Histone carbonylation occurs in proliferating cells
Chromatin is a dynamic structure formed mainly by DNA and histones, and chemical modifications on these elements regulate its compaction. Histone posttranslational modifications (PTMs) have a direct impact on chromatin conformation, controlling important cellular events such as cell proliferation an...
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| Veröffentlicht in: | Free radical biology & medicine 2012-04, Vol.52 (8), p.1453-1464 |
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| creator | García-Giménez, José Luis Ledesma, Ana María Velázquez Esmoris, Isabel Romá-Mateo, Carlos Sanz, Pascual Viña, José Pallardó, Federico V. |
| description | Chromatin is a dynamic structure formed mainly by DNA and histones, and chemical modifications on these elements regulate its compaction. Histone posttranslational modifications (PTMs) have a direct impact on chromatin conformation, controlling important cellular events such as cell proliferation and differentiation. Redox-related posttranslational modifications may have important effects on chromatin structure and function, offering a new intriguing area of research termed “redox epigenetics.” Little is known about histone carbonylation, a PTM that may be related to modifications in the cellular redox environment. The aim of our study was to determine the carbonylation of the various histones during cell proliferation, a moment in cell life during which important redox changes take place. Here, we describe changes in histone carbonylation during cell proliferation in NIH3T3 fibroblasts. In addition, we have studied the variations of poly(ADP-ribosyl)ation and phospho-H2AX at the same time, because both modifications are related to DNA damage responses. High levels of carbonylation on specific histones (H1, H10, and H3.1 dimers) were found when cells were in an active phase of DNA synthesis. The modification decreased when nuclear proteasome activity was activated. However, these results did not correlate completely with poly(ADP-ribosyl)ation and phospho-H2AX levels. Therefore, histone carbonylation may represent a specific event during cell proliferation. We describe a new methodology named oxy-2D-TAU Western blot that allowed us to separate and analyze the carbonylation patterns of the histone variants. In addition we offer a new role for histone carbonylation and its implication in redox epigenetics. Our results suggest that histone carbonylation is involved in histone detoxification during DNA synthesis.
► Carbonylation is a histone modification that occurs during cell proliferation. ► Histone carbonylation follows a pattern similar to that of cellular GSH levels. ► Histone carbonylation is involved in histone degradation by the nuclear proteasome. ► PARP activity is important for histone detoxification. |
| doi_str_mv | 10.1016/j.freeradbiomed.2012.01.022 |
| format | Article |
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► Carbonylation is a histone modification that occurs during cell proliferation. ► Histone carbonylation follows a pattern similar to that of cellular GSH levels. ► Histone carbonylation is involved in histone degradation by the nuclear proteasome. ► PARP activity is important for histone detoxification.</description><identifier>ISSN: 0891-5849</identifier><identifier>EISSN: 1873-4596</identifier><identifier>DOI: 10.1016/j.freeradbiomed.2012.01.022</identifier><identifier>PMID: 22342519</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>ADP-ribosylation ; Animals ; Blotting, Western ; Carbonylation ; Cell Proliferation ; Chemical modification ; Chromatin ; Compaction ; Conformation ; Detoxification ; Differentiation ; DNA ; DNA biosynthesis ; DNA damage ; DNA Replication ; Epigenetics ; Fibroblasts ; Free radicals ; Histone H1 ; Histones ; Histones - metabolism ; Mice ; NIH 3T3 Cells ; Phosphorylation ; Poly(ADP-ribosyl)ation ; post-translational modification ; proteasome endopeptidase complex ; proteasomes ; Structure-function relationships ; Western blotting</subject><ispartof>Free radical biology & medicine, 2012-04, Vol.52 (8), p.1453-1464</ispartof><rights>2012 Elsevier Inc.</rights><rights>Copyright © 2012 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c492t-e9ad0ac00882dc1a24d0f94c0b0086baa90f8a2931f3876e7cf9f1bad4fd416a3</citedby><cites>FETCH-LOGICAL-c492t-e9ad0ac00882dc1a24d0f94c0b0086baa90f8a2931f3876e7cf9f1bad4fd416a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0891584912000664$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22342519$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>García-Giménez, José Luis</creatorcontrib><creatorcontrib>Ledesma, Ana María Velázquez</creatorcontrib><creatorcontrib>Esmoris, Isabel</creatorcontrib><creatorcontrib>Romá-Mateo, Carlos</creatorcontrib><creatorcontrib>Sanz, Pascual</creatorcontrib><creatorcontrib>Viña, José</creatorcontrib><creatorcontrib>Pallardó, Federico V.