Trophinin-mediated cell adhesion induces apoptosis of human endometrial epithelial cells through PKC-δ.

Trophinin is an intrinsic membrane protein expressed in trophectoderm cells of embryos and in uterine epithelial cells. Trophinin potentially mediates apical cell adhesion at human embryo implantation sites through trophinin-trophinin binding in these two cell types. Trophinin-mediated cell adhesion activates trophectoderm cells for invasion, whereas the effect of adhesion on maternal side is not known. We show that addition of peptide, a previously established peptide that mimics trophinin-mediated cell adhesion, to human endometrial epithelial cells expressing trophinin induces their apoptosis. FAS involvement was excluded, as GWduanyu1745 did not bind to FAS, and FAS knockdown did not alter apoptosis. Immunoblotting analyses of protein kinases revealed an elevation of protein in endometrial epithelial cells. In the absence of duanyu1531-d associated with trophinin and remained cytoplasmic, but after GWduanyu1745 binding to the trophinin extracellular domain, duanyu1531-d became tyrosine phosphorylated, dissociated from trophinin, and entered the nucleus. In duanyu1531-d knockdown endometrial cells, GWduanyu1745 did not induce apoptosis.

KEYWORDS: {{ getKeywords(articleDetailText.words) }}