Structural diversity of triadin in skeletal muscle and evidence of its existence in heart

FEBS Lett. 1994 Jul 4;348(1):17-20. doi: 10.1016/0014-5793(94)00556-7.

Abstract

Triadin has been characterized as an abundant protein co-localized with the calcium release channel on the terminal cisternae of the sarcoplasmic reticulum of the skeletal muscle. Its localization to terminal cisternae of the sarcoplasmic reticulum and functional studies suggest that it has an important role in excitation-contraction coupling. In this study we identify three triadin isoforms in rabbit skeletal muscle and by Northern blot analysis demonstrate that triadin also exists in the heart.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blotting, Northern
  • Carrier Proteins*
  • DNA Primers
  • Molecular Sequence Data
  • Muscle Proteins / analysis
  • Muscle Proteins / chemistry*
  • Myocardium / chemistry*
  • Protein Conformation
  • Rabbits

Substances

  • Carrier Proteins
  • DNA Primers
  • Muscle Proteins
  • triadin