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PMID:28449683
Author:Wang LF; Wang XN; Huang CC; Hu L; Xiao YF; Guan XH; Qian YS; Deng KY; Xin HB
Address:Institute of Translational Medicine, Nanchang University, 999 Xuefu Load, Honggutan District, Nanchang, 330031, China.
Title:Inhibition of NAMPT aggravates high fat diet-induced hepatic steatosis in mice through regulating Sirt1/AMPKα/SREBP1 signaling pathway.
Source:Lipids Health Dis; 16(1):82, 2017 Apr 27.
ISSN:1476-511X
Country of publication:England
Language:eng
Abstract:BACKGROUND: Nonalcoholic fatty liver disease is one of the most common liver diseases in the world and is a typical hepatic manifestation of metabolic syndrome which is characterized with lipid accumulation in liver. Nicotinamide phosphoribosyltransferase (NAMPT) has been recently identified as an enzyme involved in nicotinamide adenine dinucleotide (NAD ) biosynthesis and plays an important role in cellular metabolism in variety of organs in mammals. The aim of this study was to investigate the effects of NAMPT on high fat diet-induced hepatic steatosis. METHODS: Hepatic steatosis model was induced by high fat diet (HFD) in C57BL/6 mice in vivo. HepG2 and Hep1-6 hepatocytes were transfected with NAMPT vector plasmid or treated with NAMPT inhibitor FK866 and then incubated with oleic acid. Lipids accumulation was examined by HE staining or oil red staining. Quantitative RT-PCR and Western blot were used to measure expressions of the genes involved in lipogenic synthesis. RESULTS: FK866 significantly promoted liver steatosis in the mice fed with HFD and hepatic lipid accumulation in vitro, accompanied by the increases of the expressions of lipogenic genes such as sterol regulatory element-binding protein 1 (SREBP1) and fatty acid synthase (FASN). Nicotinamide mononucleotide (NMN) and NAD significantly rescued the actions of FK866 in vitro. In contrast, overexpression of NAMPT in HepG2 and Hep1-6 hepatocytes ameliorated hepatic lipid accumulation. In addition, FK866 decreased the protein levels of Sirt1 and phospho-AMPKα in liver of the HFD fed mice. Furthermore, Resveratrol, a Sirt1 activator, significantly reduced lipogenic gene expressions, while EX-527, a Sirt1 specific inhibitor, had the opposite effects. CONCLUSION: Our results demonstrated that inhibition of NAMPT aggravated the HFD- or oleic acid-induced hepatic steatosis through suppressing Sirt1-mediated signaling pathway. On the one hand, the inhibition of NAMPT reduced the production of NAD through inhibiting the NAD salvage pathway, resulting in the decrease of Sirt1 activity, and then attenuated the deacetylation of SREBP1 in which the inhibition of SREBP1 activity promoted the expressions of FASN and ACC. On the other hand, the reduced Sirt1 activity alleviated the activation of AMPKα to further enhance SREBP1 activities.
Publication type:JOURNAL ARTICLE
Name of substance:0 (6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide); 0 (Acrylamides); 0 (Carbazoles); 0 (Cytokines); 0 (Enzyme Inhibitors); 0 (N-(4-(1-benzoylpiperidin-4-yl)butyl)-3-(pyridin-3-yl)acrylamide); 0 (Piperidines); 0 (Srebf1 protein, mouse); 0 (Sterol Regulatory Element Binding Protein 1); 0 (Stilbenes); 0U46U6E8UK (NAD); 1094-61-7 (Nicotinamide Mononucleotide); 2UMI9U37CP (Oleic Acid); EC 2.4.2.12 (Nicotinamide Phosphoribosyltransferase); EC 2.4.2.12 (nicotinamide phosphoribosyltransferase, mouse); EC 2.7.11.1 (AMPK alpha1 subunit, mouse); EC 2.7.11.31 (AMP-Activated Protein Kinases); EC 3.5.1.- (Sirt1 protein, mouse); EC 3.5.1.- (Sirtuin 1); Q369O8926L (resveratrol)


  2 / 297 MEDLINE  
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PMID:28455340
Author:Wang X; Zhou YJ; Wang L; Liu W; Liu Y; Peng C; Zhao ZK
Address:Division of Biotechnology, Dalian Institute of Chemical Physics, CAS, Dalian, People's Republic of China.
