Current insights into the role of citrullination in thrombosis

Protein citrullination is a post-translational modification of arginine that controls a diverse array of cellular processes, including gene regulation, protein stability, and neutrophil extracellular trap (NET) formation. Histone citrullination promotes chromatin decondensation and NET formation, a...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Current opinion in chemical biology 2023-08, Vol.75, p.102313-102313, Article 102313
Hauptverfasser: Green, R. Madison, Thompson, Paul R.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 102313
container_issue
container_start_page 102313
container_title Current opinion in chemical biology
container_volume 75
creator Green, R. Madison
Thompson, Paul R.
description Protein citrullination is a post-translational modification of arginine that controls a diverse array of cellular processes, including gene regulation, protein stability, and neutrophil extracellular trap (NET) formation. Histone citrullination promotes chromatin decondensation and NET formation, a pro-inflammatory form of cell death that is aberrantly increased in numerous immune disorders. This review will provide insights into NETosis and how this novel form of cell death contributes to inflammatory diseases, with a particular emphasis on its role in thrombosis. We will also discuss recent efforts to develop PAD-specific inhibitors.
doi_str_mv 10.1016/j.cbpa.2023.102313
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10523988</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1367593123000510</els_id><sourcerecordid>2810920820</sourcerecordid><originalsourceid>FETCH-LOGICAL-c456t-adfb24b0931aed9b4b0633a7c6a1696c1a32e772b5a9d93ee56022345b8c79223</originalsourceid><addsrcrecordid>eNp9kN1LwzAUxYMobk7_AR-kj7505qNNGxBFhl8w8EWfQ5rebhldM5N04H9vRufQF59yyDn33MsPoUuCpwQTfrOa6mqjphRTFj8oI-wIjUlZiBRnmB5HzXiR5oKRETrzfoUx5rTMT9GIFSQrecbG6G7WOwddSEznzWIZfBTBJmEJibMtJLZJtAmub1vTqWBsF_3oOruurDf-HJ00qvVwsX8n6OPp8X32ks7fnl9nD_NUZzkPqaqbimYVjqcoqEUVJWdMFZorwgXXRDEKRUGrXIlaMICcY0pZllelLkRUE3Q_9G76ag21jhc71cqNM2vlvqRVRv51OrOUC7uVBOeUibKMDdf7Bmc_e_BBro3X0LaqA9t7SUuCBcUlxTFKh6h21nsHzWEPwXJHXq7kjrzckZcD-Th09fvCw8gP6hi4HQIQOW0NOOm1gU5DbRzoIGtr_uv_BuStlSw</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2810920820</pqid></control><display><type>article</type><title>Current insights into the role of citrullination in thrombosis</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><creator>Green, R. Madison ; Thompson, Paul R.</creator><creatorcontrib>Green, R. Madison ; Thompson, Paul R.</creatorcontrib><description>Protein citrullination is a post-translational modification of arginine that controls a diverse array of cellular processes, including gene regulation, protein stability, and neutrophil extracellular trap (NET) formation. Histone citrullination promotes chromatin decondensation and NET formation, a pro-inflammatory form of cell death that is aberrantly increased in numerous immune disorders. This review will provide insights into NETosis and how this novel form of cell death contributes to inflammatory diseases, with a particular emphasis on its role in thrombosis. We will also discuss recent efforts to develop PAD-specific inhibitors.</description><identifier>ISSN: 1367-5931</identifier><identifier>ISSN: 1879-0402</identifier><identifier>EISSN: 1879-0402</identifier><identifier>DOI: 10.1016/j.cbpa.2023.102313</identifier><identifier>PMID: 37148643</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Chromatin - metabolism ; Citrullination ; Extracellular Traps - metabolism ; Humans ; Protein Processing, Post-Translational ; Thrombosis - metabolism</subject><ispartof>Current opinion in chemical biology, 2023-08, Vol.75, p.102313-102313, Article 102313</ispartof><rights>2023 Elsevier Ltd</rights><rights>Copyright © 2023 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c456t-adfb24b0931aed9b4b0633a7c6a1696c1a32e772b5a9d93ee56022345b8c79223</citedby><cites>FETCH-LOGICAL-c456t-adfb24b0931aed9b4b0633a7c6a1696c1a32e772b5a9d93ee56022345b8c79223</cites><orcidid>0000-0002-1621-3372</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.cbpa.2023.102313$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,315,782,786,887,3552,27931,27932,46002</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37148643$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Green, R. Madison</creatorcontrib><creatorcontrib>Thompson, Paul R.</creatorcontrib><title>Current insights into the role of citrullination in thrombosis</title><title>Current opinion in chemical biology</title><addtitle>Curr Opin Chem Biol</addtitle><description>Protein citrullination is a post-translational modification of arginine that controls a diverse array of cellular processes, including gene regulation, protein stability, and neutrophil extracellular trap (NET) formation. Histone citrullination promotes chromatin decondensation and NET formation, a pro-inflammatory form of cell death that is aberrantly increased in numerous immune disorders. This review will provide insights into NETosis and how this novel form of cell death contributes to inflammatory diseases, with a particular emphasis on its role in thrombosis. We will also discuss recent efforts to develop PAD-specific inhibitors.