1. Cyclic ADP-ribose does not affect cardiac or skeletal muscle ryanodine receptors
- Author
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Charles F. Louis, James R. Mickelson, Bradley R. Fruen, Patricio Velez, and Nirah H. Shomer
- Subjects
Swine ,Lipid Bilayers ,Sarcoplasmic reticulum ,Biophysics ,Muscle Proteins ,Biochemistry ,Ryanodine receptor 2 ,Cyclic ADP-ribose ,03 medical and health sciences ,chemistry.chemical_compound ,0302 clinical medicine ,Structural Biology ,Genetics ,medicine ,Animals ,Molecular Biology ,030304 developmental biology ,Adenosine Diphosphate Ribose ,0303 health sciences ,Voltage-dependent calcium channel ,Ryanodine ,Ryanodine receptor ,Adenosine diphosphate ribose ,Myocardium ,Endoplasmic reticulum ,Cardiac muscle ,Skeletal muscle ,Ryanodine Receptor Calcium Release Channel ,Cell Biology ,NAD ,musculoskeletal system ,medicine.anatomical_structure ,chemistry ,cardiovascular system ,Calcium ,Calcium Channels ,Ca2+ release channel ,030217 neurology & neurosurgery - Abstract
The cardiac muscle isoform of the ryanodine receptor/Ca2+ release channel (RYR) has been proposed to be an important target of cyclic ADP-ribose (cADPR) action in mammalian cells. However, we now demonstrate that neither cADPR (0.1-5 microM), nor the related metabolites beta-NAD+ (0.1-30 mM) and ADP-ribose (0.1-5 microM), affected cardiac RYR activity as determined by [3H]ryanodine binding to cardiac sarcoplasmic reticulum (SR) vesicles. Similarly, cADPR (1 microM) failed to activate single cardiac RYR channels in planar lipid bilayers. Skeletal muscle SR [3H]ryanodine binding was also unaffected by cADPR (up to 30 microM). These results argue against a direct role for the well-characterized RYRs of cardiac or skeletal muscle in mediating cADPR-activated Ca2+ release.
- Published
- 1994
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