A Mutation in the CASQ1 Gene Causes a Vacuolar Myopathy with Accumulation of Sarcoplasmic Reticulum Protein Aggregates. Issue 10 (10th September 2014)

• Record Type: Journal Article
• Authors: Rossi, Daniela; Vezzani, Bianca; Galli, Lucia; Paolini, Cecilia; Toniolo, Luana; Pierantozzi, Enrico; Spinozzi, Simone; Barone, Virginia; Pegoraro, Elena; Bello, Luca; Cenacchi, Giovanna; Vattemi, Gaetano; Tomelleri, Giuliano; Ricci, Giulia; Siciliano, Gabriele; Protasi, Feliciano; Reggiani, Carlo; Sorrentino, Vincenzo
• Is Part Of: Human mutation. Volume 35:Issue 10(2014:Oct.)
• Page Start: 1163
• Page End: 1170
• Publication Date: 2014-09-10
• Subjects: Human chromosome abnormalities -- Periodicals; Mutation (Biology) -- Periodicals; 616.04205
• DOI: 10.1002/humu.22631
• Languages: English
• ISSNs: 1059-7794

Abstract

<abstract abstract-type="graphical" xml:lang="en" id="humu22631-abs-0001"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Calsequestrin‐1 (CASQ1) is the major Ca²⁺ binding protein of the sarcoplasmic reticulum (SR) of skeletal muscles. We report the first mutation in the <italic>CASQ1</italic> gene in patients with a skeletal myopathy, characterized by muscle weakness, fatigue and the presence of aggregates of SR proteins. The <italic>CASQ1</italic> c.731A&gt;G (p.Asp244Gly) mutation is located in one of the high affinity Ca²⁺ binding sites in CASQ1 and causes the formation of protein aggregates, resulting in altered Ca²⁺ release in skeletal muscle fibers of patients. <boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgh1f9dbxkv" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>