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Cells
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Intracellular Regulation Mechanism of Nicotinamide
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Intracellular Regulation Mechanism of Nicotinamide

A special issue of Cells (ISSN 2073-4409).

Deadline for manuscript submissions: closed (30 November 2021) | Viewed by 11602

Special Issue Editor

Prof. Dr. Eun Seong Hwang

E-Mail Website
Guest Editor
Department of Life Science, University of Seoul, Seoul, Korea
Interests: cellular senescence and aging; mitochondria biology; biochemistry of nicotinamide
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

In 1938, Elvehjem et al. reported that pellagra, a major manifestation of vitamin B3 deficiency, could be cured by nicotinamide (NAM), a dietary source of nicotinamide adenine dinucleotide (NAD+). NAM cures not only dermatitis, the main manifestation of pellagra, but also treats seemingly remote symptoms such as psychosensory and psychomotor disturbances, both of which eventually lead to dementia. Since then, NAM treatment has been clinically shown or experimentally proposed to exert diverse beneficiary effects that range from neuroprotection against ischemia/reperfusion to alleviation or prevention against inflammation, diabetes, fibrosis, renal diseases, AIDS, and cancer metastasis. In addition, NAM’s skin-protective effects have made it a popular ingredient in cosmetic products. NAM administration alters NAD+ and tryptophan metabolisms. Mainly based on this, mechanisms at molecular and cellular levels have been proposed for NAM’s therapeutic effects. Our understanding, however, is largely limited to those associated with NAD+ and SIRT1 (and other sirtuin family proteins), NAD+-dependent deacetylases playing diverse roles against metabolic problems. While more understanding on the effects induced by sirtuin activation is needed, studies beyond this topic are warranted. NAM acts as an inhibitor for families of proteins that degrade NAD+ to generate NAM itself. Furthermore, high level NAM in cells and blood can affect gene expression and metabolisms by altering cellular methyl pool, and this raises concerns for possible adversary effects. This Special Issue is called upon to promote and expand in-depth understanding on the mechanisms of molecular and cellular regulatory effects of NAM. In addition, efforts to collectively review NAM’s association to cellular activities such as autophagy and energy metabolism would provide invaluable information on the cellular processes of aging and shed light on its efficacy as an anti-aging regimen. Also, improved understanding on potential toxic effects of high doses of NAM helps avoiding adversary effects. This collection of the papers on these subjects is expected to encourage and broaden therapeutic and nutraceutical applications of NAM and related chemicals.

Prof. Dr. Eun Seong Hwang
Guest Editor

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Keywords

  • nicotinamide
  • NAD+
  • nicotinamide ribose
  • nicotinic acid
  • SIRT1
  • sirtuins
  • mitochondria
  • reactive oxygen species (ROS)
  • methylation
  • neuroprotection

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Published Papers (3 papers)

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Research

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16 pages, 9083 KiB  
Article
Nicotinamide Treatment Facilitates Mitochondrial Fission through Drp1 Activation Mediated by SIRT1-Induced Changes in Cellular Levels of cAMP and Ca2+
by Seon Beom Song, Jin Sung Park, So Young Jang and Eun Seong Hwang
Cells 2021, 10(3), 612; https://doi.org/10.3390/cells10030612 - 10 Mar 2021
Cited by 16 | Viewed by 3891
Abstract
Mitochondrial autophagy (or mitophagy) is essential for mitochondrial quality control, which is critical for cellular and organismal health by attenuating reactive oxygen species generation and maintaining bioenergy homeostasis. Previously, we showed that mitophagy is activated in human cells through SIRT1 activation upon treatment [...] Read more.
Mitochondrial autophagy (or mitophagy) is essential for mitochondrial quality control, which is critical for cellular and organismal health by attenuating reactive oxygen species generation and maintaining bioenergy homeostasis. Previously, we showed that mitophagy is activated in human cells through SIRT1 activation upon treatment of nicotinamide (NAM). Further, mitochondria are maintained as short fragments in the treated cells. In the current study, molecular pathways for NAM-induced mitochondrial fragmentation were sought. NAM treatment induced mitochondrial fission, at least in part by activating dynamin-1-like protein (Drp1), and this was through attenuation of the inhibitory phosphorylation at serine 637 (S637) of Drp1. This Drp1 hypo-phosphorylation was attributed to SIRT1-mediated activation of AMP-activated protein kinase (AMPK), which in turn induced a decrease in cellular levels of cyclic AMP (cAMP) and protein kinase A (PKA) activity, a kinase targeting S637 of Drp1. Furthermore, in NAM-treated cells, cytosolic Ca2+ was highly maintained; and, as a consequence, activity of calcineurin, a Drp1-dephosphorylating phosphatase, is expected to be elevated. These results suggest that NAD+-mediated SIRT1 activation facilitates mitochondrial fission through activation of Drp1 by suppressing its phosphorylation and accelerating its dephosphorylation. Additionally, it is suggested that there is a cycle of mitochondrial fragmentation and cytosolic Ca2+-mediated Drp1 dephosphorylation that may drive sustained mitochondrial fragmentation. Full article
(This article belongs to the Special Issue Intracellular Regulation Mechanism of Nicotinamide)
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Review

