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Steel factor enhances integrin-mediated tyrosine phosphorylation of focal
adhesion kinase (pp125FAK) and paxillin
H Takahira, A Gotoh, A Ritchie and HE Broxmeyer
Department of Medicine (Hematology/Oncology), Indiana University School of
Medicine, Indianapolis 46202-5121, USA.
Integrin-mediated interaction of hematopoietic progenitor cells with bone
marrow stromal extracellular matrix components is important in
hematopoiesis. Focal adhesion kinase (pp125FAK) plays a central role in
signal transduction through integrin receptors. We studied matrix- integrin
interaction and subsequent signaling in human growth factor- dependent cell
line, TF-1. Adherence of unstimulated TF-1 cells to fibronectin-coated
wells was blocked by antiintegrin beta 1 and combination of anti-alpha 4
with anti-alpha 5 antibodies, indicating alpha 4 beta 1 and alpha 5 beta 1
integrin mediated adherence. Steel factor (SLF) increased TF-1 adhesion to
fibronectin dose-dependently and 10(-7) mol/L wortmannin suppressed
SLF-induced adhesion. Immunoprecipitation and immunoblotting with
antiphosphotyrosine antibody showed that adherence of TF-1 cells to
fibronectin without cytokine caused tyrosine phosphorylation of several
proteins identified as pp125FAK and paxillin. SLF induced spreading of
adherent TF-1 cells and enhanced tyrosine phosphorylation of pp125FAK and
paxillin in a dose-dependent manner. Treatment with SLF without plating on
fibronectin did not induce tyrosine phosphorylation of pp125FAK.
Wortmannin, at 10(-7) mol/L, completely abolished SLF-induced enhancement
of pp125FAK tyrosine phosphorylation, while c-kit autophosphorylation was
not affected. This suggests that increase of pp125FAK tyrosine
phosphorylation was mediated through a wortmannin sensitive pathway, rather
than by direct action on c-kit tyrosine kinase. Treatment of adherent TF-1
cells with RGDS peptide plus anti- alpha 4 antibody also inhibited
SLF-induced enhancement of pp125FAK tyrosine phosphorylation without
detachment of TF-1 cells. These data suggest that SLF enhances
integrin-fibronectin-dependent tyrosine phosphorylation of pp125FAK through
activation of integrin ("inside- out" signaling) and following integrin
occupancy. This establishes a novel linkage between c-kit/SLF pathway and
integrin fibronectin signaling.
Volume 89,
Issue 5,
pp. 1574-1584,
03/01/1997
Copyright © 1997 by The American Society of Hematology
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