Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Tryptophan and kynurenine stimulate human decidualization via activating Aryl hydrocarbon receptor : Short title: Kynurenine action on human decidualization

Wang, Peng Chao ; Chen, Si Ting ; Hong, Zhi Kai ; Li, Shu Yun ; Yang, Zhen Shan LU orcid ; Quan, Song and Yang, Zeng Ming (2020) In Reproductive Toxicology 96. p.282-292
Abstract

Decidualization is essential for successful pregnancy in rodents and primates. Although L-Tryptophan and its metabolites are essential for mammalian pregnancy, the underlying mechanism is poorly defined. We explored effects of tryptophan and kynurenine on human in vitro decidualization in human endometrial stromal cell line and primary endometrial stromal cells. Tryptophan significantly stimulates the expression of prolactin and insulin growth factor binding protein 1, reliable markers for human decidualization. When stromal cells are treated with tryptophan, tryptophan hydroxylase-1 remains unchanged, but indoleamine 2,3-dioxygenase 1 is significantly increased, suggesting tryptophan is mainly metabolized through kynurenine pathway.... (More)

Decidualization is essential for successful pregnancy in rodents and primates. Although L-Tryptophan and its metabolites are essential for mammalian pregnancy, the underlying mechanism is poorly defined. We explored effects of tryptophan and kynurenine on human in vitro decidualization in human endometrial stromal cell line and primary endometrial stromal cells. Tryptophan significantly stimulates the expression of prolactin and insulin growth factor binding protein 1, reliable markers for human decidualization. When stromal cells are treated with tryptophan, tryptophan hydroxylase-1 remains unchanged, but indoleamine 2,3-dioxygenase 1 is significantly increased, suggesting tryptophan is mainly metabolized through kynurenine pathway. Kynurenine significantly stimulates insulin growth factor binding protein 1 expression. Aryl hydrocarbon receptor and its target genes (P450 1A1 and P450 1B1) are significantly increased by tryptophan and kynurenine. The induction of tryptophan and kynurenine on insulin growth factor binding protein 1 is abrogated by CH223191, an aryl hydrocarbon receptor inhibitor. Cytochrome P450 1A1 and P450 1B1 catalyze the oxidative metabolism of estradiol to catechol estrogens (2-hydroxy estradiol and 4-hydroxy estradiol), respectively. Insulin growth factor binding protein 1 is up-regulated by 2-hydroxy estradiol and 4-hydroxy estradiol. Interferon-γ significantly induces the expression of indoleamine 2,3-dioxygenase 1, aryl hydrocarbon receptor and insulin growth factor binding protein 1. All the data are also verified in primary human stromal cells. Our data indicate that Interferon-γ-induced kynurenine pathway promotes human decidualization via aryl hydrocarbon receptor signaling.

(Less)
Please use this url to cite or link to this publication:
author
; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
keywords
AHR, Decidualization, IFNγ, IGFBP1, Kynurenine, L-Tryptophan
in
Reproductive Toxicology
volume
96
pages
282 - 292
publisher
Elsevier
external identifiers
  • scopus:85089515858
  • pmid:32781018
ISSN
0890-6238
DOI
10.1016/j.reprotox.2020.07.011
language
English
LU publication?
no
additional info
Funding Information: This work was supported by National Key Research and Development Program of China ( 2018YFC1004403 ) and National Natural Science Foundation of China ( 31871511 and 31671563 ). Publisher Copyright: © 2020 The Author(s)
id
a11b2c32-ea9b-45df-b1ab-edea850a67a2
date added to LUP
2024-02-28 14:55:21
date last changed
2024-06-09 21:44:20
@article{a11b2c32-ea9b-45df-b1ab-edea850a67a2,
  abstract     = {{<p>Decidualization is essential for successful pregnancy in rodents and primates. Although L-Tryptophan and its metabolites are essential for mammalian pregnancy, the underlying mechanism is poorly defined. We explored effects of tryptophan and kynurenine on human in vitro decidualization in human endometrial stromal cell line and primary endometrial stromal cells. Tryptophan significantly stimulates the expression of prolactin and insulin growth factor binding protein 1, reliable markers for human decidualization. When stromal cells are treated with tryptophan, tryptophan hydroxylase-1 remains unchanged, but indoleamine 2,3-dioxygenase 1 is significantly increased, suggesting tryptophan is mainly metabolized through kynurenine pathway. Kynurenine significantly stimulates insulin growth factor binding protein 1 expression. Aryl hydrocarbon receptor and its target genes (P450 1A1 and P450 1B1) are significantly increased by tryptophan and kynurenine. The induction of tryptophan and kynurenine on insulin growth factor binding protein 1 is abrogated by CH223191, an aryl hydrocarbon receptor inhibitor. Cytochrome P450 1A1 and P450 1B1 catalyze the oxidative metabolism of estradiol to catechol estrogens (2-hydroxy estradiol and 4-hydroxy estradiol), respectively. Insulin growth factor binding protein 1 is up-regulated by 2-hydroxy estradiol and 4-hydroxy estradiol. Interferon-γ significantly induces the expression of indoleamine 2,3-dioxygenase 1, aryl hydrocarbon receptor and insulin growth factor binding protein 1. All the data are also verified in primary human stromal cells. Our data indicate that Interferon-γ-induced kynurenine pathway promotes human decidualization via aryl hydrocarbon receptor signaling.</p>}},
  author       = {{Wang, Peng Chao and Chen, Si Ting and Hong, Zhi Kai and Li, Shu Yun and Yang, Zhen Shan and Quan, Song and Yang, Zeng Ming}},
  issn         = {{0890-6238}},
  keywords     = {{AHR; Decidualization; IFNγ; IGFBP1; Kynurenine; L-Tryptophan}},
  language     = {{eng}},
  pages        = {{282--292}},
  publisher    = {{Elsevier}},
  series       = {{Reproductive Toxicology}},
  title        = {{Tryptophan and kynurenine stimulate human decidualization via activating Aryl hydrocarbon receptor : Short title: Kynurenine action on human decidualization}},
  url          = {{http://dx.doi.org/10.1016/j.reprotox.2020.07.011}},
  doi          = {{10.1016/j.reprotox.2020.07.011}},
  volume       = {{96}},
  year         = {{2020}},
}