ZFIN ID: ZDB-PUB-090424-21
Myofibrillogenesis in skeletal muscle cells in zebrafish
Sanger, J.W., Wang, J., Holloway, B., Du, A., and Sanger, J.M.
Date: 2009
Source: Cell motility and the cytoskeleton   66(8): 556-566 (Journal)
Registered Authors: Holloway, Beth A.
Keywords: myofibrillogenesis, myofibril, alpha-actinin, myosin, A-bands, premyofibril, nascent myofibril, mature myofibril, fluorescence recovery after photobleaching, FRAP
MeSH Terms:
  • Actinin/genetics
  • Actinin/metabolism
  • Animals
  • Embryo, Nonmammalian/metabolism
  • Fluorescence Recovery After Photobleaching
  • Humans
  • Muscle Development/physiology*
  • Muscle, Skeletal/cytology*
  • Muscle, Skeletal/metabolism*
  • Myofibrils/metabolism*
  • Myosin Type II/genetics
  • Myosin Type II/metabolism
  • Zebrafish/embryology*
  • Zebrafish/metabolism*
  • Zebrafish Proteins/metabolism
PubMed: 19382198 Full text @ Cell Motil. Cytoskeleton
The "premyofibril" model of myofibrillogenesis, based on observations in cultured avian muscle cells, proposes that mature myofibrils are preceded by two intermediary structures: premyofibrils and nascent myofibrils. To determine if this model applies to zebrafish skeletal muscle development, we stained developing embryos with antibodies to sarcomeric alpha-actinin and myosin II. In the youngest muscle cells, sarcomeric alpha-actinin and non-muscle myosin II were each localized in linear arrays of small bands that resembled the premyofibrils in avian myocytes. The distribution of muscle-specific myosin II began as scattered short filaments followed in time by overlapping bundles of filaments and organized A-bands in the older somites. Alpha-actinin organization changed from small z-bodies to beaded Z-bands and ordered Z-bands in myofibrils that extended the length of the elongating somites. In older somites with mature myofibrils, premyofibrils were also present at the ends of the mature myofibrils, suggesting that as the cells and somites grew longer, premyofibrils were involved in the elongation of existing mature myofibrils. Fluorescence Recovery After Photobleaching showed that the exchange of proteins (actin, alpha-actinin, FATZ, myotilin and telethonin) between sarcoplasm and the Z-bands of mature myofibrils in zebrafish resembled that seen for the same proteins in cultured avian myotubes, suggesting that myofibril assembly and maintenance in zebrafish share common properties with avian muscle.