Cartilage oligomeric matrix protein enhances matrix assembly during chondrogenesis of human mesenchymal stem cells
Identifieur interne : 003872 ( Istex/Corpus ); précédent : 003871; suivant : 003873Cartilage oligomeric matrix protein enhances matrix assembly during chondrogenesis of human mesenchymal stem cells
Auteurs : Hana Haleem-Smith ; Raul Calderon ; Yingjie Song ; Rocky S. Tuan ; Faye H. ChenSource :
- Journal of Cellular Biochemistry [ 0730-2312 ] ; 2012-04.
English descriptors
- KwdEn :
- Aggrecan, Alginate, Alginate cultures, Articular, Articular cartilage, Biochemistry, Biol, Bone marrow, Cartilage, Cartilage matrix proteins, Cartilage oligomeric matrix protein, Cdna, Cellular biochemistry, Cesare, Chem, Chen, Chondrogenesis, Chondrogenic, Chondrogenic differentiation, Chondrogenic medium, Collagen, Collagen type, Comp, Comp cdna, Comp production, Comp protein, Comp regulation, Comp transfected cultures, Comp transfected pellets, Comp transfected samples, Comp transfection, Control vector, Culture media, Early onset, Health research scholars program, Hecht, Higher levels, Human mesenchymal, Lawler, Matrix, Mesenchymal, Mrna, Mrna expression, Msc, Multiple epiphyseal dysplasia, Mutation, National institutes, Oligomeric, Pellet, Pellet cultures, Pseudoachondroplasia, Sgag, Sgag content, Sgag contents, Time points, Transfected, Transfection, Tuan.
- Teeft :
- Aggrecan, Alginate, Alginate cultures, Articular, Articular cartilage, Biochemistry, Biol, Bone marrow, Cartilage, Cartilage matrix proteins, Cartilage oligomeric matrix protein, Cdna, Cellular biochemistry, Cesare, Chem, Chen, Chondrogenesis, Chondrogenic, Chondrogenic differentiation, Chondrogenic medium, Collagen, Collagen type, Comp, Comp cdna, Comp production, Comp protein, Comp regulation, Comp transfected cultures, Comp transfected pellets, Comp transfected samples, Comp transfection, Control vector, Culture media, Early onset, Health research scholars program, Hecht, Higher levels, Human mesenchymal, Lawler, Matrix, Mesenchymal, Mrna, Mrna expression, Msc, Multiple epiphyseal dysplasia, Mutation, National institutes, Oligomeric, Pellet, Pellet cultures, Pseudoachondroplasia, Sgag, Sgag content, Sgag contents, Time points, Transfected, Transfection, Tuan.
Abstract
Cartilage oligomeric matrix protein/thrombospondin‐5 (COMP/TSP5) is an abundant cartilage extracellular matrix (ECM) protein that interacts with major cartilage ECM components, including aggrecan and collagens. To test our hypothesis that COMP/TSP5 functions in the assembly of the ECM during cartilage morphogenesis, we have employed mesenchymal stem cell (MSC) chondrogenesis in vitro as a model to examine the effects of COMP over‐expression on neo‐cartilage formation. Human bone marrow‐derived MSCs were transfected with either full‐length COMP cDNA or control plasmid, followed by chondrogenic induction in three‐dimensional pellet or alginate hydrogel culture. MSC chondrogenesis and ECM production was estimated based on quantitation of sulfated glycosaminoglycan (sGAG) accumulation, immunohistochemistry of the presence and distribution of cartilage ECM proteins, and real‐time RT‐PCR analyis of mRNA expression of cartilage markers. Our results showed that COMP over‐expression resulted in increased total sGAG content during the early phase of MSC chondrogenesis, and increased immuno‐detectable levels of aggrecan and collagen type II in the ECM of COMP‐transfected pellet and alginate cultures, indicating more abundant cartilaginous matrix. COMP transfection did not significantly increase the transcript levels of the early chondrogenic marker, Sox9, or aggrecan, suggesting that enhancement of MSC cartilage ECM was effected at post‐transcriptional levels. These findings strongly suggest that COMP functions in mesenchymal chondrogenesis by enhancing cartilage ECM organization and assembly. The action of COMP is most likely mediated not via direct changes in cartilage matrix gene expression but via interactions of COMP with other cartilage ECM proteins, such as aggrecan and collagens, that result in enhanced assembly and retention. J. Cell. Biochem. 113: 1245–1252, 2012. Published 2011. This article is a U.S. Government work and is in the public domain in the USA.
