Structure of a model lipid membrane oxidized by human 15-lipoxygenase-2.

Jamil Nemri, Cosme Morales, Nathaniel C Gilbert, Jaroslaw Majewski, Marcia E Newcomer, Crystal M Vander Zanden

Abstract read

In one paragraph

Article in Biochemical and biophysical research communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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1citing papers in PubMed

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1 citing paper in PubMed.

Open life sciences · 2025
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5 · Who and what money

Authors and funding

6 authors.

Jamil NemriDepartment of Chemistry and Biochemistry, University of Colorado Colorado Springs, 1420 Austin Bluffs Pwky, Colorado Springs, CO, 80918, USA. Electronic address: jnemri@uccs.edu.

Cosme MoralesDepartment of Chemistry and Biochemistry, University of Colorado Colorado Springs, 1420 Austin Bluffs Pwky, Colorado Springs, CO, 80918, USA. Electronic address: cmorale4@uccs.edu.

Nathaniel C GilbertDepartment of Biological Sciences, Louisiana State University, 202 Life Sciences Building, Baton Rouge, LA, 70803, USA. Electronic address: ngilbert@lsu.edu.

Jaroslaw MajewskiDivision of Molecular and Cellular Biosciences, National Science Foundation, Alexandria, VA, USA; Theoretical Biology and Biophysics at Los Alamos National Laboratory, Los Alamos National Laboratory, Los Alamos, NM, 87545, USA; Department of Chemical and Biological Engineering and Center for Biomedical Engineering, University of New Mexico, Albuquerque, NM, 87131, USA. Electronic address: jmajewsk@nsf.gov.

Marcia E NewcomerDepartment of Biological Sciences, Louisiana State University, 202 Life Sciences Building, Baton Rouge, LA, 70803, USA. Electronic address: newcomer@lsu.edu.

Crystal M Vander ZandenDepartment of Chemistry and Biochemistry, University of Colorado Colorado Springs, 1420 Austin Bluffs Pwky, Colorado Springs, CO, 80918, USA. Electronic address: cvanderz@uccs.edu.

Funding

Conformational Flexibility of Lipoxygenases and its Role in Regulation and Substrate Acquisition.R15GM143724 · NIGMS · LOUISIANA STATE UNIV A&M COL BATON ROUGE · PI GILBERT, NATHANIEL · 2021 to 2021

$444k

NIGMS NIH HHS R15 GM143724

6 · The paper itself

Abstract

Enzyme-mediated lipid oxidation is an important regulatory event in cell signaling, with oxidized lipids being potent signaling molecules that can illicit dramatic changes in cell behavior. For example, peroxidation of an arachidonoyl poly-unsaturated fatty acid by the human enzyme 15-lipoxygenase-2 (15-LOX-2) has been associated with formation of atherosclerotic plaques. Previous work on synthetically oxidized membranes has shown that oxidized lipid tails will change their conformation to facilitate interactions between the peroxide group and the lipid headgroups. However, this phenomenon has not been directly observed for a lipid membrane that has undergone enzyme-catalyzed oxidation. In this study, we report on the structure of a model lipid membrane before and after oxidation by 15-LOX-2. A model lipid membrane monolayer at the air-liquid interface was constructed from 1-stearoyl-2-arachidonoyl-sn-glycero-3-phosphocholine (SAPC) in a Langmuir trough, and X-ray reflectivity measurements were conducted to determine the electron density profile of the system. Exposure to 15-LOX-2 caused a dramatic change in the SAPC structure, namely a blurred distinction between the lipid tail/head layers and shortening of the average lipid tail length by ∼3 Å. The electron density profile of the oxidized SAPC monolayer is similar to that of a synthetically oxidized substrate mimic. Overall, this reported observation of an enzymatically-oxidized membrane structure in situ is helping to bridge a gap in the literature between structural studies on synthetically oxidized membranes and cellular studies aiming to understand physiological responses.

Indexed as

Arachidonate 15-LipoxygenaseOxidation-ReductionHumansLipid PeroxidationMembrane LipidsALOX15B protein, humanArachidonate 15-LipoxygenaseMembrane Lipids15-Lipoxygenase-2Arachidonic acidLipoxygenaseMembranesOxidationX-ray reflectivity

Identifiers

PMID39142138

DOI10.1016/j.bbrc.2024.150533

PMCPMC12782027

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