Abstract
BackgroundPeroxiredoxin V (Prdx V) plays a major role in preventing oxidative damage as an effective antioxidant protein within a variety of cells through peroxidase activity. However, the function of Prdx V is not limited to peroxidase enzymatic activity per se. It appears to have unique function in regulating cellular response to external stimuli by directing interaction with signaling protein. In this study, we identified Prdx V interacting partners in mouse kidney under hypoxic stress using immunoprecipitation and shotgun proteomic analysis (LC-MS/MS).ResultsImmunoprecipitation coupled with nano-UPLC-MSE shotgun proteomics was employed to identify putative interacting partners of Prdx V in mouse kidney in the setting of hypoxia. A total of 17 proteins were identified as potential interacting partners of Prdx V by a comparative interactomics analysis in kidney under normoxia versus hypoxia. Dihydrolipoamide branched chain transacylase E2 (DBT) appeared to be a prominent candidate protein displaying enhanced interaction with Prdx V under hypoxic stress. Moreover, hypoxic kidney exhibited altered DBT enzymatic activity compared to normoxia. An enhanced colocalization of these two proteins under hypoxic stress was successfully observed in vitro. Furthermore, peroxidatic cysteine residue (Cys48) of Prdx V is likely to be responsible for interacting with DBT.ConclusionsWe identified several proteins interacting with Prdx V under hypoxic condition known to induce renal oxidative stress. In hypoxic condition, we observed an enhanced interaction of Prdx V and DBT protein as well as increased DBT enzymatic activity. The results from this study will contribute to enhance our understanding of Prdx V’s role in hypoxic stress and may suggest new directions for future research.Electronic supplementary materialThe online version of this article (doi:10.1186/s12953-014-0061-2) contains supplementary material, which is available to authorized users.
Highlights
Peroxiredoxin V (Prdx V) plays a major role in preventing oxidative damage as an effective antioxidant protein within a variety of cells through peroxidase activity
Identification of Prdx V interactome in normoxic and hypoxic mouse kidney Previously, we reported that Prdx V was a novel regulator of renal homeostasis under hypoxic stress, altering protein networks associated with oxidative stress, fatty acid metabolism, and mitochondrial dysfunction [13]
We have shown that Prdx V protein was interacting with other proteins in mouse kidney responding to hypoxic stress
Summary
Peroxiredoxin V (Prdx V) plays a major role in preventing oxidative damage as an effective antioxidant protein within a variety of cells through peroxidase activity. We identified Prdx V interacting partners in mouse kidney under hypoxic stress using immunoprecipitation and shotgun proteomic analysis (LC-MS/MS). Prdxs play major roles in preventing oxidative damage as the effective antioxidant proteins within a variety of cells through peroxidase activity [2]. Mitochondrial biogenesis and its consequent processes enhance metabolic pathways such as fatty acid oxidation and boost antioxidant defense mechanisms that remediate injury from tissue hypoxia, and glucose or fatty acid overburden, all of which would otherwise contribute to the pathogenesis of acute and chronic kidney disease [12]
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