Functional proteomic analysis of promyelocytic leukaemia nuclear bodies in irradiation-induced MCF-7 cells
It is well established that promyelocytic leukaemia nuclear bodies (PML NBs) play important roles in DNA damage responses (DDR). After irradiation, PML NBs dynamically recruit or release important proteins involved in cell-cycle regulation, DNA repair and apoptosis. As PML protein is the key molecul...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 2010-12, Vol.148 (6), p.659-667 |
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| container_title | Journal of biochemistry (Tokyo) |
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| creator | Liu, Jinfeng Song, Yi Tian, Baolei Qian, Junjie Dong, Yan Liu, Jilai Liu, Bin Sun, Zhixian |
| description | It is well established that promyelocytic leukaemia nuclear bodies (PML NBs) play important roles in DNA damage responses (DDR). After irradiation, PML NBs dynamically recruit or release important proteins involved in cell-cycle regulation, DNA repair and apoptosis. As PML protein is the key molecule of PML NBs' dynamic assembling, we aimed to characterize the PML-interacting proteins in ⁶⁰Co-irradiated MCF-7 cells. A proteomic approach using CoIP, mono-dimensional electrophoresis and tandem mass spectrometry, allowed us to identify a total of 124 proteins that may associate with PML after irradiation. Bioinformatic analysis of the identified proteins showed that most of them were related to characterized PML functions, such as transcriptional regulation, cell-cycle regulation, cell-death regulation and response to stress. Four proteins, B23, MVP, G3BP1 and DHX9, were verified to co-localize with PML differentially before and after ionizing radiation (IR) treatment. The proteins identified in this study will significantly improve our understanding of the dynamic organization and multiple functions of PML NBs in DDR. |
| doi_str_mv | 10.1093/jb/mvq105 |
| format | Article |
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After irradiation, PML NBs dynamically recruit or release important proteins involved in cell-cycle regulation, DNA repair and apoptosis. As PML protein is the key molecule of PML NBs' dynamic assembling, we aimed to characterize the PML-interacting proteins in ⁶⁰Co-irradiated MCF-7 cells. A proteomic approach using CoIP, mono-dimensional electrophoresis and tandem mass spectrometry, allowed us to identify a total of 124 proteins that may associate with PML after irradiation. Bioinformatic analysis of the identified proteins showed that most of them were related to characterized PML functions, such as transcriptional regulation, cell-cycle regulation, cell-death regulation and response to stress. Four proteins, B23, MVP, G3BP1 and DHX9, were verified to co-localize with PML differentially before and after ionizing radiation (IR) treatment. The proteins identified in this study will significantly improve our understanding of the dynamic organization and multiple functions of PML NBs in DDR.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/jb/mvq105</identifier><identifier>PMID: 20823370</identifier><language>eng</language><publisher>England: Japanese Biochemical Society</publisher><subject>Apoptosis - radiation effects ; Breast Neoplasms - metabolism ; Cell Cycle Proteins - physiology ; Cell Line, Tumor ; Cell Nucleus Structures - metabolism ; Cell Nucleus Structures - radiation effects ; Cell Nucleus Structures - ultrastructure ; DNA Damage - radiation effects ; DNA damage response ; DNA Repair - radiation effects ; DNA, Neoplasm - metabolism ; Female ; Humans ; Leukemia, Promyelocytic, Acute - metabolism ; Microscopy, Fluorescence ; Neoplasm Proteins - metabolism ; Neoplasm Proteins - ultrastructure ; Nuclear Proteins - metabolism ; Nuclear Proteins - ultrastructure ; PML NBs ; Promyelocytic Leukemia Protein ; proteomic analysis ; Proteomics ; Transcription Factors - metabolism ; Transcription Factors - ultrastructure ; Tumor Suppressor Proteins - metabolism ; Tumor Suppressor Proteins - physiology ; Tumor Suppressor Proteins - radiation effects ; Tumor Suppressor Proteins - ultrastructure</subject><ispartof>Journal of biochemistry (Tokyo), 2010-12, Vol.148 (6), p.659-667</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c370t-bbeb67ea389cf6530dadfa2a7b9b733235b6818b79de41b97f53193c517031973</citedby><cites>FETCH-LOGICAL-c370t-bbeb67ea389cf6530dadfa2a7b9b733235b6818b79de41b97f53193c517031973</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20823370$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Jinfeng</creatorcontrib><creatorcontrib>Song, Yi</creatorcontrib><creatorcontrib>Tian, Baolei</creatorcontrib><creatorcontrib>Qian, Junjie</creatorcontrib><creatorcontrib>Dong, Yan</creatorcontrib><creatorcontrib>Liu, Jilai</creatorcontrib><creatorcontrib>Liu, Bin</creatorcontrib><creatorcontrib>Sun, Zhixian</creatorcontrib><title>Functional