烟酰胺腺嘌呤二核苷酸（NAD）类似物，烟酰胺鸟嘌呤二核苷酸（NGD）和烟酰胺次黄嘌呤二核苷酸（NHD）的代谢和生化特性。,Scientific Reports

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烟酰胺腺嘌呤二核苷酸（NAD）类似物，烟酰胺鸟嘌呤二核苷酸（NGD）和烟酰胺次黄嘌呤二核苷酸（NHD）的代谢和生化特性。
Scientific Reports ( IF 3.8 ) Pub Date : 2019-09-11 , DOI: 10.1038/s41598-019-49547-6
Keisuke Yaku ₁ , Keisuke Okabe _{1,

2} , Maryam Gulshan ₁ , Kiyoshi Takatsu _{3,

4} , Hiroshi Okamoto _{5,

6} , Takashi Nakagawa _{1,

7}

Affiliation

烟酰胺腺嘌呤二核苷酸（NAD）是一种重要的辅酶，可调节各种代谢途径，包括糖酵解，β-氧化和氧化磷酸化。此外，NAD可用作聚（ADP-核糖）聚合酶（PARP），sirtuin和NAD糖水解酶的底物，并调节DNA修复，基因表达，能量代谢和应激反应。许多研究表明，NAD代谢与衰老和衰老相关疾病密切相关。以前，我们证明了，作为NAD类似物的烟酰胺鸟嘌呤二核苷酸（NGD）和烟酰胺次黄嘌呤二核苷酸（NHD）在过表达Nmnat3的小鼠中显着增加。但是，对体内NGD和NHD的了解不足。在目前的研究中，我们旨在研究这些NAD类似物的代谢和生化特性。我们证明了内源性NGD和NHD被发现在各种鼠类组织中，它们的合成和降解部分依赖于Nmnat3和CD38。我们还显示了NGD和NHD在体外可作为乙醇脱氢酶（ADH）的辅酶，尽管它们的亲和力远低于NAD。另一方面，NGD和NHD不能用作SIRT1，SIRT3和PARP1的底物。这些结果揭示了NGD和NHD的基本代谢，并突出了它们作为辅酶的生物学功能。尽管它们的亲和力远低于NAD。另一方面，NGD和NHD不能用作SIRT1，SIRT3和PARP1的底物。这些结果揭示了NGD和NHD的基本代谢，并突出了它们作为辅酶的生物学功能。尽管它们的亲和力远低于NAD。另一方面，NGD和NHD不能用作SIRT1，SIRT3和PARP1的底物。这些结果揭示了NGD和NHD的基本代谢，并突出了它们作为辅酶的生物学功能。

"点击查看英文标题和摘要"

Metabolism and biochemical properties of nicotinamide adenine dinucleotide (NAD) analogs, nicotinamide guanine dinucleotide (NGD) and nicotinamide hypoxanthine dinucleotide (NHD).

Nicotinamide adenine dinucleotide (NAD) is an important coenzyme that regulates various metabolic pathways, including glycolysis, β-oxidation, and oxidative phosphorylation. Additionally, NAD serves as a substrate for poly(ADP-ribose) polymerase (PARP), sirtuin, and NAD glycohydrolase, and it regulates DNA repair, gene expression, energy metabolism, and stress responses. Many studies have demonstrated that NAD metabolism is deeply involved in aging and aging-related diseases. Previously, we demonstrated that nicotinamide guanine dinucleotide (NGD) and nicotinamide hypoxanthine dinucleotide (NHD), which are analogs of NAD, are significantly increased in Nmnat3-overexpressing mice. However, there is insufficient knowledge about NGD and NHD in vivo. In the present study, we aimed to investigate the metabolism and biochemical properties of these NAD analogs. We demonstrated that endogenous NGD and NHD were found in various murine tissues, and their synthesis and degradation partially rely on Nmnat3 and CD38. We have also shown that NGD and NHD serve as coenzymes for alcohol dehydrogenase (ADH) in vitro, although their affinity is much lower than that of NAD. On the other hand, NGD and NHD cannot be used as substrates for SIRT1, SIRT3, and PARP1. These results reveal the basic metabolism of NGD and NHD and also highlight their biological function as coenzymes.

更新日期：2019-09-11

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