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Ephrin‐B3 Binds Specifically to B Lymphocytes in Blood and Induces Migration
Author(s) -
Holen H. L.,
Zernichow L.,
Fjelland K. E.,
Evenroed I. M.,
Tveit H.,
Aasheim H.C.
Publication year - 2011
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.2011.02563.x
Subject(s) - ephrin , erythropoietin producing hepatocellular (eph) receptor , receptor , biology , binding site , eph receptor a2 , microbiology and biotechnology , chemistry , biochemistry , receptor tyrosine kinase
Eph receptors and ephrin ligands have been shown to be differentially expressed on leucocytes. Here, we show that one member of the ephrin‐B subfamily of ephrins, ephrin‐B3, specifically binds to B lymphocytes in blood. No binding was observed to T lymphocytes or monocytes. The ephrin‐B3 binding receptor on B lymphocytes is so far not identified, but our results here indicate that ephrin‐B3 binds to a protein not belonging to the Eph receptor family. Recently, we have shown that ephrin‐B3 binds to a sulphated cell surface receptor on HEK293T cells and that this binding can be blocked with heparin. Ephrin‐B3 binding to B lymphocytes is partially affected by heparin, and a basic amino acid in the extracellular juxtamembrane region, Arg‐188, is here shown to be involved in this binding. The functional consequence of ephrin‐B3 binding to B lymphocytes is induced migration, in particular of the memory cells. To conclude, ephrin‐B3 binds to B lymphocytes, most likely via a non‐classical receptor, and induces migration of the memory B cell subpopulation.