Title:Engineering Escherichia coli Nicotinic Acid Mononucleotide Adenylyltransferase for Fully Active Amidated NAD Biosynthesis.
Source:Appl Environ Microbiol; 83(13), 2017 Jul 01.
ISSN:1098-5336
Country of publication:United States
Language:eng
Abstract:NAD and its reduced form NADH function as essential redox cofactors and have major roles in determining cellular metabolic features. NAD can be synthesized through the deamidated and amidated pathways, for which the key reaction involves adenylylation of nicotinic acid mononucleotide (NaMN) and nicotinamide mononucleotide (NMN), respectively. In , NAD biosynthesis depends on the protein NadD-catalyzed adenylylation of NaMN to nicotinic acid adenine dinucleotide (NaAD), followed by NAD synthase-catalyzed amidation. In this study, we engineered NadD to favor NMN for improved amidated pathway activity. We designed NadD mutant libraries, screened by a malic enzyme-coupled colorimetric assay, and identified two variants, 11B4 (Y84V/Y118D) and 16D8 (A86W/Y118N), with a high preference for NMN. Whereas in the presence of NMN both variants were capable of enabling the viability of cells of BW25113-derived NAD-auxotrophic strain YJE003, for which the last step of the deamidated pathway is blocked, the 16D8 expression strain could grow without exogenous NMN and accumulated a higher cellular NAD(H) level than BW25113 in the stationary phase. These mutants established fully active amidated NAD biosynthesis and offered a new opportunity to manipulate NAD metabolism for biocatalysis and metabolic engineering. Adenylylation of nicotinic acid mononucleotide (NaMN) and adenylylation of nicotinamide mononucleotide (NMN), respectively, are the key steps in the deamidated and amidated pathways for NAD biosynthesis. In most organisms, canonical NAD biosynthesis follows the deamidated pathway. Here we engineered NaMN adenylyltransferase to favor NMN and expressed the mutant enzyme in an NAD-auxotrophic strain that has the last step of the deamidated pathway blocked. The engineered strain survived in M9 medium, which indicated the implementation of a functional amidated pathway for NAD biosynthesis. These results enrich our understanding of NAD biosynthesis and are valuable for manipulation of NAD homeostasis for metabolic engineering.
Publication type:JOURNAL ARTICLE
Name of substance:0U46U6E8UK (NAD); 1094-61-7 (Nicotinamide Mononucleotide); 321-02-8 (nicotinate mononucleotide); 6450-77-7 (nicotinic acid adenine dinucleotide); EC 2.7.7.1 (Nicotinamide-Nucleotide Adenylyltransferase); EC 2.7.7.18 (nicotinic acid mononucleotide adenylyltransferase)


  3 / 297 MEDLINE  
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PMID:28435063
Author:Yoon J; Lee KJ; Oh GS; Kim GH; Kim SW
Address:Department of Pharmacology, Asan Medical Center, University of Ulsan College of Medicine, Seoul 05505, Republic of Korea; Bio-medical Institute of Technology, University of Ulsan College of Medicine, Seoul 05505, Republic of Korea.
Title:Regulation of Nampt expression by transcriptional coactivator NCOA6 in pancreatic ß-cells.
Source:Biochem Biophys Res Commun; 487(3):600-606, 2017 Jun 03.
