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J. Biol. Chem. 275 (14): 10527-10531

© 2000 by The American Society for Biochemistry and Molecular Biology, Inc.

J Biol Chem, Vol. 275, Issue 14, 10527-10531, April 7, 2000

Platelet-derived Growth Factor-induced H2O2 Production Requires the Activation of Phosphatidylinositol 3-Kinase*

Yun Soo BaeDagger §, Jee-Young SungDagger , Ohn-Soon KimDagger , Yeun Ju KimDagger , Kyu Chung HurDagger , Andrius Kazlauskas, and Sue Goo Rhee||**

From the Dagger  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

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-gamma 1 (PLC-gamma 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-gamma 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-gamma 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.


* This work was supported in part by Center of Excellence Grant 1998G0202 and International Joint Research Laboratory Grant 1999L0001 from the Korean Science and Engineering Foundation.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence may be addressed: Center for Cell Signaling Research, Ewha Womans University, 11-1 Daehyun-Dong, Seodaemoon-gu, Seoul 120-750, Korea. Tel.: 82-2-3277-2729; Fax: 82-2-3277-3760; E-mail: baeys@mm.ewha.ac.kr.

** Bldg. 3, Rm. 122, National Institutes of Health, Bethesda, MD 20892. Tel.: 301-496-9646; Fax: 301-480-0357; E-mail: sgrhee@nih.gov.


Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.

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