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Linking Two Immuno-Suppressive Molecules: Indoleamine 2,3 Dioxygenase Can Modify HLA-G Cell-Surface Expression1
Authors: Gonzalez-Hernandez, A. (Álvaro)
LeMaoult, J. (Joël)
Lopez, A. (Ana)
Alegre, E. (Estíbaliz)
Caumartin, J. (Julien)
Le-Rond, S. (Solene)
Daouya, M. (Marina)
Moreau, P. (Philippe)
Carosella, E.D. (Edgardo D.)
Keywords: Embryo
Issue Date: 2005
Publisher: Society for the Study of Reproduction
Publisher version:
ISSN: 0006-3363
Citation: Gonzalez-Hernandez A, LeMaoult J, Lopez A, Alegre E, Caumartin J, Le Rond S, et al. Linking two immuno-suppressive molecules: indoleamine 2,3 dioxygenase can modify HLA-G cell-surface expression. Biol Reprod 2005 Sep;73(3):571-578.
Nonclassical human leukocyte antigen (HLA) class I molecule HLA-G and indoleamine 2,3 dioxygenase (INDO) in humans and mice, respectively, have been shown to play crucial immunosuppressive roles in fetal-maternal tolerance. HLA-G inhibits natural killer and T cell function by high-affinity interaction with inhibitory receptors, and INDO acts by depleting the surrounding microenvironment of the essential amino acid tryptophan, thus inhibiting T cell proliferation. We investigated whether HLA-G expression and INDO function were linked. Working with antigen-presenting cell (APC) lines and monocytes, we found that functional inhibition of INDO by 1-methyl-tryptophan induced cell surface expression of HLA-G1 by HLA-G1- negative APCs that were originally cell-surface negative, and that in reverse, the functional boost of INDO by high concentrations of tryptophan induced a complete loss of HLA-G1 cell surface expression by APCs that were originally cell-surface HLA-G1-positive. This mechanism was shown to be posttranslational because HLA-G protein cell contents remained unaffected by the treatments used. Furthermore, HLA-G cell surface expression regulation by INDO seems to relate to INDO function, but not to tryptophan catabolism itself. Potential
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