ISSN:1090-2104
Country of publication:United States
Language:eng
Abstract:Nuclear receptor coactivator 6 (NCOA6) is a transcriptional coactivator and crucial for insulin secretion and glucose metabolism in pancreatic ß-cells. However, the regulatory mechanism of ß-cell function by NCOA6 is largely unknown. In this study, we found that the transcript levels of nicotinamide phosphoribosyltransferase (Nampt) were decreased in islets of NCOA6 mice compared with NCOA6 mice. Moreover, NCOA6 overexpression increased the levels of Nampt transcripts in the mouse pancreatic ß-cell line NIT-1. Promoter analyses showed that transcriptional activity of the Nampt promoter was stimulated by cooperation of sterol regulatory element binding protein-1c (SREBP-1c) and NCOA6. Additional studies using mutant promoters demonstrated that SREBP-1c activates Nampt promoter through the sterol regulatory element (SRE), but not through the E-box. Using chromatin immunoprecipitation assay, NCOA6 was also shown to be directly recruited to the SRE region of the Nampt promoter. Furthermore, treatment with nicotinamide mononucleotide (NMN), a product of the Nampt reaction and a key NAD intermediate, ameliorates glucose-stimulated insulin secretion from NCOA6 islets. These results suggest that NCOA6 stimulates insulin secretion, at least partially, by modulating Nampt expression in pancreatic ß-cells.
Publication type:JOURNAL ARTICLE
Name of substance:0 (Cytokines); 0 (Ncoa6 protein, mouse); 0 (Nuclear Receptor Coactivators); 1094-61-7 (Nicotinamide Mononucleotide); EC 2.4.2.12 (Nicotinamide Phosphoribosyltransferase); EC 2.4.2.12 (nicotinamide phosphoribosyltransferase, mouse)


  4 / 297 MEDLINE  
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PMID:28330719
Author:Yao Z; Yang W; Gao Z; Jia P
Address:Department of Neurology, YangPu Hospital, Tongji University School of Medicine, Shanghai 200092, China.
Title:Nicotinamide mononucleotide inhibits JNK activation to reverse Alzheimer disease.
Source:Neurosci Lett; 647:133-140, 2017 Apr 24.
ISSN:1872-7972
Country of publication:Ireland
Language:eng
Abstract:Amyloid-ß (Aß) oligomers have been accepted as major neurotoxic agents in the therapy of Alzheimer's disease (AD). It has been shown that the activity of nicotinamide adenine dinucleotide (NAD+) is related with the decline of Aß toxicity in AD. Nicotinamide mononucleotide (NMN), the important precursor of NAD+, is produced during the reaction of nicotinamide phosphoribosyl transferase (Nampt). This study aimed to figure out the potential therapeutic effects of NMN and its underlying mechanisms in APPswe/PS1dE9 (AD-Tg) mice. We found that NMN gave rise to a substantial improvement in behavioral measures of cognitive impairments compared to control AD-Tg mice. In addition, NMN treatment significantly decreased ß-amyloid production, amyloid plaque burden, synaptic loss, and inflammatory responses in transgenic animals. Mechanistically, NMN effectively controlled JNK activation. Furthermore, NMN potently progressed nonamyloidogenic amyloid precursor protein (APP) and suppressed amyloidogenic APP by mediating the expression of APP cleavage secretase in AD-Tg mice. Based on our findings, it was suggested that NMN substantially decreases multiple AD-associated pathological characteristically at least partially by the inhibition of JNK activation.
Publication type:JOURNAL ARTICLE
Name of substance:0 (Amyloid beta-Protein Precursor); 1094-61-7 (Nicotinamide Mononucleotide); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases); EC 3.4.- (Amyloid Precursor Protein Secretases)


  5 / 297 MEDLINE  
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PMID:28246130
Author:Guan Y; Wang SR; Huang XZ; Xie QH; Xu YY; Shang D; Hao CM
Address:Division of Nephrology, Huashan Hospital, and Nephrology Research Institute, Fudan University, Shanghai, China.
Title:Nicotinamide Mononucleotide, an NAD Precursor, Rescues Age-Associated Susceptibility to AKI in a Sirtuin 1-Dependent Manner.
Source:J Am Soc Nephrol; 28(8):2337-2352, 2017 Aug.
