پديد آورندگان :
Forouzandeh Farshad نويسنده , Bahar Mohammad Ali نويسنده , Ghahary Aziz نويسنده , Jalili Reza B. نويسنده
چكيده لاتين :
Indolemine 2, :,)-dioxygenase (IDO) is a cytosolic monomeric hemoprotein enzyme that
catalyses tryptophan, the least available essential amino acid in the human body, to Nformylkynurenine,
which in turn rapidly degrades to give kynurenine. IDO is expressed in
different tissues, especially and prominently in some subsets of antigen presenting cells
(APes) of lymphoid organs and also in the placenta of human and other mammals.
Expression of IDO by certain dendritic cells, monocvtes and macrophages has a regulatory
effect on T cells probably by providing a tryptophan-deficient microenvironment and/or
accumulation of toxic metabolites of tryptophan. This immunomodulatory function of IDO
plays an essential role in different physiological and pathological states, IDO was shown to
prevent rejection of the fetus during pregnancy, possibly by inhibiting alloreactive T cells.
Moreover, IDO expression in APes was suggested to control autoreactive immune
responses. In this review we discuss the molecular and biological characteristics of IDO and
its function in immune system as well as the potential application of this enzyme in
improving the outcome of allogeneic transplantation as a local immunosuppressive factor.