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Calsequestrins in skeletal and cardiac muscle from adult Danio rerio

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Abstract

Calsequestrin (Casq) is a high capacity, low affinity Ca2+-binding protein, critical for Ca2+-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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Abbreviations

B2M:

Beta-2 microglobulin

casq :

Zebrafish calsequestrin genes

Casq:

Zebrafish calsequestrin proteins

DTT:

DL-Dithiothreitol

EF1a:

Elongation factor 1-alpha

NDUFS3:

NADH dehydrogenase [ubiquinone] iron-sulfur protein 3

EGTA:

Ethylene glycol-bis(2-aminoethylether)-N,N,N′,N′-tetraacetic acid

HEPES:

4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acid

MOPS:

4-Morpholinepropanesulfonic acid

PMSF:

Phenylmethylsulfonyl fluoride

Ryr:

Ryanodine receptor

SDS:

Sodium dodecyl sulfate

SERCA1:

Sarcoplasmic/endoplasmic reticulum calcium ATPase 1

SR:

Sarcoplasmic reticulum

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Acknowledgments

We thank Matthias Mann for his support in Mass Spectrometry data generation and analysis, Martina Milanetto, Korbinian Mayr, Igor Paron and Gabriele Sowa for their technical assistance. This work was supported by research funds from the University of Padova (ex 60 %).

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Authors and Affiliations

  1. Institute of Neuroscience Consiglio Nazionale delle Ricerche, Viale G. Colombo 3, 35121, Padua, Italy

    Sandra Furlan & Pompeo Volpe

  2. Department of Biomedical Sciences, Istituto Interuniversitario di Miologia, University of Padova, Viale G. Colombo 3, 35121, Padua, Italy

    Simone Mosole, Marta Murgia, Pompeo Volpe & Alessandra Nori

  3. Department of Proteomics and Signal Transduction, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany

    Marta Murgia & Nagarjuna Nagaraj

  4. Department of Biology, University of Padova, Via U.Bassi 58/B, 35121, Padua, Italy

    Francesco Argenton

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  1. Sandra Furlan
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  2. Simone Mosole
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  3. Marta Murgia
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  4. Nagarjuna Nagaraj
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  5. Francesco Argenton
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  7. Alessandra Nori
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Correspondence to Alessandra Nori.

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Furlan, S., Mosole, S., Murgia, M. et al. Calsequestrins in skeletal and cardiac muscle from adult Danio rerio . J Muscle Res Cell Motil 37, 27–39 (2016). https://doi.org/10.1007/s10974-015-9432-2

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  • DOI: https://doi.org/10.1007/s10974-015-9432-2

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