{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2022,4,20]],"date-time":"2022-04-20T02:26:12Z","timestamp":1650421572539},"reference-count":45,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2011,9,1]]},"abstract":"<jats:p>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 Ca2+ channel, and this process is called activation-link formation [Gangopadhyay and Ikemoto (2008) Biochem. J. 411, 415\u2013423]. 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 Ca2+ 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.<\/jats:p>","DOI":"10.1042\/bj20110203","type":"journal-article","created":{"date-parts":[[2011,7,4]],"date-time":"2011-07-04T15:49:08Z","timestamp":1309794548000},"page":"379-387","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Aberrant interaction of calmodulin with the ryanodine receptor develops hypertrophy in the neonatal cardiomyocyte"],"prefix":"10.1042","volume":"438","author":[{"given":"Jaya\u00a0P.","family":"Gangopadhyay","sequence":"first","affiliation":[{"name":"Boston Biomedical Research Institute, Watertown, MA 02472, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Noriaki","family":"Ikemoto","sequence":"additional","affiliation":[{"name":"Boston Biomedical Research Institute, Watertown, MA 02472, U.S.A."},{"name":"Department of Neurology, Harvard Medical School, Boston, MA 02115, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2011,8,12]]},"reference":[{"key":"2021112214533279700_B1","doi-asserted-by":"crossref","first-page":"3065","DOI":"10.1016\/S0021-9258(18)61469-3","article-title":"Rapid calcium release from cardiac sarcoplasmic reticulum vesicles is dependent on Ca2+ and is modulated by Mg2+, adenine nucleotide, and calmodulin","volume":"262","author":"Meissner","year":"1987","journal-title":"J. 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