The simultaneous measurement of nicotinamide adenine dinucleotide and related compounds by liquid chromatography/electrospray ionization tandem mass spectrometry

Yamada, Kazuo; Hara, Nobumasa; Shibata, Tomoko; Osago, Harumi; Tsuchiya, Masaharu

doi:10.1016/j.ab.2006.02.017

Cited by 139 publications

(104 citation statements)

References 14 publications

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“…Under intense exercise conditions, however, pyruvate may be used to oxidize NADH, resulting in lactate accumulation and acidosis (52), reducing cytosolic pH from ϳ7.0 in resting muscle to as low as pH 6.2-6.4 (38 -42). Cytosolic NAD ϩ concentration is believed to be in the range 0.3-0.7 mM (35)(36)(37). In this range NAD ϩ inhibited ClC-1 channels at pH 6.8, but inhibition was greatly enhanced when pH was reduced to 6.2.…”

Section: Discussionmentioning

confidence: 99%

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Intracellular β-Nicotinamide Adenine Dinucleotide Inhibits the Skeletal Muscle ClC-1 Chloride Channel

Bennetts

Chen

et al. 2012

Journal of Biological Chemistry

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Background: Weakly voltage-dependent ClC-1 chloride channels regulate skeletal muscle excitability. Results: Intracellular NAD(H) altered the voltage dependence of ClC-1 gating, and specific mutations attenuated this effect. Conclusion: NAD(H) directly inhibits ClC-1 chloride channels by binding to intracellular domains. Significance: ClC-1 inhibition by NAD(H) may play an important role in muscle fatigue and the pathophysiology of myotonia congenita.

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Section: Discussionmentioning

confidence: 99%

“…2C). Current estimates place the cytosolic NAD ϩ concentration in the range 0.3-0.7 mM (35)(36)(37). At intracellular pH 6.8, inclusion of 0.3 mM NAD ϩ or NADH in the intracellular solution had only a slight effect on common gating (Fig.…”

Section: Intracellular Nad(h) Inhibits Clc-1 By Modulatingmentioning

confidence: 99%

Intracellular β-Nicotinamide Adenine Dinucleotide Inhibits the Skeletal Muscle ClC-1 Chloride Channel

Bennetts

Chen

et al. 2012

Journal of Biological Chemistry

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“…The cellular concentration of NAD ϩ has been estimated to be between 0.3 to 0.4 mM (Yamada et al, 2006;Yang et al, 2007), although the concentrations within neurons are not well established. We tested various concentrations of NAD ϩ to evaluate the minimal concentrations of NAD ϩ needed to cause a significant facilitation in open probability.…”

Section: Nadmentioning

confidence: 99%

NAD⁺Activates K_NaChannels in Dorsal Root Ganglion Neurons

Picchione²,

2009

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Although sodium-activated potassium channels (K Na ) have been suggested to shape various firing patterns in neurons, including action potential repolarization, their requirement for high concentrations of Na ϩ to gate conflicts with this view. We characterized K Na channels in adult rat dorsal root ganglion (DRG) neurons. Using immunohistochemistry, we found ubiquitous expression of the Slack K Na channel subunit in small-, medium-, and large-diameter DRG neurons. Basal K Na channel activity could be recorded from cell-attached patches of acutely dissociated neurons bathed in physiological saline, and yet in excised inside-out membrane patches, the Na ϩ EC 50 for K Na channels was typically high, ϳ50 mM. In some cases, however, K Na channel activity remained considerable after initial patch excision but decreased rapidly over time. Channel activity was restored in patches with high Na ϩ . The channel rundown after initial excision suggested that modulation of channels might be occurring through a diffusible cytoplasmic factor. Sequence analysis indicated that the Slack channel contains a putative nicotinamide adenine dinucleotide (NAD ϩ )-binding site; accordingly, we examined the modulation of native K Na and Slack channels by NAD ϩ . In inside-out-excised neuronal patch recordings, we found a decrease in the Na ϩ EC 50 for K Na channels from ϳ50 to ϳ20 mM when NAD ϩ was included in the perfusate. NAD ϩ also potentiated recombinant Slack channel activity. NAD ϩ modulation may allow K Na channels to operate under physiologically relevant levels of intracellular Na ϩ and hence provides an explanation as to how K Na channel can control normal neuronal excitability.

