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NAD+ homeostasis in health and disease

Nature Metabolism, 2020
The conceptual evolution of nicotinamide adenine dinucleotide (NAD+) from being seen as a simple metabolic cofactor to a pivotal cosubstrate for proteins regulating metabolism and longevity, including the sirtuin family of protein deacylases, has led to a new wave of scientific interest in NAD+. NAD+ levels decline during ageing, and alterations in NAD+
E. Katsyuba   +3 more
semanticscholar   +3 more sources

NAD+ and cardiovascular diseases

Clinica Chimica Acta, 2021
Nicotinamide adenine dinucleotide (NAD) plays pivotal roles in controlling many biochemical processes. 'NAD' refers to the chemical backbone irrespective of charge, whereas 'NAD+' and 'NADH' refers to oxidized and reduced forms, respectively. NAD+/NADH ratio is essential for maintaining cellular reduction-oxidation (redox) homeostasis and for ...
Yaozhong Liu   +4 more
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NAD+-pyridoxine and NAD+-pyridoxamine complexes

Biochimica et Biophysica Acta (BBA) - General Subjects, 1971
Abstract 1. 1. NAD+-pyridoxamine complexes were studied by fluorescence techniques at 30° over a pH range of 8.4–10.0. 2. 2. The polarization factor was seen to increase with increasing NAD+ concentration in all cases. 3. 3. Fluorescence quenching studis established large complex formation constants for both complexes. 4. 4.
W.R. Carper, V.D. Anand
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Evidence for binding of NAD dimers to NAD-dependent dehydrogenases

Biochimica et Biophysica Acta (BBA) - Enzymology, 1981
The binding of dimers of nicotinamide adenine dinucleotide, (NAD)2, to lactate, malate and alcohol dehydrogenase has been studied by the fluorescence quenching technique. While the alcohol dehydrogenase shows a low binding ability, malate and lactate dehydrogenases have been found to bind (NAD)2 in a specific way with high affinity.
FINAZZI AGRÒ A.   +4 more
openaire   +4 more sources

NAD on the rise again

Nature Metabolism, 2020
Maintaining cellular NAD levels through supplementation with intermediates of NAD synthesis has considerable health benefits. A new study demonstrates that the reduced form of nicotinamide riboside, NRH, can be converted to NAD in a biosynthetic pathway that involves adenosine kinase, thus strongly boosting NAD levels in cells and tissues.
Mathias Ziegler, Andrey A. Nikiforov
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Adriamycin-catalyzed aerobic photooxidation of NAD dimers to NAD+

Biochimica et Biophysica Acta (BBA) - General Subjects, 1989
The photooxidation of the dimers of nicotinamide adenine dinucleotide, (NAD)2, is catalyzed by adriamycin under aerobic conditions. (NAD)2 and O2 react in 1:1 molar ratio to yield 2 mol of NAD+. Experiments carried out by irradiating at 340 and 485 nm, corresponding to the absorption maxima of (NAD)2 and adriamycin, respectively, clearly indicate that ...
A. Finazzi Agrò   +5 more
openaire   +3 more sources

NAD to the Rescue

Science, 2004
Identified 15 years ago, the Wld mouse carries a spontaneous mutation that encodes a fusion protein with neuroprotective properties. In a Perspective, [Simon][1] discusses new work ([ Araki et al .][2]) that identifies the Nmnat1 fragment of the fusion protein as mediating neuroprotection by boosting NAD biosynthesis and increasing the activity of the ...
Antonio Bedalov, Julian A. Simon
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NAD+ cleavage activity by animal and plant TIR domains in cell death pathways

Science, 2019
NAD depletion as pathogen response One way that plants respond to pathogen infection is by sacrificing the infected cells. The nucleotide-binding leucine-rich repeat immune receptors responsible for this hypersensitive response carry Toll/interleukin-1 ...
S. Horsefield   +26 more
semanticscholar   +1 more source

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