Evidence map›Paper›PMID 31511627›Full record

ArticleScientific reports2019

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

Keisuke Yaku, Keisuke Okabe, Maryam Gulshan, Kiyoshi Takatsu, Hiroshi Okamoto, Takashi Nakagawa

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 39 citations in OpenAlex.

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  19. An Overview of the Mechanism ofEvidence-based complementary and alternative medicine : eCAM · 2020
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 1 country.

Keisuke YakuDepartment of Metabolism and Nutrition, Graduate School of Medicine and Pharmaceutical Science for Research, University of Toyama, Toyama, 930-0194, Japan.
Keisuke OkabeDepartment of Metabolism and Nutrition, Graduate School of Medicine and Pharmaceutical Science for Research, University of Toyama, Toyama, 930-0194, Japan.
Maryam GulshanDepartment of Metabolism and Nutrition, Graduate School of Medicine and Pharmaceutical Science for Research, University of Toyama, Toyama, 930-0194, Japan.
Kiyoshi TakatsuToyama Prefectural Institute for Pharmaceutical Research, Toyama, 939-0363, Japan.
Hiroshi OkamotoDepartment of Biochemistry, Tohoku University Graduate School of Medicine, Sendai, 980-8575, Japan.
Takashi NakagawaDepartment of Metabolism and Nutrition, Graduate School of Medicine and Pharmaceutical Science for Research, University of Toyama, Toyama, 930-0194, Japan. nakagawa@med.u-toyama.ac.jp.ORCID http://orcid.org/0000-0001-5539-7605
University of Toyama · JPKanazawa University · JPToyama College · JPToyama Prefectural Institute for Pharmaceutical Research · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

AgingAnimalsGuanine NucleotidesGuanosine TriphosphateInosine TriphosphateMiceNADPoly(ADP-ribose) PolymerasesSirtuinsGuanine NucleotidesGuanosine TriphosphateInosine TriphosphateNADnicotinamide guanine dinucleotidenicotinamide-hypoxanthine dinucleotidePoly(ADP-ribose) PolymerasesSirtuins

Identifiers

PMID31511627
PMCPMC6739475
OpenAlexW2973205401

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.