Počet záznamů: 1
The role of peroxiredoxin 6 in biosynthesis of FAHFAs
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SYSNO ASEP 0565458 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název The role of peroxiredoxin 6 in biosynthesis of FAHFAs Tvůrce(i) Palůchová, Veronika (FGU-C) ORCID, RID
Čajka, Tomáš (FGU-C) RID, ORCID, SAI
Durand, T. (FR)
Vigor, C. (FR)
Dodia, Ch. (US)
Chatterjee, S. (US)
Fisher, A. B. (US)
Kuda, Ondřej (FGU-C) RID, ORCID, SAIZdroj.dok. Free Radical Biology and Medicine. - : Elsevier - ISSN 0891-5849
Roč. 193, Nov 20 Part 2 (2022), s. 787-794Poč.str. 8 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova peroxiredoxin ; FAHFA ; lipid oxidation ; adipose tissue ; linoleic acid Obor OECD Biochemistry and molecular biology CEP LTAUSA18104 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Způsob publikování Omezený přístup Institucionální podpora FGU-C - RVO:67985823 UT WOS 000956591700001 EID SCOPUS 85142529420 DOI 10.1016/j.freeradbiomed.2022.11.015 Anotace Peroxiredoxin 6 (Prdx6) is a multifunctional enzyme, a unique member of the peroxiredoxin family, with an important role in antioxidant defense. Moreover, it has also been linked with the biosynthesis of anti-inflammatory and anti-diabetic lipids called fatty acid esters of hydroxy fatty acids (FAHFAs) and many diseases, including cancer, inflammation, and metabolic disorders. Here, we performed metabolomic and lipidomic profiling of subcutaneous adipose tissue from mouse models with genetically modified Prdx6. Deletion of Prdx6 resulted in reduced levels of FAHFAs containing 13-hydroxylinoleic acid (13-HLA). Mutation of Prdx6 C47S impaired the glutathione peroxidase activity and reduced FAHFA levels, while D140A mutation, responsible for phospholipase A2 activity, showed only minor effects. Targeted analysis of oxidized phospholipids and triacylglycerols in adipocytes highlighted a correlation between FAHFA and hydroxy fatty acid production by Prdx6 or glutathione peroxidase 4. FAHFA regioisomer abundance was negatively affected by the Prdx6 deletion, and this effect was more pronounced in longer and more unsaturated FAHFAs. The predicted protein model of Prdx6 suggested that the monomer-dimer transition mechanism might be involved in the repair of longer-chain peroxidized phospholipids bound over two monomers and that the role of Prdx6 in FAHFA synthesis might be restricted to branching positions further from carbon 9. In conclusion, our work linked the peroxidase activity of Prdx6 with the levels of FAHFAs in adipose tissue. Pracoviště Fyziologický ústav Kontakt Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Rok sběru 2023 Elektronická adresa https://doi.org/10.1016/j.freeradbiomed.2022.11.015
Počet záznamů: 1