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Second messenger function and the structure-activity relationship of cyclic adenosine diphosphoribose (cADPR) Guse AHFEBS J 2005[Sep]; 272 (18): 4590-7Cyclic ADP-ribose (cADPR) is a Ca2+ mobilizing second messenger found in various cell types, tissues and organisms. Receptor-mediated formation of cADPR may proceed via transmembrane shuttling of the substrate NAD and involvement of the ectoenzyme CD38, or via so far unidentified ADP-ribosyl cyclases located within the cytosol or in internal membranes. cADPR activates intracellular Ca2+ release via type 2 and 3 ryanodine receptors. The exact molecular mechanism, however, remains to be elucidated. Possibilities are the direct binding of cADPR to the ryanodine receptor or binding via a separate cADPR binding protein. In addition to Ca2+ release, cADPR also evokes Ca2+ entry. The underlying mechanism(s) may comprise activation of capacitative Ca2+ entry and/or activation of the cation channel TRPM2 in conjunction with adenosine diphosphoribose. The development of novel cADPR analogues revealed new insights into the structure-activity relationship. Substitution of either the northern ribose or both the northern and southern ribose resulted in much simpler molecules, which still retained significant biological activity.|Animals[MESH]|Calcium Signaling[MESH]|Calcium/metabolism[MESH]|Clusterin[MESH]|Cyclic ADP-Ribose/chemistry/metabolism/*physiology[MESH]|Glycoproteins/metabolism[MESH]|Humans[MESH]|Molecular Chaperones/metabolism[MESH]|Ryanodine Receptor Calcium Release Channel/metabolism[MESH]|Second Messenger Systems/*physiology[MESH]|Structure-Activity Relationship[MESH] |
