ArticleRedox biology2018
Peroxidasin-mediated crosslinking of collagen IV is independent of NADPH oxidases.
Article in Redox biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Peroxidasin enables melanoma immune escape by inhibiting natural killer cell cytotoxicity.Molecular oncology · 2026Article
- Machine learning selection of basement membrane-associated genes and development of a predictive model for kidney fibrosis.Scientific reports · 2025Article
- Measuring peroxidasin activity in live cells using bromide addition for signal amplification.Redox biology · 2022Article
- Computational insights into the formation and nature of the sulfilimine bond in collagen-IV.RSC advances · 2022Article
- Mammalian peroxidasin (PXDN): From physiology to pathology.Free radical biology & medicine · 2022Review
- Characterization of the Proprotein Convertase-Mediated Processing of Peroxidasin and Peroxidasin-like Protein.Antioxidants (Basel, Switzerland) · 2021Article
- The hydrogen-peroxide producing NADPH oxidase 4 does not limit neointima development after vascular injury in mice.Redox biology · 2021Article
- Peroxidasin mediates bromination of tyrosine residues in the extracellular matrix.The Journal of biological chemistry · 2020Article
- Peroxidasin-mediated bromine enrichment of basement membranes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Identification of putative biomarkers for Infantile Hemangiomas and Propranolol treatment via data integration.Scientific reports · 2020Article
- Biallelic Deletion ofInternational journal of molecular sciences · 2019Article
- The Relationship of NADPH Oxidases and Heme Peroxidases: Fallin' in and Out.Frontiers in immunology · 2019Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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 H
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Registered trials
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.