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The Role of Posttranslational Protein Modifications in Rheumatological Diseases: Focus on Rheumatoid Arthritis
The definition of posttranslational modification (PTM) encompasses a wide group of chemical reactions that allow modification and modulation of protein functions. The regulation of PTMs is crucial for the activity and survival of the cells. Dysregulation of PTMs has been observed in several patholog...
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Published in: | Journal of immunology research 2015-01, Vol.2015 (2015), p.1-10 |
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creator | Miranda, Francesca Spinelli, F. R. Conti, Fabrizio Alessandri, Cristiano Massaro, Laura Truglia, Simona Pendolino, Monica Sabatinelli, Danilo Pecani, Arbi Barbati, C. Colasanti, Tania Mastrangelo, Andrea Mancini, Riccardo |
description | The definition of posttranslational modification (PTM) encompasses a wide group of chemical reactions that allow modification and modulation of protein functions. The regulation of PTMs is crucial for the activity and survival of the cells. Dysregulation of PTMs has been observed in several pathological conditions, including rheumatoid arthritis (RA). RA is a systemic autoimmune disease primarily targeting the joints. The three PTMs mainly involved in this disease are glycosylation, citrullination, and carbamylation. Glycosylation is essential for antigen processing and presentation and can modulate immunoglobulin activity. Citrullination of self-antigens is strongly associated with RA, as demonstrated by the presence of antibodies directed to anti-citrullinated proteins in patients’ sera. Carbamylation and its dysregulation have been recently associated with RA. Aim of this review is to illustrate the most significant alterations of these PTMs in RA and to evaluate their possible involvement in the pathogenesis of the disease. |
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R. ; Conti, Fabrizio ; Alessandri, Cristiano ; Massaro, Laura ; Truglia, Simona ; Pendolino, Monica ; Sabatinelli, Danilo ; Pecani, Arbi ; Barbati, C. ; Colasanti, Tania ; Mastrangelo, Andrea ; Mancini, Riccardo</creator><contributor>Kaplan, David</contributor><creatorcontrib>Miranda, Francesca ; Spinelli, F. R. ; Conti, Fabrizio ; Alessandri, Cristiano ; Massaro, Laura ; Truglia, Simona ; Pendolino, Monica ; Sabatinelli, Danilo ; Pecani, Arbi ; Barbati, C. ; Colasanti, Tania ; Mastrangelo, Andrea ; Mancini, Riccardo ; Kaplan, David</creatorcontrib><description>The definition of posttranslational modification (PTM) encompasses a wide group of chemical reactions that allow modification and modulation of protein functions. The regulation of PTMs is crucial for the activity and survival of the cells. Dysregulation of PTMs has been observed in several pathological conditions, including rheumatoid arthritis (RA). RA is a systemic autoimmune disease primarily targeting the joints. The three PTMs mainly involved in this disease are glycosylation, citrullination, and carbamylation. Glycosylation is essential for antigen processing and presentation and can modulate immunoglobulin activity. Citrullination of self-antigens is strongly associated with RA, as demonstrated by the presence of antibodies directed to anti-citrullinated proteins in patients’ sera. Carbamylation and its dysregulation have been recently associated with RA. Aim of this review is to illustrate the most significant alterations of these PTMs in RA and to evaluate their possible involvement in the pathogenesis of the disease.</description><identifier>ISSN: 2314-8861</identifier><identifier>EISSN: 2314-7156</identifier><identifier>DOI: 10.1155/2015/712490</identifier><identifier>PMID: 26090496</identifier><language>eng</language><publisher>Cairo, Egypt: Hindawi Publishing Corporation</publisher><subject>Animals ; Antibodies - immunology ; Antigens - immunology ; Arthritis, Rheumatoid - immunology ; Collagen ; Disease ; Glycosylation ; Humans ; Immune system ; Immunology ; Lymphocytes ; Pathogenesis ; Peptides ; Physiology ; Protein Processing, Post-Translational - immunology ; Proteins ; Review ; Rheumatoid arthritis ; Studies</subject><ispartof>Journal of immunology research, 2015-01, Vol.2015 (2015), p.1-10</ispartof><rights>Copyright © 2015 Andrea Mastrangelo et al.</rights><rights>Copyright © 2015 Andrea Mastrangelo et al. 