Resolvin D4 biosynthetic evidence by an epoxide hydrolase and identification in human brain

Resolvin D4 biosynthetic evidence by an epoxide hydrolase and identification in human brain | Authorea try { document.documentElement.classList.add('js'); } catch (e) { } var _gaq = _gaq || []; _gaq.push(['_setAccount', 'G-8VDV14Y67G']); _gaq.push(['_trackPageview']); (function() { var ga = document.createElement('script'); ga.type = 'text/javascript'; ga.async = true; ga.src = ('https:' == document.location.protocol ? 'https://ssl' : 'http://www') + '.google-analytics.com/ga.js'; var s = document.getElementsByTagName('script')[0]; s.parentNode.insertBefore(ga, s); })(); Skip to main content Preprints Collections Wiley Open Research IET Open Research Ecological Society of Japan All Collections About About Authorea FAQs Contact Us Quick Search anywhere Search for preprint articles, keywords, etc. Search Search ADVANCED SEARCH SCROLL British Journal of Pharmacology This is a preprint and has not been peer reviewed. Data may be preliminary. 12 May 2026 V1 Latest version Share on Resolvin D4 biosynthetic evidence by an epoxide hydrolase and identification in human brain Authors : Robert Nshimiyimana 0000-0003-0832-9938 [email protected] and Charles Serhan [email protected] Authors Info & Affiliations https://doi.org/10.22541/authorea.15003182/v1 33 views 15 downloads Contents Abstract Supplementary Material Information & Authors Metrics & Citations View Options References Figures Tables Media Share Abstract Resolvins play pivotal roles in inflammation resolution and tissue homeostasis. These active compounds are formed by enzymatic oxygenation and further transformation of omega-3 polyunsaturated fatty acids in mammalian cells. Here, we report analytical data for the identification of resolvin D4 (4S,5R,17S-trihydroxy-6E,8E,10Z,13Z,15E,19Z-docosahexaenoic acid) in human brain tissues and confirm the involvement of the soluble epoxide hydrolase (sEH) in the biosynthesis of this potent bioactive product. Using synthetic 4,5(S,S) epoxide intermediate (4S,5S-oxido-17S-hydroxy-6E,8E,10Z,13Z,15E,19Z-docosahexaenoic acid) prepared by total chemical synthesis, UV, and liquid chromatography–tandem mass spectrometry (LC-MS/MS)-based analyses including linear ion trap MS 3 fragmentation, our results demonstrated that this allylic epoxide is a substrate for human recombinant sEH. Incubation of the epoxide with sEH in H 2 18O-enriched buffer led to incorporation of 18O into resolvin D4 at C-5 position, as judged by MS 3 ion trap experiments. These results give direct evidence for the role of the 4,5(S,S) epoxide in the biosynthesis of resolvin D4 by epoxide hydrolases such as sEH. Supplementary Material File (supplementary material – 4,5(s,s) epoxide_bjp_2026.05.01.pdf) supplementary material – 4,5(s,s) epoxide_bjp_2026.05.01 Download 2.86 MB Information & Authors Information Version history V1 Version 1 12 May 2026 Collection British Journal of Pharmacology Authors Affiliations Robert Nshimiyimana 0000-0003-0832-9938 [email protected] Brigham and Women's Hospital Department of Anesthesiology Perioperative and Pain Medicine, Boston, United States, 02115 View all articles by this author Charles Serhan [email protected] Brigham and Women's Hospital Department of Anesthesiology Perioperative and Pain Medicine, Boston, United States, 02115 View all articles by this author Metrics & Citations Metrics Article Usage 33 views 15 downloads .FvxKWukQNSOunydq8rnd { width: 100px; } Citations Download citation Robert Nshimiyimana, Charles Serhan. Resolvin D4 biosynthetic evidence by an epoxide hydrolase and identification in human brain. Authorea . 12 May 2026. 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