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Peroxiredoxin II Is an Essential Antioxidant Enzyme that Prevents the Oxidative Inactivation of VEGF Receptor-2 in Vascular Endothelial Cells

Title
Peroxiredoxin II Is an Essential Antioxidant Enzyme that Prevents the Oxidative Inactivation of VEGF Receptor-2 in Vascular Endothelial Cells
Authors
Kang D.Lee D.Lee K.Park Y.Lee J.Lee S.-H.Koh Y.Koh G.-Y.Choi C.Yu D.-Y.Kim J.Kang S.
Ewha Authors
강상원김재상
SCOPUS Author ID
강상원scopus; 김재상scopus
Issue Date
2011
Journal Title
Molecular Cell
ISSN
1097-2765JCR Link
Citation
vol. 44, no. 4, pp. 545 - 558
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Cellular antioxidant enzymes play crucial roles in aerobic organisms by eliminating detrimental oxidants and maintaining the intracellular redox homeostasis. Therefore, the function of antioxidant enzymes is inextricably linked to the redox-dependent activities of multiple proteins and signaling pathways. Here, we report that the VEGFR2 RTK has an oxidation-sensitive cysteine residue whose reduced state is preserved specifically by peroxiredoxin II (PrxII) in vascular endothelial cells. In the absence of PrxII, the cellular H 2O 2 level is markedly increased and the VEGFR2 becomes inactive, no longer responding to VEGF stimulation. Such VEGFR2 inactivation is due to the formation of intramolecular disulfide linkage between Cys1199 and Cys1206 in the C-terminal tail. Interestingly, the PrxII-mediated VEGFR2 protection is achieved by association of two proteins in the caveolae. Furthermore, PrxII deficiency suppresses tumor angiogenesis in vivo. This study thus demonstrates a physiological function of PrxII as the residential antioxidant safeguard specific to the redox-sensitive VEGFR2. © 2011 Elsevier Inc.
DOI
10.1016/j.molcel.2011.08.040
Appears in Collections:
자연과학대학 > 생명과학전공 > Journal papers
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