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J Biol Chem, Vol. 275, Issue 14, 10527-10531, April 7, 2000
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From the Autophosphorylation of the platelet-derived
growth factor (PDGF) receptor triggers intracellular signaling cascades
as a result of recruitment of Src homology 2 domain-containing enzymes,
including phosphatidylinositol 3-kinase (PI3K), the
GTPase-activating protein of Ras (GAP), the protein-tyrosine
phosphatase SHP-2, and phospholipase C- Center for Cell Signaling Research, Division
of Molecular Life Sciences, and Department of Biological Sciences, Ewha
Womans University, Seoul 120-750, Korea, the ¶ Schepens Eye
Research Institute, Harvard Medical School,
Boston, Massachusetts 02114, the International Joint Research
Laboratory of Center for Cell Signaling Research and Laboratory of Cell
Signaling, NHLBI, National Institutes of Health,
Bethesda, Maryland 20892
1 (PLC-1), to specific
phosphotyrosine residues. The roles of these various effectors in
PDGF-induced generation of H2O2 have now
been investigated in HepG2 cells expressing various PDGF receptor
mutants. These mutants included a kinase-deficient receptor and
receptors in which various combinations of the tyrosine residues required for the binding of PI3K (Tyr740 and
Tyr751), GAP (Tyr771), SHP-2
(Tyr1009), or PLC-1 (Tyr1021) were mutated
to Phe. PDGF failed to increase H2O2 production in cells expressing either the kinase-deficient mutant or a receptor in
which the two Tyr residues required for the binding of PI3K were
replaced by Phe. In contrast, PDGF-induced H2O2
production in cells expressing a receptor in which the binding sites
for GAP, SHP-2, and PLC-1 were all mutated was slightly greater than that in cells expressing the wild-type receptor. Only the PI3K binding
site was alone sufficient for PDGF-induced H2O2
production. The effect of PDGF on H2O2
generation was blocked by the PI3K inhibitors LY294002 and wortmannin
or by overexpression of a dominant negative mutant of Rac1. These
results suggest that a product of PI3K is required for PDGF-induced
production of H2O2 in nonphagocytic cells, and
that Rac1 mediates signaling between the PI3K product and the putative
NADPH oxidase.
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