Alterations in the functional properties of skinned fibers from denervated rabbit skeletal muscle

Am J Physiol. 1990 Sep;259(3 Pt 1):C503-6. doi: 10.1152/ajpcell.1990.259.3.C503.

Abstract

Isometric tension was recorded in vitro from chemically skinned fibers obtained from normal and 14-day-denervated extensor digitorum longus muscles of the rabbit. Denervation potentiated the tensions elicited by pCa 6.0 but did not modify the pCa value (5.6) required for maximum tension. Ca2+ transport across the membranes of the sarcoplasmic reticulum (SR) was markedly affected by denervation. Thus the rate of ATP-dependent net Ca2+ uptake increased significantly, and the spontaneous release ("leakage") of the Ca2+ stored in the SR was significantly reduced in denervated fibers. These effects lead to increased accumulation of Ca2+ in the lumen of the SR. The dose-response curve for the halothane-induced contractures of Ca2(+)-loaded skinned fibers was displaced to the left after denervation. Thus 0.7 mM halothane, a concentration that elicited no tension in 10 control fibers, induced contractures in the 10 denervated fibers tested. The potentiation of the halothane-induced tensions is attributed mainly to the larger stores of Ca2+ in the SR of denervated fibers. The possibility that denervation may also affect the interaction of halothane with the SR membranes is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • Caffeine / pharmacology
  • Calcium / metabolism
  • Calcium / pharmacology
  • Halothane / pharmacology
  • In Vitro Techniques
  • Muscle Contraction* / drug effects
  • Muscle Denervation*
  • Muscles / drug effects
  • Muscles / innervation
  • Muscles / physiology*
  • Rabbits
  • Sarcoplasmic Reticulum / drug effects
  • Sarcoplasmic Reticulum / metabolism

Substances

  • Caffeine
  • Adenosine Triphosphate
  • Calcium
  • Halothane