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• W2417605433 endingPage "2910" @default.
• W2417605433 startingPage "2896" @default.
• W2417605433 abstract "The NADPH oxidase is the sole enzymatic complex that produces, in a controlled way, superoxide anions. In phagocytes, it is constituted by the assembly of four cytosolic (p67(phox) , p47(phox) , p40(phox) and Rac) and two membrane (p22(phox) and Nox2) proteins. In response to pro-inflammatory mediators, the NADPH oxidase is activated. In cells, arachidonic acid (cis-AA), released by activated phospholipase A2, also plays a role in activation of the NADPH oxidase complex, but the mechanism of action of cis-AA is still a matter for debate. In cell-free systems, cis-AA is commonly used for activation. We have shown previously that trans-AA isomers were unable to activate the NADPH oxidase complex. Here, we aim to evaluate the structural changes in p47(phox) and p67(phox) induced by AA. The structural impact of both AA isomers on both cytosolic proteins was investigated by the accessibility of the thiol group and by circular dichroism in the far-UV for global folds. cis-AA induces secondary structure changes of p47(phox) and p67(phox) , while the trans isomer does not, suggesting that the changes observed are of importance for the activation process of these proteins. While five of the nine thiol groups in p67(phox) and all of them in p47(phox) have low access to the solvent when proteins are alone in solution, all of them become fully accessible when proteins are together. In conclusion, the secondary structures of p47(phox) and p67(phox) are both dependent on the presence of the partner protein in solution and on the presence of the activator molecule cis-AA." @default.
• W2417605433 created "2016-06-24" @default.
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• W2417605433 date "2016-06-26" @default.
• W2417605433 modified "2023-10-13" @default.
• W2417605433 title "Exploring the arachidonic acid-induced structural changes in phagocyte NADPH oxidase p47^<i>phox</i>and p67^<i>phox</i>via thiol accessibility and SRCD spectroscopy" @default.
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• W2417605433 doi "https://doi.org/10.1111/febs.13779" @default.
• W2417605433 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27284000" @default.
• W2417605433 hasPublicationYear "2016" @default.
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