Url:
DOI: 10.1002/jcb.23455
Links to Exploration step
ISTEX:EDA6C2A26595862704EBF8C64CD19238B7C7081ALe document en format XML
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Chen</name><affiliation><mods:affiliation>Cartilage Biology and Orthopaedics Branch, Department of Health and Human Services, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Journal of Cellular Biochemistry</title><title level="j" type="alt">JOURNAL OF CELLULAR BIOCHEMISTRY</title><idno type="ISSN">0730-2312</idno><idno type="eISSN">1097-4644</idno><imprint><biblScope unit="vol">113</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="1245">1245</biblScope><biblScope unit="page" to="1252">1252</biblScope><biblScope unit="page-count">8</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2012-04">2012-04</date></imprint><idno type="ISSN">0730-2312</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0730-2312</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aggrecan</term><term>Alginate</term><term>Alginate cultures</term><term>Articular</term><term>Articular cartilage</term><term>Biochemistry</term><term>Biol</term><term>Bone marrow</term><term>Cartilage</term><term>Cartilage matrix proteins</term><term>Cartilage oligomeric matrix protein</term><term>Cdna</term><term>Cellular biochemistry</term><term>Cesare</term><term>Chem</term><term>Chen</term><term>Chondrogenesis</term><term>Chondrogenic</term><term>Chondrogenic differentiation</term><term>Chondrogenic medium</term><term>Collagen</term><term>Collagen type</term><term>Comp</term><term>Comp cdna</term><term>Comp production</term><term>Comp protein</term><term>Comp regulation</term><term>Comp transfected cultures</term><term>Comp transfected pellets</term><term>Comp transfected samples</term><term>Comp transfection</term><term>Control vector</term><term>Culture media</term><term>Early onset</term><term>Health research scholars program</term><term>Hecht</term><term>Higher levels</term><term>Human mesenchymal</term><term>Lawler</term><term>Matrix</term><term>Mesenchymal</term><term>Mrna</term><term>Mrna expression</term><term>Msc</term><term>Multiple epiphyseal dysplasia</term><term>Mutation</term><term>National institutes</term><term>Oligomeric</term><term>Pellet</term><term>Pellet cultures</term><term>Pseudoachondroplasia</term><term>Sgag</term><term>Sgag content</term><term>Sgag contents</term><term>Time points</term><term>Transfected</term><term>Transfection</term><term>Tuan</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Aggrecan</term><term>Alginate</term><term>Alginate cultures</term><term>Articular</term><term>Articular cartilage</term><term>Biochemistry</term><term>Biol</term><term>Bone marrow</term><term>Cartilage</term><term>Cartilage matrix proteins</term><term>Cartilage oligomeric matrix protein</term><term>Cdna</term><term>Cellular biochemistry</term><term>Cesare</term><term>Chem</term><term>Chen</term><term>Chondrogenesis</term><term>Chondrogenic</term><term>Chondrogenic differentiation</term><term>Chondrogenic medium</term><term>Collagen</term><term>Collagen type</term><term>Comp</term><term>Comp cdna</term><term>Comp production</term><term>Comp protein</term><term>Comp regulation</term><term>Comp transfected cultures</term><term>Comp transfected pellets</term><term>Comp transfected samples</term><term>Comp transfection</term><term>Control vector</term><term>Culture media</term><term>Early onset</term><term>Health research scholars program</term><term>Hecht</term><term>Higher levels</term><term>Human mesenchymal</term><term>Lawler</term><term>Matrix</term><term>Mesenchymal</term><term>Mrna</term><term>Mrna expression</term><term>Msc</term><term>Multiple epiphyseal dysplasia</term><term>Mutation</term><term>National institutes</term><term>Oligomeric</term><term>Pellet</term><term>Pellet cultures</term><term>Pseudoachondroplasia</term><term>Sgag</term><term>Sgag content</term><term>Sgag contents</term><term>Time points</term><term>Transfected</term><term>Transfection</term><term>Tuan</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cartilage oligomeric matrix protein/thrombospondin‐5 (COMP/TSP5) is an abundant cartilage extracellular matrix (ECM) protein that interacts with major cartilage ECM components, including aggrecan and collagens. To test our hypothesis that COMP/TSP5 functions in the assembly of the ECM during cartilage morphogenesis, we have employed mesenchymal stem cell (MSC) chondrogenesis in vitro as a model to examine the effects of COMP over‐expression on neo‐cartilage formation. Human bone marrow‐derived MSCs were transfected