Expression pattern of muscleblind-like proteins differs in differentiating myoblasts
Muscleblind-like (MBNL) proteins are believed to be regulators of myogenesis and are implicated in myotonic dystrophy. While Drosophila melanogaster muscleblind is required for terminal muscle differentiation, mammalian MBNL3 functions as an inhibitor of myogenesis. In this study, we analyzed the ex...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2007-09, Vol.361 (1), p.151-155 |
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| creator | Lee, Kyung-Soon Squillace, Rachel M. Wang, Edith H. |
| description | Muscleblind-like (MBNL) proteins are believed to be regulators of myogenesis and are implicated in myotonic dystrophy. While
Drosophila melanogaster muscleblind is required for terminal muscle differentiation, mammalian MBNL3 functions as an inhibitor of myogenesis. In this study, we analyzed the expression pattern of MBNL3 in different adult mouse tissues and tissue culture cells. MBNL3 transcript is enriched in the lung, spleen, and testis and not in heart and skeletal muscle. By Western blotting, we found that MBNL3 was expressed in C2C12 myoblasts and ts13 myofibroblasts, but was detected at significantly lower levels in fibroblasts. MBNL3 protein levels decreased when cells were shifted to muscle differentiation conditions, but the closely related MBNL1 protein was unaffected. These results suggest that myoblasts and fibroblasts respond to differentiation conditions by activating signaling pathways that repress MBNL3 but not MBNL1 expression. |
| doi_str_mv | 10.1016/j.bbrc.2007.06.165 |
| format | Article |
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Drosophila melanogaster muscleblind is required for terminal muscle differentiation, mammalian MBNL3 functions as an inhibitor of myogenesis. In this study, we analyzed the expression pattern of MBNL3 in different adult mouse tissues and tissue culture cells. MBNL3 transcript is enriched in the lung, spleen, and testis and not in heart and skeletal muscle. By Western blotting, we found that MBNL3 was expressed in C2C12 myoblasts and ts13 myofibroblasts, but was detected at significantly lower levels in fibroblasts. MBNL3 protein levels decreased when cells were shifted to muscle differentiation conditions, but the closely related MBNL1 protein was unaffected. These results suggest that myoblasts and fibroblasts respond to differentiation conditions by activating signaling pathways that repress MBNL3 but not MBNL1 expression.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2007.06.165</identifier><identifier>PMID: 17644069</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell Differentiation ; Cell Line ; Cricetinae ; Cys3His zinc finger ; DNA-Binding Proteins - metabolism ; Fibroblasts ; Fibroblasts - metabolism ; Gene Expression ; MBNL proteins ; Mice ; Muscle differentiation ; Muscleblind ; Myoblasts ; Myoblasts - cytology ; Myoblasts - metabolism ; Nuclear Proteins - metabolism ; RNA-Binding Proteins - metabolism ; Tissue Distribution</subject><ispartof>Biochemical and biophysical research communications, 2007-09, Vol.361 (1), p.151-155</ispartof><rights>2007 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c519t-4e3b012c41c0d5f56ee01824a3024808ff304a052e811e07744f38120f3e515d3</citedby><cites>FETCH-LOGICAL-c519t-4e3b012c41c0d5f56ee01824a3024808ff304a052e811e07744f38120f3e515d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X0701443X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17644069$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, Kyung-Soon</creatorcontrib><creatorcontrib>Squillace, Rachel M.</creatorcontrib><creatorcontrib>Wang, Edith H.</creatorcontrib><title>Expression pattern of muscleblind-like proteins differs in differentiating myoblasts</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Muscleblind-like (MBNL) proteins are believed to be regulators of myogenesis and are implicated in myotonic dystrophy. While
Drosophila melanogaster muscleblind is required for terminal muscle differentiation, mammalian MBNL3 functions as an inhibitor of myogenesis. In this study, we analyzed the expression pattern of MBNL3 in different adult mouse tissues and tissue culture cells. MBNL3 transcript is enriched in the lung, spleen, and testis and not in heart and skeletal muscle. By Western blotting, we found that MBNL3 was expressed in C2C12 myoblasts and ts13 myofibroblasts, but was detected at significantly lower levels in fibroblasts. MBNL3 protein levels decreased when cells were shifted to muscle differentiation conditions, but the closely related MBNL1 protein was unaffected. These results suggest that myoblasts and fibroblasts respond to differentiation conditions by activating signaling pathways that repress MBNL3 but not MBNL1 expression.