TRPC1 binds to caveolin-3 and is regulated by Src kinase - role in Duchenne muscular dystrophy
Transient receptor potential canonical 1 (TRPC1), a widely expressed calcium (Ca²⁺)-permeable channel, is potentially involved in the pathogenesis of Duchenne muscular dystrophy (DMD). Ca²⁺ influx through stretch-activated channels, possibly formed by TRPC1, induces muscle-cell damage in the mdx mou...
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| Veröffentlicht in: | Journal of cell science 2008-07, Vol.121 (13), p.2246-2255 |
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| creator | Gervásio, Othon L Whitehead, Nicholas P Yeung, Ella W Phillips, William D Allen, David G |
| description | Transient receptor potential canonical 1 (TRPC1), a widely expressed calcium (Ca²⁺)-permeable channel, is potentially involved in the pathogenesis of Duchenne muscular dystrophy (DMD). Ca²⁺ influx through stretch-activated channels, possibly formed by TRPC1, induces muscle-cell damage in the mdx mouse, an animal model of DMD. In this study, we showed that TRPC1, caveolin-3 and Src-kinase protein levels are increased in mdx muscle compared with wild type. TRPC1 and caveolin-3 colocalised and co-immunoprecipitated. Direct binding of TRPC1-CFP to caveolin-3-YFP was confirmed in C2 myoblasts by fluorescence energy resonance transfer (FRET). Caveolin-3-YFP targeted TRPC1-CFP to the plasma membrane. Hydrogen peroxide, a reactive oxygen species (ROS), increased Src activity and enhanced Ca²⁺ influx, but only in C2 myoblasts co-expressing TRPC1 and caveolin-3. In mdx muscle, Tiron, a ROS scavenger, and PP2, a Src inhibitor, reduced stretch-induced Ca²⁺ entry and increased force recovery. Because ROS production is increased in mdx/DMD, these results suggest that a ROS-Src-TRPC1/caveolin-3 pathway contributes to the pathogenesis of mdx/DMD. |
| doi_str_mv | 10.1242/jcs.032003 |
| format | Article |
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Ca²⁺ influx through stretch-activated channels, possibly formed by TRPC1, induces muscle-cell damage in the mdx mouse, an animal model of DMD. In this study, we showed that TRPC1, caveolin-3 and Src-kinase protein levels are increased in mdx muscle compared with wild type. TRPC1 and caveolin-3 colocalised and co-immunoprecipitated. Direct binding of TRPC1-CFP to caveolin-3-YFP was confirmed in C2 myoblasts by fluorescence energy resonance transfer (FRET). Caveolin-3-YFP targeted TRPC1-CFP to the plasma membrane. Hydrogen peroxide, a reactive oxygen species (ROS), increased Src activity and enhanced Ca²⁺ influx, but only in C2 myoblasts co-expressing TRPC1 and caveolin-3. In mdx muscle, Tiron, a ROS scavenger, and PP2, a Src inhibitor, reduced stretch-induced Ca²⁺ entry and increased force recovery. Because ROS production is increased in mdx/DMD, these results suggest that a ROS-Src-TRPC1/caveolin-3 pathway contributes to the pathogenesis of mdx/DMD.</description><identifier>ISSN: 0021-9533</identifier><identifier>EISSN: 1477-9137</identifier><identifier>DOI: 10.1242/jcs.032003</identifier><identifier>PMID: 18544631</identifier><language>eng</language><publisher>England: The Company of Biologists Limited</publisher><subject>Animals ; Caveolin 3 - metabolism ; Cell Membrane - metabolism ; Humans ; Hydrogen Peroxide - metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Muscle, Skeletal - metabolism ; Muscle, Skeletal - pathology ; Muscular Dystrophy, Animal - metabolism ; Muscular Dystrophy, Animal - pathology ; Muscular Dystrophy, Duchenne - etiology ; Muscular Dystrophy, Duchenne - metabolism ; Protein Binding ; Reactive Oxygen Species - metabolism ; Signal Transduction ; src-Family Kinases - metabolism ; TRPC Cation Channels - metabolism</subject><ispartof>Journal of cell science, 2008-07, Vol.121 (13), p.2246-2255</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c484t-502612f6eb8f66426d8290730d5be3b59420a4eb6e50d7267b27c86fbe2b716b3</citedby><cites>FETCH-LOGICAL-c484t-502612f6eb8f66426d8290730d5be3b59420a4eb6e50d7267b27c86fbe2b716b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,3665,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18544631$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gervásio, Othon L</creatorcontrib><creatorcontrib>Whitehead, Nicholas P</creatorcontrib><creatorcontrib>Yeung, Ella W</creatorcontrib><creatorcontrib>Phillips, William D</creatorcontrib><creatorcontrib>Allen, David G</creatorcontrib><title>TRPC1 binds to caveolin-3 and is regulated by Src kinase - role in Duchenne muscular dystrophy</title><title>Journal of cell science</title><addtitle>J Cell Sci</addtitle><description>Transient receptor potential canonical 1 (TRPC1), a widely expressed calcium (Ca²⁺)-permeable channel, is potentially involved in the pathogenesis of Duchenne muscular dystrophy (DMD). Ca²⁺ influx through stretch-activated channels, possibly formed by TRPC1, induces muscle-cell damage in the mdx mouse, an animal model of DMD. In this study, we showed that TRPC1, caveolin-3 and Src-kinase protein levels are increased in mdx muscle compared with wild type. TRPC1 and caveolin-3 colocalised and co-immunoprecipitated. Direct binding of TRPC1-CFP to caveolin-3-YFP was confirmed in C2 myoblasts by fluorescence energy resonance transfer (FRET). Caveolin-3-YFP targeted TRPC1-CFP to the plasma membrane. Hydrogen peroxide, a reactive oxygen species (ROS), increased Src activity and enhanced Ca²⁺ influx, but only in C2 myoblasts co-expressing TRPC1 and caveolin-3. In mdx muscle, Tiron, a ROS scavenger, and PP2, a Src inhibitor, reduced stretch-induced Ca²⁺ entry and increased force recovery. Because ROS production is increased in mdx/DMD, these results suggest that a ROS-Src-TRPC1/caveolin-3 pathway contributes to the pathogenesis of mdx/DMD.</description><subject>Animals</subject><subject>Caveolin 3 - metabolism</subject><subject>Cell Membrane - metabolism</subject><subject>Humans</subject><subject>Hydrogen Peroxide - metabolism</subject><subject>Male</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Muscle, Skeletal - metabolism</subject><subject>Muscle, Skeletal - pathology</subject><subject>Muscular Dystrophy, Animal - metabolism</subject><subject>Muscular Dystrophy, Animal - pathology</subject><subject>Muscular Dystrophy, Duchenne - etiology</subject><subject>Muscular Dystrophy, Duchenne - metabolism</subject><subject>Protein Binding</subject><subject>Reactive Oxygen Species - metabolism</subject><subject>Signal Transduction</subject><subject>src-Family Kinases - metabolism</subject><subject>TRPC Cation Channels - metabolism</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0E1P4zAQxnFrtWjbZbnwAcAnDisFxmPHTo6rsi9ISCBermvZzqRNSZNiJ0j99gS10h73NJefRnr-jJ0KuBSo8God0iVIBJCf2FwoY7JSSPOZzQFQZGUu5Yx9TWkNAAZL84XNRJErpaWYs79PD_cLwX3TVYkPPQ_ujfq26TLJXVfxJvFIy7F1A1Xc7_hjDPyl6VwinvHYt8Sbjl-PYUVdR3wzpjDZyKtdGmK_Xe2-saPatYlODveYPf_6-bT4k93e_b5Z_LjNgirUkOWAWmCtyRe11gp1VWAJRkKVe5I-LxWCU-Q15VAZ1MajCYWuPaE3Qnt5zC72f7exfx0pDXbTpEBt6zrqx2R1iRLzafL_IIKZ2ohygt_3MMQ-pUi13cZm4-LOCrAf2e2U3e6zT_js8HX0G6r-0UPnCZzvQe1665axSfb5EUFIgGlnKYR8B8SThLk</recordid><startdate>20080701</startdate><enddate>20080701</enddate><creator>Gervásio, Othon L</creator><creator>Whitehead, Nicholas P</creator><creator>Yeung, Ella W</creator><creator>Phillips, William D</creator><creator>Allen, David G</creator><general>The Company of Biologists Limited</general><scope>FBQ</scope><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>7QP</scope><scope>7X8</scope></search><sort><creationdate>20080701</creationdate><title>TRPC1 binds to caveolin-3 and is regulated by Src kinase - role in Duchenne muscular dystrophy</title><author>Gervásio, Othon L ; Whitehead, Nicholas P ; Yeung, Ella