with either full‐length COMP cDNA or control plasmid, followed by chondrogenic induction in three‐dimensional pellet or alginate hydrogel culture. MSC chondrogenesis and ECM production was estimated based on quantitation of sulfated glycosaminoglycan (sGAG) accumulation, immunohistochemistry of the presence and distribution of cartilage ECM proteins, and real‐time RT‐PCR analyis of mRNA expression of cartilage markers. Our results showed that COMP over‐expression resulted in increased total sGAG content during the early phase of MSC chondrogenesis, and increased immuno‐detectable levels of aggrecan and collagen type II in the ECM of COMP‐transfected pellet and alginate cultures, indicating more abundant cartilaginous matrix. COMP transfection did not significantly increase the transcript levels of the early chondrogenic marker, Sox9, or aggrecan, suggesting that enhancement of MSC cartilage ECM was effected at post‐transcriptional levels. These findings strongly suggest that COMP functions in mesenchymal chondrogenesis by enhancing cartilage ECM organization and assembly. The action of COMP is most likely mediated not via direct changes in cartilage matrix gene expression but via interactions of COMP with other cartilage ECM proteins, such as aggrecan and collagens, that result in enhanced assembly and retention. J. Cell. Biochem. 113: 1245–1252, 2012. Published 2011. 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Tuan</name><affiliations><json:string>Cartilage Biology and Orthopaedics Branch, Department of Health and Human Services, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892</json:string><json:string>Center for Cellular and Molecular Engineering, Department of Orthopaedic Surgery, University of Pittsburgh, Pittsburgh, Pennsylvania 15219</json:string><json:string>E-mail: rst13@pitt.edu</json:string><json:string>Correspondence address: Center for Cellular and Molecular Engineering, Department of Orthopaedic Surgery, University of Pittsburgh, Room 221, Bridgeside Point II, 450 Technology Drive, Pittsburgh, PA 15219.</json:string></affiliations></json:item><json:item><name>Faye H. Chen</name><affiliations><json:string>Cartilage Biology and Orthopaedics Branch, Department of Health and Human Services, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>CARTILAGE OLIGOMERIC MATRIX PROTEIN</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>MESENCHYMAL STEM CELLS</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>EXTRACELLULAR MATRIX</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>CARTILAGE DEVELOPMENT</value></json:item></subject><articleId><json:string>JCB23455</json:string></articleId><arkIstex>ark:/67375/WNG-5F0S11L4-0</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>Cartilage oligomeric matrix protein/thrombospondin‐5 (COMP/TSP5) is an abundant cartilage extracellular matrix (ECM) protein that interacts with major cartilage ECM components, including aggrecan and collagens. To test our hypothesis that COMP/TSP5 functions in the assembly of the ECM during cartilage morphogenesis, we have employed mesenchymal stem cell (MSC) chondrogenesis in vitro as a model to examine the effects of COMP over‐expression on neo‐cartilage formation. Human bone marrow‐derived MSCs were transfected with either full‐length COMP cDNA or control plasmid, followed by chondrogenic induction in three‐dimensional pellet or alginate hydrogel culture. MSC chondrogenesis and ECM production was estimated based on quantitation of sulfated glycosaminoglycan (sGAG) accumulation, immunohistochemistry of the presence and distribution of cartilage ECM proteins, and real‐time RT‐PCR analyis of mRNA expression of cartilage markers. Our results showed that COMP over‐expression resulted in increased total sGAG content during the early phase of MSC chondrogenesis, and increased immuno‐detectable levels of aggrecan and collagen type II in the ECM of COMP‐transfected pellet and alginate cultures, indicating more abundant cartilaginous matrix. COMP transfection did not significantly increase the transcript levels of the early chondrogenic marker, Sox9, or aggrecan, suggesting that enhancement of MSC cartilage ECM was effected at post‐transcriptional levels. These findings strongly suggest that COMP functions in mesenchymal chondrogenesis by enhancing cartilage ECM organization and assembly. The action of COMP is most likely mediated not via direct changes in cartilage matrix gene expression but via interactions of COMP with other cartilage ECM proteins, such as aggrecan and collagens, that result in enhanced assembly and retention. J. Cell. Biochem. 