Murine tenascin-W: a novel mammalian tenascin expressed in kidney and at sites of bone and smooth muscle development
We cloned and characterized a novel member of the tenascin family of extracellular matrix proteins--the murine orthologue of zebrafish tenascin-W. Full-length recombinant tenascin-W was expressed and purified from mammalian cell cultures. Rotary shadowing followed by electron microscopy showed that...
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Veröffentlicht in: | Journal of cell science 2004-02, Vol.117 (Pt 4), p.571-581 |
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creator | Scherberich, A Tucker, R P Samandari, E Brown-Luedi, M Martin, D Chiquet-Ehrismann, R |
description | We cloned and characterized a novel member of the tenascin family of extracellular matrix proteins--the murine orthologue of zebrafish tenascin-W. Full-length recombinant tenascin-W was expressed and purified from mammalian cell cultures. Rotary shadowing followed by electron microscopy showed that tenascin-W forms hexabrachions. We studied its expression during development and in the adult by immunohistochemistry, in situ hybridization and immunoblotting. Tenascin-W is expressed during palate formation, osteogenesis and smooth muscle development. In the adult, tenascin-W is found in the kidney, cardiac semilunar valves, corneal limbus and periosteum. Tenascin-W and tenascin-C expression overlap in many of these areas. Bone-morphogenic-protein-2 treated C2C12 cells secrete tenascin-W and are able to adhere to and to extend actin-rich processes on a tenascin-W substratum. In vitro, cells bind to tenascin-W in an RGD-dependent manner. This adhesion is increased by transfection of alpha8 integrin, which localizes with tenascin-W in the periosteum and kidney. |
doi_str_mv | 10.1242/jcs.00867 |
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Full-length recombinant tenascin-W was expressed and purified from mammalian cell cultures. Rotary shadowing followed by electron microscopy showed that tenascin-W forms hexabrachions. We studied its expression during development and in the adult by immunohistochemistry, in situ hybridization and immunoblotting. Tenascin-W is expressed during palate formation, osteogenesis and smooth muscle development. In the adult, tenascin-W is found in the kidney, cardiac semilunar valves, corneal limbus and periosteum. Tenascin-W and tenascin-C expression overlap in many of these areas. Bone-morphogenic-protein-2 treated C2C12 cells secrete tenascin-W and are able to adhere to and to extend actin-rich processes on a tenascin-W substratum. In vitro, cells bind to tenascin-W in an RGD-dependent manner. This adhesion is increased by transfection of alpha8 integrin, which localizes with tenascin-W in the periosteum and kidney.</description><identifier>ISSN: 0021-9533</identifier><identifier>EISSN: 1477-9137</identifier><identifier>DOI: 10.1242/jcs.00867</identifier><identifier>PMID: 14709716</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Sequence ; Animals ; Bone and Bones - embryology ; Bone and Bones - metabolism ; Cell Adhesion - physiology ; Cells, Cultured ; Cloning, Molecular ; DNA, Complementary - genetics ; DNA, Complementary - isolation & purification ; Gene Expression Regulation, Developmental ; Humans ; Immunohistochemistry ; In Situ Hybridization ; Kidney - embryology ; Kidney - metabolism ; Mice ; Molecular Sequence Data ; Muscle, Smooth - embryology ; Muscle, Smooth - metabolism ; Organ Specificity ; Phylogeny ; Recombinant Proteins - genetics ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Tenascin - analogs & derivatives ; Tenascin - biosynthesis ; Tenascin - genetics ; Tenascin - isolation & purification ; Zebrafish ; Zebrafish Proteins - genetics</subject><ispartof>Journal of cell science, 2004-02, Vol.117 (Pt 