W ; Phillips, William D ; Allen, David G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c484t-502612f6eb8f66426d8290730d5be3b59420a4eb6e50d7267b27c86fbe2b716b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Animals</topic><topic>Caveolin 3 - metabolism</topic><topic>Cell Membrane - metabolism</topic><topic>Humans</topic><topic>Hydrogen Peroxide - metabolism</topic><topic>Male</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Muscle, Skeletal - metabolism</topic><topic>Muscle, Skeletal - pathology</topic><topic>Muscular Dystrophy, Animal - metabolism</topic><topic>Muscular Dystrophy, Animal - pathology</topic><topic>Muscular Dystrophy, Duchenne - etiology</topic><topic>Muscular Dystrophy, Duchenne - metabolism</topic><topic>Protein Binding</topic><topic>Reactive Oxygen Species - metabolism</topic><topic>Signal Transduction</topic><topic>src-Family Kinases - metabolism</topic><topic>TRPC Cation Channels - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gervásio, Othon L</creatorcontrib><creatorcontrib>Whitehead, Nicholas P</creatorcontrib><creatorcontrib>Yeung, Ella W</creatorcontrib><creatorcontrib>Phillips, William D</creatorcontrib><creatorcontrib>Allen, David G</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of cell science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gervásio, Othon L</au><au>Whitehead, Nicholas P</au><au>Yeung, Ella W</au><au>Phillips, William D</au><au>Allen, David G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>TRPC1 binds to caveolin-3 and is regulated by Src kinase - role in Duchenne muscular dystrophy</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>2008-07-01</date><risdate>2008</risdate><volume>121</volume><issue>13</issue><spage>2246</spage><epage>2255</epage><pages>2246-2255</pages><issn>0021-9533</issn><eissn>1477-9137</eissn><abstract>Transient receptor potential canonical 1 (TRPC1), a widely expressed calcium (Ca²⁺)-permeable channel, is potentially involved in the pathogenesis of Duchenne muscular dystrophy (DMD). Ca²⁺ influx through stretch-activated channels, possibly formed by TRPC1, induces muscle-cell damage in the mdx mouse, an animal model of DMD. In this study, we showed that TRPC1, caveolin-3 and Src-kinase protein levels are increased in mdx muscle compared with wild type. TRPC1 and caveolin-3 colocalised and co-immunoprecipitated. Direct binding of TRPC1-CFP to caveolin-3-YFP was confirmed in C2 myoblasts by fluorescence energy resonance transfer (FRET). Caveolin-3-YFP targeted TRPC1-CFP to the plasma membrane. Hydrogen peroxide, a reactive oxygen species (ROS), increased Src activity and enhanced Ca²⁺ influx, but only in C2 myoblasts co-expressing TRPC1 and caveolin-3. In mdx muscle, Tiron, a ROS scavenger, and PP2, a Src inhibitor, reduced stretch-induced Ca²⁺ entry and increased force recovery. Because ROS production is increased in mdx/DMD, these results suggest that a ROS-Src-TRPC1/caveolin-3 pathway contributes to the pathogenesis of mdx/DMD.</abstract><cop>England</cop><pub>The Company of Biologists Limited</pub><pmid>18544631</pmid><doi>10.1242/jcs.032003</doi><tpages>10</tpages></addata></record> |
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| subjects | Animals Caveolin 3 - metabolism Cell Membrane - metabolism Humans Hydrogen Peroxide - metabolism Male Mice Mice, Inbred C57BL Muscle, Skeletal - metabolism Muscle, Skeletal - pathology Muscular Dystrophy, Animal - metabolism Muscular Dystrophy, Animal - pathology Muscular Dystrophy, Duchenne - etiology Muscular Dystrophy, Duchenne - metabolism Protein Binding Reactive Oxygen Species - metabolism Signal Transduction src-Family Kinases - metabolism TRPC Cation Channels - metabolism |
| title | TRPC1 binds to caveolin-3 and is regulated by Src kinase - role in Duchenne muscular dystrophy |
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