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Crystallin αB acts as a molecular guard in mouse decidualization: Regulation and function during early pregnancy
Author(s) -
Zuo Ru-Juan,
Zhao Yue-Chao,
Lei Wei,
Wang Tong-Song,
Wang Bao-Cheng,
Yang Zeng-Ming
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.05.045
Subject(s) - decidualization , decidua , stromal cell , decidual cells , microbiology and biotechnology , p38 mitogen activated protein kinases , gene knockdown , heat shock protein , oxidative stress , mapk/erk pathway , biology , chemistry , apoptosis , medicine , pregnancy , endocrinology , phosphorylation , cancer research , fetus , gene , placenta , biochemistry , genetics
Although decidualization is crucial for the establishment of successful pregnancy, the molecular mechanism underlying decidualization remains poorly understood. Crystallin αB (CryAB), a small heat shock protein (sHSP), is up‐regulated and phosphorylated in mouse decidua. In mouse primary endometrial stromal cells, CryAB is induced upon progesterone treatment via HIF1α. In addition, CryAB is strongly phosphorylated through the p38‐MAPK pathway under stress or during in vitro decidualization. Knockdown of CryAB results in the increase of apoptosis of stromal cells and inhibits decidualization under oxidative or inflammatory stress. Our data indicate that CryAB protects decidualization against stress conditions.