Similar Ca2+ dependences of [3H]ryanodine binding to alpha- and beta-ryanodine receptors purified from bullfrog skeletal muscle in an isotonic medium

FEBS Lett. 1996 Feb 19;380(3):267-71. doi: 10.1016/0014-5793(96)00053-1.

Abstract

To understand the functions of the two ryanodine receptor isoforms (alpha- and beta-RyRs) in nonmammalian skeletal muscles, we determined [3H]ryanodine binding to these isoforms purified from bullfrog skeletal muscle. In 0.17 M-NaCl medium both isoforms demonstrated similar Ca2+ dependent ryanodine binding activities, while the Ca2+ sensitivity for activation of beta-RyR was increased in 1 M-NaCl medium. This enhancement in Ca2+ sensitivity depended on the kinds of salts used. These results imply that alpha- and beta-RyRs may have similar properties as Ca2+-induced Ca2+ release channels in bullfrog skeletal muscle.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / analogs & derivatives
  • Adenosine Triphosphate / pharmacology
  • Animals
  • Caffeine / pharmacology
  • Calcium / pharmacology*
  • Calcium Channels / drug effects
  • Calcium Channels / isolation & purification
  • Calcium Channels / metabolism*
  • Cholic Acids / pharmacology
  • Muscle Proteins / drug effects
  • Muscle Proteins / isolation & purification
  • Muscle Proteins / metabolism*
  • Muscle, Skeletal / chemistry*
  • Phospholipids / pharmacology
  • Rana catesbeiana
  • Ryanodine / metabolism*
  • Ryanodine Receptor Calcium Release Channel
  • Sodium Chloride
  • Tritium

Substances

  • Calcium Channels
  • Cholic Acids
  • Muscle Proteins
  • Phospholipids
  • Ryanodine Receptor Calcium Release Channel
  • Tritium
  • Ryanodine
  • 5'-adenylyl (beta,gamma-methylene)diphosphonate
  • Caffeine
  • Sodium Chloride
  • Adenosine Triphosphate
  • alpha,beta-methyleneadenosine 5'-triphosphate
  • 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate
  • Calcium