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Cell Journal، جلد ۱۹، شماره ۳، صفحات ۴۴۳-۴۵۱
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عنوان انگلیسی Subcellular Distribution of S-Nitrosylated H-Ras in Differentiated and Undifferentiated PC12 Cells during Hypoxia
چکیده انگلیسی مقاله Objective: Hypoxia or exposure to excessive reactive oxygen or nitrogen species could induce S-nitrosylation of various target proteins, including GTPases of Ras superfamily. In the hypoxic conditions, Ras protein is translocated to the cytosol, where it interacts with Golgi complex, endoplasmic reticulum and mitochondria. The mobility and translocation of Ras depend on the oxidative status of cells. However, the importance of relocated s-nitrosylated H-Ras (NO-H-Ras) in proliferation/differentiation processes is not completely understood. Here, we determined the content of soluble and membrane-bound s-nitrosylated Ras in differentiated and undifferentiated rat pheochromocytoma (PC12) cells in hypoxic and normoxic conditions. Materials and methods: The levels of NO-H-Ras were analyzed in hypoxic and normoxic conditions in membrane and soluble fractions of undifferentiated and NGF-treated PC12 cells with and without treating the cells with nitric oxide donor–SNP, with the S-nitrosylated kit, immunoprecipitation and western blotting techniques. The action of nitrosylated H-Ras on oxidative metabolism of isolated mitochondria was assessed by determining mitochondrial hydrogen peroxide generation with scopoletin oxidation method, and ATP production, estimated by the luminometric method. Results: The hypoxia did not influence the nitrosylation of soluble H-Ras in undifferentiated PC12 cells; whereas in hypoxic conditions, the nitrosylation of soluble H-Ras was greatly decreased in differentiated PC12 cells in this study. Nitric oxide donor – sodium nitroprusside (SNP) did not change the levels of nitrosylation of soluble H-Ras, either in hypoxic or normoxic conditions. On the other hand, hypoxia, per se, did not affect the nitrosylation of membrane-bound H-Ras in differentiated and undifferentiated PC12 cells. However, the SNP-dependent nitrosylation of membrane-bound H-Ras was greatly increased in differentiated PC12 cells. In addition, we have found that unmodified normal, as well as mutated H-Ras enhanced the mitochondrial synthesis of ATP, whereas the stimulatory effects on ATP synthesis were eliminated after S-nitrosylation of H-Ras. Conclusion: By these findings, it may be proposed that hypoxia can decrease S-nitrosylation of soluble H-Ras in differentiated PC12 cells and abolish the inhibitory effect of nitrosylated H-Ras in mitochondrial oxidative metabolism.
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نویسندگان مقاله | Tamar Barbakadze


| Galina Goloshvili


| Nana Narmania


| Elene Zhuravliova


| David Mikeladze


نشانی اینترنتی http://celljournal.org/journal/article/abstract/4546
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