ISSN:1533-3450
Country of publication:United States
Language:eng
Abstract:The rapid growth of an aging population creates challenges regarding age-related diseases, including AKI, for which both the prevalence and death rate increase with age. The molecular mechanism by which the aged kidney becomes more susceptible to acute injury has not been completely elucidated. In this study, we found that, compared with the kidneys of 3-month-old mice, the kidneys of 20-month-old mice expressed reduced levels of the renal protective molecule sirtuin 1 (SIRT1) and its cofactor NAD Supplementation with nicotinamide mononucleotide (NMN), an NAD precursor, restored renal SIRT1 activity and NAD content in 20-month-old mice and further increased both in 3-month-old mice. Moreover, supplementation with NMN significantly protected mice in both age groups from cisplatin-induced AKI. SIRT1 deficiency blunted the protective effect of NMN, and microarray data revealed that c-Jun N-terminal kinase (JNK) signaling activation associated with renal injury in SIRT1 heterozygotes. , SIRT1 attenuated the stress response by modulating the JNK signaling pathway, probably the deacetylation of a JNK phosphatase, DUSP16. Taken together, our findings reveal SIRT1 as a crucial mediator in the renal aging process. Furthermore, manipulation of SIRT1 activity by NMN seems to be a potential pharmaceutical intervention for AKI that could contribute to the precise treatment of aged patients with AKI.
Publication type:JOURNAL ARTICLE
Name of substance:0U46U6E8UK (NAD); 1094-61-7 (Nicotinamide Mononucleotide); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases); EC 3.5.1.- (Sirtuin 1)


  6 / 297 MEDLINE  
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PMID:27979136
Author:Ummarino S; Mozzon M; Zamporlini F; Amici A; Mazzola F; Orsomando G; Ruggieri S; Raffaelli N
Address:Department of Agricultural, Food and Environmental Sciences, Università Politecnica delle Marche, Via Brecce Bianche, Ancona 60131, Italy. Electronic address: s.ummarino@univpm.it.
Title:Simultaneous quantitation of nicotinamide riboside, nicotinamide mononucleotide and nicotinamide adenine dinucleotide in milk by a novel enzyme-coupled assay.
Source:Food Chem; 221:161-168, 2017 Apr 15.
ISSN:0308-8146
Country of publication:England
Language:eng
Abstract:Nicotinamide riboside, the most recently discovered form of vitamin B3, and its phosphorylated form nicotinamide mononucleotide, have been shown to be potent supplements boosting intracellular nicotinamide adenine dinucleotide (NAD) levels, thus preventing or ameliorating metabolic and mitochondrial diseases in mouse models. Here we report for the first time on the simultaneous quantitation of nicotinamide riboside, nicotinamide mononucleotide and NAD in milk by means of a fluorometric, enzyme-coupled assay. Application of this assay to milk from different species revealed that the three vitamers were present in human and donkey milk, while being selectively distributed in the other milks. Human milk was the richest source of nicotinamide mononucleotide. Overall, the three vitamers accounted for a significant fraction of total vitamin B3 content. Pasteurization did not affect the bovine milk content of nicotinamide riboside, whereas UHT processing fully destroyed the vitamin. In human milk, NAD levels were significantly affected by the lactation time.
Publication type:JOURNAL ARTICLE
Name of substance:0I8H2M0L7N (nicotinamide-beta-riboside); 0U46U6E8UK (NAD); 1094-61-7 (Nicotinamide Mononucleotide); 25X51I8RD4 (Niacinamide)


  7 / 297 MEDLINE  
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PMID:27748967
Author:Mattes TA; Escalante-Semerena JC
Address:Department of Microbiology, University of Georgia, Athens, GA, 30602, USA.
Title:Salmonella enterica synthesizes 5,6-dimethylbenzimidazolyl-(DMB)-α-riboside. Why some Firmicutes do not require the canonical DMB activation system to synthesize adenosylcobalamin.
Source:Mol Microbiol; 103(2):269-281, 2017 Jan.