113: 1245–1252, 2012. Published 2011. This article is a U.S. Government work and is in the public domain in the USA.</abstract><qualityIndicators><refBibsNative>true</refBibsNative><abstractWordCount>275</abstractWordCount><abstractCharCount>1990</abstractCharCount><keywordCount>4</keywordCount><score>9.69</score><pdfWordCount>4690</pdfWordCount><pdfCharCount>31349</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>8</pdfPageCount><pdfPageSize>590 x 788 pts</pdfPageSize></qualityIndicators><title>Cartilage oligomeric matrix protein enhances matrix assembly during chondrogenesis of human mesenchymal stem cells</title><pmid><json:string>22095699</json:string></pmid><genre><json:string>article</json:string></genre><host><title>Journal of Cellular Biochemistry</title><language><json:string>unknown</json:string></language><doi><json:string>10.1002/(ISSN)1097-4644</json:string></doi><issn><json:string>0730-2312</json:string></issn><eissn><json:string>1097-4644</json:string></eissn><publisherId><json:string>JCB</json:string></publisherId><volume>113</volume><issue>4</issue><pages><first>1245</first><last>1252</last><total>8</total></pages><genre><json:string>journal</json:string></genre><subject><json:item><value>Article</value></json:item></subject></host><namedEntities><unitex><date><json:string>2012</json:string></date><geogName></geogName><orgName><json:string>Wiley Periodicals, Inc.</json:string><json:string>Health Research Scholars Program</json:string><json:string>Department of Health and Human Services</json:string><json:string>National Institute of Arthritis</json:string><json:string>Pennsylvania Department of Health</json:string><json:string>Pierce Biotechnology Inc</json:string><json:string>Department of Orthopaedic Surgery, University of Pittsburgh, Room</json:string><json:string>Biochem</json:string><json:string>D Systems, Minneapolis</json:string><json:string>National Institutes of Health</json:string><json:string>National Institutes of Health, Bethesda, Maryland</json:string><json:string>Tuan, Center for Cellular and Molecular Engineering</json:string><json:string>Howard Hughes Medical Institute-National Institutes of Health Research Scholars Program, National Institute of Arthritis</json:string><json:string>Medical Institute-National Institutes of Health Research Scholars Program, and the Commonwealth of Pennsylvania Department of Health</json:string><json:string>Accurate Chemical</json:string><json:string>Department of Orthopaedic Surgery, University of Pittsburgh, Pittsburgh, Pennsylvania</json:string><json:string>University of Washington</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Rocky S. Tuan</json:string><json:string>J. Cell</json:string><json:string>Faye H. Chen</json:string><json:string>Raul Calderon</json:string></persName><placeName><json:string>Iowa City</json:string><json:string>Bedford</json:string><json:string>IL</json:string><json:string>Foster City</json:string><json:string>Switzerland</json:string><json:string>IA</json:string><json:string>Valencia</json:string><json:string>Seattle</json:string><json:string>Basel</json:string><json:string>San Francisco</json:string><json:string>CA</json:string><json:string>MA</json:string><json:string>Rockford</json:string><json:string>WA</json:string><json:string>PA</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Soltz and Ateshian, 1998</json:string><json:string>Chen et al., 2007</json:string><json:string>Hecht et al., 1995</json:string><json:string>Robbins and Goldring, 1998</json:string><json:string>Hauser et al., 1995</json:string><json:string>Maroudas, 1979</json:string><json:string>Yang et al., 2004</json:string><json:string>Majumdar et al., 2000</json:string><json:string>Hardingham et al., 1992</json:string><json:string>Neidhart et al., 1997</json:string><json:string>Mankin et al., 1994</json:string><json:string>Petersson et al., 1998</json:string><json:string>Williamson et al., 2001</json:string><json:string>Barry et al., 2001</json:string><json:string>Chen et al., 2000</json:string><json:string>Murphy et al., 1999</json:string><json:string>Chen and Tuan, 2008</json:string><json:string>Roman-Blas et al. 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This article is a U.S. Government work and is in the public domain in the USA.