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J Biol Chem, Vol. 273, Issue 36, 23169-23175, September 4, 1998
-Chemokine, Stromal Cell-derived Factor-1, Binds to the
Transmembrane G-protein-coupled CXCR-4 Receptor and Activates
Multiple Signal Transduction Pathways
,, and
From the Divisions of Experimental Medicine, and
Hematology/Oncology, Beth Israel Deaconess Medical Center, Harvard
Medical School, Boston, Massachusetts 02215 and
The LeukoSite, Inc., Cambridge, Massachusetts 02142
-chemokine stromal cell-derived factor
(SDF)-1 binds to the seven transmembrane G-protein-coupled CXCR-4
receptor and acts to modulate cell migration and proliferation. The
signaling pathways that mediate the effects of SDF-1 are not well
characterized. We studied events following SDF-1 binding to CXCR-4
in a model murine pre-B cell line transfected with human CXCR-4. There
was enhanced tyrosine phosphorylation and association of components of
focal adhesion complexes such as the related adhesion focal tyrosine
kinase, paxillin, and Crk. We also observed activation of
phosphatidylinositol 3-kinase. Wortmannin, a selective inhibitor of
phosphatidylinositol 3-kinase, partially inhibited the SDF-1-induced migration and tyrosine phosphorylation of paxillin. SDF-1 treatment selectively activated p44/42 mitogen-activated protein kinase (Erk 1 and Erk 2) and its upstream kinase mitogen-activated protein kinase
kinase but not p38 mitogen-activated protein kinase, c-Jun amino-terminal kinase or mitogen activated protein kinase kinase. We
also observed that SDF-1 treatment increased NF-
B activity in
nuclear extracts from the CXCR-4 transfectants. Taken together, these
studies revealed that SDF-1 activates distinct signaling pathways
that may mediate cell growth, migration, and transcriptional activation.
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