Open AccessFrom Eggs to Hearts: What Is the Link between Cyclic ADP‐Ribose and Ryanodine Receptors?
Author(s) -
Venturi Elisa,
Pitt Samantha,
Galfré Elena,
Sitsapesan Rebecca
Publication year - 2012
Publication title -
cardiovascular therapeutics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 46
eISSN - 1755-5922
pISSN - 1755-5914
DOI - 10.1111/j.1755-5922.2010.00236.x
Subject(s) - ryanodine receptor , cyclic adp ribose , nad+ kinase , receptor , intracellular , nicotinamide adenine dinucleotide , nicotinamide adenine dinucleotide phosphate , medicine , biochemistry , microbiology and biotechnology , chemistry , biology , cd38 , enzyme , stem cell , cd34 , oxidase test
SUMMARY It was first proposed that cyclic ADP‐ribose (cADPR) could activate ryanodine receptors (RyR) in 1991. Following a subsequent report that cADPR could activate cardiac RyR (RyR2) reconstituted into artificial membranes and stimulate Ca 2+ ‐release from isolated cardiac SR, there has been a steadily mounting stockpile of publications proclaiming the physiological and pathophysiological importance of cADPR in the cardiovascular system. It was only 2 years earlier, in 1989, that cADPR was first identified as the active metabolite of nicotinamide adenine dinucleotide (NAD), responsible for triggering the release of Ca 2+ from crude homogenates of sea urchin eggs. Twenty years later, can we boast of being any closer to unraveling the mechanisms by which cADPR modulates intracellular Ca 2+ ‐release? This review sets out to examine the mechanisms underlying the effects of cADPR and ask whether cADPR is an important signaling molecule in the heart.