Cyclic ADP-ribose
(Synonyms: 环二磷酸腺苷核酸糖,cADPR) 目录号 : GC62179
An endogenous Ca2+ mobilizer
Cas No.:119340-53-3
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
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- Purity: >95.00%
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- Datasheet
Cyclic ADP-ribose (cADP-ribose) is an endogenous metabolite of NAD+ that mobilizes the release of stored Ca2+ in the endoplasmic reticulum via ryanodine receptors in various cell types.1,2,3,4,5 This second messenger is generated via the cADP-ribose synthases CD38 and CD157.6,5,7 cADP-Ribose may also trigger the cell surface Ca2+ influx channel TRPM2 in a temperature-dependent manner.8 In vitro, cADP-ribose modulates Ca2+ signaling in rat and mouse cardiomyocytes treated with isoproterenol , and treatment with this metabolite at 100 ?M under heat stress conditions induces the release of oxytocin from the mouse hypothalamus.9,4
1.Lee, H.C., Walseth, T.F., Bratt, G.T., et al.Structural determination of a cyclic metabolite of NAD+ with intracellular Ca2+ -mobilizing activityJ. Biol. Chem.264(3)1608-1615(1989) 2.Guse, A.H.Biochemistry, biology, and pharmacology of cyclic adenosine diphosphoribose (cADPR)Curr. Med. Chem.11847-855(2004) 3.Houtkooper, R.H., Cantó, C., Wanders, R.J., et al.The secret life of NAD+: An old metabolite controlling new metabolic signaling pathwaysEndocr. Rev.31(2)194-223(2010) 4.Zhong, J., Amina, S., Liang, M., et al.Cyclic ADP-ribose and heat regulate oxytocin release via CD38 and TRPM2 in the hypothalamus during social or psychological stress in miceFront. Neurosci.10(304)1-14(2016) 5.Nikiforov, A., Kulikova, V., and Ziegler, M.The human NAD metabolome: Functions, metabolism and compartmentalizationCrit. Rev. Biochem. Mol. Biol.50(4)284-297(2015) 6.Houtkooper, R.H., Cantó, C., Wanders, R.J., et al.The secret life of NAD+: An old metabolite controlling new metabolic signaling pathwaysEndocr. Rev.31(2)194-223(2010) 7.Gul, R., Park, D.-R., Shawl, A.I., et al.Nicotinic acid adenine dinucleotide phosphate (NAADP) and cyclic ADP-ribose (cADPR) mediate Ca2+ signaling in cardiac hypertrophy induced by β-adrenergic stimulationPLoS One11(3)e0149125(2016) 8.Lee, H.C.Cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate (NAADP) as messengers for calcium mobilizationJ. Biol. Chem.287(38)31633-31640(2012) 9.Gul, R., Park, D.-R., Shawl, A.I., et al.Nicotinic acid adenine dinucleotide phosphate (NAADP) and cyclic ADP-ribose (cADPR) mediate Ca2+ signaling in cardiac hypertrophy induced by β-adrenergic stimulationPLoS One11(3)e0149125(2016)
| Cas No. | 119340-53-3 | SDF | |
| 别名 | 环二磷酸腺苷核酸糖,cADPR | ||
| 分子式 | C15H21N5O13P2 | 分子量 | 541.3 |
| 溶解度 | 储存条件 | -80°C | |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 1.8474 mL | 9.237 mL | 18.474 mL |
| 5 mM | 0.3695 mL | 1.8474 mL | 3.6948 mL |
| 10 mM | 0.1847 mL | 0.9237 mL | 1.8474 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Cyclic ADP-ribose
J Mol Med (Berl) 2000;78(1):26-35.PMID:10759027DOI:10.1007/s001090000076.
The Ca2+-mobilizing natural compound Cyclic ADP-ribose was discovered in sea urchin egg homogenates. Recently the involvement of Cyclic ADP-ribose in Ca2+ signaling has been demonstrated in diverse biological systems spanning protozoa, plants, and cells from invertebrate, mammalian, and human sources. ADP-ribosyl cyclases synthesize Cyclic ADP-ribose. Several candidate proteins for these enzymes have been proposed, including membrane-bound NAD+ glycohydrolases such as CD38 and soluble enzyme activities from various tissues and cells. Ca2+ mobilization by Cyclic ADP-ribose is believed to proceed via the ryanodine receptor/Ca2+ channel, probably via binding proteins for Cyclic ADP-ribose. Several antagonistic derivatives of Cyclic ADP-ribose have been synthesized, some of which have been successfully used to demonstrate the involvement of Cyclic ADP-ribose in sea urchin egg fertilization, glucose-dependent insulin secretion in pancreatic beta-cells, and activation and proliferation of human T-lymphocytes.