4), p.571-581</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c382t-6e520d99ce62067936c2c99393e08a6171dba9b8003097a4e4767ba9ee284a73</citedby><cites>FETCH-LOGICAL-c382t-6e520d99ce62067936c2c99393e08a6171dba9b8003097a4e4767ba9ee284a73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,3678,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14709716$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Scherberich, A</creatorcontrib><creatorcontrib>Tucker, R P</creatorcontrib><creatorcontrib>Samandari, E</creatorcontrib><creatorcontrib>Brown-Luedi, M</creatorcontrib><creatorcontrib>Martin, D</creatorcontrib><creatorcontrib>Chiquet-Ehrismann, R</creatorcontrib><title>Murine tenascin-W: a novel mammalian tenascin expressed in kidney and at sites of bone and smooth muscle development</title><title>Journal of cell science</title><addtitle>J Cell Sci</addtitle><description>We cloned and characterized a novel member of the tenascin family of extracellular matrix proteins--the murine orthologue of zebrafish tenascin-W. Full-length recombinant tenascin-W was expressed and purified from mammalian cell cultures. Rotary shadowing followed by electron microscopy showed that tenascin-W forms hexabrachions. We studied its expression during development and in the adult by immunohistochemistry, in situ hybridization and immunoblotting. Tenascin-W is expressed during palate formation, osteogenesis and smooth muscle development. In the adult, tenascin-W is found in the kidney, cardiac semilunar valves, corneal limbus and periosteum. Tenascin-W and tenascin-C expression overlap in many of these areas. Bone-morphogenic-protein-2 treated C2C12 cells secrete tenascin-W and are able to adhere to and to extend actin-rich processes on a tenascin-W substratum. In vitro, cells bind to tenascin-W in an RGD-dependent manner. This adhesion is increased by transfection of alpha8 integrin, which localizes with tenascin-W in the periosteum and kidney.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Bone and Bones - embryology</subject><subject>Bone and Bones - metabolism</subject><subject>Cell Adhesion - physiology</subject><subject>Cells, Cultured</subject><subject>Cloning, Molecular</subject><subject>DNA, Complementary - genetics</subject><subject>DNA, Complementary - isolation & purification</subject><subject>Gene Expression Regulation, Developmental</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>In Situ Hybridization</subject><subject>Kidney - embryology</subject><subject>Kidney - metabolism</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Muscle, Smooth - embryology</subject><subject>Muscle, Smooth - metabolism</subject><subject>Organ Specificity</subject><subject>Phylogeny</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Tenascin - analogs & derivatives</subject><subject>Tenascin - biosynthesis</subject><subject>Tenascin - genetics</subject><subject>Tenascin - isolation & purification</subject><subject>Zebrafish</subject><subject>Zebrafish Proteins - genetics</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkE1LAzEQhoMotlYP_gHJSfCwOkm2m403KX5BxUvB45LNTnHrJqmbrNh_b2qLnoZ55-GFeQg5Z3DNeM5vViZcA5SFPCBjlkuZKSbkIRkDcJapqRAjchLCCgAkV_KYjBIESrJiTOLL0LcOaUSng2ld9nZLNXX-CztqtbW6a7X7u1L8XvcYAjY0LR9t43BDtWuojjS0EQP1S1r71LcNg_U-vlM7BNMhbTB1-rVFF0_J0VJ3Ac_2c0IWD_eL2VM2f318nt3NMyNKHrMCpxwapQwWHAqpRGG4UUoogVDqgknW1FrVJYBI3-gcc1nIlCDyMtdSTMjlrnbd-88BQ6xsGwx2nXboh1CVwEBMWZnAqx1oeh9Cj8tq3bdW95uKQbU1XCXD1a_hxF7sS4faYvNP7pWKH6rPdyU</recordid><startdate>20040201</startdate><enddate>20040201</enddate><creator>Scherberich, A</creator><creator>Tucker, R P</creator><creator>Samandari, E</creator><creator>Brown-Luedi, M</creator><creator>Martin, D</creator><creator>Chiquet-Ehrismann, R</creator><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></search><sort><creationdate>20040201</creationdate><title>Murine tenascin-W: a novel mammalian tenascin expressed in kidney and at sites of bone and smooth muscle development</title><author>Scherberich, A ; Tucker, R P ; Samandari, E ; Brown-Luedi, M ; Martin, D ; Chiquet-Ehrismann, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c382t-6e520d99ce62067936c2c99393e08a6171dba9b8003097a4e4767ba9ee284a73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Bone