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Calsequestrins in skeletal and cardiac muscle from adult Danio rerio.
Furlan, Sandra; Mosole, Simone; Murgia, Marta; Nagaraj, Nagarjuna; Argenton, Francesco; Volpe, Pompeo; Nori, Alessandra.
Affiliation
  • Furlan S; Institute of Neuroscience Consiglio Nazionale delle Ricerche, Viale G. Colombo 3, 35121, Padua, Italy.
  • Mosole S; Department of Biomedical Sciences, Istituto Interuniversitario di Miologia, University of Padova, Viale G. Colombo 3, 35121, Padua, Italy.
  • Murgia M; Department of Biomedical Sciences, Istituto Interuniversitario di Miologia, University of Padova, Viale G. Colombo 3, 35121, Padua, Italy.
  • Nagaraj N; Department of Proteomics and Signal Transduction, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.
  • Argenton F; Department of Proteomics and Signal Transduction, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.
  • Volpe P; Department of Biology, University of Padova, Via U.Bassi 58/B, 35121, Padua, Italy.
  • Nori A; Institute of Neuroscience Consiglio Nazionale delle Ricerche, Viale G. Colombo 3, 35121, Padua, Italy.
J Muscle Res Cell Motil ; 37(1-2): 27-39, 2016 04.
Article de En | MEDLINE | ID: mdl-26585961
ABSTRACT
Calsequestrin (Casq) is a high capacity, low affinity Ca(2+)-binding protein, critical for Ca(2+)-buffering in cardiac and skeletal muscle sarcoplasmic reticulum. All vertebrates have multiple genes encoding for different Casq isoforms. Increasing interest has been focused on mammalian and human Casq genes since mutations of both cardiac (Casq2) and skeletal muscle (Casq1) isoforms cause different, and sometime severe, human pathologies. Danio rerio (zebrafish) is a powerful model for studying function and mutations of human proteins. In this work, expression, biochemical properties cellular and sub-cellular localization of D. rerio native Casq isoforms are investigated. By quantitative PCR, three mRNAs were detected in skeletal muscle and heart with different abundances. Three zebrafish Casqs Casq1a, Casq1b and Casq2 were identified by mass spectrometry (Data are available via ProteomeXchange with identifier PXD002455). Skeletal and cardiac zebrafish calsequestrins share properties with mammalian Casq1 and Casq2. Skeletal Casqs were found primarily, but not exclusively, at the sarcomere Z-line level where terminal cisternae of sarcoplasmic reticulum are located.
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Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Calséquestrine / Muscles squelettiques / Protéines de poisson-zèbre / Myocarde Limites: Animals Langue: En Journal: J Muscle Res Cell Motil Année: 2016 Type de document: Article Pays d'affiliation: Italie

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Calséquestrine / Muscles squelettiques / Protéines de poisson-zèbre / Myocarde Limites: Animals Langue: En Journal: J Muscle Res Cell Motil Année: 2016 Type de document: Article Pays d'affiliation: Italie