The Reaction Specificity of Mammalian ALOX15 Orthologs is Changed During Late Primate Evolution and These Alterations Might Offer Evolutionary Advantages for Hominidae.

eicosanoids ferroptosis lipid peroxidation oxidative stress recombinant proteins

Journal

Frontiers in cell and developmental biology
ISSN: 2296-634X
Titre abrégé: Front Cell Dev Biol
Pays: Switzerland
ID NLM: 101630250

Informations de publication

Date de publication:
2022
Historique:
received: 08 02 2022
accepted: 01 04 2022
entrez: 9 5 2022
pubmed: 10 5 2022
medline: 10 5 2022
Statut: epublish

Résumé

Arachidonic acid lipoxygenases (ALOXs) have been implicated in the immune response of mammals. The reaction specificity of these enzymes is decisive for their biological functions and ALOX classification is based on this enzyme property. Comparing the amino acid sequences and the functional properties of selected mammalian ALOX15 orthologs we previously hypothesized that the reaction specificity of these enzymes can be predicted based on their amino acid sequences (Triad Concept) and that mammals, which are ranked in evolution below gibbons, express arachidonic acid 12-lipoxygenating ALOX15 orthologs. In contrast, Hominidae involving the great apes and humans possess 15-lipoxygenating enzymes (Evolutionary Hypothesis). These two hypotheses were based on sequence data of some 60 mammalian ALOX15 orthologs and about half of them were functionally characterized. Here, we compared the ALOX15 sequences of 152 mammals representing all major mammalian subclades expressed 44 novel ALOX15 orthologs and performed extensive mutagenesis studies of their triad determinants. We found that

Identifiants

pubmed: 35531094
doi: 10.3389/fcell.2022.871585
pii: 871585
pmc: PMC9068934
doi:

Types de publication

Journal Article

Langues

eng

Pagination

871585

Informations de copyright

Copyright © 2022 Heydeck, Reisch, Schäfer, Kakularam, Roigas, Stehling, Püschel and Kuhn.

Déclaration de conflit d'intérêts

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

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Auteurs

Dagmar Heydeck (D)

Department of Biochemistry, Charité-Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt Universität zu Berlin, Berlin, Germany.

Florian Reisch (F)

Department of Biochemistry, Charité-Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt Universität zu Berlin, Berlin, Germany.
Institute for Nutritional Sciences, University Potsdam, Potsdam, Germany.

Marjann Schäfer (M)

Department of Biochemistry, Charité-Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt Universität zu Berlin, Berlin, Germany.
Institute for Nutritional Sciences, University Potsdam, Potsdam, Germany.

Kumar R Kakularam (KR)

Department of Biochemistry, Charité-Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt Universität zu Berlin, Berlin, Germany.

Sophie A Roigas (SA)

Department of Biochemistry, Charité-Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt Universität zu Berlin, Berlin, Germany.

Sabine Stehling (S)

Department of Biochemistry, Charité-Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt Universität zu Berlin, Berlin, Germany.

Gerhard P Püschel (GP)

Institute for Nutritional Sciences, University Potsdam, Potsdam, Germany.

Hartmut Kuhn (H)

Department of Biochemistry, Charité-Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt Universität zu Berlin, Berlin, Germany.

Classifications MeSH