ZFIN ID: ZDB-PUB-151121-6
Calsequestrins in skeletal and cardiac muscle from adult Danio rerio
Furlan, S., Mosole, S., Murgia, M., Nagaraj, N., Argenton, F., Volpe, P., Nori, A.
Date: 2016
Source: Journal of muscle research and cell motility   37(1-2): 27-39 (Journal)
Registered Authors: Argenton, Francesco
Keywords: Animal models, Ca2+-binding proteins, Danio rerio, Sarcoplasmic reticulum
MeSH Terms:
  • Animals
  • Calsequestrin/genetics
  • Calsequestrin/metabolism*
  • Muscle, Skeletal/metabolism*
  • Mutation
  • Myocardium/metabolism*
  • Protein Isoforms/genetics
  • Protein Isoforms/metabolism
  • Zebrafish
  • Zebrafish Proteins/genetics
  • Zebrafish Proteins/metabolism*
PubMed: 26585961 Full text @ J. Muscle Res. Cell Motil.
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.