</description><subject>Animals</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Differentiation</subject><subject>Cell Line</subject><subject>Cricetinae</subject><subject>Cys3His zinc finger</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Fibroblasts</subject><subject>Fibroblasts - metabolism</subject><subject>Gene Expression</subject><subject>MBNL proteins</subject><subject>Mice</subject><subject>Muscle differentiation</subject><subject>Muscleblind</subject><subject>Myoblasts</subject><subject>Myoblasts - cytology</subject><subject>Myoblasts - metabolism</subject><subject>Nuclear Proteins - metabolism</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>Tissue Distribution</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9UcFu1TAQtBCIPlp-gAPKiVvSXcdxEgkhoapApUpcitSb5Tjr4kdiB9uvav-ePL0noJeedqWdmR3NMPYOoUJAeb6thiGaigO0FcgKZfOCbRB6KDmCeMk2ACBL3uPtCXuT0hYAUcj-NTvBVgoBst-wm8uHJVJKLvhi0TlT9EWwxbxLZqJhcn4sJ_eLiiWGTM6nYnTWUkyF88eVfHY6O39XzI9hmHTK6Yy9snpK9PY4T9mPL5c3F9_K6-9fry4-X5emwT6XguoBkBuBBsbGNpIIsONC18BFB521NQgNDacOkaBthbB1hxxsTQ02Y33KPh10l90w02hWK1FPaolu1vFRBe3U04t3P9VduFfY9wJavgp8OArE8HtHKavZJUPTpD2FXVJy_Ya9FCuQH4AmhpQi2b9PENS-DLVV-zLUvgwFUq1lrKT3_9v7RzmmvwI-HgC0hnTvKKpkHHlDo4tkshqDe07_D5YAnPw</recordid><startdate>20070914</startdate><enddate>20070914</enddate><creator>Lee, Kyung-Soon</creator><creator>Squillace, Rachel M.</creator><creator>Wang, Edith H.</creator><general>Elsevier Inc</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20070914</creationdate><title>Expression pattern of muscleblind-like proteins differs in differentiating myoblasts</title><author>Lee, Kyung-Soon ; Squillace, Rachel M. ; Wang, Edith H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c519t-4e3b012c41c0d5f56ee01824a3024808ff304a052e811e07744f38120f3e515d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Animals</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Differentiation</topic><topic>Cell Line</topic><topic>Cricetinae</topic><topic>Cys3His zinc finger</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Fibroblasts</topic><topic>Fibroblasts - metabolism</topic><topic>Gene Expression</topic><topic>MBNL proteins</topic><topic>Mice</topic><topic>Muscle differentiation</topic><topic>Muscleblind</topic><topic>Myoblasts</topic><topic>Myoblasts - cytology</topic><topic>Myoblasts - metabolism</topic><topic>Nuclear Proteins - metabolism</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>Tissue Distribution</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, Kyung-Soon</creatorcontrib><creatorcontrib>Squillace, Rachel M.</creatorcontrib><creatorcontrib>Wang, Edith H.</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, Kyung-Soon</au><au>Squillace, Rachel M.</au><au>Wang, Edith H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression pattern of muscleblind-like proteins differs in differentiating myoblasts</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2007-09-14</date><risdate>2007</risdate><volume>361</volume><issue>1</issue><spage>151</spage><epage>155</epage><pages>151-155</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Muscleblind-like (MBNL) proteins are believed to be regulators of myogenesis and are implicated in myotonic dystrophy. While
Drosophila melanogaster muscleblind is required for terminal muscle differentiation, mammalian MBNL3 functions as an inhibitor of myogenesis. In this study, we analyzed the expression pattern of MBNL3 in different adult mouse tissues and tissue culture cells. MBNL3 transcript is enriched in the lung, spleen, and testis and not in heart and skeletal muscle. By Western blotting, we found that MBNL3 was expressed in C2C12 myoblasts and ts13 myofibroblasts, but was detected at significantly lower levels in fibroblasts. MBNL3 protein levels decreased when cells were shifted to muscle differentiation conditions, but the closely related MBNL1 protein was unaffected. These results suggest that myoblasts and fibroblasts respond to differentiation conditions by activating signaling pathways that repress MBNL3 but not MBNL1 expression.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17644069</pmid><doi>10.1016/j.bbrc.2007.06.165</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Animals Carrier Proteins - genetics Carrier Proteins - metabolism Cell Differentiation Cell Line Cricetinae Cys3His zinc finger DNA-Binding Proteins - metabolism Fibroblasts Fibroblasts - metabolism Gene Expression MBNL proteins Mice Muscle differentiation Muscleblind Myoblasts Myoblasts - cytology Myoblasts - metabolism Nuclear Proteins - metabolism RNA-Binding Proteins - metabolism Tissue Distribution |
| title | Expression pattern of muscleblind-like proteins differs in differentiating myoblasts |
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