{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Shih PB"],"funding":["NIDDK NIH HHS","NIEHS NIH HHS","NIMH NIH HHS"],"pagination":["537-46"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4591075"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["21(4)"],"pubmed_abstract":["Individuals with anorexia nervosa (AN) restrict eating and become emaciated. They tend to have an aversion to foods rich in fat. Because epoxide hydrolase 2 (EPHX2) was identified as a novel AN susceptibility gene, and because its protein product, soluble epoxide hydrolase (sEH), converts bioactive epoxides of polyunsaturated fatty acid (PUFA) to the corresponding diols, lipidomic and metabolomic targets of EPHX2 were assessed to evaluate the biological functions of EPHX2 and their role in AN. Epoxide substrates of sEH and associated oxylipins were measured in ill AN, recovered AN and gender- and race-matched controls. PUFA and oxylipin markers were tested as potential biomarkers for AN. Oxylipin ratios were calculated as proxy markers of in vivo sEH activity. Several free- and total PUFAs"],"journal":["Molecular psychiatry"],"pubmed_title":["Dysregulation of soluble epoxide hydrolase and lipidomic profiles in anorexia nervosa."],"pmcid":["PMC4591075"],"funding_grant_id":["R01 ES002710","1K01DK087813-01A1","K01 DK087813","U24DK097154","R01 MH106781","U24 DK097154","P42 ES004699"],"pubmed_authors":["Yang J","Shih PB","Schork N","Halmi KA","Hammock BD","Zeeland AA","Berrettini W","German JB","Bergen AW","Kaye W","Magistretti P","Armando AM","Morisseau C","Quehenberger O"],"additional_accession":[]},"is_claimable":false,"name":"Dysregulation of soluble epoxide hydrolase and lipidomic profiles in anorexia nervosa.","description":"Individuals with anorexia nervosa (AN) restrict eating and become emaciated. They tend to have an aversion to foods rich in fat. Because epoxide hydrolase 2 (EPHX2) was identified as a novel AN susceptibility gene, and because its protein product, soluble epoxide hydrolase (sEH), converts bioactive epoxides of polyunsaturated fatty acid (PUFA) to the corresponding diols, lipidomic and metabolomic targets of EPHX2 were assessed to evaluate the biological functions of EPHX2 and their role in AN. Epoxide substrates of sEH and associated oxylipins were measured in ill AN, recovered AN and gender- and race-matched controls. PUFA and oxylipin markers were tested as potential biomarkers for AN. Oxylipin ratios were calculated as proxy markers of in vivo sEH activity. Several free- and total PUFAs","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Apr","modification":"2026-04-29T22:16:58.144Z","creation":"2019-03-27T01:59:24Z"},"accession":"S-EPMC4591075","cross_references":{"pubmed":["25824304"],"doi":["10.1038/mp.2015.26"]}}