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The role of peroxiredoxin 6 in biosynthesis of FAHFAs

SYSNO ASEP	0565458
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	The role of peroxiredoxin 6 in biosynthesis of FAHFAs
Author(s)	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, SAI}
Source Title	Free Radical Biology and Medicine. - : Elsevier - ISSN 0891-5849 Roč. 193, Nov 20 Part 2 (2022), s. 787-794
Number of pages	8 s.
Language	eng - English
Country	US - United States
Keywords	peroxiredoxin ; FAHFA ; lipid oxidation ; adipose tissue ; linoleic acid
OECD category	Biochemistry and molecular biology
R&D Projects	LTAUSA18104 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
Method of publishing	Limited access
Institutional support	FGU-C - RVO:67985823
UT WOS	000956591700001
EID SCOPUS	85142529420
DOI	10.1016/j.freeradbiomed.2022.11.015
Annotation	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.
Workplace	Institute of Physiology
Contact	Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400
Year of Publishing	2023
Electronic address	https://doi.org/10.1016/j.freeradbiomed.2022.11.015

Number of the records: 1