</creatorcontrib><title>Histone carbonylation occurs in proliferating cells</title><title>Free radical biology & medicine</title><addtitle>Free Radic Biol Med</addtitle><description>Chromatin is a dynamic structure formed mainly by DNA and histones, and chemical modifications on these elements regulate its compaction. Histone posttranslational modifications (PTMs) have a direct impact on chromatin conformation, controlling important cellular events such as cell proliferation and differentiation. Redox-related posttranslational modifications may have important effects on chromatin structure and function, offering a new intriguing area of research termed “redox epigenetics.” Little is known about histone carbonylation, a PTM that may be related to modifications in the cellular redox environment. The aim of our study was to determine the carbonylation of the various histones during cell proliferation, a moment in cell life during which important redox changes take place. Here, we describe changes in histone carbonylation during cell proliferation in NIH3T3 fibroblasts. In addition, we have studied the variations of poly(ADP-ribosyl)ation and phospho-H2AX at the same time, because both modifications are related to DNA damage responses. High levels of carbonylation on specific histones (H1, H10, and H3.1 dimers) were found when cells were in an active phase of DNA synthesis. The modification decreased when nuclear proteasome activity was activated. However, these results did not correlate completely with poly(ADP-ribosyl)ation and phospho-H2AX levels. Therefore, histone carbonylation may represent a specific event during cell proliferation. We describe a new methodology named oxy-2D-TAU Western blot that allowed us to separate and analyze the carbonylation patterns of the histone variants. In addition we offer a new role for histone carbonylation and its implication in redox epigenetics. Our results suggest that histone carbonylation is involved in histone detoxification during DNA synthesis.
► Carbonylation is a histone modification that occurs during cell proliferation. ► Histone carbonylation follows a pattern similar to that of cellular GSH levels. ► Histone carbonylation is involved in histone degradation by the nuclear proteasome. ► PARP activity is important for histone detoxification.</description><subject>ADP-ribosylation</subject><subject>Animals</subject><subject>Blotting, Western</subject><subject>Carbonylation</subject><subject>Cell Proliferation</subject><subject>Chemical modification</subject><subject>Chromatin</subject><subject>Compaction</subject><subject>Conformation</subject><subject>Detoxification</subject><subject>Differentiation</subject><subject>DNA</subject><subject>DNA biosynthesis</subject><subject>DNA damage</subject><subject>DNA Replication</subject><subject>Epigenetics</subject><subject>Fibroblasts</subject><subject>Free radicals</subject><subject>Histone H1</subject><subject>Histones</subject><subject>Histones - metabolism</subject><subject>Mice</subject><subject>NIH 3T3 Cells</subject><subject>Phosphorylation</subject><subject>Poly(ADP-ribosyl)ation</subject><subject>post-translational modification</subject><subject>proteasome endopeptidase complex</subject><subject>proteasomes</subject><subject>Structure-function relationships</subject><subject>Western blotting</subject><issn>0891-5849</issn><issn>1873-4596</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE1LHEEQhhtJ0I3JX9CBHMxlJlX9MdONJxETA4IH47np6Q_pZXZau2cD_nt7WT14kZwKqp6qenkI-Y7QIWD_c92F7H02boxp411HAWkH2AGlB2SFcmAtF6r_RFYgFbZCcnVEvpSyBgAumDwkR5QyTgWqFWHXsSxp9o01eUzz82SWmOYmWbvNpYlz85jTFEN9t8T5obF-mspX8jmYqfhvr_WY3P-6-nt53d7c_v5zeXHTWq7o0nplHBgLICV1Fg3lDoLiFsba6kdjFARpqGIYmBx6P9igAo7G8eA49oYdk7P93ZrhaevLojex7BKY2adt0YpLBWoQQyV_fEgiMNkjCtFX9HyP2pxKyT7oxxw3Jj9XSO_86rV-51fv_GpAXf3W7ZPXR9txN3vbfRNagdM9EEzS5iHHou_v6gUBgKyXQlbiak_4qu5f9FkXG_1svYvZ20W7FP8rygt1oJyu</recordid><startdate>20120415</startdate><enddate>20120415</enddate><creator>García-Giménez, José Luis</creator><creator>Ledesma, Ana María Velázquez</creator><creator>Esmoris, Isabel</creator><creator>Romá-Mateo, Carlos</creator><creator>Sanz, Pascual</creator><creator>Viña, José</creator><creator>Pallardó, Federico V.</creator><general>Elsevier Inc</general><scope>FBQ</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>7TM</scope><scope>7X8</scope></search><sort><creationdate>20120415</creationdate><title>Histone carbonylation occurs in proliferating cells</title><author>García-Giménez, José Luis ; Ledesma, Ana María Velázquez ; Esmoris, Isabel ; Romá-Mateo, Carlos ; Sanz, Pascual ; Viña, José ; Pallardó, Federico V.