Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UMLS:C0001511 (
Adhesion
)
5,955
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The vascular endothelium is a crucial interface that controls the recruitment of circulating leukocytes. Based on the luminal expression of the
ephrin-B2
ligand by endothelial cells (ECs) and the expression of EphB receptors (EphBRs) by circulating monocytes, we hypothesized that EphBR-ephrinB interactions are involved in monocyte adhesion.
Adhesion
experiments with monocytic cells were performed on ECs that overexpressed either full-length
ephrin-B2
or cytoplasmically truncated
ephrin-B2
(DeltaC-
ephrin-B2
). Atomic force microscopy confirmed similar adhesive strengths of EphBR-expressing J774 cells to ECs that either overexpressed full-length
ephrin-B2
or truncated DeltaC-
ephrin-B2
(1-minute interaction). Yet, adhesion experiments under static or flow conditions for 30 minutes demonstrated the preferential adhesion of monocytic cells to ECs that overexpressed full-length
ephrin-B2
but not to DeltaC-
ephrin-B2
or to ECs that had been mock transduced.
Adhesion
was blocked by
ephrin-B2
-specific and EphBR-specific antibodies. Correspondingly, adhesion of EphB4-receptor-overexpressing monocytes to
ephrin-B2
-positive ECs was further augmented. Trafficking experiments of cell-surface molecules revealed that, prior to internalization, the resulting EphB4-receptor-
ephrin-B2
complex translocated from the luminal surface to inter-endothelial junctions. Lastly, full-length
ephrin-B2
in ECs was also involved in monocyte transmigration. Collectively, our study identifies a role of EphBR-ephrinB interactions as a new step in the cascade of events leading to monocyte adhesion and transmigration through the vascular endothelium.
...
PMID:Involvement of endothelial ephrin-B2 in adhesion and transmigration of EphB-receptor-expressing monocytes. 1895 13