Premium
Molecular characterization of lysyl oxidase‐mediated extracellular matrix remodeling during mouse decidualization
Author(s) -
Li ShuYun,
Yan Jiaqi,
Song Zhuo,
Liu YueFang,
Song MinJie,
Qin JiaWen,
Yang ZengMing,
Liang XiaoHuan
Publication year - 2017
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 - 10.1002/1873-3468.12645
Subject(s) - lysyl oxidase , decidualization , stromal cell , elastin , extracellular matrix , decidual cells , chemistry , microbiology and biotechnology , blastocyst , endocrinology , medicine , embryo , biology , biochemistry , embryogenesis , placenta , pregnancy , fetus , genetics
The establishment of decidualization is a prerequisite of successful pregnancy. Lysyl oxidase (Lox) is a copper‐containing amine oxidase which catalyzes cross‐linking of collagen and elastin in the ECM. Lox is expressed in the subluminal stroma surrounding the implanting blastocyst on day 5 of pregnancy. From days 6 to 8, the signals for Lox mRNA and protein are strongly detected in the decidual cells. The expression of Lox is under the control of estrogen via the GSK‐3β/β‐catenin/c‐myc pathway. Dtprp is decreased by the inhibition of Lox activity. Furthermore, the inhibition of Lox activity decreases stromal cell migration and embryo adhesion. Our findings highlight the crucial role of Lox in endometrial stromal cells and deepen our understanding of decidualization.