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Stimulation of tyrosine phosphorylation after ligation of beta7 and beta1
integrins on human B cells
SN Manie, A Astier, D Wang, JS Phifer, J Chen, AI Lazarovits, C Morimoto and AS Freedman
Department of Medicine, Harvard Medical School, Boston, MA, USA.
B lymphocytes express several members of the integrin family of adhesion
molecules that mediate cell-cell and cell-extracellular matrix
interactions. In addition to beta1 integrins, predominantly alpha4 beta1,
mature B cells also express alpha4 beta7, which is a receptor for vascular
cell adhesion molecule-1 and fibronectin, and is also involved in the
homing of B cells to mucosal sites through binding to a third ligand,
mucosal address in cell adhesion molecule-1. Here we describe that
crosslinking of alpha4 beta7 integrins on B cell lines and normal tonsillar
B cells, induces tyrosine phosphorylation of multiple substrates of 105-130
kD, indicating that beta7 integrin plays a role as signaling molecule in B
cells. This pattern of phosphorylated proteins was very similar to that
induced following ligation of alpha4 beta1. Interestingly, ligation of
alpha5 beta1 or alpha6 beta1 also stimulated the 105-125 kD group of
phosphorylated proteins, whereas ligation of beta2 integrins did not. The
focal adhesion tyrosine kinase p125FAK was identified as one of these
substrates. Beta1 or beta7 mediated tyrosine phosphorylations were markedly
decreased when the microfilament assembly was inhibited by cytochalasin B.
These results suggest that intracellular signals initiated by different
integrins in B cells may converge, to similar cytoskeleton-dependent
tyrosine phosphorylated proteins.
Volume 87,
Issue 5,
pp. 1855-1861,
03/01/1996
Copyright © 1996 by The American Society of Hematology
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