</description><subject>Chromatin - metabolism</subject><subject>Citrullination</subject><subject>Extracellular Traps - metabolism</subject><subject>Humans</subject><subject>Protein Processing, Post-Translational</subject><subject>Thrombosis - metabolism</subject><issn>1367-5931</issn><issn>1879-0402</issn><issn>1879-0402</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kN1LwzAUxYMobk7_AR-kj7505qNNGxBFhl8w8EWfQ5rebhldM5N04H9vRufQF59yyDn33MsPoUuCpwQTfrOa6mqjphRTFj8oI-wIjUlZiBRnmB5HzXiR5oKRETrzfoUx5rTMT9GIFSQrecbG6G7WOwddSEznzWIZfBTBJmEJibMtJLZJtAmub1vTqWBsF_3oOruurDf-HJ00qvVwsX8n6OPp8X32ks7fnl9nD_NUZzkPqaqbimYVjqcoqEUVJWdMFZorwgXXRDEKRUGrXIlaMICcY0pZllelLkRUE3Q_9G76ag21jhc71cqNM2vlvqRVRv51OrOUC7uVBOeUibKMDdf7Bmc_e_BBro3X0LaqA9t7SUuCBcUlxTFKh6h21nsHzWEPwXJHXq7kjrzckZcD-Th09fvCw8gP6hi4HQIQOW0NOOm1gU5DbRzoIGtr_uv_BuStlSw</recordid><startdate>20230801</startdate><enddate>20230801</enddate><creator>Green, R. Madison</creator><creator>Thompson, Paul R.</creator><general>Elsevier Ltd</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>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-1621-3372</orcidid></search><sort><creationdate>20230801</creationdate><title>Current insights into the role of citrullination in thrombosis</title><author>Green, R. Madison ; Thompson, Paul R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c456t-adfb24b0931aed9b4b0633a7c6a1696c1a32e772b5a9d93ee56022345b8c79223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Chromatin - metabolism</topic><topic>Citrullination</topic><topic>Extracellular Traps - metabolism</topic><topic>Humans</topic><topic>Protein Processing, Post-Translational</topic><topic>Thrombosis - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Green, R. Madison</creatorcontrib><creatorcontrib>Thompson, Paul R.</creatorcontrib><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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Current opinion in chemical biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Green, R. Madison</au><au>Thompson, Paul R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Current insights into the role of citrullination in thrombosis</atitle><jtitle>Current opinion in chemical biology</jtitle><addtitle>Curr Opin Chem Biol</addtitle><date>2023-08-01</date><risdate>2023</risdate><volume>75</volume><spage>102313</spage><epage>102313</epage><pages>102313-102313</pages><artnum>102313</artnum><issn>1367-5931</issn><issn>1879-0402</issn><eissn>1879-0402</eissn><abstract>Protein citrullination is a post-translational modification of arginine that controls a diverse array of cellular processes, including gene regulation, protein stability, and neutrophil extracellular trap (NET) formation. Histone citrullination promotes chromatin decondensation and NET formation, a pro-inflammatory form of cell death that is aberrantly increased in numerous immune disorders. This review will provide insights into NETosis and how this novel form of cell death contributes to inflammatory diseases, with a particular emphasis on its role in thrombosis. We will also discuss recent efforts to develop PAD-specific inhibitors.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>37148643</pmid><doi>10.1016/j.cbpa.2023.102313</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-1621-3372</orcidid><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1367-5931
ispartof Current opinion in chemical biology, 2023-08, Vol.75, p.102313-102313, Article 102313
issn 1367-5931
1879-0402
1879-0402
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10523988
source MEDLINE; Access via ScienceDirect (Elsevier)
subjects Chromatin - metabolism
Citrullination
Extracellular Traps - metabolism
Humans
Protein Processing, Post-Translational
Thrombosis - metabolism
title Current insights into the role of citrullination in thrombosis
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-04T19%3A26%3A41IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Current%20insights%20into%20the%20role%20of%20citrullination%20in%20thrombosis&rft.jtitle=Current%20opinion%20in%20chemical%20biology&rft.au=Green,%20R.%20Madison&rft.date=2023-08-01&rft.volume=75&rft.spage=102313&rft.epage=102313&rft.pages=102313-102313&rft.artnum=102313&rft.issn=1367-5931&rft.eissn=1879-0402&rft_id=info:doi/10.1016/j.cbpa.2023.102313&rft_dat=%3Cproquest_pubme%3E2810920820%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2810920820&rft_id=info:pmid/37148643&rft_els_id=S1367593123000510&rfr_iscdi=true