Arginine deiminase modulates endothelial tip cells via excessive synthesis of reactive oxygen species. (21st September 2011)

• Record Type: Journal Article
• Authors: Zhuo, Wei; Song, Xiaomin; Zhou, Hao; Luo, Yongzhang
• Is Part Of: Biochemical Society transactions. Volume 39:Number 5(2011)
• Page Start: 1376
• Page End: 1381
• Publication Date: 2011-09-21
• Subjects: angiogenesis -- apoptosis -- arginine deiminase -- endothelial tip cell -- reactive oxygen species; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0391376
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : ADI (arginine deiminase), an enzyme that hydrolyses arginine, has been reported as an anti-angiogenesis agent. However, its molecular mechanism is unclear. We have demonstrated for the first time that ADI modulates the angiogenic activity of endothelial tip cells. By arginine depletion, ADI disturbs actin filament in endothelial tip cells, causing disordered migratory direction and decreased migration ability. Furthermore, ADI induces excessive synthesis of ROS (reactive oxygen species), and activates caspase 8-, but not caspase 9-, dependent apoptosis in endothelial cells. These findings provide a novel mechanism by which ADI inhibits tumour angiogenesis through modulating endothelial tip cells.