Dystrophin-related protein in the fetal and denervated skeletal muscles of normal and mdx mice

Biochem Biophys Res Commun. 1991 Nov 14;180(3):1179-86. doi: 10.1016/s0006-291x(05)81320-8.

Abstract

The amino acid sequence of the polyclonal antibodies we developed against the carboxyl terminus of the dystrophin-related protein, the putative gene product of B3 cDNA, had no homologous sequence to the dystrophin molecule except for two amino acids located at its ends for immunization. By immunohistochemical examination in C57B1/10ScSn and C57B1/10ScSn-mdx mice we found that the DRP was expressed on the surface membrane of fetal muscle fibers, was assembled at the neuromuscular junctions of the mature muscle fibers, and reappeared on the surface membrane of muscle fibers after denervation. Its localization was similar to that of the acetylcholine receptor, suggesting that DRP is one of the cytoskeletons which organize and stabilize the cytoplasmic domain of the acetylcholine receptor.

MeSH terms

  • Aging
  • Amino Acid Sequence
  • Animals
  • Cytoskeletal Proteins / analysis
  • Cytoskeletal Proteins / genetics*
  • Cytoskeletal Proteins / immunology
  • Dystrophin / genetics
  • Embryonic and Fetal Development
  • Fluorescent Antibody Technique
  • Membrane Proteins*
  • Mice
  • Mice, Inbred C57BL
  • Mice, Mutant Strains
  • Molecular Sequence Data
  • Muscle Denervation*
  • Muscle Development
  • Muscles / embryology
  • Muscles / physiology*
  • Peptide Fragments / immunology
  • Peptides / chemical synthesis
  • Peptides / immunology
  • Utrophin

Substances

  • Cytoskeletal Proteins
  • Dystrophin
  • Membrane Proteins
  • Peptide Fragments
  • Peptides
  • Utrn protein, mouse
  • Utrophin