proteomic analysis of promyelocytic leukaemia nuclear bodies in irradiation-induced MCF-7 cells</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>It is well established that promyelocytic leukaemia nuclear bodies (PML NBs) play important roles in DNA damage responses (DDR). After irradiation, PML NBs dynamically recruit or release important proteins involved in cell-cycle regulation, DNA repair and apoptosis. As PML protein is the key molecule of PML NBs' dynamic assembling, we aimed to characterize the PML-interacting proteins in ⁶⁰Co-irradiated MCF-7 cells. A proteomic approach using CoIP, mono-dimensional electrophoresis and tandem mass spectrometry, allowed us to identify a total of 124 proteins that may associate with PML after irradiation. Bioinformatic analysis of the identified proteins showed that most of them were related to characterized PML functions, such as transcriptional regulation, cell-cycle regulation, cell-death regulation and response to stress. Four proteins, B23, MVP, G3BP1 and DHX9, were verified to co-localize with PML differentially before and after ionizing radiation (IR) treatment. The proteins identified in this study will significantly improve our understanding of the dynamic organization and multiple functions of PML NBs in DDR.</description><subject>Apoptosis - radiation effects</subject><subject>Breast Neoplasms - metabolism</subject><subject>Cell Cycle Proteins - physiology</subject><subject>Cell Line, Tumor</subject><subject>Cell Nucleus Structures - metabolism</subject><subject>Cell Nucleus Structures - radiation effects</subject><subject>Cell Nucleus Structures - ultrastructure</subject><subject>DNA Damage - radiation effects</subject><subject>DNA damage response</subject><subject>DNA Repair - radiation effects</subject><subject>DNA, Neoplasm - metabolism</subject><subject>Female</subject><subject>Humans</subject><subject>Leukemia, Promyelocytic, Acute - metabolism</subject><subject>Microscopy, Fluorescence</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Neoplasm Proteins - ultrastructure</subject><subject>Nuclear Proteins - metabolism</subject><subject>Nuclear Proteins - ultrastructure</subject><subject>PML NBs</subject><subject>Promyelocytic Leukemia Protein</subject><subject>proteomic analysis</subject><subject>Proteomics</subject><subject>Transcription Factors - metabolism</subject><subject>Transcription Factors - ultrastructure</subject><subject>Tumor Suppressor Proteins - metabolism</subject><subject>Tumor Suppressor Proteins - physiology</subject><subject>Tumor Suppressor Proteins - radiation effects</subject><subject>Tumor Suppressor Proteins - ultrastructure</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kM1u1DAUhS0EotPCghcA71AXoXZc2_ESpgxFGsQCKlVsrGvnBnmaxK2dIObtcZTS1f37dHTuIeQNZx84M-Li4C6GPw-cyWdkw7VUVa0kf042jNW8MvXl7Qk5zfmwjLUQL8lJzZrSaLYhh908-inEEXp6n-KEcQieQhmPOWQau2U7HLGP_jiVS4_zHeAQgI6z7xESdbENmGkYaUgJ2gCLWhXGdvbY0m_bXaWpx77Pr8iLDvqMrx_rGbnZff65va7237983X7cV744mirn0CmNIBrjOyUFa6HtoAbtjNNC1EI61fDGadPiJXdGd1JwI7zkmpVGizPyftUtzh9mzJMdQl4cwIhxzrbh0qgiIQt5vpI-xZwTdvY-hQHS0XJml2Ttwdk12cK-fVSd3YDtE_k_ygJUKxDyhH-f7pDurNJCS3t9-8vyq09XSuyF3Rb-3cp3EC38TiHbmx8144Jxw5Uuj_wDY2qOAw</recordid><startdate>20101201</startdate><enddate>20101201</enddate><creator>Liu, Jinfeng</creator><creator>Song, Yi</creator><creator>Tian, Baolei</creator><creator>Qian, Junjie</creator><creator>Dong, Yan</creator><creator>Liu, Jilai</creator><creator>Liu, Bin</creator><creator>Sun, Zhixian</creator><general>Japanese Biochemical Society</general><general>Oxford University Press</general><scope>FBQ</scope><scope>BSCLL</scope><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>7X8</scope></search><sort><creationdate>20101201</creationdate><title>Functional proteomic analysis of promyelocytic leukaemia nuclear bodies in irradiation-induced MCF-7 cells</title><author>Liu, Jinfeng ; Song, Yi ; Tian, Baolei ; Qian, Junjie ; Dong, Yan ; Liu, Jilai ; Liu, Bin ; Sun, Zhixian</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c370t-bbeb67ea389cf6530dadfa2a7b9b733235b6818b79de41b97f53193c517031973</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Apoptosis - radiation effects</topic><topic>Breast Neoplasms - metabolism</topic><topic>Cell