92 research outputs found
Manipulation of iron and energy status of cells as a tool fot triggering apoptosis. Key role for inactivation of mitochondrial ATP synthase
No full textH2O2 induces apoptosis in heme-synthesizig erytrholeukemia cells with a mechanism indeoendent from nF-kB activation and mediated by decline in mitochondrial bioenergy
No full textInactivation of mitochondrial ATPsynthase through manipulation of iron status as a tool for triggering apoptosis
No full textEndogenous pro-oxidant status and H2O2-mediated impairment of cell mitochondrial functions, ATP content and proliferative capacity
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Il danno di H2O2 su F1ATPasi mitocondriale può essere mediato da Fe++ e da Fe+++ legati alla proteina
No full textIron-binding sites onmitochondrial F1ATPase. EPR detection of protein-derived radicals in the reaction of H2O2 with iron bound to the enzyme
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In vitro and in vivo studies of F(0)F(1)ATP synthase regulation by inhibitor protein IF1 in goat heart
No full textA method has been developed to allow the level of F(0)F(1)ATP synthase capacity and the quantity of IF(1) bound to this enzyme be measured in single biopsy samples of goat heart. ATP synthase capacity was determined from the maximal mitochondrial ATP hydrolysis rate and IF(1) content was determined by detergent extraction followed by blue native gel electrophoresis, two-dimensional SDS-PAGE and immunoblotting with anti-IF(1) antibodies. Anaesthetized open-chest goats were subjected to ischemic preconditioning and/or sudden increases of coronary blood flow (CBF) (reactive hyperemia). When hyperemia was induced before ischemic preconditioning, a steep increase in synthase capacity, followed by a deep decrease, was observed. In contrast, hyperemia did not affect synthase capacity when applied after ischemic preconditioning. Similar effects could be produced in vitro by treatment of heart biopsy samples with anoxia (down-regulation of the ATP synthase) or high-salt or high-pH buffers (up-regulation). We show that both in vitro and in vivo the same close inverse correlation exists between enzyme activity and IF(1) content, demonstrating that under all conditions tested the only significant modulator of the enzyme activity was IF(1). In addition, both in vivo and in vitro, 1.3-1.4 mol of IF(1) was predicted to fully inactivate 1 mol of synthase, thus excluding the existence of significant numbers of non-inhibitory binding sites for IF(1) in the F(0) sector
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