ATP-induced activation of expressed RyR3 at low free calcium

FEBS Lett. 2000 Apr 14;471(2-3):256-60. doi: 10.1016/s0014-5793(00)01385-5.

Abstract

Ca(2+) channel properties of the mink ryanodine receptor type 3 (RyR3), expressed in HEK293 cells, were studied in planar lipid bilayers to which RyR3 rich membrane fragments had been fused. RyR3 channels were not active at resting levels of Ca(2+)(free) but were gated by an additional 1 mM ATP, exhibiting long open times. The second major finding was the absence of channel inactivation at millimolar Ca(2+)(free). Insertion of a myc tag at the N-terminus of RyR3 did not affect the channel properties. As to skeletal muscle, the observed type 3 channel properties appear physiologically meaningful by assisting type 1 channels in calcium release.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Adenosine Triphosphate / pharmacology*
  • Animals
  • Calcium / metabolism*
  • Calcium / pharmacology
  • Cell Line
  • Electric Conductivity
  • Humans
  • Ion Channel Gating / drug effects*
  • Kinetics
  • Lipid Bilayers / metabolism
  • Microsomes / drug effects
  • Microsomes / metabolism
  • Mink
  • Protein Isoforms / chemistry
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Ryanodine Receptor Calcium Release Channel / chemistry
  • Ryanodine Receptor Calcium Release Channel / genetics
  • Ryanodine Receptor Calcium Release Channel / metabolism*
  • Sarcoplasmic Reticulum / drug effects
  • Sarcoplasmic Reticulum / metabolism
  • Transfection

Substances

  • Lipid Bilayers
  • Protein Isoforms
  • Recombinant Fusion Proteins
  • Ryanodine Receptor Calcium Release Channel
  • Adenosine Triphosphate
  • Calcium