Untranslated regions</topic><topic>3' Untranslated Regions - genetics</topic><topic>Animal Anatomy</topic><topic>Animal Biochemistry</topic><topic>Argonaute 2 protein</topic><topic>Base Sequence</topic><topic>Binding sites</topic><topic>Binding Sites - genetics</topic><topic>Biomedical and Life Sciences</topic><topic>Breast cancer</topic><topic>Breast Neoplasms - enzymology</topic><topic>Breast Neoplasms - genetics</topic><topic>Cell Line, Tumor</topic><topic>Computer Simulation</topic><topic>Down-regulation</topic><topic>Down-Regulation - genetics</topic><topic>Enzymatic activity</topic><topic>Female</topic><topic>Gelatinase A</topic><topic>Gene Expression Regulation, Neoplastic</topic><topic>Gene regulation</topic><topic>Histology</topic><topic>Humans</topic><topic>Immunoprecipitation</topic><topic>Invasiveness</topic><topic>Life Sciences</topic><topic>Matrix metalloproteinase</topic><topic>Matrix Metalloproteinase 2 - genetics</topic><topic>Matrix Metalloproteinase 2 - metabolism</topic><topic>Mesenchyme</topic><topic>Metalloproteinase</topic><topic>Metastases</topic><topic>MicroRNAs - genetics</topic><topic>MicroRNAs - metabolism</topic><topic>miRNA</topic><topic>Morphology</topic><topic>mRNA stability</topic><topic>Nucleolin</topic><topic>Original Article</topic><topic>Overexpression</topic><topic>Phosphoproteins - metabolism</topic><topic>Post-transcription</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>RNA Stability - genetics</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>Tumor cell lines</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Das, Sayantani</creatorcontrib><creatorcontrib>De, Soumasree</creatorcontrib><creatorcontrib>Sengupta, Sumita</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 China</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>Das, Sayantani</au><au>De, Soumasree</au><au>Sengupta, Sumita</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Post-transcriptional regulation of MMP2 mRNA by its interaction with miR-20a and Nucleolin in breast cancer cell lines</atitle><jtitle>Molecular biology reports</jtitle><stitle>Mol Biol Rep</stitle><addtitle>Mol Biol Rep</addtitle><date>2021-03-01</date><risdate>2021</risdate><volume>48</volume><issue>3</issue><spage>2315</spage><epage>2324</epage><pages>2315-2324</pages><issn>0301-4851</issn><eissn>1573-4978</eissn><abstract>Matrix-metalloproteinase-2 (MMP2) is a foremost MMP, governing invasion of breast cancer cells during metastasis. miR-20a was reported to induce mesenchymal to epithelial transition in MDA-MB-231 cells and its endogenous expression varies directly with invasiveness of breast cancer cells. The inverse and direct correlation of invasiveness with miR-20a and Nucleolin respectively led us to study the post-transcriptional regulation of MMP2 by miR-20a and mRNA stabilizing protein, Nucleolin. Thus, understanding the mechanism of its regulation will enable modification of the invasion potential. MMP2 was found to be higher in MDA-MB-231 than MCF-7 cells both at RNA and protein levels. RNA–protein co-immunoprecipitation assay with Argonaute 2 revealed that
MMP2
undergoes miRNA-mediated post-transcriptional regulation. miR-20a decreased MMP2 expression as well as its enzymatic activity as found by zymogram assay. Reporter assay showed that miR-20a directly binds to its putative binding site in
MMP2
3′-UTR as per in silico prediction. miR-20a additionally impeded
MMP2
mRNA stability, and binding of stabilizing trans-factor Nucleolin to its 3′-UTR was confirmed by RNA–protein co-immunoprecipitation assay. Partial down-regulation of Nucleolin by Si-RNA resulted in the downregulation of MMP2 and Nucleolin over-expression rescued the inhibitory effect of miR-20a on MMP2 expression. Delineating the mechanism of post-transcriptional regulation of MMP2, two of its potent regulators, miR-20a and Nucleolin were identified. It was established for the first time that MMP2 is a direct target of miR-20a. The results also elucidated that Nucleolin binds to
MMP2
3′ UTR and its abundance affects MMP2 expression.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>33788053</pmid><doi>10.1007/s11033-021-06261-9</doi><tpages>10</tpages></addata></record> |
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| subjects | 3' Untranslated regions 3' Untranslated Regions - genetics Animal Anatomy Animal Biochemistry Argonaute 2 protein Base Sequence Binding sites Binding Sites - genetics Biomedical and Life Sciences Breast cancer Breast Neoplasms - enzymology Breast Neoplasms - genetics Cell Line, Tumor Computer Simulation Down-regulation Down-Regulation - genetics Enzymatic activity Female Gelatinase A Gene Expression Regulation, Neoplastic Gene regulation Histology Humans Immunoprecipitation Invasiveness Life Sciences Matrix metalloproteinase Matrix Metalloproteinase 2 - genetics Matrix Metalloproteinase 2 - metabolism Mesenchyme Metalloproteinase Metastases MicroRNAs - genetics MicroRNAs - metabolism miRNA Morphology mRNA stability Nucleolin Original Article Overexpression Phosphoproteins - metabolism Post-transcription Protein Binding Proteins RNA Stability - genetics RNA, Messenger - genetics RNA, Messenger - metabolism RNA-Binding Proteins - metabolism Tumor cell lines |
| title | Post-transcriptional regulation of MMP2 mRNA by its interaction with miR-20a and Nucleolin in breast cancer cell lines |
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