Requirement of argininosuccinate lyase for systemic nitric oxide production
Open accessAbstract
Nitric oxide (NO) is crucial in diverse physiological and pathological processes. We show that a hypomorphic mouse model of argininosuccinate lyase (encoded by Asl) deficiency has a distinct phenotype of multiorgan dysfunction and NO deficiency. Loss of Asl in both humans and mice leads to reduced NO synthesis, owing to both decreased endogenous arginine synthesis and an impaired ability to use extracellular arginine for NO production. Administration of nitrite, which can be converted into NO in vivo, rescued the manifestations of NO deficiency in hypomorphic Asl mice, and a nitric oxide synthase (NOS)-independent NO donor restored NO-dependent vascular reactivity in humans with ASL deficiency. Mechanistic studies showed that ASL has a structural function in addition to its catalytic activity, by which it contributes to the formation of a multiprotein complex required for NO production. Our data demonstrate a previously unappreciated role for ASL in NOS function and NO homeostasis. Hence, ASL may serve as a target for manipulating NO production in experimental models, as well as for the treatment of NO-related diseases.
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A membrane metabolon including arginine succinate lyase, argininosuccinate synthetase, hsp90, and eNOS associates in caveolae and is necessary for regular eNOS function.
“A membrane metabolon including arginine succinate lyase, argininosuccinate synthetase, hsp90, and eNOS associates in the caveolae and is necessary for regular eNOS function (270, 294, 634).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [270]
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- Authors
- Erez, A., Nagamani, S. C. S., Shchelochkov, O. A., Premkumar, M. H., Campeau, P. M., Chen, Y., Garg, H. K., Li, L., Mian, A., Bertin, T. K., Black, J. O., Zeng, H., Tang, Y., Reddy, A. K., Summar, M., O'Brien, W. E., Harrison, D. G., Mitch, W. E., Marini, J. C., Aschner, J. L., Bryan, N. S., & Lee, B.
- Affiliations
- Baylor College of Medicine (US)
- Howard Hughes Medical Institute (US)
- Brown Foundation Institute of Molecular Medicine for the Prevention of Human Diseases (US)
- Emory University (US)
- Texas Children's Hospital (US)
- Vanderbilt University Medical Center (US)
- Houston Methodist (US)
- Agricultural Research Service (US)
- Corresponding author
- Lee, Brendan
- ORCID
- Venue
- Nature Medicine
- Published
- 2011-11-13
- Volume
- 17
- Issue
- 12
- Pages
- 1619-1626
- ISSN
- 1078-8956 (ISSN-L)
- 1546-170X
- PMC
- PMC3348956
- OpenAlex
- W2087900616
- Cited by
- 233
- References
- 44
- Citations by year
- 2026: 16 · 2025: 13 · 2024: 11 · 2023: 15 · 2022: 7 · 2021: 15 · 2020: 16 · 2019: 18 · 2018: 14 · 2017: 16 · 2016: 14 · 2015: 16 · 2014: 21 · 2013: 21 · 2012: 18
- FWCI
- 13.53
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Medicine (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eCommons - AKU (Aga Khan University) (submittedVersion)
- Funders
- Canadian Institutes of Health Research
- National Heart, Lung, and Blood Institute (HL75511, R01HL022512, R01HL075511)
- National Institute of General Medical Sciences (GM90310, R01GM090310, GM-07526, T32GM007526)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK081735, R01DK054450, R37DK037175, K08DK081735, DK54450, DK-37175, R01DK037175)
- National Center for Research Resources (U54RR019453, RR 00188, RR19453, RR024173, K01RR000188, K01RR024173, M01RR000188)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (U54HD061221)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Keywords
- argininosuccinate lyase, nitric oxide production, arginine metabolism, urea cycle disorders, nitrite, nitric oxide synthase, vascular reactivity, multiple organ failure, enzyme complex formation, nitric oxide homeostasis
- MeSH terms
- Animals, Arginine, Argininosuccinate Lyase, Argininosuccinate Synthase, Cell Line, Disease Models, Animal, Female, Fibroblasts, Humans, Male, Mice, Inbred C57BL, Nitric Oxide, Nitrites, Swine, Sequence Analysis, DNA, Mice, Knockout, Nitric Oxide Synthase, RNA, Small Interfering, Endothelial Cells, Mice, Gene Knockdown Techniques, Argininosuccinic Aciduria
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