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20 pages, 2060 KiB  
Review
Nicotinamide Adenine Dinucleotide Phosphate Oxidases in Glucose Homeostasis and Diabetes-Related Endothelial Cell Dysfunction
by Oliver Ian Brown, Katherine Isabella Bridge and Mark Thomas Kearney
Cells 2021, 10(9), 2315; https://doi.org/10.3390/cells10092315 - 4 Sep 2021
Cited by 17 | Viewed by 3706
Abstract
Oxidative stress within the vascular endothelium, due to excess generation of reactive oxygen species (ROS), is thought to be fundamental to the initiation and progression of the cardiovascular complications of type 2 diabetes mellitus. The term ROS encompasses a variety of chemical species [...] Read more.
Oxidative stress within the vascular endothelium, due to excess generation of reactive oxygen species (ROS), is thought to be fundamental to the initiation and progression of the cardiovascular complications of type 2 diabetes mellitus. The term ROS encompasses a variety of chemical species including superoxide anion (O2•−), hydroxyl radical (OH−) and hydrogen peroxide (H2O2). While constitutive generation of low concentrations of ROS are indispensable for normal cellular function, excess O2•− can result in irreversible tissue damage. Excess ROS generation is catalysed by xanthine oxidase, uncoupled nitric oxide synthases, the mitochondrial electron transport chain and the nicotinamide adenine dinucleotide phosphate (NADPH) oxidases. Amongst enzymatic sources of O2•− the Nox2 isoform of NADPH oxidase is thought to be critical to the oxidative stress found in type 2 diabetes mellitus. In contrast, the transcriptionally regulated Nox4 isoform, which generates H2O2, may fulfil a protective role and contribute to normal glucose homeostasis. This review describes the key roles of Nox2 and Nox4, as well as Nox1 and Nox5, in glucose homeostasis, endothelial function and oxidative stress, with a key focus on how they are regulated in health, and dysregulated in type 2 diabetes mellitus. Full article
(This article belongs to the Special Issue Intracellular Regulation Mechanism of Nicotinamide)
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14 pages, 1468 KiB  
Review
Human Vascular Smooth Muscle Function and Oxidative Stress Induced by NADPH Oxidase with the Clinical Implications
by Kazumi Takaishi, Hiroyuki Kinoshita, Shingo Kawashima and Shinji Kawahito
Cells 2021, 10(8), 1947; https://doi.org/10.3390/cells10081947 - 31 Jul 2021
Cited by 13 | Viewed by 3146
Abstract
Among reactive oxygen species, superoxide mediates the critical vascular redox signaling, resulting in the regulation of the human cardiovascular system. The reduced form of nicotinamide adenine dinucleotide phosphate oxidase (NADPH oxidase, NOX) is the source of superoxide and relates to the crucial intracellular [...] Read more.
Among reactive oxygen species, superoxide mediates the critical vascular redox signaling, resulting in the regulation of the human cardiovascular system. The reduced form of nicotinamide adenine dinucleotide phosphate oxidase (NADPH oxidase, NOX) is the source of superoxide and relates to the crucial intracellular pathology and physiology of vascular smooth muscle cells, including contraction, proliferation, apoptosis, and inflammatory response. Human vascular smooth muscle cells express NOX1, 2, 4, and 5 in physiological and pathological conditions, and those enzymes play roles in most cardiovascular disorders caused by hypertension, diabetes, inflammation, and arteriosclerosis. Various physiologically active substances, including angiotensin II, stimulate NOX via the cytosolic subunits’ translocation toward the vascular smooth muscle cell membrane. As we have shown, some pathological stimuli such as high glucose augment the enzymatic activity mediated by the phosphatidylinositol 3-kinase-Akt pathway, resulting in the membrane translocation of cytosolic subunits of NOXs. This review highlights and details the roles of human vascular smooth muscle NOXs in the pathophysiology and clinical aspects. The regulation of the enzyme expressed in the vascular smooth muscle cells may lead to the prevention and treatment of human cardiovascular diseases. Full article
(This article belongs to the Special Issue Intracellular Regulation Mechanism of Nicotinamide)
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