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Blood, Vol. 95 No. 8 (April 15), 2000:
pp. 2505-2513
Stromal cell-derived factor-1 stimulates tyrosine
phosphorylation of multiple focal adhesion proteins and induces
migration of hematopoietic progenitor cells: roles of
phosphoinositide-3 kinase and protein kinase C
Jian-Feng Wang,
In-Woo Park, and
Jerome E. Groopman
From the Divisions of Experimental Medicine and Hematology/Oncology,
Beth Israel Deaconess Medical Center, Harvard Medical School, Boston,
MA.
The stromal cell-derived factor-1 (SDF-1) is an alpha chemokine that
binds to the CXCR4 receptor. Knock-out studies in mice demonstrate that
this ligand-receptor pair is essential in hematopoiesis. One function
of SDF-1 appears to be the regulation of migration of hematopoietic
progenitor cells. We previously characterized signal transduction
pathways induced by SDF-1 in human hematopoietic progenitors and
found tyrosine phosphorylation of focal adhesion components, including
the related adhesion focal tyrosine kinase (RAFTK), the adaptor
molecule p130 Cas, and the cytoskeletal protein paxillin. To better
understand the functional role of signaling molecules connecting the
CXCR4 receptor to the process of hematopoietic migration, we studied
SDF-1-mediated pathways in a model hematopoietic progenitor cell
line (CTS), as well as in primary human bone marrow CD34+
cells. We observed that several other focal adhesion components, including focal adhesion kinase (FAK) and the adaptor molecules Crk and
Crk-L, are phosphorylated on SDF-1 stimulation. Using a series of
specific small molecule inhibitors, both protein kinase C (PKC) and
phosphoinositide-3 kinase (PI-3K) appeared to be required for
SDF-1-mediated phosphorylation of focal adhesion proteins and the
migration of both CTS and primary marrow CD34+ cells,
whereas the mitogen-activated protein kinases ERK-1 and -2 were not.
These studies further delineate the molecular pathways mediating
hematopoietic progenitor migration and response to an essential
chemokine, SDF-1.
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