Biochemical characterization of the Ca2+release channel of skeletal and cardiac sarcoplasmic reticulum
โ Scribed by Gerhard Meissner; Eric Rousseau; F. Anthony Lai; Qi-Yi Liu; Kristin A. Anderson
- Publisher
- Springer
- Year
- 1988
- Tongue
- English
- Weight
- 498 KB
- Volume
- 82
- Category
- Article
- ISSN
- 0300-8177
No coin nor oath required. For personal study only.
โฆ Synopsis
Rapid mixing-vesicle ion flux and planar lipid bilayer-single channel measurements have shown that a high-conductance, ligand-gated Ca2+ release channel is present in 'heavy', junctional-derived membrane fractions of skeletal and cardiac muscle sarcoplasmic reticulum. Using the release channel-specific probe, ryanodine, a 30S protein complex composed of polypeptides of Mr approximately 400,000 has been isolated from cardiac and skeletal muscle. Reconstitution of the complex into planar lipid bilayers has revealed a Ca2+ conductance with properties characteristic of the native Ca2+ release channel.
๐ SIMILAR VOLUMES
Ryanodine is a neutral plant alkaloid which functions as a probe for an intracellular Ca2+ release channel (ryanodine receptor) in excitable tissues. Using [3H]ryanodine, a 30 S protein complex comprised of four polypeptides of Mr 565,000 has been isolated and functionally reconstituted into planar
Ca2+ release from skeletal sarcoplasmic reticulum (SR) could be regulated by at least three mechanisms: 1) Ca2+, 2) calmodulin, and 3) Ca2+/calmodulin-dependent phosphorylation. Bell-shaped Ca(2+)-dependence of Ca2+ release from both actively- and passively-loaded SR vesicles suggest that opening an
The purified ryanodine receptor channel of the sheep cardiac muscle sarcoplasmic reticulum (SR) membrane functions as a calcium-activated cation-selective channel under voltage-clamp conditions following reconstitution into planar phospholipid bilayers. We have investigated the effects of the tetra-
Annexin VI has eight highly conserved repeated domains; all other annexins have four. Diaz-Muiioz et al. ( J Biol Chem 265:15894, 1990) reported that annexin VI alters the gating properties of the ryanodine-sensitive Ca2+-release channel isolated from sarcoplasmic reticulum. To investigate the domai