Cardiac thin filament regulation and the Frank-Starling mechanism

J Physiol Sci. 2014 Jul;64(4):221-32. doi: 10.1007/s12576-014-0314-y. Epub 2014 May 1.

Abstract

The heart has an intrinsic ability to increase systolic force in response to a rise in ventricular filling (the Frank-Starling law of the heart). It is widely accepted that the length dependence of myocardial activation underlies the Frank-Starling law of the heart. Recent advances in muscle physiology have enabled the identification of the factors involved in length-dependent activation, viz., titin (connectin)-based interfilament lattice spacing reduction and thin filament "on-off" regulation, with the former triggering length-dependent activation and the latter determining the number of myosin molecules recruited to thin filaments. Patients with a failing heart have demonstrated reduced exercise tolerance at least in part via depression of the Frank-Starling mechanism. Recent studies revealed that various mutations occur in the thin filament regulatory proteins, such as troponin, in the ventricular muscle of failing hearts, which consequently alter the Frank-Starling mechanism. In this article, we review the molecular mechanisms of length-dependent activation, and the influence of troponin mutations on the phenomenon.

Publication types

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

MeSH terms

  • Animals
  • Cardiac Myosins / metabolism
  • Connectin / metabolism
  • Heart / physiology*
  • Humans
  • Myocardium / metabolism*
  • Sarcomeres / metabolism*
  • Starlings / physiology*
  • Troponin / metabolism

Substances

  • Connectin
  • Troponin
  • Cardiac Myosins