Cited by 513Advanced Fluorescence Microscopy TechniquesRedox biology and oxidative stressbioluminescence and chemiluminescence research

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Imaging cytosolic NADH-NAD(+) redox state with a genetically encoded fluorescent biosensor

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Hung, Yin Pun, Albeck, John G., Tantama, Mathew, Yellen, Gary·2011·Cell Metabolism

DOI 10.1016/j.cmet.2011.08.012PMC PMC3190165

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Abstract

NADH is a key metabolic cofactor whose sensitive and specific detection in the cytosol of live cells has been difficult. We constructed a fluorescent biosensor of the cytosolic NADH-NAD(+) redox state by combining a circularly permuted GFP T-Sapphire with a bacterial NADH-binding protein, Rex. Although the initial construct reported [NADH] × [H(+)] / [NAD(+)], its pH sensitivity was eliminated by mutagenesis. The engineered biosensor Peredox reports cytosolic NADH:NAD(+) ratios and can be calibrated with exogenous lactate and pyruvate. We demonstrated its utility in several cultured and primary cell types. We found that glycolysis opposed the lactate dehydrogenase equilibrium to produce a reduced cytosolic NADH-NAD(+) redox state. We also observed different redox states in primary mouse astrocytes and neurons, consistent with hypothesized metabolic differences. Furthermore, using high-content image analysis, we monitored NADH responses to PI3K pathway inhibition in hundreds of live cells. As an NADH reporter, Peredox should enable better understanding of bioenergetics.

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Authors: Hung, Y. P., Albeck, J. G., Tantama, M., & Yellen, G.
Affiliations: Harvard University (US)
Corresponding author: Yellen, Gary
ORCID: Hung, Yin Pun
Albeck, John G.
Tantama, Mathew
Yellen, Gary
Venue: Cell Metabolism
Publisher: Elsevier BV
Published: 2011-10
Volume: 14
Issue: 4
Pages: 545-554
ISSN: 1550-4131 (ISSN-L)
DOI: 10.1016/j.cmet.2011.08.012
PMC: PMC3190165
OpenAlex: W2155184340
Cited by: 509
References: 58
Citations by year: 2026: 31 · 2025: 29 · 2024: 32 · 2023: 34 · 2022: 34 · 2021: 43 · 2020: 59 · 2019: 29 · 2018: 46 · 2017: 39 · 2016: 30 · 2015: 29 · 2014: 34 · 2013: 26 · 2012: 12
FWCI: 13.40
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 655 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Cell Metabolism (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: U.S. Army (W81XWH-08-1-0609)
National Institutes of Health (R01 NS055031, F32 NS066613)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Advanced Fluorescence Microscopy Techniques
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › bioluminescence and chemiluminescence research
Keywords: genetically encoded fluorescent sensors, circularly permuted GFP, glycolysis, lactate dehydrogenase, astrocytes, neurons, bioenergetics, live-cell imaging
MeSH terms: Phosphoinositide-3 Kinase Inhibitors, Animals, Bacterial Proteins, Cells, Cultured, Cytosol, Glycolysis, Hydrogen-Ion Concentration, L-Lactate Dehydrogenase, Luminescent Proteins, NAD, Oxidation-Reduction, Recombinant Fusion Proteins, Biosensing Techniques, Phosphatidylinositol 3-Kinases, Mice

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Imaging cytosolic NADH-NAD(+) redox state with a genetically encoded fluorescent biosensor

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