4.6 Article

Molecules in focus: Indoleamine 2,3-dioxygenase

Journal

INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
Volume 39, Issue 12, Pages 2167-2172

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.biocel.2007.01.004

Keywords

indoleamine 2,3-dioxygenase; L-tryptophan; interferon gamma; immune response; dendritic cells

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Indoleamine 2,3-dioxygenase (IDO) is a heme enzyme that initiates the oxidative degradation of the least abundant, essential amino acid, L-tryptophan, along the kynurenine pathway. The local cellular depletion Of L-tryptophan that results may enable the host to inhibit the growth of various infectious pathogens in vivo. However, over the past decade, it has become increasingly apparent that IDO also represents an important immune control enzyme. Thus, cells expressing IDO, seemingly paradoxically, are capable of suppressing local T cell responses to promote immune tolerance under various physiological and pathophysiological conditions of medical importance, including infectious diseases, foetal rejection, organ transplantation, neuropathology, inflammatory and auto-immune disorders and cancer. In this review, we briefly outline the biochemical properties of IDO, its known and hypothetical functions and the medical implications for inhibition or induction of IDO and/or its downstream catabolites in health and disease. (C) 2007 Elsevier Ltd. All rights reserved.

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