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Appropriately glcosylated beta1‐integrin serves as an E‐selectin ligand
Author(s) -
Lin Regina Junhui,
Chong SiewMeng,
Lim YawChyn
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.lb329
Subject(s) - selectin , extravasation , integrin , chemistry , cell adhesion molecule , e selectin , cd44 , p selectin , microbiology and biotechnology , cell adhesion , sialyl lewis x , ligand (biochemistry) , l selectin , biochemistry , cell , immunology , biology , receptor , platelet , platelet activation
The interactions between selectins and their ligands are important for the extravasation of leukocytes into target tissues. Aim To identify adhesion molecules that mediate E‐ and P‐selectin interactions under defined flow conditions. Methods The interactions of NB‐DLB‐1 cells (a lymphoma cell line) with E‐ or P‐selectin were examined in parallel plate flow chamber studies. Putative selectin ligands were identified by function blocking assays, affinity capture and Western blot. Results NB‐DLB‐1 cells interact with E‐ and P‐selectin in a shear‐dependent manner under defined flow conditions. Function blocking assays identify PSGL‐1 and CD44 as the major P‐selectin ligands; and L‐selectin and beta1‐integrin as the E‐selectin ligands. Affinity capture using E‐selectin/IgG reveals that the E‐selectin‐binding beta1‐integrin is of the high molecular weight glycoform(s). Conclusion NB‐DLB‐1 cells interactions with E‐ and P‐selectin are mediated by different adhesion molecules. Our data show that L‐selectin and the extensively‐glycosylated form(s) of beta1‐integrin are E‐selectin ligands on NB‐DLB‐1 cells. This novel function of beta1‐integrin implies that in addition to the classical VLA‐4‐VCAM‐1 interactions, appropriately glycosylated beta1‐integrin can bind to E‐selectin. Study funded by ARF, NUS and NMRC, Singapore.