Calcium Ion Permeation through the Calcium Release Channel (Ryanodine Receptor) of Cardiac Muscle

2003 ◽  
Vol 107 (34) ◽  
pp. 9139-9145 ◽  
Author(s):  
Duan P. Chen ◽  
Le Xu ◽  
Bob Eisenberg ◽  
Gerhard Meissner
Keyword(s):  
Cardiac Muscle ◽  
Ryanodine Receptor ◽  
Calcium Ion ◽  
Calcium Release ◽  
Ion Permeation ◽  
Calcium Release Channel ◽  
Release Channel

scholarly journals Calmodulin Binding and Inhibition of Cardiac Muscle Calcium Release Channel (Ryanodine Receptor)

2001 ◽  
Vol 276 (23) ◽  
pp. 20144-20153 ◽  
Author(s):  
David M. Balshaw ◽  
Le Xu ◽  
Naohiro Yamaguchi ◽  
Daniel A. Pasek ◽  
Gerhard Meissner
Keyword(s):  
Cardiac Muscle ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Calmodulin Binding ◽  
Muscle Calcium

scholarly journals The human cardiac muscle ryanodine receptor-calcium release channel: identification, primary structure and topological analysis

1996 ◽  
Vol 318 (2) ◽  
pp. 477-487 ◽  
Author(s):  
Richard E. A. TUNWELL ◽  
Colin WICKENDEN ◽  
Bénédicte M. A. BERTRAND ◽  
Valery I. SHEVCHENKO ◽  
Martina B. WALSH ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cardiac Muscle ◽  
Ryanodine Receptor ◽  
Primary Structure ◽  
Calcium Release ◽  
Topological Analysis ◽  
Cdna Clones ◽  
Amino Acid Residues ◽  
Calcium Release Channel ◽  
Release Channel

Rapid Ca2+ efflux from intracellular stores during cardiac muscle excitation–contraction coupling is mediated by the ryanodine-sensitive calcium-release channel, a large homotetrameric complex present in the sarcoplasmic reticulum. We report here the identification, primary structure and topological analysis of the ryanodine receptor–calcium release channel from human cardiac muscle (hRyR-2). Consistent with sedimentation and immunoblotting studies on the hRyR-2 protein, sequence analysis of ten overlapping cDNA clones reveals an open reading frame of 14901 nucleotides encoding a protein of 4967 amino acid residues with a predicted molecular mass of 564569 Da for hRyR-2. In-frame insertions corresponding to eight and ten amino acid residues were found in two of the ten cDNAs isolated, suggesting that novel, alternatively spliced transcripts of the hRyR-2 gene might exist. Six hydrophobic stretches, which are present within the hRyR-2 C-terminal 500 amino acids and are conserved in all RyR sequences, may be involved in forming the transmembrane domain that constitutes the Ca2+-conducting pathway, in agreement with competitive ELISA studies with a RyR-2-specific antibody. Sequence alignment of hRyR-2 with other RyR isoforms indicates a high level of overall identity within the RyR family, with the exception of two important regions that exhibit substantial variability. Phylogenetic analysis suggests that the RyR-2 isoform diverged from a single ancestral gene before the RyR-1 and RyR-3 isoforms to form a distinct branch of the RyR family tree.

scholarly journals Protein Kinase A Phosphorylation of the Cardiac Calcium Release Channel (Ryanodine Receptor) in Normal and Failing Hearts

2002 ◽  
Vol 278 (1) ◽  
pp. 444-453 ◽  
Author(s):  
Steven Reiken ◽  
Marta Gaburjakova ◽  
Silvia Guatimosim ◽  
Ana M. Gomez ◽  
Jeanine D'Armiento ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Kinase A

Inactivation of the cardiac ryanodine receptor calcium release channel by nitric oxide

Cell Calcium ◽  
1997 ◽  
Vol 22 (6) ◽  
pp. 447-453 ◽  
Author(s):  
Alexandra Zahradníková ◽  
Igor Minarovic ◽  
Richard C. Venema ◽  
LászlóG. Meszaros
Keyword(s):  
Nitric Oxide ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Cardiac Ryanodine Receptor
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