Evidence map›Paper›PMID 27435673›Full record

ArticleThe Journal of biological chemistry2016

Membrane-dependent Activities of Human 15-LOX-2 and Its Murine Counterpart: IMPLICATIONS FOR MURINE MODELS OF ATHEROSCLEROSIS.

Gunes Bender, Erin E Schexnaydre, Robert C Murphy, Charis Uhlson, Marcia E Newcomer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

30 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. KRAS/ABHD17C/ALOX15B Axis Promotes Pancreatic Cancer Progression via Ferroptosis Evasion.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Structure of a model lipid membrane oxidized by human 15-lipoxygenase-2.Biochemical and biophysical research communications · 2024
    Article
  10. Murine Alox8 versus the human ALOX15B ortholog: differences and similarities.Pflugers Archiv : European journal of physiology · 2024
    Review
  11. Lipoxygenases at the Intersection of Infection and Carcinogenesis.International journal of molecular sciences · 2024
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. FAF1 blocks ferroptosis by inhibiting peroxidation of polyunsaturated fatty acids.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Gunes BenderFrom the Department of Biological Sciences, Louisiana State University, Baton Rouge, Louisiana 70803 and.
Erin E SchexnaydreFrom the Department of Biological Sciences, Louisiana State University, Baton Rouge, Louisiana 70803 and.
Robert C Murphythe Department of Pharmacology, University of Colorado at Denver, Aurora, Colorado 80045.
Charis Uhlsonthe Department of Pharmacology, University of Colorado at Denver, Aurora, Colorado 80045.
Marcia E NewcomerFrom the Department of Biological Sciences, Louisiana State University, Baton Rouge, Louisiana 70803 and newcomer@lsu.edu.
Louisiana State University · USUniversity of Colorado Denver · US

Funding

Pilot Study: POPULATION PHARMACOLOGYU54HL117798 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI GROSSER, TILO · 2012 to 2016
$18.5M
The Structural Basis for Control of 5-Lipoxgenease ActivityR01HL107887 · NHLBI · LOUISIANA STATE UNIV A&M COL BATON ROUGE · PI NEWCOMER, MARCIA E. · 2011 to 2014
$1.4M
NHLBI NIH HHS R01 HL107887NHLBI NIH HHS U54 HL117798
6 · The paper itself

Abstract

The enzyme encoded by the ALOX15B gene has been linked to the development of atherosclerotic plaques in humans and in a mouse model of hypercholesterolemia. In vitro, these enzymes, which share 78% sequence identity, generate distinct products from their substrate arachidonic acid: the human enzyme, a 15-S-hydroperoxy product; and the murine enzyme, an 8-S-product. We probed the activities of these enzymes with nanodiscs as membrane mimics to determine whether they can access substrate esterified in a bilayer and characterized their activities at the membrane interface. We observed that both enzymes transform phospholipid-esterified arachidonic acid to a 15-S-product. Moreover, when expressed in transfected HEK cells, both enzymes result in significant increases in the amounts of 15-hydroxyderivatives of eicosanoids detected. In addition, we show that 15-LOX-2 is distributed at the plasma membrane when the HEK293 cells are stimulated by the addition Ca(2+) ionophore and that cellular localization is dependent upon the presence of a putative membrane insertion loop. We also report that sequence differences between the human and mouse enzymes in this loop appear to confer distinct mechanisms of enzyme-membrane interaction for the homologues.

Indexed as

Arachidonate 15-LipoxygenaseArachidonic AcidsAtherosclerosisCell MembraneAnimalsCalcium IonophoresDisease Models, AnimalHEK293 CellsHumansMiceProtein Structure, SecondaryProtein TransportALOX15B protein, humanArachidonate 15-LipoxygenaseArachidonic AcidsCalcium Ionophoresarachidonic acid (AA) (ARA)eicosanoidlipid signalinglipoxygenase pathwayphospholipid

Identifiers

PMID27435673
PMCPMC5016680
OpenAlexW2480230194

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.