{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,3]],"date-time":"2026-04-03T04:35:35Z","timestamp":1775190935131,"version":"3.50.1"},"reference-count":171,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2022,10,12]],"date-time":"2022-10-12T00:00:00Z","timestamp":1665532800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100002426","name":"Fondazione Telethon","doi-asserted-by":"publisher","award":["GGP19231"],"award-info":[{"award-number":["GGP19231"]}],"id":[{"id":"10.13039\/501100002426","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AR059646"],"award-info":[{"award-number":["AR059646"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Physiol."],"abstract":"<jats:p><jats:bold>Introduction:<\/jats:bold> Ca<jats:sup>2+<\/jats:sup> levels in adult skeletal muscle fibers are mainly controlled by excitation-contraction (EC) coupling, a mechanism that translates action potentials in release of Ca<jats:sup>2+<\/jats:sup> from the sarcoplasmic reticulum (SR) release channels, i.e. the ryanodine receptors type-1 (RyR1). Calsequestrin (Casq) is a protein that binds large amounts of Ca<jats:sup>2+<\/jats:sup> in the lumen of the SR terminal cisternae, near sites of Ca<jats:sup>2+<\/jats:sup> release. There is general agreement that Casq is not only important for the SR ability to store Ca<jats:sup>2+<\/jats:sup>, but also for modulating the opening probability of the RyR Ca<jats:sup>2+<\/jats:sup> release channels.<\/jats:p><jats:p><jats:bold>The initial studies:<\/jats:bold> About 20\u00a0years ago we generated a mouse model lacking Casq1 (Casq1-null mice), the isoform predominantly expressed in adult fast twitch skeletal muscle. While the knockout was not lethal as expected, lack of Casq1 caused a striking remodeling of membranes of SR and of transverse tubules (TTs), and mitochondrial damage. Functionally, CASQ1-knockout resulted in reduced SR Ca<jats:sup>2+<\/jats:sup> content, smaller Ca<jats:sup>2+<\/jats:sup> transients, and severe SR depletion during repetitive stimulation.<\/jats:p><jats:p><jats:bold>The myopathic phenotype of Casq1-null mice:<\/jats:bold> After the initial studies, we discovered that Casq1-null mice were prone to sudden death when exposed to halogenated anaesthetics, heat and even strenuous exercise. These syndromes are similar to human malignant hyperthermia susceptibility (MHS) and environmental-exertional heat stroke (HS). We learned that mechanisms underlying these syndromes involved excessive SR Ca<jats:sup>2+<\/jats:sup> leak and excessive production of oxidative species: indeed, mortality and mitochondrial damage were significantly prevented by administration of antioxidants and reduction of oxidative stress. Though, how Casq1-null mice could survive without the most important SR Ca<jats:sup>2+<\/jats:sup> binding protein was a puzzling issue that was not solved.<\/jats:p><jats:p><jats:bold>Unravelling the mystery:<\/jats:bold> The mystery was finally solved in 2020, when we discovered that in Casq1-null mice the SR undergoes adaptations that result in constitutively active store-operated Ca<jats:sup>2+<\/jats:sup> entry (SOCE). SOCE is a mechanism that allows skeletal fibers to use external Ca<jats:sup>2+<\/jats:sup> when SR stores are depleted. The post-natal compensatory mechanism that allows Casq1-null mice to survive involves the assembly of new SR-TT junctions (named Ca<jats:sup>2+<\/jats:sup> entry units) containing Stim1 and Orai1, the two proteins that mediate SOCE.<\/jats:p>","DOI":"10.3389\/fphys.2022.1033300","type":"journal-article","created":{"date-parts":[[2022,10,12]],"date-time":"2022-10-12T12:28:54Z","timestamp":1665577734000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":9,"title":["Ablation of Calsequestrin-1, Ca2+ unbalance, and susceptibility to heat stroke"],"prefix":"10.3389","volume":"13","author":[{"given":"Feliciano","family":"Protasi","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Barbara","family":"Girolami","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Matteo","family":"Serano","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Laura","family":"Pietrangelo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cecilia","family":"Paolini","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1965","published-online":{"date-parts":[[2022,10,12]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"275","DOI":"10.1016\/0378-1119(91)90621-h","article-title":"Cloning and characterization of the gene encoding rabbit cardiac calsequestrin","volume":"109","author":"Arai","year":"1991","journal-title":"Gene"},{"key":"B2","doi-asserted-by":"publisher","first-page":"3444","DOI":"10.1529\/biophysj.104.051441","article-title":"Regulation of ryanodine receptors by calsequestrin: Effect of high luminal Ca2+ and phosphorylation","volume":"88","author":"Beard","year":"2005","journal-title":"Biophys. 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