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c492t-e9ad0ac00882dc1a24d0f94c0b0086baa90f8a2931f3876e7cf9f1bad4fd416a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>ADP-ribosylation</topic><topic>Animals</topic><topic>Blotting, Western</topic><topic>Carbonylation</topic><topic>Cell Proliferation</topic><topic>Chemical modification</topic><topic>Chromatin</topic><topic>Compaction</topic><topic>Conformation</topic><topic>Detoxification</topic><topic>Differentiation</topic><topic>DNA</topic><topic>DNA biosynthesis</topic><topic>DNA damage</topic><topic>DNA Replication</topic><topic>Epigenetics</topic><topic>Fibroblasts</topic><topic>Free radicals</topic><topic>Histone H1</topic><topic>Histones</topic><topic>Histones - metabolism</topic><topic>Mice</topic><topic>NIH 3T3 Cells</topic><topic>Phosphorylation</topic><topic>Poly(ADP-ribosyl)ation</topic><topic>post-translational modification</topic><topic>proteasome endopeptidase complex</topic><topic>proteasomes</topic><topic>Structure-function relationships</topic><topic>Western blotting</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>García-Giménez, José Luis</creatorcontrib><creatorcontrib>Ledesma, Ana María Velázquez</creatorcontrib><creatorcontrib>Esmoris, Isabel</creatorcontrib><creatorcontrib>Romá-Mateo, Carlos</creatorcontrib><creatorcontrib>Sanz, Pascual</creatorcontrib><creatorcontrib>Viña, José</creatorcontrib><creatorcontrib>Pallardó, Federico V.</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Free radical biology & medicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>García-Giménez, José Luis</au><au>Ledesma, Ana María Velázquez</au><au>Esmoris, Isabel</au><au>Romá-Mateo, Carlos</au><au>Sanz, Pascual</au><au>Viña, José</au><au>Pallardó, Federico V.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Histone carbonylation occurs in proliferating cells</atitle><jtitle>Free radical biology & medicine</jtitle><addtitle>Free Radic Biol Med</addtitle><date>2012-04-15</date><risdate>2012</risdate><volume>52</volume><issue>8</issue><spage>1453</spage><epage>1464</epage><pages>1453-1464</pages><issn>0891-5849</issn><eissn>1873-4596</eissn><abstract>Chromatin is a dynamic structure formed mainly by DNA and histones, and chemical modifications on these elements regulate its compaction. Histone posttranslational modifications (PTMs) have a direct impact on chromatin conformation, controlling important cellular events such as cell proliferation and differentiation. Redox-related posttranslational modifications may have important effects on chromatin structure and function, offering a new intriguing area of research termed “redox epigenetics.” Little is known about histone carbonylation, a PTM that may be related to modifications in the cellular redox environment. The aim of our study was to determine the carbonylation of the various histones during cell proliferation, a moment in cell life during which important redox changes take place. Here, we describe changes in histone carbonylation during cell proliferation in NIH3T3 fibroblasts. In addition, we have studied the variations of poly(ADP-ribosyl)ation and phospho-H2AX at the same time, because both modifications are related to DNA damage responses. High levels of carbonylation on specific histones (H1, H10, and H3.1 dimers) were found when cells were in an active phase of DNA synthesis. The modification decreased when nuclear proteasome activity was activated. However, these results did not correlate completely with poly(ADP-ribosyl)ation and phospho-H2AX levels. Therefore, histone carbonylation may represent a specific event during cell proliferation. We describe a new methodology named oxy-2D-TAU Western blot that allowed us to separate and analyze the carbonylation patterns of the histone variants. In addition we offer a new role for histone carbonylation and its implication in redox epigenetics. Our results suggest that histone carbonylation is involved in histone detoxification during DNA synthesis.
► Carbonylation is a histone modification that occurs during cell proliferation. ► Histone carbonylation follows a pattern similar to that of cellular GSH levels. ► Histone carbonylation is involved in histone degradation by the nuclear proteasome. ► PARP activity is important for histone detoxification.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>22342519</pmid><doi>10.1016/j.freeradbiomed.2012.01.022</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | ADP-ribosylation Animals Blotting, Western Carbonylation Cell Proliferation Chemical modification Chromatin Compaction Conformation Detoxification Differentiation DNA DNA biosynthesis DNA damage DNA Replication Epigenetics Fibroblasts Free radicals Histone H1 Histones Histones - metabolism Mice NIH 3T3 Cells Phosphorylation Poly(ADP-ribosyl)ation post-translational modification proteasome endopeptidase complex proteasomes Structure-function relationships Western blotting |
| title | Histone carbonylation occurs in proliferating cells |
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