Indoleamine 2,3 dioxygenase and metabolic control of immune responses
Open accessAbstract
Sustained access to nutrients is a fundamental biological need, especially for proliferating cells, and controlling nutrient supply is an ancient strategy to regulate cellular responses to stimuli. By catabolizing the essential amino acid TRP, cells expressing the enzyme indoleamine 2,3 dioxygenase (IDO) can mediate potent local effects on innate and adaptive immune responses to inflammatory insults. Here, we discuss recent progress in elucidating how IDO activity promotes local metabolic changes that impact cellular and systemic responses to inflammatory and immunological signals. These recent developments identify potential new targets for therapy in a range of clinical settings, including cancer, chronic infections, autoimmune and allergic syndromes, and transplantation.
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IDO is an immune inducible enzyme that metabolizes TRP through the KYN pathway and plays an important role in the immune response.
“Indoleamine 2,3 dioxygenase (IDO) is an immune inducible enzyme that metabolizes TRP through the KYN pathway and plays an important role in the immune response. 236”
From Major depressive disorder: hypothesis, mechanism, prevention and treatment (2024) · cites this paper as [236]
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Regulation of PD-1/PD-L1 pathway and resistance to PD-1/PD-L1 blockade
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- Authors
- Munn, D. H., & Mellor, A. L.
- Affiliations
- Augusta University Health (US)
- Corresponding author
- Mellor, Andrew L.
- Venue
- Trends in Immunology
- Publisher
- Elsevier BV
- Published
- 2013-03
- Volume
- 34
- Issue
- 3
- Pages
- 137-143
- ISSN
- 1471-4906 (ISSN-L)
- PMC
- PMC3594632
- OpenAlex
- W2012836981
- Cited by
- 1,037
- References
- 85
- Citations by year
- 2026: 69 · 2025: 64 · 2024: 54 · 2023: 80 · 2022: 72 · 2021: 109 · 2020: 105 · 2019: 89 · 2018: 94 · 2017: 86 · 2016: 72 · 2015: 78 · 2014: 34 · 2013: 27 · 2012: 2
- FWCI
- 2.83
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Trends in Immunology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (R01CA096651, R01CA103320)
- National Institute of Allergy and Infectious Diseases (R01AI103347, R01AI063402, U01AI083005, R01AI075165)
- Topics
- Life Sciences › Neuroscience › Biological Psychiatry › Tryptophan and brain disorders
- Life Sciences › Immunology and Microbiology › Immunology › Immune cells in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Keywords
- indoleamine 2,3-dioxygenase, tryptophan catabolism, immune regulation, inflammation, innate immunity, adaptive immunity, kynurenine pathway, cancer immunotherapy, chronic infection, autoimmune disease, allergic diseases, transplantation
- MeSH terms
- Animals, Communicable Diseases, Humans, Immunity, Innate, Neoplasms, Tryptophan, Indoleamine-Pyrrole 2,3,-Dioxygenase, Adaptive Immunity
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