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Control and expression of cystatin C by mouse decidual cultures
Author(s) -
Afonso Suzanne,
Tovar Chris,
Romagnano Linda,
Babiarz Bruce
Publication year - 2002
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/mrd.1142
Subject(s) - decidua , trophoblast , biology , decidual cells , cystatin , cystatin c , stromal cell , andrology , downregulation and upregulation , cell culture , microbiology and biotechnology , endocrinology , medicine , placenta , fetus , cancer research , biochemistry , gene , pregnancy , genetics , renal function
During mouse embryo implantation, trophoblast invasion is controlled in part by a balance of trophoblast‐derived proteinases and uterine decidual proteinase inhibitors. Our work has focused on cystatin C, the secreted inhibitor of cathepsins B and L. We have previously shown that cystatin C is synthesized by the uterine decidua and localized to the cells in close contact with the trophoblast during implantation in vivo. In the work reported here we have established that decidualizing cultures show a similar upregulation of cystatin C. Using Northern and Western blotting and immunolocalization techniques both cystatin C mRNA and secreted protein increased with the morphological differentiation of stromal or decidual capsule cultures. In an effort to understand the regulation of cystatin C expression, decidual cells were analyzed under various culture conditions. Cystatin C expression was upregulated by increased cell density and by the presence of serum in the media. The growth factors TGF‐β 1 and EGF were found to induce cystatin C to levels comparable to serum stimulation. Co‐culture with ectoplacental cones (EPCs) likewise induced expression and resulted in the localization of cystatin at the decidua:trophoblast interface. This work shows that decidualizing cultures are a good system to study cystatin C expression and that the expression is controlled in part by TGF‐β 1 and EGF signaling. Mol. Reprod. Dev. 61: 155–163, 2002. © 2002 Wiley‐Liss, Inc.