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Magnesium Inhibition of Ryanodine-Receptor Calcium Channels: Evidence for Two Independent Mechanisms
It is shown that Type-I inhibition is not the sole mechanism responsible for Mg2+ inhibition, as is often assumed, and the physiological implications of this finding are discussed. Expand
Calsequestrin and the calcium release channel of skeletal and cardiac muscle.
Calsequestrin plays a major role in calcium homeostasis that extends well beyond its ability to buffer Ca2+ ions, as indicated by the kinase activity of the protein, its thioredoxin-like structure and its influence over store operated Ca 2+ entry. Expand
Altered mRNA splicing of the skeletal muscle ryanodine receptor and sarcoplasmic/endoplasmic reticulum Ca2+-ATPase in myotonic dystrophy type 1.
It is suggested that aberrant splicing of RyR1 and SERCA1 mRNAs might contribute to impaired Ca2+ homeostasis in DM1 muscle. Expand
Subconductance states in single-channel activity of skeletal muscle ryanodine receptors after removal of FKBP12.
The results show that FKBP12 coordinates the gating of channel activity in control and ryanodine-modified RyRs, and activation and inhibition of channels from control-incubated and native terminal cisternae vesicles were activated and inhibited. Expand
The relative contributions of the folds and caveolae to the surface membrane of frog skeletal muscle fibres at different sarcomere lengths.
The maintenance of constant plasmalemma area, even after excessive stretch, suggests that the plas malemma is relatively inelastic in this situation. Expand
The effects of β‐adrenoceptor activation on contraction in isolated fast‐ and slow‐twitch skeletal muscle fibres of the rat
The results suggest that the increase in peak twitch and tetanic force and abbreviation of tetanic relaxation induced by terbutaline depend on the activation of β‐adrenoceptors and a consequent increase in the myoplasmic cyclic AMP concentration. Expand
Adverse Effects of Doxorubicin and Its Metabolic Product on Cardiac RyR2 and SERCA2A
Novel evidence is provided that doxorubicin and its metabolite, doxorbicinol, bind to the cardiac ryanodine receptor (RyR2) and to the sarco/endoplasmic reticulum Ca2+ ATPase (SERCA2A) and deleteriously alter their activity and that the metabolite acts with greater efficacy than the parent compound. Expand
  • A. Dulhunty
  • Chemistry, Medicine
  • Clinical and experimental pharmacology…
  • 1 September 2006
The authors' current understanding of this amazingly efficient molecular signal transduction machine has evolved over the past 50 years, and a multitude of questions about the molecular interactions and structures of the proteins and their interaction sites remain to be answered and provide a challenge for the next 50 years. Expand
Skeletal muscle excitation-contraction coupling: who are the dancing partners?
A major candidate for a role in the coupling mechanism is thebeta subunit of the dihydropyridine receptor, because specific residues in both the beta subunit and ryanodine receptor have been identified that facilitate an interaction between the two proteins and these also impact on excitation-contraction coupling. Expand
Ca2+ signaling in striated muscle: the elusive roles of triadin, junctin, and calsequestrin
The review of molecular interactions between calsequestrin, triadin, junctin and the ryanodine receptor in the lumen of the sarcoplasmic reticulum finds that cal sequestrin plays a different role in the heart and skeletal muscle, enhancing Ca2+ release in theHeart, but depressing Ca2- release in skeletal muscle. Expand