Abstract
The lymphocyte integrin α4β7is a cell surface adhesion receptor involved in initiating lymphocyte homing to gut-associated/mucosal lymphoid tissues by binding the mucosal addressin cell adhesion molecule-1 (MAdCAM-1). Other known ligands are vascular cell adhesion molecule-1, fibronectin, and the α4integrin chain itself. Here, we demonstrate that stimulation of the α4β7integrin through its α4subunit (mAb R1-2), β7subunit (mAb M293), or the combinatory epitope (mAb DATK32) enhances tyrosine phosphorylation of several cellular proteins in the murine TK1 lymphoma cell line. The two src-kinases p56lck and p59fyn were identified as possible mediators and substrates of the detected tyrosine phosphorylation. Furthermore, we observed activation of the MAP-kinases ERK1/2.
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