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首页> 外文期刊>Proteome science >Interaction of peroxiredoxin V with dihydrolipoamide branched chain transacylase E2 (DBT) in mouse kidney under hypoxia
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Interaction of peroxiredoxin V with dihydrolipoamide branched chain transacylase E2 (DBT) in mouse kidney under hypoxia

机译：低氧条件下小鼠肾脏中过氧化物酶毒素V与二氢脂酰胺支链转酰基酶E2（DBT）的相互作用

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Background 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. 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). Results Immunoprecipitation 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. Conclusions We 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.
机译：背景过氧化物酶毒素V（Prdx V）通过过氧化物酶活性作为多种细胞内的有效抗氧化剂，在预防氧化损伤中起着重要作用。然而，Prdx V的功能本身不限于过氧化物酶的酶活性。通过指导与信号蛋白的相互作用，它似乎在调节细胞对外部刺激的反应中具有独特的功能。在这项研究中，我们使用免疫沉淀和shot弹枪蛋白质组分析（LC-MS / MS）在缺氧应激下的小鼠肾脏中鉴定了Prdx V相互作用的伴侣。结果免疫沉淀结合纳米UPLC-MSE shot弹枪蛋白质组学被用于确定在缺氧情况下小鼠肾脏中Prdx V的假定相互作用伙伴。通过在正常氧与低氧条件下肾脏中的比较相互作用组学分析，总共鉴定出17种蛋白是Prdx V的潜在相互作用伴侣。二氢脂酰胺支链转酰基酶E2（DBT）似乎是一个突出的候选蛋白，在缺氧胁迫下显示与Prdx V的相互作用增强。此外，与正常氧相比，低氧肾表现出改变的DBT酶活性。在体外低氧应激下成功观察到这两种蛋白质的共定位增强。此外，Prdx V的过氧化物半胱氨酸残基（Cys48）可能与DBT相互作用。结论我们确定了几种在低氧条件下与Prdx V相互作用的蛋白，已知这些蛋白会诱导肾氧化应激。在低氧条件下，我们观察到Prdx V和DBT蛋白的相互作用增强，并且DBT酶活性增强。这项研究的结果将有助于增进我们对Prdx V在低氧应激中的作用的了解，并可能为未来的研究提供新的方向。

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