</licence></availability><date type="published" when="2012-04"></date></publicationStmt><notesStmt><note type="content-type" subtype="article" source="article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</note><note type="publication-type" subtype="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="article"><analytic><title level="a" type="main" xml:lang="en">Cartilage oligomeric matrix protein enhances matrix assembly during chondrogenesis of human mesenchymal stem cells</title><title level="a" type="short" xml:lang="en">COMP Regulation of MSC Chondrogenesis</title><author xml:id="author-0000"><persName><forename type="first">Hana</forename><surname>Haleem‐Smith</surname></persName><affiliation>Cartilage Biology and Orthopaedics Branch, Department of Health and Human Services, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892<address><country key="US"></country></address></affiliation></author><author xml:id="author-0001"><persName><forename type="first">Raul</forename><surname>Calderon</surname></persName><affiliation>Cartilage Biology and Orthopaedics Branch, Department of Health and Human Services, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892<address><country key="US"></country></address></affiliation><affiliation>Department of Health and Human Services, Howard Hughes Medical Institute‐National Institutes of Health Research Scholars Program, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892<address><country key="US"></country></address></affiliation></author><author xml:id="author-0002"><persName><forename type="first">Yingjie</forename><surname>Song</surname></persName><affiliation>Cartilage Biology and Orthopaedics Branch, Department of Health and Human Services, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892<address><country key="US"></country></address></affiliation></author><author xml:id="author-0003" role="corresp"><persName><forename type="first">Rocky S.</forename><surname>Tuan</surname></persName><email>rst13@pitt.edu</email><affiliation>Cartilage Biology and Orthopaedics Branch, Department of Health and Human Services, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892<address><country key="US"></country></address></affiliation><affiliation>Center for Cellular and Molecular Engineering, Department of Orthopaedic Surgery, University of Pittsburgh, Pittsburgh, Pennsylvania 15219<address><country key="US"></country></address></affiliation><affiliation>Center for Cellular and Molecular Engineering, Department of Orthopaedic Surgery, University of Pittsburgh, Room 221, Bridgeside Point II, 450 Technology Drive, Pittsburgh, PA 15219.</affiliation></author><author xml:id="author-0004"><persName><forename type="first">Faye H.</forename><surname>Chen</surname></persName><affiliation>Cartilage Biology and Orthopaedics Branch, Department of Health and Human Services, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892<address><country key="US"></country></address></affiliation></author><idno type="istex">EDA6C2A26595862704EBF8C64CD19238B7C7081A</idno><idno type="ark">ark:/67375/WNG-5F0S11L4-0</idno><idno type="DOI">10.1002/jcb.23455</idno><idno type="unit">JCB23455</idno><idno type="toTypesetVersion">file:JCB.JCB23455.pdf</idno></analytic><monogr><title level="j" type="main">Journal of Cellular Biochemistry</title><title level="j" type="alt">JOURNAL OF CELLULAR BIOCHEMISTRY</title><idno type="pISSN">0730-2312</idno><idno type="eISSN">1097-4644</idno><idno type="book-DOI">10.1002/(ISSN)1097-4644</idno><idno type="book-part-DOI">10.1002/jcb.v113.4</idno><idno type="product">JCB</idno><imprint><biblScope unit="vol">113</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="1245">1245</biblScope><biblScope unit="page" to="1252">1252</biblScope><biblScope unit="page-count">8</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2012-04"></date></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><abstract xml:lang="en" style="main"><head>Abstract</head><p>Cartilage oligomeric matrix protein/thrombospondin‐5 (COMP/TSP5) is an abundant cartilage extracellular matrix (ECM) protein that interacts with major cartilage ECM components, including aggrecan and collagens. To test our hypothesis that COMP/TSP5 functions in the assembly of the ECM during cartilage morphogenesis, we have employed mesenchymal stem cell (MSC) chondrogenesis in vitro as a model to examine the effects of COMP over‐expression on neo‐cartilage formation. Human bone marrow‐derived MSCs were transfected with either full‐length COMP cDNA or control plasmid, followed by chondrogenic induction in three‐dimensional pellet or alginate hydrogel culture. MSC chondrogenesis and ECM production was estimated based on quantitation of sulfated glycosaminoglycan (sGAG) accumulation, immunohistochemistry of the presence and distribution