Beta-synemin expression in cardiotoxin-injected rat skeletal muscle
<p>Abstract</p> <p>Background</p> <p>β-synemin was originally identified in humans as an α-dystrobrevin-binding protein through a yeast two-hybrid screen using an amino acid sequence derived from exons 1 through 16 of α-dystrobrevin, a region common to both α-dystrobrev...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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BMC
2007-05-01
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| Series: | BMC Musculoskeletal Disorders |
| Online Access: | http://www.biomedcentral.com/1471-2474/8/40 |
| _version_ | 1818118592191791104 |
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| author | Okamoto Koichi Tamaoka Akira Ohkoshi Norio Hoshino Sachiko Ishii Akiko Guyon Jeffrey R Mizuno Yuji Kunkel Louis M |
| author_facet | Okamoto Koichi Tamaoka Akira Ohkoshi Norio Hoshino Sachiko Ishii Akiko Guyon Jeffrey R Mizuno Yuji Kunkel Louis M |
| author_sort | Okamoto Koichi |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>β-synemin was originally identified in humans as an α-dystrobrevin-binding protein through a yeast two-hybrid screen using an amino acid sequence derived from exons 1 through 16 of α-dystrobrevin, a region common to both α-dystrobrevin-1 and -2. α-Dystrobrevin-1 and -2 are both expressed in muscle and co-localization experiments have determined which isoform preferentially functions with β-synemin <it>in vivo</it>. The aim of our study is to show whether each α-dystrobrevin isoform has the same affinity for β-synemin or whether one of the isoforms preferentially functions with β-synemin in muscle.</p> <p>Methods</p> <p>The two α-dystrobrevin isoforms (-1 and -2) and β-synemin were localized in regenerating rat tibialis anterior muscle using immunoprecipitation, immunohistochemical and immunoblot analyses. Immunoprecipitation and co-localization studies for α-dystrobrevin and β-synemin were performed in regenerating muscle following cardiotoxin injection. Protein expression was then compared to that of developing rat muscle using immunoblot analysis.</p> <p>Results</p> <p>With an anti-α-dystrobrevin antibody, β-synemin co-immunoprecipitated with α-dystrobrevin whereas with an anti-β-synemin antibody, α-dystrobrevin-1 (rather than the -2 isoform) preferentially co-immunoprecipitated with β-synemin. Immunohistochemical experiments show that β-synemin and α-dystrobrevin co-localize in rat skeletal muscle. In regenerating muscle, β-synemin is first expressed at the sarcolemma and in the cytoplasm at day 5 following cardiotoxin injection. Similarly, β-synemin and α-dystrobrevin-1 are detected by immunoblot analysis as weak bands by day 7. In contrast, immunoblot analysis shows that α-dystrobrevin-2 is expressed as early as 1 day post-injection in regenerating muscle. These results are similar to that of developing muscle. For example, in embryonic rats, immunoblot analysis shows that β-synemin and α-dystrobevin-1 are weakly expressed in developing lower limb muscle at 5 days post-birth, while α-dystrobrevin-2 is detectable before birth in 20-day post-fertilization embryos.</p> <p>Conclusion</p> <p>Our results clearly show that β-synemin expression correlates with that of α-dystrobrevin-1, suggesting that β-synemin preferentially functions with α-dystrobrevin-1 <it>in vivo </it>and that these proteins are likely to function coordinately to play a vital role in developing and regenerating muscle.</p> |
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| format | Article |
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| institution | Directory Open Access Journal |
| issn | 1471-2474 |
| language | English |
| last_indexed | 2024-12-11T04:56:45Z |
| publishDate | 2007-05-01 |
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| series | BMC Musculoskeletal Disorders |
| spelling | doaj.art-7d5b88fa7eed46fbb259d40fa4dc0aa22022-12-22T01:20:15ZengBMCBMC Musculoskeletal Disorders1471-24742007-05-01814010.1186/1471-2474-8-40Beta-synemin expression in cardiotoxin-injected rat skeletal muscleOkamoto KoichiTamaoka AkiraOhkoshi NorioHoshino SachikoIshii AkikoGuyon Jeffrey RMizuno YujiKunkel Louis M<p>Abstract</p> <p>Background</p> <p>β-synemin was originally identified in humans as an α-dystrobrevin-binding protein through a yeast two-hybrid screen using an amino acid sequence derived from exons 1 through 16 of α-dystrobrevin, a region common to both α-dystrobrevin-1 and -2. α-Dystrobrevin-1 and -2 are both expressed in muscle and co-localization experiments have determined which isoform preferentially functions with β-synemin <it>in vivo</it>. The aim of our study is to show whether each α-dystrobrevin isoform has the same affinity for β-synemin or whether one of the isoforms preferentially functions with β-synemin in muscle.</p> <p>Methods</p> <p>The two α-dystrobrevin isoforms (-1 and -2) and β-synemin were localized in regenerating rat tibialis anterior muscle using immunoprecipitation, immunohistochemical and immunoblot analyses. Immunoprecipitation and co-localization studies for α-dystrobrevin and β-synemin were performed in regenerating muscle following cardiotoxin injection. Protein expression was then compared to that of developing rat muscle using immunoblot analysis.</p> <p>Results</p> <p>With an anti-α-dystrobrevin antibody, β-synemin co-immunoprecipitated with α-dystrobrevin whereas with an anti-β-synemin antibody, α-dystrobrevin-1 (rather than the -2 isoform) preferentially co-immunoprecipitated with β-synemin. Immunohistochemical experiments show that β-synemin and α-dystrobrevin co-localize in rat skeletal muscle. In regenerating muscle, β-synemin is first expressed at the sarcolemma and in the cytoplasm at day 5 following cardiotoxin injection. Similarly, β-synemin and α-dystrobrevin-1 are detected by immunoblot analysis as weak bands by day 7. In contrast, immunoblot analysis shows that α-dystrobrevin-2 is expressed as early as 1 day post-injection in regenerating muscle. These results are similar to that of developing muscle. For example, in embryonic rats, immunoblot analysis shows that β-synemin and α-dystrobevin-1 are weakly expressed in developing lower limb muscle at 5 days post-birth, while α-dystrobrevin-2 is detectable before birth in 20-day post-fertilization embryos.</p> <p>Conclusion</p> <p>Our results clearly show that β-synemin expression correlates with that of α-dystrobrevin-1, suggesting that β-synemin preferentially functions with α-dystrobrevin-1 <it>in vivo </it>and that these proteins are likely to function coordinately to play a vital role in developing and regenerating muscle.</p>http://www.biomedcentral.com/1471-2474/8/40 |
| spellingShingle | Okamoto Koichi Tamaoka Akira Ohkoshi Norio Hoshino Sachiko Ishii Akiko Guyon Jeffrey R Mizuno Yuji Kunkel Louis M Beta-synemin expression in cardiotoxin-injected rat skeletal muscle BMC Musculoskeletal Disorders |
| title | Beta-synemin expression in cardiotoxin-injected rat skeletal muscle |
| title_full | Beta-synemin expression in cardiotoxin-injected rat skeletal muscle |
| title_fullStr | Beta-synemin expression in cardiotoxin-injected rat skeletal muscle |
| title_full_unstemmed | Beta-synemin expression in cardiotoxin-injected rat skeletal muscle |
| title_short | Beta-synemin expression in cardiotoxin-injected rat skeletal muscle |
| title_sort | beta synemin expression in cardiotoxin injected rat skeletal muscle |
| url | http://www.biomedcentral.com/1471-2474/8/40 |
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