Journal Article Review Research Support, Non-U.S. Gov't Epublish 3 citations
PubMed: 39120289 DOI: 10.3390/cells13151259
Kynurenines as a Novel Target for the Treatment of Inflammatory Disorders.
Cells 13(15)
Authors: Adrian Mor, Anna Tankiewicz-Kwedlo, Marianna Ciwun, Janina Lewkowicz, Dariusz Pawlak
Affiliations
- Department of Pharmacodynamics, Medical University of Bialystok, A. Mickiewicza 2C, 15-222 Bialystok, Poland.
- Department of Internal Medicine and Metabolic Diseases, Medical University of Bialystok, M. Sklodowskiej-Curie 24A, 15-276 Bialystok, Poland.
Abstract
This review discusses the potential of targeting the kynurenine pathway (KP) in the treatment of inflammatory diseases. The KP, responsible for the catabolism of the amino acid tryptophan (TRP), produces metabolites that regulate various physiological processes, including inflammation, cell cycle, and neurotransmission. These metabolites, although necessary to maintain immune balance, may accumulate excessively during inflammation, leading to systemic disorders. Key KP enzymes such as indoleamine 2,3-dioxygenase 1 (IDO1), indoleamine 2,3-dioxygenase 2 (IDO2), tryptophan 2,3-dioxygenase (TDO), and kynurenine 3-monooxygenase (KMO) have been considered promising therapeutic targets. It was highlighted that both inhibition and activation of these enzymes may be beneficial, depending on the specific inflammatory disorder. Several inflammatory conditions, including autoimmune diseases, for which modulation of KP activity holds therapeutic promise, have been described in detail. Preclinical studies suggest that this modulation may be an effective treatment strategy for diseases for which treatment options are currently limited. Taken together, this review highlights the importance of further research on the clinical application of KP enzyme modulation in the development of new therapeutic strategies for inflammatory diseases.
MeSH
Cells, Dioxygenases, Tryptophan, Kynurenine, Kynurenine 3-Monooxygenase, Enzymes, Therapeutics, Immunosuppression Therapy, Tryptophan Oxygenase, Indoleamine-Pyrrole 2,3,-Dioxygenase
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