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]
Names | |
---|---|
Other names
ADP ribose
ADPR Adenosine 5'-diphosphoribose | |
Identifiers | |
3D model (JSmol)
|
|
ChEMBL | |
ChemSpider | |
MeSH | Adenosine Diphosphate Ribose |
PubChem CID
|
|
UNII | |
| |
| |
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).
|
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 the ribose sugar may play a role in activating the TRPM2 ion channel.[5]
Researchers believe that co-targeting DNA-dependent protein kinase and poly(adenosine diphosphate-ribose) polymerase-1 does not promote apoptosis or mitotic catastrophe of cancer cells after radiation.[6]
See also
editReferences
edit- ^ 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 29634344.251-294&rft.date=2019&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6277084#id-name=PMC&rft_id=info:pmid/29634344&rft_id=info:doi/10.1089/ars.2017.7269&rft.aulast=Braidy&rft.aufirst=N&rft.au=Berg, J&rft.au=Clement, J&rft.au=Sachdev, P&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6277084&rfr_id=info:sid/en.wikipedia.org:Adenosine diphosphate ribose" class="Z3988">
- ^ 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 15302683.186-92&rft.date=2004-09&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1575275#id-name=PMC&rft_id=info:pmid/15302683&rft_id=info:doi/10.1038/sj.bjp.0705914&rft.aulast=Fonfria&rft.aufirst=E&rft.au=Marshall, IC&rft.au=Benham, CD&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1575275&rfr_id=info:sid/en.wikipedia.org:Adenosine diphosphate ribose" class="Z3988">
- ^ 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 24286381.699-711&rft.date=2011&rft_id=https://api.semanticscholar.org/CorpusID:24286381#id-name=S2CID&rft_id=info:pmid/21786193&rft_id=info:doi/10.1007/s11427-011-4197-3&rft.au=Lee HC&rft_id=https://doi.org/10.1007%2Fs11427-011-4197-3&rfr_id=info:sid/en.wikipedia.org:Adenosine diphosphate ribose" class="Z3988">
- ^ Baszczyňski, Ondřej; Watt, Joanna M.; Rozewitz, Monika D.; Guse, Andreas H.; Fliegert, Ralf; Potter, Barry V. L. (2019). "Synthesis of Terminal Ribose Analogues of Adenosine 5′-Diphosphate Ribose as Probes for the Transient Receptor Potential Cation Channel TRPM2". The Journal of Organic Chemistry. 84 (10): 6143–6157. doi:10.1021/acs.joc.9b00338. PMC 6528165. PMID 30978018.6143-6157&rft.date=2019&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6528165#id-name=PMC&rft_id=info:pmid/30978018&rft_id=info:doi/10.1021/acs.joc.9b00338&rft.aulast=Baszczyňski&rft.aufirst=Ondřej&rft.au=Watt, Joanna M.&rft.au=Rozewitz, Monika D.&rft.au=Guse, Andreas H.&rft.au=Fliegert, Ralf&rft.au=Potter, Barry V. L.&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6528165&rfr_id=info:sid/en.wikipedia.org:Adenosine diphosphate ribose" class="Z3988">
- ^ Azad, Arun; Bukczynska, Patricia; Jackson, Susan; Haput, Ygal; Cullinane, Carleen; McArthur, Grant A.; Solomon, Benjamin (2014-02-01). "Co-targeting Deoxyribonucleic Acid–Dependent Protein Kinase and Poly(Adenosine Diphosphate-Ribose) Polymerase-1 Promotes Accelerated Senescence of Irradiated Cancer Cells". International Journal of Radiation Oncology, Biology and Physics. 88 (2): 385–394. doi:10.1016/j.ijrobp.2013.10.043. ISSN 0360-3016. PMID 24411611 – via Elsevier Science Direct.385-394&rft.date=2014-02-01&rft.issn=0360-3016&rft_id=info:pmid/24411611&rft_id=info:doi/10.1016/j.ijrobp.2013.10.043&rft.aulast=Azad&rft.aufirst=Arun&rft.au=Bukczynska, Patricia&rft.au=Jackson, Susan&rft.au=Haput, Ygal&rft.au=Cullinane, Carleen&rft.au=McArthur, Grant A.&rft.au=Solomon, Benjamin&rft_id=https://www.sciencedirect.com/science/article/abs/pii/S0360301613033026&rfr_id=info:sid/en.wikipedia.org:Adenosine diphosphate ribose" class="Z3988">