A synthetic peptide mimics troponin I function in the calcium-dependent regulation of muscle contraction

FEBS Lett. 1993 Jun 1;323(3):223-8. doi: 10.1016/0014-5793(93)81344-y.

Abstract

A new technique for treating skinned cardiac muscle fibers has been developed in which troponin I is extracted, giving rise to unregulated fibers. The effect of the 12-residue troponin I peptide on these fibers indicates that this region of troponin I is solely responsible for muscle relaxation (inhibition of force). Furthermore, troponin I peptide-troponin C reconstituted fibers are stable through several contraction-relaxation cycles indicating the peptide can switch binding sites between actin and troponin C. The troponin I peptide can substitute for the native protein as part of the calcium-sensitive molecular switch that controls muscle regulation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcium / pharmacology*
  • Cattle
  • Dose-Response Relationship, Drug
  • Electrophoresis, Polyacrylamide Gel
  • Immunoblotting
  • In Vitro Techniques
  • Isometric Contraction / drug effects*
  • Molecular Sequence Data
  • Muscles / drug effects
  • Muscles / physiology*
  • Peptide Fragments / chemical synthesis
  • Peptide Fragments / pharmacology*
  • Swine
  • Troponin / isolation & purification
  • Troponin / pharmacology
  • Troponin / physiology*
  • Troponin I
  • Vanadates / pharmacology

Substances

  • Peptide Fragments
  • Troponin
  • Troponin I
  • Vanadates
  • Calcium