Proteome Alterations in Equine Osteochondrotic Chondrocytes
Osteochondrosis is a failure of the endochondral ossification that affects developing joints in humans and several animal species. It is a localized idiopathic joint disorder characterized by focal chondronecrosis and growing cartilage retention, which can lead to the formation of fissures, subchond...
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description | Osteochondrosis is a failure of the endochondral ossification that affects developing joints in humans and several animal species. It is a localized idiopathic joint disorder characterized by focal chondronecrosis and growing cartilage retention, which can lead to the formation of fissures, subchondral bone cysts, or intra-articular fragments. Osteochondrosis is a complex multifactorial disease associated with extracellular matrix alterations and failure in chondrocyte differentiation, mainly due to genetic, biochemical, and nutritional factors, as well as traumas. This study describes the main proteomic alterations occurring in chondrocytes isolated from osteochondrotic cartilage fragments. A comparative analysis performed on equine osteochondrotic and healthy chondrocytes showed 26 protein species as differentially represented. In particular, quantitative changes in the extracellular matrix, cytoskeletal and chaperone proteins, and in cell adhesion and signaling molecules were observed in osteochondrotic cells, compared to healthy controls. Functional group analysis annotated most of these proteins in "growth plate and cartilage development", while others were included in "glycolysis and gluconeogenesis", "positive regulation of protein import", "cell-cell adhesion mediator activity", and "mitochondrion nucleoid". These results may help to clarify some chondrocyte functional alterations that may play a significant role in determining the onset and progression of equine osteochondrosis and, being related, of human juvenile osteochondrosis. |
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It is a localized idiopathic joint disorder characterized by focal chondronecrosis and growing cartilage retention, which can lead to the formation of fissures, subchondral bone cysts, or intra-articular fragments. Osteochondrosis is a complex multifactorial disease associated with extracellular matrix alterations and failure in chondrocyte differentiation, mainly due to genetic, biochemical, and nutritional factors, as well as traumas. This study describes the main proteomic alterations occurring in chondrocytes isolated from osteochondrotic cartilage fragments. A comparative analysis performed on equine osteochondrotic and healthy chondrocytes showed 26 protein species as differentially represented. In particular, quantitative changes in the extracellular matrix, cytoskeletal and chaperone proteins, and in cell adhesion and signaling molecules were observed in osteochondrotic cells, compared to healthy controls. Functional group analysis annotated most of these proteins in "growth plate and cartilage development", while others were included in "glycolysis and gluconeogenesis", "positive regulation of protein import", "cell-cell adhesion mediator activity", and "mitochondrion nucleoid". These results may help to clarify some chondrocyte functional alterations that may play a significant role in determining the onset and progression of equine osteochondrosis and, being related, of human juvenile osteochondrosis.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms20246179</identifier><identifier>PMID: 31817880</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Animals ; Arthritis ; Biomedical materials ; Bone growth ; Cartilage ; Cell adhesion ; Cell adhesion & migration ; Cell adhesion molecules ; Cells, Cultured ; Chondrocytes ; Chondrocytes - cytology ; Chondrocytes - metabolism ; Chondrogenesis ; Collagen ; Comparative analysis ; Cysts ; Cytoskeleton ; Endochondral bone ; Endoplasmic reticulum ; Enzymes ; Extracellular matrix ; Fragments ; Functional groups ; Genes ; Gluconeogenesis ; Glycolysis ; Growth plate ; Horse Diseases - metabolism ; Horse Diseases - pathology ; Horses ; Male ; Mass spectrometry ; Metabolism ; Ossification ; Osteochondrosis ; Osteochondrosis - metabolism ; Osteochondrosis - pathology ; Pathogenesis ; Protein transport ; Proteins ; Proteome - analysis ; Proteome - metabolism ; Proteomes ; Proteomics ; Scientific imaging ; Subchondral bone</subject><ispartof>International journal of molecular sciences, 2019-12, Vol.20 (24), p.6179</ispartof><rights>2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2019 by the authors. 