Reduction of N ω-hydroxy-L-arginine by the mitochondrial amidoxime reducing component (mARC)
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NOSs (nitric oxide synthases) catalyse the oxidation of L-arginine to L-citrulline and nitric oxide via the intermediate NOHA (Nω-hydroxy-L-arginine). This intermediate is rapidly converted further, but to a small extent can also be liberated from the active site of NOSs and act as a transportable precursor of nitric oxide or potent physiological inhibitor of arginases. Thus its formation is of enormous importance for the nitric-oxide-generating system. It has also been shown that NOHA is reduced by microsomes and mitochondria to L-arginine. In the present study, we show for the first time that both human isoforms of the newly identified mARC (mitochondrial amidoxime reducing component) enhance the rate of reduction of NOHA, in the presence of NADH cytochrome b5 reductase and cytochrome b5, by more than 500-fold. Consequently, these results provide the first hints that mARC might be involved in mitochondrial NOHA reduction and could be of physiological significance in affecting endogenous nitric oxide levels. Possibly, this reduction represents another regulative mechanism in the complex regulation of nitric oxide biosynthesis, considering a mitochondrial NOS has been identified. Moreover, this reduction is not restricted to NOHA since the analogous arginase inhibitor NHAM (Nω-hydroxy-Nδ-methyl-L-arginine) is also reduced by this system.
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Sepiapterin supplementation improves endothelial function in several mouse models, including atherosclerosis ApoE−/− mice, diabetes models, and obesity models.
“Sepiapterin supplementation improves endothelial function in several mouse models, including the atherosclerosis model ApoE−/− mice (560), diabetes models (721), or obesity models (527).”
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- Authors
- Kotthaus, J., Wahl, B., Havemeyer, A., Kotthaus, J., Schade, D., Garbe-Schönberg, D., Mendel, R., Bittner, F., & Clement, B.
- Affiliations
- Christian-Albrechts-Universität zu Kiel (DE)
- Technische Universität Braunschweig (DE)
- ICPMS Laboratory Institute of Geosciences, Christian-Albrechts-University of Kiel, Ludewig-Meyn-Str. 10, D-24118 Kiel, Germany
- Corresponding author
- Havemeyer, Antje
- Kotthaus, Joscha
- Schade, Dennis
- Clement, Bernd
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2010-12-22
- Volume
- 433
- Issue
- 2
- Pages
- 383-391
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1989353969
- Cited by
- 88
- References
- 47
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 2 · 2023: 5 · 2022: 5 · 2021: 2 · 2020: 7 · 2019: 5 · 2018: 7 · 2017: 2 · 2016: 3 · 2015: 4 · 2014: 12 · 2013: 10 · 2012: 8
- FWCI
- 6.28
- Type
- journal article
- Language
- en
- Open access
- green
- hal.science
- Licence
- other-oa
- Locations
- Biochemical Journal (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Keywords
- nitric oxide synthase, nitric oxide production, NADH-cytochrome b5 reductase, cytochrome b5, arginase inhibition
- MeSH terms
- Animals, Arginine, Benzamidines, Humans, Oxidation-Reduction, Oxidoreductases, Swine, Mitochondrial Proteins, Hep G2 Cells
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