ISSN:1365-2958
Country of publication:England
Language:eng
Abstract:5,6-Dimethylbenzimidazolyl-(DMB)-α-ribotide [α-ribazole-5'-phosphate (α-RP)] is an intermediate in the biosynthesis of adenosylcobalamin (AdoCbl) in many prokaryotes. In such microbes, α-RP is synthesized by nicotinate mononucleotide (NaMN):DMB phosphoribosyltransferases (CobT in Salmonella enterica), in a reaction that is considered to be the canonical step for the activation of the base of the nucleotide present in adenosylcobamides. Some Firmicutes lack CobT-type enzymes but have a two-protein system comprised of a transporter (i.e., CblT) and a kinase (i.e., CblS) that can salvage exogenous α-ribazole (α-R) from the environment using CblT to take up α-R, followed by α-R phosphorylation by CblS. We report that Geobacillus kaustophilus CblT and CblS proteins restore α-RP synthesis in S. enterica lacking the CobT enzyme. We also show that a S. enterica cobT strain that synthesizes GkCblS ectopically makes only AdoCbl, even under growth conditions where the synthesis of pseudoCbl is favored. Our results indicate that S. enterica synthesizes α-R, a metabolite that had not been detected in this bacterium and that GkCblS has a strong preference for DMB-ribose over adenine-ribose as substrate. We propose that in some Firmicutes DMB is activated to α-RP via α-R using an as-yet-unknown route to convert DMB to α-R and CblS to convert α-R to α-RP.
Publication type:JOURNAL ARTICLE
Name of substance:0 (Bacterial Proteins); 0 (Cobamides); 0 (Multienzyme Complexes); 0 (Ribonucleosides); 1094-61-7 (Nicotinamide Mononucleotide); 132-13-8 (alpha-ribazole); 321-02-8 (nicotinate mononucleotide); EC 2.4.2.12 (Nicotinamide Phosphoribosyltransferase); EC 2.7.7.- (Nucleotidyltransferases); F0R1QK73KB (cobamamide)


  8 / 297 MEDLINE  
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PMID:28068222
Author:Mills KF; Yoshida S; Stein LR; Grozio A; Kubota S; Sasaki Y; Redpath P; Migaud ME; Apte RS; Uchida K; Yoshino J; Imai SI
Address:Department of Developmental Biology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Title:Long-Term Administration of Nicotinamide Mononucleotide Mitigates Age-Associated Physiological Decline in Mice.
Source:Cell Metab; 24(6):795-806, 2016 Dec 13.
ISSN:1932-7420
Country of publication:United States
Language:eng
Abstract:NAD availability decreases with age and in certain disease conditions. Nicotinamide mononucleotide (NMN), a key NAD intermediate, has been shown to enhance NAD biosynthesis and ameliorate various pathologies in mouse disease models. In this study, we conducted a 12-month-long NMN administration to regular chow-fed wild-type C57BL/6N mice during their normal aging. Orally administered NMN was quickly utilized to synthesize NAD in tissues. Remarkably, NMN effectively mitigates age-associated physiological decline in mice. Without any obvious toxicity or deleterious effects, NMN suppressed age-associated body weight gain, enhanced energy metabolism, promoted physical activity, improved insulin sensitivity and plasma lipid profile, and ameliorated eye function and other pathophysiologies. Consistent with these phenotypes, NMN prevented age-associated gene expression changes in key metabolic organs and enhanced mitochondrial oxidative metabolism and mitonuclear protein imbalance in skeletal muscle. These effects of NMN highlight the preventive and therapeutic potential of NAD intermediates as effective anti-aging interventions in humans.
Publication type:JOURNAL ARTICLE
Name of substance:0 (Insulin); 0 (Lipids); 0U46U6E8UK (NAD); 1094-61-7 (Nicotinamide Mononucleotide)


  9 / 297 MEDLINE  
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PMID:27984041
Author:Bathke J; Fritz-Wolf K; Brandstädter C; Burkhardt A; Jortzik E; Rahlfs S; Becker K
Address:Biochemistry and Molecular Biology, Interdisciplinary Research Center, Justus Liebig University, D-35392 Giessen, Germany.