2019</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c478t-44372dbc855a81c6488c0be7b9e895eb4623557997d1a64c4e31c7ea974dd453</citedby><cites>FETCH-LOGICAL-c478t-44372dbc855a81c6488c0be7b9e895eb4623557997d1a64c4e31c7ea974dd453</cites><orcidid>0000-0002-7613-6540 ; 0000-0002-2750-6226</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6940994/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6940994/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27923,27924,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31817880$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chiaradia, Elisabetta</creatorcontrib><creatorcontrib>Pepe, Marco</creatorcontrib><creatorcontrib>Orvietani, Pier Luigi</creatorcontrib><creatorcontrib>Renzone, Giovanni</creatorcontrib><creatorcontrib>Magini, Alessandro</creatorcontrib><creatorcontrib>Sforna, Monica</creatorcontrib><creatorcontrib>Emiliani, Carla</creatorcontrib><creatorcontrib>Di Meo, Antonio</creatorcontrib><creatorcontrib>Scaloni, Andrea</creatorcontrib><title>Proteome Alterations in Equine Osteochondrotic Chondrocytes</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>Osteochondrosis is a failure of the endochondral ossification that affects developing joints in humans and several animal species. It is a localized idiopathic joint disorder characterized by focal chondronecrosis and growing cartilage retention, which can lead to the formation of fissures, subchondral bone cysts, or intra-articular fragments. Osteochondrosis is a complex multifactorial disease associated with extracellular matrix alterations and failure in chondrocyte differentiation, mainly due to genetic, biochemical, and nutritional factors, as well as traumas. This study describes the main proteomic alterations occurring in chondrocytes isolated from osteochondrotic cartilage fragments. A comparative analysis performed on equine osteochondrotic and healthy chondrocytes showed 26 protein species as differentially represented. In particular, quantitative changes in the extracellular matrix, cytoskeletal and chaperone proteins, and in cell adhesion and signaling molecules were observed in osteochondrotic cells, compared to healthy controls. Functional group analysis annotated most of these proteins in "growth plate and cartilage development", while others were included in "glycolysis and gluconeogenesis", "positive regulation of protein import", "cell-cell adhesion mediator activity", and "mitochondrion nucleoid". These results may help to clarify some chondrocyte functional alterations that may play a significant role in determining the onset and progression of equine osteochondrosis and, being related, of human juvenile osteochondrosis.</description><subject>Animals</subject><subject>Arthritis</subject><subject>Biomedical materials</subject><subject>Bone growth</subject><subject>Cartilage</subject><subject>Cell adhesion</subject><subject>Cell adhesion & migration</subject><subject>Cell adhesion molecules</subject><subject>Cells, Cultured</subject><subject>Chondrocytes</subject><subject>Chondrocytes - cytology</subject><subject>Chondrocytes - metabolism</subject><subject>Chondrogenesis</subject><subject>Collagen</subject><subject>Comparative analysis</subject><subject>Cysts</subject><subject>Cytoskeleton</subject><subject>Endochondral bone</subject><subject>Endoplasmic reticulum</subject><subject>Enzymes</subject><subject>Extracellular matrix</subject><subject>Fragments</subject><subject>Functional groups</subject><subject>Genes</subject><subject>Gluconeogenesis</subject><subject>Glycolysis</subject><subject>Growth plate</subject><subject>Horse Diseases - metabolism</subject><subject>Horse Diseases - pathology</subject><subject>Horses</subject><subject>Male</subject><subject>Mass spectrometry</subject><subject>Metabolism</subject><subject>Ossification</subject><subject>Osteochondrosis</subject><subject>Osteochondrosis - metabolism</subject><subject>Osteochondrosis - pathology</subject><subject>Pathogenesis</subject><subject>Protein transport</subject><subject>Proteins</subject><subject>Proteome - analysis</subject><subject>Proteome - metabolism</subject><subject>Proteomes</subject><subject>Proteomics</subject><subject>Scientific imaging</subject><subject>Subchondral bone</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkc1LAzEQxYMoWqs3z7LgxYPVfG4SBKEUv0Coh95DNjtqym5ik12h_70rVakehhmYH4958xA6IfiSMY2v_LLNFFNeEql30IhwSicYl3J3az5AhzkvMaaMCr2PDhhRRCqFR-j6OcUOYgvFtOkg2c7HkAsfittV7wMU8zxs3VsM9cB5V8w2o1t3kI_Q3ottMhx_9zFa3N0uZg-Tp_n942z6NHFcqm7COZO0rpwSwiriSq6UwxXISoPSAipeUiaE1FrWxJbccWDESbBa8rrmgo3RzUb2va9aqB2ELtnGvCff2rQ20XrzdxP8m3mNH6bUHGvNB4Hzb4EUVz3kzrQ-O2gaGyD22QxfYVxKocmAnv1Dl7FPYXBnqOCqLJkYaowuNpRLMecEL7_HEGy-QjHboQz46baBX_gnBfYJLWWITw</recordid><startdate>20191207</startdate><enddate>20191207</enddate><creator>Chiaradia, Elisabetta</creator><creator>Pepe, Marco</creator><creator>Orvietani, Pier Luigi</creator><creator>Renzone, Giovanni</creator><creator>Magini, Alessandro</creator><creator>Sforna, Monica</creator><creator>Emiliani, Carla</creator><creator>Di Meo, Antonio</creator><creator>Scaloni, Andrea</creator><general>MDPI AG</general><general>MDPI</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>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-7613-6540</orcidid><orcidid>https://orcid.org/0000-0002-2750-6226</orcidid></search><sort><creationdate>20191207</creationdate><title>Proteome Alterations in Equine Osteochondrotic Chondrocytes</title><author>Chiaradia, Elisabetta ; Pepe, Marco ; Orvietani, Pier Luigi ; Renzone, Giovanni ; Magini, Alessandro ; Sforna, Monica ; Emiliani, Carla ; Di Meo, Antonio ; Scaloni, Andrea</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c478t-44372dbc855a81c6488c0be7b9e895eb4623557997d1a64c4e31c7ea974dd453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Animals</topic><topic>Arthritis</topic><topic>Biomedical