Indoleamine 2,3-dioxygenase: distribution and function in the developing human placenta.
Studies in mice have suggested that the placenta is protected from immune rejection by maternal T cells by means of localised indoleamine 2,3-dioxygenase dependent depletion of tryptophan. To determine whether such mechanisms might operate in the human placenta, we have studied the physiological imp...
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
2004
|
| _version_ | 1797069911276650496 |
|---|---|
| author | Kudo, Y Boyd, C Spyropoulou, I Redman, C Takikawa, O Katsuki, T Hara, T Ohama, K Sargent, I |
| author_facet | Kudo, Y Boyd, C Spyropoulou, I Redman, C Takikawa, O Katsuki, T Hara, T Ohama, K Sargent, I |
| author_sort | Kudo, Y |
| collection | OXFORD |
| description | Studies in mice have suggested that the placenta is protected from immune rejection by maternal T cells by means of localised indoleamine 2,3-dioxygenase dependent depletion of tryptophan. To determine whether such mechanisms might operate in the human placenta, we have studied the physiological importance of human placental indoleamine 2,3-dioxygenase immunohistochemically and functionally. Indoleamine 2,3-dioxygenase is detectable immunohistochemically from day 6 human blastocysts and thereafter throughout pregnancy in syncytiotrophoblasts, extravillous cytotrophoblasts and macrophages in the villous stroma and in the fetal membranes. Interferon-gamma added to villous explants markedly stimulates indoleamine 2,3-dioxygenase protein expression in macrophages. Indoleamine 2,3-dioxygenase-mediated tryptophan degradation in the first trimester villous and decidual tissue explants is stimulated by interferon-gamma and inhibited by 1-methyl-tryptophan (an inhibitor of indoleamine 2,3-dioxygenase). Peripheral blood mononuclear cell proliferation is controlled by indoleamine 2,3-dioxygenase-mediated tryptophan degradation. These results suggest the cellular basis of a mechanism present at the human maternal-fetal interface involved in regulating the maternal immune response to conceptus. |
| first_indexed | 2024-03-06T22:31:23Z |
| format | Journal article |
| id | oxford-uuid:5866146b-975f-4ee0-8a7a-fed09c752ea1 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:31:23Z |
| publishDate | 2004 |
| record_format | dspace |
| spelling | oxford-uuid:5866146b-975f-4ee0-8a7a-fed09c752ea12022-03-26T17:03:05ZIndoleamine 2,3-dioxygenase: distribution and function in the developing human placenta.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:5866146b-975f-4ee0-8a7a-fed09c752ea1EnglishSymplectic Elements at Oxford2004Kudo, YBoyd, CSpyropoulou, IRedman, CTakikawa, OKatsuki, THara, TOhama, KSargent, IStudies in mice have suggested that the placenta is protected from immune rejection by maternal T cells by means of localised indoleamine 2,3-dioxygenase dependent depletion of tryptophan. To determine whether such mechanisms might operate in the human placenta, we have studied the physiological importance of human placental indoleamine 2,3-dioxygenase immunohistochemically and functionally. Indoleamine 2,3-dioxygenase is detectable immunohistochemically from day 6 human blastocysts and thereafter throughout pregnancy in syncytiotrophoblasts, extravillous cytotrophoblasts and macrophages in the villous stroma and in the fetal membranes. Interferon-gamma added to villous explants markedly stimulates indoleamine 2,3-dioxygenase protein expression in macrophages. Indoleamine 2,3-dioxygenase-mediated tryptophan degradation in the first trimester villous and decidual tissue explants is stimulated by interferon-gamma and inhibited by 1-methyl-tryptophan (an inhibitor of indoleamine 2,3-dioxygenase). Peripheral blood mononuclear cell proliferation is controlled by indoleamine 2,3-dioxygenase-mediated tryptophan degradation. These results suggest the cellular basis of a mechanism present at the human maternal-fetal interface involved in regulating the maternal immune response to conceptus. |
| spellingShingle | Kudo, Y Boyd, C Spyropoulou, I Redman, C Takikawa, O Katsuki, T Hara, T Ohama, K Sargent, I Indoleamine 2,3-dioxygenase: distribution and function in the developing human placenta. |
| title | Indoleamine 2,3-dioxygenase: distribution and function in the developing human placenta. |
| title_full | Indoleamine 2,3-dioxygenase: distribution and function in the developing human placenta. |
| title_fullStr | Indoleamine 2,3-dioxygenase: distribution and function in the developing human placenta. |
| title_full_unstemmed | Indoleamine 2,3-dioxygenase: distribution and function in the developing human placenta. |
| title_short | Indoleamine 2,3-dioxygenase: distribution and function in the developing human placenta. |
| title_sort | indoleamine 2 3 dioxygenase distribution and function in the developing human placenta |
| work_keys_str_mv | AT kudoy indoleamine23dioxygenasedistributionandfunctioninthedevelopinghumanplacenta AT boydc indoleamine23dioxygenasedistributionandfunctioninthedevelopinghumanplacenta AT spyropouloui indoleamine23dioxygenasedistributionandfunctioninthedevelopinghumanplacenta AT redmanc indoleamine23dioxygenasedistributionandfunctioninthedevelopinghumanplacenta AT takikawao indoleamine23dioxygenasedistributionandfunctioninthedevelopinghumanplacenta AT katsukit indoleamine23dioxygenasedistributionandfunctioninthedevelopinghumanplacenta AT harat indoleamine23dioxygenasedistributionandfunctioninthedevelopinghumanplacenta AT ohamak indoleamine23dioxygenasedistributionandfunctioninthedevelopinghumanplacenta AT sargenti indoleamine23dioxygenasedistributionandfunctioninthedevelopinghumanplacenta |