Title:Structural and Functional Characterization of Plasmodium falciparum Nicotinic Acid Mononucleotide Adenylyltransferase.
Source:J Mol Biol; 428(24 Pt B):4946-4961, 2016 Dec 04.
ISSN:1089-8638
Country of publication:England
Language:eng
Abstract:Nicotinic acid mononucleotide adenylyltransferase (NaMNAT) is an indispensable enzyme for the synthesis of NAD and NAD phosphate. It catalyzes the adenylylation of nicotinic acid mononucleotide (NaMN) to yield nicotinic acid adenine dinucleotide (NaAD). Since NAD(H) and NAD phosphate(H) are essentially involved in metabolic and redox regulatory reactions, NaMNAT is an attractive drug target in the fight against bacterial and parasitic infections. Notably, NaMNAT of the malaria parasite Plasmodium falciparum possesses only 20% sequence identity with the homologous human enzyme. Here, we present for the first time the two X-ray structures of P. falciparum NaMNAT (PfNaMNAT)-in the product-bound state with NaAD and complexed with an α,ß-non-hydrolizable ATP analog-the structures were determined to a resolution of 2.2Å and 2.5Å, respectively. The overall architecture of PfNaMNAT was found to be more similar to its bacterial homologs than its human counterparts although the PPHK motif conserved in bacteria is missing. Furthermore, PfNaMNAT possesses two cysteine residues within the active site that have not been described for any other NaMNATase so far and are likely to be involved in redox regulation of PfNaMNAT activity. Enzymatic studies and surface plasmon resonance data reveal that PfNaMNAT is capable of utilizing NaMN and nicotinamide mononucleotide with a slight preference for NaMN. Surprisingly, a comparison with the active site of Escherichia coli NaMNAT showed very similar architectures, despite different substrate preferences.
Publication type:JOURNAL ARTICLE
Name of substance:0U46U6E8UK (NAD); 1094-61-7 (Nicotinamide Mononucleotide); 321-02-8 (nicotinate mononucleotide); 53-59-8 (NADP); EC 2.7.7.1 (Nicotinamide-Nucleotide Adenylyltransferase); EC 2.7.7.18 (nicotinic acid mononucleotide adenylyltransferase); K848JZ4886 (Cysteine)


  10 / 297 MEDLINE  
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PMID:27725413
Author:Kawamura T; Mori N; Shibata K
Address:Department of Nutrition, School of Human Cultures, The University of Shiga Prefecture.
Title:ß-Nicotinamide Mononucleotide, an Anti-Aging Candidate Compound, Is Retained in the Body for Longer than Nicotinamide in Rats.
Source:J Nutr Sci Vitaminol (Tokyo); 62(4):272-276, 2016.
ISSN:1881-7742
Country of publication:Japan
Language:eng
Abstract:The turnover of the oxidized form of nicotinamide adenine dinucleotide (NAD ) has attracted interest in regard to longevity. Thus, compounds that can rapidly increase the cellular NAD concentration have been surveyed by many researchers. Of those, ß-nicotinamide mononucleotide (ß-NMN) has been focused on. Studies on the biosynthesis of NAD from ß-NMN have been reported at the cellular level, but not at the whole animal level. In the present study, we investigated whether ß-NMN is superior to nicotinamide (Nam) as a precursor of NAD in whole animal experiments. To this end we compared the NAD concentration in the blood and the urinary excretion amounts of NAD catabolites. Rats were intraperitoneally injected with ß-NMN or Nam. After the injection, blood samples and urine samples were collected at 3-h intervals. The concentration of blood total NAD (NAD11NADH) in each sample showed no significant differences between the two groups. The urinary excretion amounts of NAD catabolites in the urine samples collected at 3-6 h after the injection were lower in the ß-NMN group than in the Nam group. These results suggest that ß-NMN is retained in the body for longer than Nam.
Publication type:JOURNAL ARTICLE
Name of substance:0U46U6E8UK (NAD); 1094-61-7 (Nicotinamide Mononucleotide); 25X51I8RD4 (Niacinamide)



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