Evidence map›Paper›PMID 17045234›Full record

ArticleArchives of biochemistry and biophysics2006

Human and mouse eLOX3 have distinct substrate specificities: implications for their linkage with lipoxygenases in skin.

Zheyong Yu, Claus Schneider, William E Boeglin, Alan R Brash

Open access · greenAbstract readComparative Study
In one paragraph

Article in Archives of biochemistry and biophysics, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

21 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Lipoxygenases at the Intersection of Infection and Carcinogenesis.International journal of molecular sciences · 2024
    Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. The Biosynthesis of Enzymatically Oxidized Lipids.Frontiers in endocrinology · 2020
    Review
  9. Review
  10. Bioactive lipids and pathological retinal angiogenesis.British journal of pharmacology · 2019
    Review
  11. Characterization of Epidermal Lipoxygenase Expression in Normal Human Skin and Tissue-Engineered Skin Substitutes.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2018
    Article
  12. Mammalian lipoxygenases and their biological relevance.Biochimica et biophysica acta · 2015
    Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Systematic analysis of rat 12/15-lipoxygenase enzymes reveals critical role for spinal eLOX3 hepoxilin synthase activity in inflammatory hyperalgesia.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
    Article
  18. Article
  19. 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

4 authors at 1 institution in 1 country.

Zheyong YuDivision of Clinical Pharmacology, Department of Pharmacology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
Claus Schneider
William E Boeglin
Alan R Brash
Vanderbilt University · US

Funding

UV, APOPTOSIS, PROTEIN PHOSPHATASE AND SKIN DISEASEP30AR041943 · NIAMS · VANDERBILT UNIVERSITY · PI MCCAWLEY, LISA JOY · 1994 to 2008
$5.3M
Linking Lipoxygenases with Essential Fatty Acids and Epidermal Barrier FormationR01AR051968 · NIAMS · VANDERBILT UNIVERSITY · PI BRASH, ALAN R. · 2005 to 2016
$3.0M
NIAMS NIH HHS AR051968NIAMS NIH HHS P30 AR041943NIAMS NIH HHS P30 AR-41943NIAMS NIH HHS R01 AR051968
6 · The paper itself

Abstract

Genetic and biochemical evidence suggests a functional link between human 12R-lipoxygenase (12R-LOX) and epidermal lipoxygenase-3 (eLOX3) in normal differentiation of the epidermis; LOX-derived fatty acid hydroperoxide is isomerized by the atypical eLOX3 into a specific epoxyalcohol that is a potential mediator in the pathway. Mouse epidermis expresses a different complement of LOX enzymes, and therefore this metabolic linkage could differ. To test this concept, we compared the substrate specificities of recombinant mouse and human eLOX3 toward sixteen hydroperoxy stereoisomers of arachidonic and linoleic acids. Both enzymes metabolized R-hydroperoxides 2-3 times faster than the corresponding S enantiomers. Whereas 12R-hydroperoxyeicosatetraenoic acid (12R-HPETE) is the best substrate for human eLOX3 (2.4 s(-1); at 30 microM substrate), mouse eLOX3 shows the highest turnover with 8R-HPETE (2.9 s(-1)) followed by 8S-HPETE (1.3 s(-1)). Novel product structures were characterized from reactions of mouse eLOX3 with 5S-, 8R-, and 8S-HPETEs. 8S-HPETE is converted specifically to a single epoxyalcohol, identified as 10R-hydroxy-8S,9S-epoxyeicosa-5Z,11Z,14Z-trienoic acid. The substrate preference of mouse eLOX3 and the unique occurrence of an 8S-LOX enzyme in mouse skin point to a potential LOX pathway for the production of epoxyalcohol in murine epidermal differentiation.

Indexed as

AnimalsArachidonate 12-LipoxygenaseArachidonic AcidsEnzyme ActivationHumansLinoleic AcidsLipoxygenaseMiceSkinSpecies SpecificityArachidonate 12-LipoxygenaseArachidonic AcidsLinoleic AcidsLipoxygenaselipoxygenase 3

Identifiers

PMID17045234
PMCPMC2636205
OpenAlexW2029387641

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.