materials</topic><topic>Bone growth</topic><topic>Cartilage</topic><topic>Cell adhesion</topic><topic>Cell adhesion & migration</topic><topic>Cell adhesion molecules</topic><topic>Cells, Cultured</topic><topic>Chondrocytes</topic><topic>Chondrocytes - cytology</topic><topic>Chondrocytes - metabolism</topic><topic>Chondrogenesis</topic><topic>Collagen</topic><topic>Comparative analysis</topic><topic>Cysts</topic><topic>Cytoskeleton</topic><topic>Endochondral bone</topic><topic>Endoplasmic reticulum</topic><topic>Enzymes</topic><topic>Extracellular matrix</topic><topic>Fragments</topic><topic>Functional groups</topic><topic>Genes</topic><topic>Gluconeogenesis</topic><topic>Glycolysis</topic><topic>Growth plate</topic><topic>Horse Diseases - metabolism</topic><topic>Horse Diseases - pathology</topic><topic>Horses</topic><topic>Male</topic><topic>Mass spectrometry</topic><topic>Metabolism</topic><topic>Ossification</topic><topic>Osteochondrosis</topic><topic>Osteochondrosis - metabolism</topic><topic>Osteochondrosis - pathology</topic><topic>Pathogenesis</topic><topic>Protein transport</topic><topic>Proteins</topic><topic>Proteome - analysis</topic><topic>Proteome - metabolism</topic><topic>Proteomes</topic><topic>Proteomics</topic><topic>Scientific imaging</topic><topic>Subchondral bone</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chiaradia, Elisabetta</creatorcontrib><creatorcontrib>Pepe, Marco</creatorcontrib><creatorcontrib>Orvietani, Pier Luigi</creatorcontrib><creatorcontrib>Renzone, Giovanni</creatorcontrib><creatorcontrib>Magini, Alessandro</creatorcontrib><creatorcontrib>Sforna, Monica</creatorcontrib><creatorcontrib>Emiliani, Carla</creatorcontrib><creatorcontrib>Di Meo, Antonio</creatorcontrib><creatorcontrib>Scaloni, Andrea</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>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content Database</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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chiaradia, Elisabetta</au><au>Pepe, Marco</au><au>Orvietani, Pier Luigi</au><au>Renzone, Giovanni</au><au>Magini, Alessandro</au><au>Sforna, Monica</au><au>Emiliani, Carla</au><au>Di Meo, Antonio</au><au>Scaloni, Andrea</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteome Alterations in Equine Osteochondrotic Chondrocytes</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2019-12-07</date><risdate>2019</risdate><volume>20</volume><issue>24</issue><spage>6179</spage><pages>6179-</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>Osteochondrosis is a failure of the endochondral ossification that affects developing joints in humans and several animal species. It is a localized idiopathic joint disorder characterized by focal chondronecrosis and growing cartilage retention, which can lead to the formation of fissures, subchondral bone cysts, or intra-articular fragments. Osteochondrosis is a complex multifactorial disease associated with extracellular matrix alterations and failure in chondrocyte differentiation, mainly due to genetic, biochemical, and nutritional factors, as well as traumas. This study describes the main proteomic alterations occurring in chondrocytes isolated from osteochondrotic cartilage fragments. A comparative analysis performed on equine osteochondrotic and healthy chondrocytes showed 26 protein species as differentially represented. In particular, quantitative changes in the extracellular matrix, cytoskeletal and chaperone proteins, and in cell adhesion and signaling molecules were observed in osteochondrotic cells, compared to healthy controls. Functional group analysis annotated most of these proteins in "growth plate and cartilage development", while others were included in "glycolysis and gluconeogenesis", "positive regulation of protein import", "cell-cell adhesion mediator activity", and "mitochondrion nucleoid". These results may help to clarify some chondrocyte functional alterations that may play a significant role in determining the onset and progression of equine osteochondrosis and, being related, of human juvenile osteochondrosis.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>31817880</pmid><doi>10.3390/ijms20246179</doi><orcidid>https://orcid.org/0000-0002-7613-6540</orcidid><orcidid>https://orcid.org/0000-0002-2750-6226</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Animals Arthritis Biomedical materials Bone growth Cartilage Cell adhesion Cell adhesion & migration Cell adhesion molecules Cells, Cultured Chondrocytes Chondrocytes - cytology Chondrocytes - metabolism Chondrogenesis Collagen Comparative analysis Cysts Cytoskeleton Endochondral bone Endoplasmic reticulum Enzymes Extracellular matrix Fragments Functional groups Genes Gluconeogenesis Glycolysis Growth plate Horse Diseases - metabolism Horse Diseases - pathology Horses Male Mass spectrometry Metabolism Ossification Osteochondrosis Osteochondrosis - metabolism Osteochondrosis - pathology Pathogenesis Protein transport Proteins Proteome - analysis Proteome - metabolism Proteomes Proteomics Scientific imaging Subchondral bone |
title | Proteome Alterations in Equine Osteochondrotic Chondrocytes |
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