of cartilage ECM proteins, and real‐time RT‐PCR analyis of mRNA expression of cartilage markers. Our results showed that COMP over‐expression resulted in increased total sGAG content during the early phase of MSC chondrogenesis, and increased immuno‐detectable levels of aggrecan and collagen type II in the ECM of COMP‐transfected pellet and alginate cultures, indicating more abundant cartilaginous matrix. COMP transfection did not significantly increase the transcript levels of the early chondrogenic marker, Sox9, or aggrecan, suggesting that enhancement of MSC cartilage ECM was effected at post‐transcriptional levels. These findings strongly suggest that COMP functions in mesenchymal chondrogenesis by enhancing cartilage ECM organization and assembly. The action of COMP is most likely mediated not via direct changes in cartilage matrix gene expression but via interactions of COMP with other cartilage ECM proteins, such as aggrecan and collagens, that result in enhanced assembly and retention. J. Cell. Biochem. 113: 1245–1252, 2012. Published 2011. This article is a U.S. Government work and is in the public domain in the USA.</p></abstract><textClass><keywords xml:lang="en"><term xml:id="kwd1">CARTILAGE OLIGOMERIC MATRIX PROTEIN</term><term xml:id="kwd2">MESENCHYMAL STEM CELLS</term><term xml:id="kwd3">EXTRACELLULAR MATRIX</term><term xml:id="kwd4">CARTILAGE DEVELOPMENT</term></keywords><keywords rend="articleCategory"><term>Article</term></keywords><keywords rend="tocHeading1"><term>Articles</term></keywords></textClass><langUsage><language ident="en"></language></langUsage></profileDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/EDA6C2A26595862704EBF8C64CD19238B7C7081A/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>Wiley Subscription Services, Inc., A Wiley Company</publisherName><publisherLoc>Hoboken</publisherLoc></publisherInfo><doi registered="yes">10.1002/(ISSN)1097-4644</doi><issn type="print">0730-2312</issn><issn type="electronic">1097-4644</issn><idGroup><id type="product" value="JCB"></id></idGroup><titleGroup><title type="main" xml:lang="en" sort="JOURNAL OF CELLULAR BIOCHEMISTRY">Journal of Cellular Biochemistry</title><title type="short">J. 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This article is a U.S. Government work and is in the public domain in the USA.</copyright><eventGroup><event type="manuscriptReceived" date="2011-11-07"></event><event type="manuscriptAccepted" date="2011-11-08"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:3.1.3 standalone mode:FullText" date="2012-02-24"></event><event type="publishedOnlineAccepted" date="2011-11-17"></event><event type="publishedOnlineFinalForm" date="2012-02-23"></event><event type="firstOnline" date="2012-02-23"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-29"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.3.4 mode:FullText" date="2015-02-24"></event></eventGroup><numberingGroup><numbering type="pageFirst">1245</numbering><numbering type="pageLast">1252</numbering></numberingGroup><correspondenceTo>Center for Cellular and Molecular Engineering, Department of Orthopaedic Surgery, University of Pittsburgh, Room 221, Bridgeside Point II, 450 Technology Drive, Pittsburgh, PA 15219.</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:JCB.JCB23455.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="5"></count><count type="tableTotal" number="0"></count><count type="referenceTotal" number="47"></count><count type="wordTotal" number="5284"></count></countGroup><titleGroup><title type="main" xml:lang="en">Cartilage oligomeric matrix protein enhances matrix assembly during chondrogenesis of human mesenchymal stem cells</title><title type="short" xml:lang="en">COMP Regulation of MSC Chondrogenesis</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Hana</givenNames><familyName>Haleem‐Smith</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af1 #af2"><personName><givenNames>Raul</givenNames><familyName>Calderon</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Yingjie</givenNames><familyName>Song</familyName></personName></creator><creator xml:id="au4" creatorRole="author" affiliationRef="#af1 #af3" corresponding="yes"><personName><givenNames>Rocky S.</givenNames><familyName>Tuan</familyName></personName><contactDetails><email>rst13@pitt.edu</email></contactDetails></creator><creator xml:id="au5" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Faye H.