The glycosaminoglycan-binding domain of decoy receptor 3 is essential for induction of monocyte adhesion.

摘要: Decoy receptor 3 (DcR3), a soluble for Fas ligand, LIGHT (homologous to lymphotoxins shows inducible expression and competes with HSV glycoprotein D herpes virus entry mediator, expressed by T lymphocytes), TNF-like molecule 1A, is highly in cancer cells tissues affected autoimmune disease. DcR3.Fc has been shown stimulate cell adhesion modulate activation differentiation triggering multiple signaling cascades that are independent of its three known ligands. In this study we found DcR3.Fc-induced was inhibited heparin heparan sulfate, unable bind Chinese hamster ovary K1 mutants defective glycosaminoglycan (GAG) synthesis. Furthermore, the negatively charged, sulfated GAGs surface proteoglycans, but not their core proteins, were identified as binding sites DcR3.Fc. A potential GAG-binding site C-terminal region DcR3, mutation basic residues, i.e., K256, R258, R259, alanines abolished ability trigger adhesion. Moreover, fusion protein comprising DcR3 an Fc fragment (DcR3_HBD.Fc) same effect activating kinase C inducing Compared wild-type THP-1 cells, induced significantly reduced both CD44v3 syndecan-2 knockdown cells. Therefore, propose model which may cross-link proteoglycans induce monocyte