期刊
AUTOIMMUNITY REVIEWS
卷 18, 期 4, 页码 334-348出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.autrev.2019.02.004
关键词
Arginase 1; Arginine metabolism; Host genetics; Indoleamine 2,3-dioxygenase 1; Immune regulation; Tryptophan metabolism
类别
资金
- European Research Council [338954-DIDO, 780807-DIDO-MS]
- Italian Ministry of Education, Universities, and Research [PRIN2015-20155C2PP7]
- Northern Portugal Regional Operational Programme (NORTE 2020), under the Portugal 2020 Partnership Agreement, through the European Regional Development Fund (FEDER) [NORTE-01-0145-FEDER-000013]
- Fundacao para a Ciencia e Tecnologia (FCT) [IF/00735/2014]
In mammals, amino acid metabolism has evolved to control immune responses. Autoimmune diseases are heterogeneous conditions that involve the breakdown of tolerogenic circuitries and consequent activation of autoreactive immune cells. Therefore, critical enzymes along amino acid degradative pathways may be hijacked to keep in check autoimmunity. We examined here current knowledge of indoleamine 2,3-dioxygenase 1 (IDO1) and arginase 1 (ARG1), the main enzymes catabolizing tryptophan and arginine, respectively, in organ-specific and systemic autoimmune diseases as well as in the development of autoantibodies to therapeutic proteins. At variance with neoplastic contexts, in which it is known to act as a pure immunosuppressive molecule, ARG1 exhibited a protective or pathogenetic profile, depending on the disease. In contrast, in several autoimmune conditions, the bulk of data indicated that drugs capable of potentiating IDO1 expression and activity may represent valuable therapeutic tools and that IDO1-based immunotherapeutic protocols could be more effective if tailored to the genetic profile of individual patients.
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