Effects of denervation on the contents of cholesterol and membrane systems involved in muscle contraction in rabbit fast-twitch sarcotubular system

Gen Physiol Biophys. 1991 Apr;10(2):175-88.

Abstract

Denervated fast-twitch rabbit muscles were progressively losing their fresh weight and the yield of sarcotubular protein was increasing. The activity of Ca(2+)-ATPase was affected but very slightly, the basal Mg(2+)-ATPase and the Mg(2+)-ATPase/Ca(2+)-ATPase ratio however increased together with a simultaneous depression of the membrane-bound acetylcholinesterase activity. We did not observe any differences in density properties of sarcotubular fractions between control and denervated muscle. However, a relative enrichment in SM and H fraction could be seen after denervation with small changes in the content of the Ca(2+)-pump protein, increased levels of calsequestrin and cholesterol, mostly in the heavy and the SM fraction. After denervation the binding sites for 3H-PN-200-110 did not show any changes in receptor affinity, but the number of putative Ca(2+)-channels increased twice along with a depression of 3H-ouabain binding sites. We suggest that the denervation of fast-twitch muscle leads to the hypertrophy of the junctional sarcoplasmic reticulum and the T-system. Changes in the cholesterol content, in the number of putative Ca(2+)-channels and in Na+, K(+)-ATPase can affect the muscle contraction.

MeSH terms

  • Acetylcholinesterase / metabolism
  • Animals
  • Ca(2+) Mg(2+)-ATPase / metabolism
  • Calcium-Transporting ATPases / metabolism
  • Calsequestrin / analysis
  • Chemical Fractionation
  • Cholesterol / analysis*
  • Dihydropyridines / metabolism
  • Dihydropyridines / pharmacology
  • Electrophoresis, Polyacrylamide Gel
  • Male
  • Muscle Contraction*
  • Muscle Denervation*
  • Muscles / chemistry
  • Muscles / innervation*
  • Muscles / ultrastructure
  • Organ Size
  • Rabbits
  • Sarcoplasmic Reticulum / chemistry*
  • Sarcoplasmic Reticulum / enzymology
  • Sarcoplasmic Reticulum / ultrastructure
  • Sodium-Potassium-Exchanging ATPase / metabolism

Substances

  • Calsequestrin
  • Dihydropyridines
  • 1,4-dihydropyridine
  • Cholesterol
  • Acetylcholinesterase
  • Ca(2+) Mg(2+)-ATPase
  • Calcium-Transporting ATPases
  • Sodium-Potassium-Exchanging ATPase