Adenosine diphosphate ribose
Appearance
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Other names
ADP ribose
ADPR Adenosine 5'-diphosphoribose | |
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3D model (JSmol)
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MeSH | Adenosine+Diphosphate+Ribose |
PubChem CID
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Properties | |
C15H23N5O14P2 | |
Molar mass | 559.316 g/mol |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Adenosine diphosphate ribose (ADPR) is an ester molecule formed into chains by the enzyme poly ADP ribose polymerase.[1] ADPR is created from cyclic ADP-ribose (cADPR) by the CD38 enzyme using nicotinamide adenine dinucleotide (NAD+) as a cofactor.[1]
ADPR binds to and activates the TRPM2 ion channel.[2] ADPR is the most potent agonist of the TRPM2 channel.[3] cADPR also binds to TPRM2, and the action of both molecules is synergistic, with both molecules enhancing the action of the other molecule in activating the TRPM2 channel.[4] Researchers are not sure how the Adenosine diphosphate reacts with the TRPM2 channel but according to Journal of Chemistry it says the ribose sugar plays a crucial part in activating the TRPM2 ion channel.
See also
References
- ^ a b Braidy N, Berg J, Clement J, Sachdev P (2019). "Role of Nicotinamide Adenine Dinucleotide and Related Precursors as Therapeutic Targets for Age-Related Degenerative Diseases: Rationale, Biochemistry, Pharmacokinetics, and Outcomes". Antioxidants & Redox Signaling. 10 (2): 251–294. doi:10.1089/ars.2017.7269. PMC 6277084. PMID 29634344.
- ^ Fonfria E, Marshall IC, Benham CD, et al. (September 2004). "TRPM2 channel opening in response to oxidative stress is dependent on activation of poly(ADP-ribose) polymerase". Br. J. Pharmacol. 143 (1): 186–92. doi:10.1038/sj.bjp.0705914. PMC 1575275. PMID 15302683.
- ^ Yu P, Cai X, Liang Y, Yang W (2019). "Roles of NAD + and Its Metabolites Regulated Calcium Channels in Cancer". Molecules. 25 (20): 4826. doi:10.3390/molecules25204826. PMC 7587972. PMID 33092205.
- ^ Lee HC (2011). "Cyclic ADP-ribose and NAADP: fraternal twin messengers for calcium signaling". Science China Life Sciences. 54 (8): 699–711. doi:10.1007/s11427-011-4197-3. PMID 21786193. S2CID 24286381.