We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Second messenger function and the structure–activity relationship of cyclic adenosine diphosphoribose (cADPR).
- Authors
Guse, Andreas H.
- Abstract
Cyclic 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.
- Subjects
SECOND messengers (Biochemistry); CELLULAR control mechanisms; CELLULAR signal transduction; INFORMATION theory in biology; ADENOSINES; ADENINE; EXTRACELLULAR enzymes; ENZYMES
- Publication
FEBS Journal, 2005, Vol 272, Issue 18, p4590
- ISSN
1742-464X
- Publication type
Article
- DOI
10.1111/j.1742-4658.2005.04863.x