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This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</rights><rights>Copyright © 2015 Andrea Mastrangelo et al. 2015</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c664t-d1c26abcacb98684ec8bacd0ea1677823274e678997b088d75de2a6a0d498ab63</citedby><cites>FETCH-LOGICAL-c664t-d1c26abcacb98684ec8bacd0ea1677823274e678997b088d75de2a6a0d498ab63</cites><orcidid>0000-0003-1969-2097</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1684439811/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1684439811?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26090496$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Kaplan, David</contributor><creatorcontrib>Miranda, Francesca</creatorcontrib><creatorcontrib>Spinelli, F. R.</creatorcontrib><creatorcontrib>Conti, Fabrizio</creatorcontrib><creatorcontrib>Alessandri, Cristiano</creatorcontrib><creatorcontrib>Massaro, Laura</creatorcontrib><creatorcontrib>Truglia, Simona</creatorcontrib><creatorcontrib>Pendolino, Monica</creatorcontrib><creatorcontrib>Sabatinelli, Danilo</creatorcontrib><creatorcontrib>Pecani, Arbi</creatorcontrib><creatorcontrib>Barbati, C.</creatorcontrib><creatorcontrib>Colasanti, Tania</creatorcontrib><creatorcontrib>Mastrangelo, Andrea</creatorcontrib><creatorcontrib>Mancini, Riccardo</creatorcontrib><title>The Role of Posttranslational Protein Modifications in Rheumatological Diseases: Focus on Rheumatoid Arthritis</title><title>Journal of immunology research</title><addtitle>J Immunol Res</addtitle><description>The definition of posttranslational modification (PTM) encompasses a wide group of chemical reactions that allow modification and modulation of protein functions. The regulation of PTMs is crucial for the activity and survival of the cells. Dysregulation of PTMs has been observed in several pathological conditions, including rheumatoid arthritis (RA). RA is a systemic autoimmune disease primarily targeting the joints. The three PTMs mainly involved in this disease are glycosylation, citrullination, and carbamylation. Glycosylation is essential for antigen processing and presentation and can modulate immunoglobulin activity. Citrullination of self-antigens is strongly associated with RA, as demonstrated by the presence of antibodies directed to anti-citrullinated proteins in patients’ sera. Carbamylation and its dysregulation have been recently associated with RA. 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R.</au><au>Conti, Fabrizio</au><au>Alessandri, Cristiano</au><au>Massaro, Laura</au><au>Truglia, Simona</au><au>Pendolino, Monica</au><au>Sabatinelli, Danilo</au><au>Pecani, Arbi</au><au>Barbati, C.</au><au>Colasanti, Tania</au><au>Mastrangelo, Andrea</au><au>Mancini, Riccardo</au><au>Kaplan, David</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Role of Posttranslational Protein Modifications in Rheumatological Diseases: Focus on Rheumatoid Arthritis</atitle><jtitle>Journal of immunology research</jtitle><addtitle>J Immunol Res</addtitle><date>2015-01-01</date><risdate>2015</risdate><volume>2015</volume><issue>2015</issue><spage>1</spage><epage>10</epage><pages>1-10</pages><issn>2314-8861</issn><eissn>2314-7156</eissn><abstract>The definition of posttranslational modification (PTM) encompasses a wide group of chemical reactions that allow modification and modulation of protein functions. The regulation of PTMs is crucial for the activity and survival of the cells. Dysregulation of PTMs has been observed in several pathological conditions, including rheumatoid arthritis (RA). RA is a systemic autoimmune disease primarily targeting the joints. The three PTMs mainly involved in this disease are glycosylation, citrullination, and carbamylation. Glycosylation is essential for antigen processing and presentation and can modulate immunoglobulin activity. Citrullination of self-antigens is strongly associated with RA, as demonstrated by the presence of antibodies directed to anti-citrullinated proteins in patients’ sera. Carbamylation and its dysregulation have been recently associated with RA. Aim of this review is to illustrate the most significant alterations of these PTMs in RA and to evaluate their possible involvement in the pathogenesis of the disease.</abstract><cop>Cairo, Egypt</cop><pub>Hindawi Publishing Corporation</pub><pmid>26090496</pmid><doi>10.1155/2015/712490</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0003-1969-2097</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Animals Antibodies - immunology Antigens - immunology Arthritis, Rheumatoid - immunology Collagen Disease Glycosylation Humans Immune system Immunology Lymphocytes Pathogenesis Peptides Physiology Protein Processing, Post-Translational - immunology Proteins Review Rheumatoid arthritis Studies |
title | The Role of Posttranslational Protein Modifications in Rheumatological Diseases: Focus on Rheumatoid Arthritis |
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