</givenNames><familyName>Chen</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="US" type="organization"><unparsedAffiliation>Cartilage Biology and Orthopaedics Branch, Department of Health and Human Services, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="US" type="organization"><unparsedAffiliation>Department of Health and Human Services, Howard Hughes Medical Institute‐National Institutes of Health Research Scholars Program, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892</unparsedAffiliation></affiliation><affiliation xml:id="af3" countryCode="US" type="organization"><unparsedAffiliation>Center for Cellular and Molecular Engineering, Department of Orthopaedic Surgery, University of Pittsburgh, Pittsburgh, Pennsylvania 15219</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">CARTILAGE OLIGOMERIC MATRIX PROTEIN</keyword><keyword xml:id="kwd2">MESENCHYMAL STEM CELLS</keyword><keyword xml:id="kwd3">EXTRACELLULAR MATRIX</keyword><keyword xml:id="kwd4">CARTILAGE DEVELOPMENT</keyword></keywordGroup><fundingInfo><fundingAgency>Intramural Research Program of the National Institutes of Health</fundingAgency><fundingNumber>Z01AR41131</fundingNumber></fundingInfo><fundingInfo><fundingAgency>Howard Hughes Medical Institute‐National Institutes of Health Research Scholars Program</fundingAgency></fundingInfo><fundingInfo><fundingAgency>Commonwealth of Pennsylvania Department of Health</fundingAgency></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>Cartilage oligomeric matrix protein/thrombospondin‐5 (COMP/TSP5) is an abundant cartilage extracellular matrix (ECM) protein that interacts with major cartilage ECM components, including aggrecan and collagens. 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Our results showed that COMP over‐expression resulted in increased total sGAG content during the early phase of MSC chondrogenesis, and increased immuno‐detectable levels of aggrecan and collagen type II in the ECM of COMP‐transfected pellet and alginate cultures, indicating more abundant cartilaginous matrix. COMP transfection did not significantly increase the transcript levels of the early chondrogenic marker, Sox9, or aggrecan, suggesting that enhancement of MSC cartilage ECM was effected at post‐transcriptional levels. These findings strongly suggest that COMP functions in mesenchymal chondrogenesis by enhancing cartilage ECM organization and assembly. The action of COMP is most likely mediated not via direct changes in cartilage matrix gene expression but via interactions of COMP with other cartilage ECM proteins, such as aggrecan and collagens, that result in enhanced assembly and retention. J. Cell. Biochem. 113: 1245–1252, 2012. Published 2011. 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To test our hypothesis that COMP/TSP5 functions in the assembly of the ECM during cartilage morphogenesis, we have employed mesenchymal stem cell (MSC) chondrogenesis in vitro as a model to examine the effects of COMP over‐expression on neo‐cartilage formation. Human bone marrow‐derived MSCs were transfected with either full‐length COMP cDNA or control plasmid, followed by chondrogenic induction in three‐dimensional pellet or alginate hydrogel culture. MSC chondrogenesis and ECM production was estimated based on quantitation of sulfated glycosaminoglycan (sGAG) accumulation, immunohistochemistry of the presence and distribution of cartilage ECM proteins, and real‐time RT‐PCR analyis of mRNA expression of cartilage markers. Our results showed that COMP over‐expression resulted in increased total sGAG content during the early phase of MSC chondrogenesis, and increased immuno‐detectable levels of aggrecan and collagen type II in the ECM of COMP‐transfected pellet and alginate cultures, indicating more abundant cartilaginous matrix. COMP transfection did not significantly increase the transcript levels of the early chondrogenic marker, Sox9, or aggrecan, suggesting that enhancement of MSC cartilage ECM was effected at post‐transcriptional levels. These findings strongly suggest that COMP functions in mesenchymal chondrogenesis by enhancing cartilage ECM organization and assembly. The action of COMP is most likely mediated not via direct changes in cartilage matrix gene expression but via interactions of COMP with other cartilage ECM proteins, such as aggrecan and collagens, that result in enhanced assembly and retention. J. Cell. Biochem. 113: 1245–1252, 2012. Published 2011. 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|texte= Cartilage oligomeric matrix protein enhances matrix assembly during chondrogenesis of human mesenchymal stem cells
}}
| This area was generated with Dilib version V0.6.38. |  |