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(Received for publication, April 30, 1996, and in revised form, August 7, 1996)
From the Platelet-derived growth factor (PDGF)-BB is a
potent chemoattractant for mesenchymal cells. Intracellular signal
transduction for PDGF-induced chemotactic response has been reported to
be dependent on phosphatidylinositol 3-kinase (PI3K) activation. Here,
we report a PI3K-independent pathway operating for PDGF-induced chemotaxis in vascular smooth muscle cells and other cell types. Two
different PI3K inhibitors, wortmannin (WT, 1 nM-1
µM) and LY294002 (100 nM-10
µM), did not inhibit PDGF-induced chemotaxis in smooth
muscle cells and Swiss 3T3 cells, whereas WT inhibited activity of PI3K
that were immunopurified from PDGF-stimulated cells as well as PI3K
purified from cells that were stimulated with PDGF in the presence of
the same concentrations of WT. Similarly, WT (100 nM)
abolished the increase in intracellular phosphatidylinositol 3,4,5-triphosphate after PDGF stimulation. Furthermore, Chinese hamster
ovary/
Volume 271, Number 46,
Issue of November 15, 1996
pp. 29342-29346
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
National Cardiovascular Center Research
Institute, 5-7-1 Fujishirodai, Suita, Osaka 565, Japan and the
§ Second Department of Internal Medicine, Kobe University
Medical School, 7-5-1 Kusunoki-cho, Chuo-ku, Kobe 650, Japan
p85 cells overexpressing a dominant negative p85 subunit of
PI3K showed a chemotactic response comparable to that of parental cells
while showing a remarkable decrease in PI3K activity. Rapamycin, a
specific inhibitor of pp70 S6 kinase, which is one of the well
characterized downstreams of PI3K, did not inhibit PDGF-induced
chemotaxis. Both WT and LY294002 inhibited PDGF-induced amino acid
uptake and actin-stress fiber reorganization and partly inhibited
PDGF-induced glucose incorporation in Swiss 3T3 cells. Our findings
indicate that, in vascular smooth muscle cells and other cell types,
the signal transduction for PDGF-induced chemotaxis is independent of
PI3K activity while the signal transduction for PDGF-induced amino acid
uptake, glucose incorporation, and cytoskeletal reorganization is
dependent on PI3K.
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