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- W2040408554 abstract "Glycodelin A (GdA) is one of the progesterone inducible endometrial factors that protect the fetal semi-allograft from maternal immune rejection. The immunoregulatory effects of GdA are varied, with diverse effects on the fate and function of most immune cell types. Its effects on T cells are particularly relevant as it is capable of regulating T cell activation, differentiation, as well as apoptosis. We have previously reported that GdA triggers mitochondrial stress and apoptosis in activated T cells by a mechanism that is distinct and independent of its effects on T cell activation. In this study we describe the characterization of a cell surface receptor for GdA on T cells. Our results reveal a novel calcium-independent galactose-binding lectin activity of GdA, which is responsible for its apoptogenic function. This discovery adds GdA to a select group of soluble immunoregulatory lectins that operate within the feto-placental compartment, the only other members being the galectin family proteins. We also report for the first time that both CD4+ and CD8+ T cell subsets are equally susceptible to inhibition with GdA, mediated by its novel lectin activity. We demonstrate that GdA selectively recognizes complex-type N-linked glycans on T cell surface glycoproteins, and propose that the galectin-1 glycoprotein receptor CD7 maybe a novel target for GdA on T cells. This study, for the first time, links the lectin activity of GdA to its biological function." @default.
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- W2040408554 date "1996-10-01" @default.
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- W2040408554 title "Interaction between the Extracellular Domain of CD7 and Concanavalin A: A Clue to the Identity of the Ligand for CD7" @default.
- W2040408554 doi "https://doi.org/10.1006/cimm.1996.0247" @default.
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