Dehydrogenase reductase 9 (SDR9C4) and related homologs recognize a broad spectrum of lipid mediator oxylipins as substrates.


Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
01 2022
Historique:
received: 05 10 2021
revised: 13 12 2021
accepted: 15 12 2021
pubmed: 27 12 2021
medline: 29 4 2022
entrez: 26 12 2021
Statut: ppublish

Résumé

Bioactive oxylipins play multiple roles during inflammation and in the immune response, with termination of their actions partly dependent on the activity of yet-to-be characterized dehydrogenases. Here, we report that human microsomal dehydrogenase reductase 9 (DHRS9, also known as SDR9C4 of the short-chain dehydrogenase/reductase (SDR) superfamily) exhibits a robust oxidative activity toward oxylipins with hydroxyl groups located at carbons C9 and C13 of octadecanoids, C12 and C15 carbons of eicosanoids, and C14 carbon of docosanoids. DHRS9/SDR9C4 is also active toward lipid inflammatory mediator dihydroxylated Leukotriene B

Identifiants

pubmed: 34953854
pii: S0021-9258(21)01337-5
doi: 10.1016/j.jbc.2021.101527
pmc: PMC8761697
pii:
doi:

Substances chimiques

Oxylipins 0
Prostaglandins 0
Leukotriene B4 1HGW4DR56D
Short Chain Dehydrogenase-Reductases EC 1.1.1.-

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

101527

Subventions

Organisme : NCI NIH HHS
ID : P01 CA210946
Pays : United States
Organisme : NIAMS NIH HHS
ID : P30 AR050948
Pays : United States
Organisme : NIDDK NIH HHS
ID : P30 DK079626
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA013148
Pays : United States
Organisme : NIAMS NIH HHS
ID : R01 AR076924
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM134548
Pays : United States

Informations de copyright

Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.

Auteurs

Olga V Belyaeva (OV)

Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, Alabama, USA.

Samuel E Wirth (SE)

Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, Alabama, USA.

William E Boeglin (WE)

Department of Pharmacology, Vanderbilt University, Nashville, Tennessee, USA.

Suman Karki (S)

Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, Alabama, USA.

Kelli R Goggans (KR)

Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, Alabama, USA.

Stacy G Wendell (SG)

Department of Pharmacology and Chemical Biology, School of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, USA.

Kirill M Popov (KM)

Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, Alabama, USA.

Alan R Brash (AR)

Department of Pharmacology, Vanderbilt University, Nashville, Tennessee, USA.

Natalia Y Kedishvili (NY)

Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, Alabama, USA. Electronic address: nkedishvili@uab.edu.

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Classifications MeSH