title: Calsequestrins in skeletal and cardiac muscle from adult Danio rerio.
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.
authors.affiliation: Institute of Neuroscience Consiglio Nazionale delle Ricerche, Viale G. Colombo 3, 35121, Padua, Italy.
authors.forename: Sandra
authors.initials: S
authors.lastname: Furlan
authors.affiliation: Department of Biomedical Sciences, Istituto Interuniversitario di Miologia, University of Padova, Viale G. Colombo 3, 35121, Padua, Italy.
authors.forename: Simone
authors.initials: S
authors.lastname: Mosole
authors.affiliation: Department of Biomedical Sciences, Istituto Interuniversitario di Miologia, University of Padova, Viale G. Colombo 3, 35121, Padua, Italy.|Department of Proteomics and Signal Transduction, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.
authors.forename: Marta
authors.initials: M
authors.lastname: Murgia
authors.affiliation: Department of Proteomics and Signal Transduction, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.
authors.forename: Nagarjuna
authors.initials: N
authors.lastname: Nagaraj
authors.affiliation: Department of Biology, University of Padova, Via U.Bassi 58/B, 35121, Padua, Italy.
authors.forename: Francesco
authors.initials: F
authors.lastname: Argenton
authors.affiliation: Institute of Neuroscience Consiglio Nazionale delle Ricerche, Viale G. Colombo 3, 35121, Padua, Italy.|Department of Biomedical Sciences, Istituto Interuniversitario di Miologia, University of Padova, Viale G. Colombo 3, 35121, Padua, Italy.
authors.forename: Pompeo
authors.initials: P
authors.lastname: Volpe
authors.affiliation: Department of Biomedical Sciences, Istituto Interuniversitario di Miologia, University of Padova, Viale G. Colombo 3, 35121, Padua, Italy. alessandra.nori@unipd.it.
authors.forename: Alessandra
authors.identifier: 0000-0003-3968-9450
authors.initials: A
authors.lastname: Nori
mesh_terms: D000818:Animals; D002155:Calsequestrin / Q000235:genetics / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000378:metabolism*; D009154:Mutation; D009206:Myocardium / Q000378:metabolism*; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D015027:Zebrafish; D029961:Zebrafish Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D002155:Calsequestrin; D020033:Protein Isoforms; D029961:Zebrafish Proteins
keywords: Animal models; Ca2+-binding proteins; Danio rerio; Sarcoplasmic reticulum