Interferons and indoleamine 2,3-dioxygenase: role in antimicrobial and antitumor effects.
Indoleamine 2,3-dioxygenase (IDO) is an interferon (IFN)-induced protein that initiates the metabolism of tryptophan along the kynurenine pathway. Although IDO can be induced by IFN-gamma in many cell types, only mononuclear phagocytes have been shown to be induced to decyclize tryptophan by all three IFN classes. Since tryptophan is an essential amino acid necessary for a variety of metabolic processes, depletion of available tryptophan may be an important mechanism for control of rapidly-dividing microbial pathogens and tumors. The purpose of this review is to present evidence that documents the effects of IFN-induced IDO on prokaryotic and eukaryotic pathogens, as well as on a variety of tumor cell lines.
Carlin
J M
JM
Department of Medical Microbiology, University of Wisconsin Medical School, Madison 53706.
Ozaki
Y
Y
Byrne
G I
GI
Brown
R R
RR
Borden
E C
EC
D000818:Animals; D001770:Blood Bactericidal Activity; D002453:Cell Cycle; D006801:Humans; D066298:In Vitro Techniques; D050503:Indoleamine-Pyrrole 2,3,-Dioxygenase; D007372:Interferons / Q000097:blood / Q000502:physiology*; D007963:Leukocytes, Mononuclear / Q000502:physiology; D009374:Neoplasms, Experimental / Q000473:pathology; D010105:Oxygenases / Q000097:blood / Q000502:physiology*; D014122:Toxoplasma / Q000276:immunology; D014364:Tryptophan / Q000378:metabolism; D014366:Tryptophan Oxygenase
D050503:Indoleamine-Pyrrole 2,3,-Dioxygenase; D014364:Tryptophan; D007372:Interferons; D010105:Oxygenases; D014366:Tryptophan Oxygenase