and Bones - embryology</topic><topic>Bone and Bones - metabolism</topic><topic>Cell Adhesion - physiology</topic><topic>Cells, Cultured</topic><topic>Cloning, Molecular</topic><topic>DNA, Complementary - genetics</topic><topic>DNA, Complementary - isolation & purification</topic><topic>Gene Expression Regulation, Developmental</topic><topic>Humans</topic><topic>Immunohistochemistry</topic><topic>In Situ Hybridization</topic><topic>Kidney - embryology</topic><topic>Kidney - metabolism</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Muscle, Smooth - embryology</topic><topic>Muscle, Smooth - metabolism</topic><topic>Organ Specificity</topic><topic>Phylogeny</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Tenascin - analogs & derivatives</topic><topic>Tenascin - biosynthesis</topic><topic>Tenascin - genetics</topic><topic>Tenascin - isolation & purification</topic><topic>Zebrafish</topic><topic>Zebrafish Proteins - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Scherberich, A</creatorcontrib><creatorcontrib>Tucker, R P</creatorcontrib><creatorcontrib>Samandari, E</creatorcontrib><creatorcontrib>Brown-Luedi, M</creatorcontrib><creatorcontrib>Martin, D</creatorcontrib><creatorcontrib>Chiquet-Ehrismann, 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><jtitle>Journal of cell science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Scherberich, A</au><au>Tucker, R P</au><au>Samandari, E</au><au>Brown-Luedi, M</au><au>Martin, D</au><au>Chiquet-Ehrismann, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Murine tenascin-W: a novel mammalian tenascin expressed in kidney and at sites of bone and smooth muscle development</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>2004-02-01</date><risdate>2004</risdate><volume>117</volume><issue>Pt 4</issue><spage>571</spage><epage>581</epage><pages>571-581</pages><issn>0021-9533</issn><eissn>1477-9137</eissn><abstract>We cloned and characterized a novel member of the tenascin family of extracellular matrix proteins--the murine orthologue of zebrafish tenascin-W. Full-length recombinant tenascin-W was expressed and purified from mammalian cell cultures. Rotary shadowing followed by electron microscopy showed that tenascin-W forms hexabrachions. We studied its expression during development and in the adult by immunohistochemistry, in situ hybridization and immunoblotting. Tenascin-W is expressed during palate formation, osteogenesis and smooth muscle development. In the adult, tenascin-W is found in the kidney, cardiac semilunar valves, corneal limbus and periosteum. Tenascin-W and tenascin-C expression overlap in many of these areas. Bone-morphogenic-protein-2 treated C2C12 cells secrete tenascin-W and are able to adhere to and to extend actin-rich processes on a tenascin-W substratum. In vitro, cells bind to tenascin-W in an RGD-dependent manner. This adhesion is increased by transfection of alpha8 integrin, which localizes with tenascin-W in the periosteum and kidney.</abstract><cop>England</cop><pmid>14709716</pmid><doi>10.1242/jcs.00867</doi><tpages>11</tpages></addata></record> |
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subjects | Amino Acid Sequence Animals Bone and Bones - embryology Bone and Bones - metabolism Cell Adhesion - physiology Cells, Cultured Cloning, Molecular DNA, Complementary - genetics DNA, Complementary - isolation & purification Gene Expression Regulation, Developmental Humans Immunohistochemistry In Situ Hybridization Kidney - embryology Kidney - metabolism Mice Molecular Sequence Data Muscle, Smooth - embryology Muscle, Smooth - metabolism Organ Specificity Phylogeny Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Tenascin - analogs & derivatives Tenascin - biosynthesis Tenascin - genetics Tenascin - isolation & purification Zebrafish Zebrafish Proteins - genetics |
title | Murine tenascin-W: a novel mammalian tenascin expressed in kidney and at sites of bone and smooth muscle development |
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