Cycle Proteins - physiology</topic><topic>Cell Line, Tumor</topic><topic>Cell Nucleus Structures - metabolism</topic><topic>Cell Nucleus Structures - radiation effects</topic><topic>Cell Nucleus Structures - ultrastructure</topic><topic>DNA Damage - radiation effects</topic><topic>DNA damage response</topic><topic>DNA Repair - radiation effects</topic><topic>DNA, Neoplasm - metabolism</topic><topic>Female</topic><topic>Humans</topic><topic>Leukemia, Promyelocytic, Acute - metabolism</topic><topic>Microscopy, Fluorescence</topic><topic>Neoplasm Proteins - metabolism</topic><topic>Neoplasm Proteins - ultrastructure</topic><topic>Nuclear Proteins - metabolism</topic><topic>Nuclear Proteins - ultrastructure</topic><topic>PML NBs</topic><topic>Promyelocytic Leukemia Protein</topic><topic>proteomic analysis</topic><topic>Proteomics</topic><topic>Transcription Factors - metabolism</topic><topic>Transcription Factors - ultrastructure</topic><topic>Tumor Suppressor Proteins - metabolism</topic><topic>Tumor Suppressor Proteins - physiology</topic><topic>Tumor Suppressor Proteins - radiation effects</topic><topic>Tumor Suppressor Proteins - ultrastructure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liu, Jinfeng</creatorcontrib><creatorcontrib>Song, Yi</creatorcontrib><creatorcontrib>Tian, Baolei</creatorcontrib><creatorcontrib>Qian, Junjie</creatorcontrib><creatorcontrib>Dong, Yan</creatorcontrib><creatorcontrib>Liu, Jilai</creatorcontrib><creatorcontrib>Liu, Bin</creatorcontrib><creatorcontrib>Sun, Zhixian</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liu, Jinfeng</au><au>Song, Yi</au><au>Tian, Baolei</au><au>Qian, Junjie</au><au>Dong, Yan</au><au>Liu, Jilai</au><au>Liu, Bin</au><au>Sun, Zhixian</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional proteomic analysis of promyelocytic leukaemia nuclear bodies in irradiation-induced MCF-7 cells</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>2010-12-01</date><risdate>2010</risdate><volume>148</volume><issue>6</issue><spage>659</spage><epage>667</epage><pages>659-667</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><abstract>It is well established that promyelocytic leukaemia nuclear bodies (PML NBs) play important roles in DNA damage responses (DDR). After irradiation, PML NBs dynamically recruit or release important proteins involved in cell-cycle regulation, DNA repair and apoptosis. As PML protein is the key molecule of PML NBs' dynamic assembling, we aimed to characterize the PML-interacting proteins in ⁶⁰Co-irradiated MCF-7 cells. A proteomic approach using CoIP, mono-dimensional electrophoresis and tandem mass spectrometry, allowed us to identify a total of 124 proteins that may associate with PML after irradiation. Bioinformatic analysis of the identified proteins showed that most of them were related to characterized PML functions, such as transcriptional regulation, cell-cycle regulation, cell-death regulation and response to stress. Four proteins, B23, MVP, G3BP1 and DHX9, were verified to co-localize with PML differentially before and after ionizing radiation (IR) treatment. The proteins identified in this study will significantly improve our understanding of the dynamic organization and multiple functions of PML NBs in DDR.</abstract><cop>England</cop><pub>Japanese Biochemical Society</pub><pmid>20823370</pmid><doi>10.1093/jb/mvq105</doi><tpages>9</tpages></addata></record> |
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| source | MEDLINE; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | Apoptosis - radiation effects Breast Neoplasms - metabolism Cell Cycle Proteins - physiology Cell Line, Tumor Cell Nucleus Structures - metabolism Cell Nucleus Structures - radiation effects Cell Nucleus Structures - ultrastructure DNA Damage - radiation effects DNA damage response DNA Repair - radiation effects DNA, Neoplasm - metabolism Female Humans Leukemia, Promyelocytic, Acute - metabolism Microscopy, Fluorescence Neoplasm Proteins - metabolism Neoplasm Proteins - ultrastructure Nuclear Proteins - metabolism Nuclear Proteins - ultrastructure PML NBs Promyelocytic Leukemia Protein proteomic analysis Proteomics Transcription Factors - metabolism Transcription Factors - ultrastructure Tumor Suppressor Proteins - metabolism Tumor Suppressor Proteins - physiology Tumor Suppressor Proteins - radiation effects Tumor Suppressor Proteins - ultrastructure |
| title | Functional proteomic analysis of promyelocytic leukaemia nuclear bodies in irradiation-induced MCF-7 cells |
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