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Peroxidasin-mediated crosslinking of collagen IV is independent of NADPH oxidases

Sirokmány, Gábor and Kovács, Hajnal A. and Lázár, Enikő and Kónya, Krisztina and Donkó, Ágnes and Enyedi, Balázs and Grasberger, Helmut and Geiszt, Miklós (2018) Peroxidasin-mediated crosslinking of collagen IV is independent of NADPH oxidases. REDOX BIOLOGY, 16. pp. 314-321. ISSN 2213-2317

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Abstract

Collagen IV is a major component of the basement membrane in epithelial tissues. The NC1 domains of collagen IV protomers are covalently linked together through sulfilimine bonds, the formation of which is catalyzed by peroxidasin. Although hydrogen peroxide is essential for this reaction, the exact source of the oxidant remains elusive. Members of the NOX/DUOX NADPH oxidase family are specifically devoted to the production of superoxide and hydrogen peroxide. Our aim in this study was to find out if NADPH oxidases contribute in vivo to the formation of collagen IV sulfilimine crosslinks. We used multiple genetically modified in vivo model systems to provide a detailed assessment of this question. Our data indicate that in various peroxidasin-expressing tissues sulfilimine crosslinks between the NC1 domains of collagen IV can be readily detected in the absence of functioning NADPH oxidases. We also analyzed how subatmospheric oxygen levels influence the collagen IV network in collagen-producing cultured cells with rapid matrix turnover. We showed that collagen IV crosslinks remain intact even under strongly hypoxic conditions. Our hypothesis is that during collagen IV network formation PXDN cooperates with a NOX/DUOX-independent H2O2 source that is functional also at very low ambient oxygen levels. © 2018

Item Type: Article
Uncontrolled Keywords: sulfilimine; Peroxidasin; NADPH OXIDASE; Hydrogen Peroxide; Collagen IV
Subjects: Q Science / természettudomány > QH Natural history / természetrajz > QH301 Biology / biológia > QH3015 Molecular biology / molekuláris biológia
SWORD Depositor: MTMT SWORD
Depositing User: MTMT SWORD
Date Deposited: 03 Apr 2018 14:21
Last Modified: 03 Apr 2018 14:21
URI: http://real.mtak.hu/id/eprint/78940

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