Mitochondrial NADPH, transhydrogenase and disease

Rydström, Jan

doi:10.1016/j.bbabio.2006.03.010

Cited by 256Mitochondrial Function and PathologySirtuins and Resveratrol in MedicineRedox biology and oxidative stress

Mitochondrial NADPH, transhydrogenase and disease

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Rydström, Jan·2006·Biochimica et Biophysica Acta (BBA) - Bioenergetics

DOI 10.1016/j.bbabio.2006.03.010

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Abstract

Ever since its discovery in 1953 by N. O. Kaplan and coworkers, the physiological role of the proton-translocating transhydrogenase has generally been assumed to be that of generating mitochondrial NADPH. Mitochondrial NADPH can be used in a number of important reactions/processes, e.g., biosynthesis, maintenance of GSH, apoptosis, aging etc. This assumed role has found some support in bacteria but not in higher eukaryotes, a situation which changed dramatically with two recent but separate findings, both using transhydrogenase knockouts, in the nematode C. elegans and the mouse strain C57BL/6J. The latter, which is due to a spontaneous deletion mutation in the Nnt gene, was serendipitously found during investigations of the diabetic properties of these mice. The implications of these findings for the overall role of transhydrogenase in cell metabolism and disease are discussed.

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Alternatively, substrate flow through the TCA cycle differs depending on substrates, which might affect the activity of NADP+-dependent isocitrate dehydrogenase and malic enzyme.
“Alternatively, the substrate flow through the TCA cycle differs depending on the substrates, which might affect the activity of the other two mitochondrial NADPH-regenerating enzymes the NADP + -dependent isocitrate dehydrogenase [119,120] and the malic enzyme [118,121].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [118]
The lower H2O2 scavenger activity with succinate may be explained by the membrane-bound transhydrogenase depending on a constant NADH supply.
“This might be explained by the fact that one of the main NADP + -reducing enzymes in the mitochondria, the membrane-bound transhydrogenase [118], depends on a constant NADH supply.”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [118]
Mitochondria typically have a high NADPH/NADP+ ratio, supported in part by interconversion of NADPH and NADH in the matrix.
“Mitochondria typically have a high NADPH/NADP+ ratio, supported in part by the ability to interconvert NADPH and NADH in the matrix (Rydstrom, 2006).”
From The Common Feature of Leukemia-Associated IDH1 and IDH2 Mutations Is a Neomorphic Enzyme Activity Converting α-Ketoglutarate to 2-Hydroxyglutarate (2010) · cites this paper as Rydstrom, 2006
In mitochondria, nicotinamide nucleotide transhydrogenase (NNT) regenerates NADPH from NADP+ utilizing NADH produced in the TCA cycle, relying on the mitochondrial electrochemical proton gradient for its activity.
“In mitochondria, the enzymatic actions of nicotinamide nucleotide transhydrogenase (NNT), which relies on the mitochondrial electrochemical proton gradient for its activity, regenerates NADPH from NADP+ utilizing NADH produced in the TCA cycle (361).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [361]
NADH can be converted to NADPH within mitochondria via a transhydrogenase absent from the cytosol.
“NADH can be converted to NADPH within the mitochondria via a transhydrogenase absent from the cytosol (Rydstrom, 2006)”
From Metabolic Reprogramming: A Cancer Hallmark Even Warburg Did Not Anticipate (2012) · cites this paper as Rydstrom, 2006

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Authors: Rydström, J.
Affiliations: University of Gothenburg (SE)
Corresponding author: Rydström, Jan
Venue: Biochimica et Biophysica Acta (BBA) - Bioenergetics
Publisher: Elsevier BV
Published: 2006-05
Volume: 1757
Issue: 5-6
Pages: 721-726
ISSN: 0005-2728 (ISSN-L)
DOI: 10.1016/j.bbabio.2006.03.010
OpenAlex: W2041128667
Cited by: 256
References: 57
Citations by year: 2026: 12 · 2025: 14 · 2024: 13 · 2023: 16 · 2022: 14 · 2021: 27 · 2020: 23 · 2019: 12 · 2018: 15 · 2017: 19 · 2016: 13 · 2015: 12 · 2014: 10 · 2013: 10 · 2012: 13
FWCI: 2.58
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 2635 d)
Locations: Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
PubMed (publishedVersion)
Funders: Vetenskapsrådet
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: transhydrogenase, Caenorhabditis elegans, C57BL/6J mice, diabetes mellitus, glutathione, apoptosis, aging, cellular metabolism, disease
MeSH terms: Aging, Animals, Diabetes Mellitus, Type 2, Electron Transport, Mice, Inbred C57BL, Mitochondria, Mutation, NADP, NADP Transhydrogenases, Mice, Knockout, Mitochondrial Diseases, Caenorhabditis elegans Proteins, Insulin-Secreting Cells, Mice

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Mitochondrial NADPH, transhydrogenase and disease

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