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Cyclic ADP‐ribose does not affect cardiac or skeletal muscle ryanodine receptors
Author(s) -
Fruen Bradley R.,
Mickelson James R.,
Shomer Nirah H.,
Velez Patricio,
Louis Charles F.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00931-7
Subject(s) - ryanodine receptor , cyclic adp ribose , skeletal muscle , endoplasmic reticulum , cardiac muscle , myocyte , chemistry , ryanodine receptor 2 , gene isoform , nad+ kinase , biochemistry , biology , medicine , endocrinology , microbiology and biotechnology , enzyme , cd38 , stem cell , cd34 , gene
The cardiac muscle isoform of the ryanodine receptor/Ca 2+ 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 μM), nor the related metabolites, β‐NAD + (0.1–30 mM) and ADP‐ribose (0.1–5 μM), affected cardiac RYR activity as determined by [ 3 H]ryanodine binding to cardiac sarcoplasmic reticulum (SR) vesicles. Similarly, cADPR (1 μM) failed to activate single cardiac RYR channels in planar lipid bilayers. Skeletal muscle SR [ 3 H]ryanodine binding was also unaffected by cADPR (up to 30 μM). These results argue against a direct role for the well‐characterized RYRs of cardiac or skeletal muscle in mediating cADPR‐activated Ca 2+ release.