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“…Determination of NAD Synthesis by Human Cells-Cellular contents of NAD and related compounds were simultaneously determined by ESI-MS analysis, as described previously (26), using a triple quadrupole mass spectrometer (API3000, Applied Biosystems, Foster City, CA).…”

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Elevation of Cellular NAD Levels by Nicotinic Acid and Involvement of Nicotinic Acid Phosphoribosyltransferase in Human Cells

Hara

Yamada

Shibata

et al. 2007

Journal of Biological Chemistry

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184

172

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NAD plays critical roles in various biological processes through the function of SIRT1. Although classical studies in mammals showed that nicotinic acid (NA) is a better precursor than nicotinamide (Nam) in elevating tissue NAD levels, molecular details of NAD synthesis from NA remain largely unknown. We here identified NA phosphoribosyltransferase (NAPRT) in humans and provided direct evidence of tight link between NAPRT and the increase in cellular NAD levels. The enzyme was abundantly expressed in the small intestine, liver, and kidney in mice and mediated [ 14 C]NAD synthesis from [ 14 C]NA in human cells. In cells expressing endogenous NAPRT, the addition of NA but not Nam almost doubled cellular NAD contents and decreased cytotoxicity by H 2 O 2 . Both effects were reversed by knockdown of NAPRT expression. These results indicate that NAPRT is essential for NA to increase cellular NAD levels and, thus, to prevent oxidative stress of the cells. Kinetic analyses revealed that NAPRT, but not Nam phosphoribosyltransferase (NamPRT, also known as pre-B-cell colony-enhancing factor or visfatin), is insensitive to the physiological concentration of NAD. Together, we conclude that NA elevates cellular NAD levels through NAPRT function and, thus, protects the cells against stress, partly due to lack of feedback inhibition of NAPRT but not NamPRT by NAD. The ability of NA to increase cellular NAD contents may account for some of the clinically observed effects of the vitamin and further implies a novel application of the vitamin to treat diseases such as those associated with the depletion of cellular NAD pools.

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The simultaneous measurement of nicotinamide adenine dinucleotide and related compounds by liquid chromatography/electrospray ionization tandem mass spectrometry

Cited by 139 publications

References 14 publications

Intracellular β-Nicotinamide Adenine Dinucleotide Inhibits the Skeletal Muscle ClC-1 Chloride Channel

Intracellular β-Nicotinamide Adenine Dinucleotide Inhibits the Skeletal Muscle ClC-1 Chloride Channel

NAD⁺Activates K_NaChannels in Dorsal Root Ganglion Neurons

Elevation of Cellular NAD Levels by Nicotinic Acid and Involvement of Nicotinic Acid Phosphoribosyltransferase in Human Cells

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The simultaneous measurement of nicotinamide adenine dinucleotide and related compounds by liquid chromatography/electrospray ionization tandem mass spectrometry

Cited by 139 publications

References 14 publications

Intracellular β-Nicotinamide Adenine Dinucleotide Inhibits the Skeletal Muscle ClC-1 Chloride Channel

Intracellular β-Nicotinamide Adenine Dinucleotide Inhibits the Skeletal Muscle ClC-1 Chloride Channel

NAD+Activates KNaChannels in Dorsal Root Ganglion Neurons

Elevation of Cellular NAD Levels by Nicotinic Acid and Involvement of Nicotinic Acid Phosphoribosyltransferase in Human Cells

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NAD⁺Activates K_NaChannels in Dorsal Root Ganglion Neurons