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- W2139549951 abstract "Objective— Localization of atherosclerotic plaques typically correlates with areas of biomechanical strain where shear stress is decreased while stretch, thought to promote atherogenesis through enhanced oxidative stress, is increased. Methods and Results— In human cultured endothelial cells, nitric oxide synthase expression was exclusively shear stress–dependent whereas expression of glutathione peroxidase-1 (GPx-1), but not that of Cu 2+ /Zn 2+ -superoxide dismutase or Mn 2+ -superoxide dismutase, was upregulated solely in response to cyclic stretch. GPx-1 expression was also enhanced in isolated mouse arteries perfused at high pressure. Combined pharmacological and decoy oligodeoxynucleotide blockade revealed that activation of p38 MAP kinase followed by nuclear translocation of CCAAT/enhancer binding protein plays a pivotal role in stretch-induced GPx-1 expression in human endothelial cells. Antisense oligodeoxynucleotide knockdown of GPx-1 reinforced both their capacity to generate hydrogen peroxide and the transient stretch-induced expression of CD40, monocyte chemoatractant protein-1, and vascular cell adhesion molecule-1. Consequently, THP-1 monocyte adhesion to the GPx-1–depleted cells was augmented. Conclusions— Stretch-induced proatherosclerotic gene expression in human endothelial cells seems to be hydrogen peroxide-mediated. The concomitant rise in GPx-1 expression, but not that of other antioxidant enzymes, may comprise an adaptive mechanism through which the cells maintain their antiatherosclerotic properties in spite of a decreased bioavailability of nitric oxide." @default.
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- W2139549951 date "2009-11-01" @default.
- W2139549951 modified "2023-09-26" @default.
- W2139549951 title "Upregulation of Glutathione Peroxidase Offsets Stretch-Induced Proatherogenic Gene Expression in Human Endothelial Cells" @default.
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- W2139549951 doi "https://doi.org/10.1161/atvbaha.109.194738" @default.
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