CD38-Cyclic ADP-Ribose Signal System in Physiology, Biochemistry, and Pathophysiology
Int J Mol Sci 2022 Apr 13;23(8):4306.PMID:35457121DOI:10.3390/ijms23084306.
Calcium (Ca2+) is a ubiquitous and fundamental signaling component that is utilized by cells to regulate a diverse range of cellular functions, such as insulin secretion from pancreatic β-cells of the islets of Langerhans. Cyclic ADP-ribose (cADPR), synthesized from NAD+ by ADP-ribosyl cyclase family proteins, such as the mammalian cluster of differentiation 38 (CD38), is important for intracellular Ca2+ mobilization for cell functioning. cADPR induces Ca2+ release from endoplasmic reticulum via the ryanodine receptor intracellular Ca2+ channel complex, in which the FK506-binding protein 12.6 works as a cADPR-binding regulatory protein. Recently, involvements of the CD38-cADPR signal system in several human diseases and animal models have been reported. This review describes the biochemical and molecular biological basis of the CD38-cADPR signal system and the diseases caused by its abnormalities.
Does Cyclic ADP-ribose (cADPR) Activate the Non-selective Cation Channel TRPM2?
Front Immunol 2020 Aug 11;11:2018.PMID:32903769DOI:10.3389/fimmu.2020.02018.
TRPM2 is a non-selective, Ca2+-permeable cation channel widely expressed in immune cells. It is firmly established that the channel can be activated by intracellular adenosine 5'-diphosphoribose (ADPR). Until recent cryo-EM structures have exhibited an additional nucleotide binding site in the N-terminus of the channel, this activation was thought to occur via binding to a C-terminal domain of the channel that is highly homologous to the ADPR pyrophosphatase NudT9. Over the years it has been controversially discussed whether the Ca2+ mobilizing second messenger cyclic ADP ribose (cADPR) might also directly activate Ca2+ entry via TRPM2. Here we will review the status of this discussion.
Cyclic ADP-ribose, the ADP-ribosyl cyclase pathway and calcium signalling
Mol Cell Endocrinol 1994 Jan;98(2):125-31.PMID:8143921DOI:10.1016/0303-7207(94)90130-9.
Cyclic adenosine diphosphate-ribose, an endogenous metabolite of nicotinamide adenine dinucleotide was first characterized as a potent Ca2+ mobilizing agent in sea urchin eggs. Mounting evidence points to it being an endogenous activator of Ca(2+)-induced Ca2+ release by non-skeletal muscle ryanodine receptors in several invertebrate and mammalian cell types. Cyclic adenosine diphosphate-ribose is synthesized by adenosine diphosphate-ribosyl cyclases, which have been found to be widespread enzymes. Recent data suggests that cyclic adenosine diphosphate-ribose may function as a second messenger in sea urchin eggs at fertilization and in stimulus secretion coupling in pancreatic beta-cells. A second messenger role for cyclic adenosine diphosphate-ribose requires that its intracellular levels be under the control of extracellular stimuli. Another second messenger, cGMP, stimulates the synthesis of cyclic adenosine diphosphate-ribose from nicotinamide adenine dinucleotide by activating the adenosine diphosphate-ribosyl cyclase pathway in sera urchin eggs and egg homogenates, suggesting that cyclic adenosine diphosphate-ribose may be an intracellular messenger for cell surface receptors or nitric oxide, which activate cGMP-producing guanylate cyclases. Cyclic adenosine diphosphate-ribose may have a similar role to inositol trisphosphate in controlling intracellular calcium signalling with these two calcium-mobilizing second messengers activating ryanodine receptors and inositol trisphosphate receptors respectively.
Cyclic ADP-ribose and its metabolic enzymes
Biochimie 1995;77(5):345-55.PMID:8527488DOI:10.1016/0300-9084(96)88145-4.
Cyclic ADP-ribose (cADPR) is a recently discovered cyclic nucleotide with Ca2+ signaling functions. There is a growing recognition that it is an endogenous modulator of the Ca(2+)-induced Ca2+ release mechanism in cells. The cyclic structure of cADPR has now been confirmed by x-ray crystallography. A series of analogs of cADPR has been synthesized, including antagonists and a novel analog, cyclic GDP-ribose. Considerable progress has been made in characterizing ADP-ribosyl cyclase, the synthetic enzyme, and cADPR hydrolase, the hydrolytic enzyme. A new class of bifunctional enzymes has been identified which catalyses both the synthesis and hydrolysis of cADPR. CD38, a lymphocyte differentiation antigen, is a member of this class. The understanding of the mechanisms of regulation of the metabolic enzymes and signaling by cADPR is likely to have important implications and several possibilities are discussed in this article.