Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II

Min Hee Choi, In Kyung Lee, Gyung Whan Kim, Bang Ul Kim, Ying-Hao Han, Dae-Yeul Yu, Hye Sun Park, Kyung Yong Kim, Jong Seo Lee, Chulhee Choi, Yun Soo Bae, Byung In Lee, Sue Goo Rhee () and Sang Won Kang ()
Additional contact information
Min Hee Choi: Ewha Womans University
In Kyung Lee: Ewha Womans University
Gyung Whan Kim: Yonsei University College of Medicine
Bang Ul Kim: Ewha Womans University
Ying-Hao Han: Korea Research Institute of Bioscience and Biotechnology
Dae-Yeul Yu: Korea Research Institute of Bioscience and Biotechnology
Hye Sun Park: Ewha Womans University
Kyung Yong Kim: Labfrontier Co. Ltd., KSBC building
Jong Seo Lee: Labfrontier Co. Ltd., KSBC building
Chulhee Choi: Ewha Womans University
Yun Soo Bae: Ewha Womans University
Byung In Lee: Yonsei University College of Medicine
Sue Goo Rhee: National Institutes of Health
Sang Won Kang: Ewha Womans University

Nature, 2005, vol. 435, issue 7040, 347-353

Abstract: Abstract Platelet-derived growth factor (PDGF) is a potent mitogenic and migratory factor that regulates the tyrosine phosphorylation of a variety of signalling proteins via intracellular production of H2O2 (refs 1, 2–3). Mammalian 2-Cys peroxiredoxin type II (Prx II; gene symbol Prdx2) is a cellular peroxidase that eliminates endogenous H2O2 produced in response to growth factors such as PDGF and epidermal growth factor4; however, its involvement in growth factor signalling is largely unknown. Here we show that Prx II is a negative regulator of PDGF signalling. Prx II deficiency results in increased production of H2O2, enhanced activation of PDGF receptor (PDGFR) and phospholipase Cγ1, and subsequently increased cell proliferation and migration in response to PDGF. These responses are suppressed by expression of wild-type Prx II, but not an inactive mutant. Notably, Prx II is recruited to PDGFR upon PDGF stimulation, and suppresses protein tyrosine phosphatase inactivation. Prx II also leads to the suppression of PDGFR activation in primary culture and a murine restenosis model, including PDGF-dependent neointimal thickening of vascular smooth muscle cells. These results demonstrate a localized role for endogenous H2O2 in PDGF signalling, and indicate a biological function of Prx II in cardiovascular disease.

Date: 2005
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DOI: 10.1038/nature03587

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