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Ephrin‐B2 is a candidate ligand for the Eph receptor, EphB6
Author(s) -
Munthe Else,
Rian Edith,
Holien Toril,
Rasmussen Anne-Marie,
Levy Finn Olav,
Aasheim Hans-Christian
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01793-7
Subject(s) - erythropoietin producing hepatocellular (eph) receptor , ephrin , ligand (biochemistry) , eph receptor a2 , receptor , chemistry , microbiology and biotechnology , receptor tyrosine kinase , biology , biochemistry
No ligand has hitherto been designated for the Eph receptor tyrosine kinase family member, EphB6. Here, expression of an EphB6 ligand in the pro‐B leukemic cell line, Reh, is demonstrated by binding of soluble EphB6‐Fc fusion protein to the Reh cells. The ligand belongs to the subgroup of membrane spanning ligands, as suggested by the fact that phosphatidylinositol‐specific phospholipase C treatment did not abrogate binding of EphB6‐Fc. Two transmembrane Eph receptor ligands, ephrin‐B1 and ephrin‐B2, were identified in Reh cells. Analysis of EphB6‐Fc fusion protein binding to ephrin‐B1 or ephrin‐B2 transfected COS cells revealed a high‐affinity saturable binding between EphB6‐Fc and ephrin‐B2, but not with ephrin‐B1. In mice, EphB6 has previously been shown to be expressed in thymus. Here, we show expression of EphB6 in human thymus, as well as the expression of ephrin‐B2 in both human and mouse thymus. We conclude that ephrin‐B2 may be a physiological ligand for the EphB6 receptor.