Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/49307
Title: INVESTIGATION OF THE REDOX SENSITIVITY OF AIF AND KEAP1 TO OXIDATIVE STRESS AND THEIR REGULATION BY THIOL REDOX SYSTEMS
Authors: SHELAR SANDEEP BALU
Keywords: oxidative stress, redox sensitivity, antioxidant systems, thiol oxidative modifications, thioredoxin, glutathione
Issue Date: 22-Aug-2013
Citation: SHELAR SANDEEP BALU (2013-08-22). INVESTIGATION OF THE REDOX SENSITIVITY OF AIF AND KEAP1 TO OXIDATIVE STRESS AND THEIR REGULATION BY THIOL REDOX SYSTEMS. ScholarBank@NUS Repository.
Abstract: Cells achieve a balance between the daily production of ROS and RNS through a number of cellular antioxidant systems, including thiol redox systems: the thioredoxin and glutathione systems. When intracellular ROS and RNS levels are excessive, transient or permanent oxidative stress sets in. Cellular proteins containing redox-sensitive cysteines that are crucial for the proteins¿ functions are therefore sensitive to oxidative stress. This PhD study had focused on two cysteine-containing proteins, namely AIF and Keap1, which were hypothesized to be sensitive to oxidative stress, and their redox states were regulated by thiol redox systems. A novel interaction between AIF and cytosolic thioredoxin was discovered. Moreover, AIF was observed to undergo intramolecular disulfide bond formation under oxidative stress, which could be reversed by the thioredoxin and glutathione systems. Similarly, investigation of the pattern of thiol oxidation in Keap1 revealed the formation of intra- and inter-molecular disulfide bonds; these disulfides were also regulated by the thioredoxin and glutathione systems.
URI: http://scholarbank.nus.edu.sg/handle/10635/49307
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