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Title 

Peroxiredoxin Il is an essential antioxidant enzyme that prevents the oxidative inactivation of VEGF receptor-2 in vascular endothelial cells

Authors 

D H KangD J LeeK W LeeY S ParkJ Y LeeS H LeeY J KohG Y KohC ChoiDae Yeul YuJ KimS W Kang

Publisher 

Elsevier (Cell Press)

Issue Date 

2011

Citation 

Molecular Cell, vol. 44, no. 4, pp. 545-558

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 H2O2 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.

ISSN 

1097-2765

Link 

http://dx.doi.org/10.1016/j.molcel.2011.08.040

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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