| pubmed-article:21649588 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21649588 | lifeskim:mentions | umls-concept:C0021289 | lld:lifeskim |
| pubmed-article:21649588 | lifeskim:mentions | umls-concept:C0225828 | lld:lifeskim |
| pubmed-article:21649588 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
| pubmed-article:21649588 | lifeskim:mentions | umls-concept:C0054493 | lld:lifeskim |
| pubmed-article:21649588 | lifeskim:mentions | umls-concept:C0020564 | lld:lifeskim |
| pubmed-article:21649588 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:21649588 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:21649588 | pubmed:dateCreated | 2011-8-12 | lld:pubmed |
| pubmed-article:21649588 | pubmed:abstractText | We have shown previously that the inter-domain interaction between the two domains of RyR (ryanodine receptor), CaMBD [CaM (calmodulin)-binding domain] and CaMLD (CaM-like domain), activates the Ca(2+) channel, and this process is called activation-link formation [Gangopadhyay and Ikemoto (2008) Biochem. J. 411, 415-423]. Thus CaM that is bound to CaMBD is expected to interfere the activation-link formation, thereby stabilizing the closed state of the channel under normal conditions. In the present paper, we report that, upon stimulation of neonatal cardiomyocytes with the pro-hypertrophy agonist ET-1 (endothelin-1), CaM dissociates from the RyR, which induces a series of intracellular events: increased frequency of Ca(2+) transients, translocation of the signalling molecules CaM, CaMKII (CaM kinase II) and the transcription factor NFAT (nuclear factor of activated T-cells) to the nucleus. These events then lead to the development of hypertrophy. Importantly, an anti-CaMBD antibody that interferes with activation-link formation prevented all of these intracellular events triggered by ET-1 and prevented the development of hypertrophy. These results indicate that the aberrant formation of the activation link between CaMBD and CaMLD of RyR is a key step in the development of hypertrophy in cultured cardiomyocytes. | lld:pubmed |
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| pubmed-article:21649588 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21649588 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21649588 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:21649588 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21649588 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:21649588 | pubmed:issn | 1470-8728 | lld:pubmed |
| pubmed-article:21649588 | pubmed:author | pubmed-author:IkemotoNoriak... | lld:pubmed |
| pubmed-article:21649588 | pubmed:author | pubmed-author:GangopadhyayJ... | lld:pubmed |
| pubmed-article:21649588 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21649588 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:21649588 | pubmed:volume | 438 | lld:pubmed |
| pubmed-article:21649588 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21649588 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21649588 | pubmed:pagination | 379-87 | lld:pubmed |
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| pubmed-article:21649588 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21649588 | pubmed:articleTitle | Aberrant interaction of calmodulin with the ryanodine receptor develops hypertrophy in the neonatal cardiomyocyte. | lld:pubmed |
| pubmed-article:21649588 | pubmed:affiliation | Boston Biomedical Research Institute, Watertown, MA 02472, USA. jaya@bbri.org | lld:pubmed |
| pubmed-article:21649588 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21649588 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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