Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91 phox
Open accessAbstract
High molecular weight homologues of gp91phox, the superoxide-generating subunit of phagocyte nicotinamide adenine dinucleotide phosphate (NADPH)-oxidase, have been identified in human (h) and Caenorhabditis elegans (Ce), and are termed Duox for “dual oxidase” because they have both a peroxidase homology domain and a gp91phox domain. A topology model predicts that the enzyme will utilize cytosolic NADPH to generate reactive oxygen, but the function of the ecto peroxidase domain was unknown. Ce-Duox1 is expressed in hypodermal cells underlying the cuticle of larval animals. To investigate function, RNA interference (RNAi) was carried out in C. elegans. RNAi animals showed complex phenotypes similar to those described previously in mutations in collagen biosynthesis that are known to affect the cuticle, an extracellular matrix. Electron micrographs showed gross abnormalities in the cuticle of RNAi animals. In cuticle, collagen and other proteins are cross-linked via di- and trityrosine linkages, and these linkages were absent in RNAi animals. The expressed peroxidase domains of both Ce-Duox1 and h-Duox showed peroxidase activity and catalyzed cross-linking of free tyrosine ethyl ester. Thus, Ce-Duox catalyzes the cross-linking of tyrosine residues involved in the stabilization of cuticular extracellular matrix.
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DUOX1 and 2 have a similar architecture to NOX5 and include an additional transmembrane domain connected to a putative extracellular peroxidase domain.
“DUOX1 and 2 have a similar architecture to NOX5 and include an additional transmembrane domain connected to a putative extracellular peroxidase domain (262).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [262]
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- Authors
- Edens, W. A., Sharling, L., Cheng, G., Shapira, R., Kinkade, J. M., Lee, T., Edens, H. A., Tang, X., Sullards, C., Flaherty, D. B., Benian, G. M., & Lambeth, J. D.
- Affiliations
- Emory University (US)
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2001-08-20
- Volume
- 154
- Issue
- 4
- Pages
- 879-892
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2196470
- OpenAlex
- W2136261717
- Cited by
- 375
- References
- 67
- Citations by year
- 2026: 3 · 2025: 9 · 2024: 4 · 2023: 20 · 2022: 8 · 2021: 17 · 2020: 12 · 2019: 18 · 2018: 13 · 2017: 16 · 2016: 14 · 2015: 12 · 2014: 20 · 2013: 19 · 2012: 18
- FWCI
- 4.19
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA-84138, R01CA084138)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK07298, T32DK007298)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR/GM-44419)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Skin and Cellular Biology Research
- Keywords
- dual oxidase, extracellular matrix cross-linking, cuticle, collagen cross-linking, peroxidase activity, NADPH oxidase, RNA interference, subcutaneous tissue
- MeSH terms
- Dual Oxidases, NADPH Oxidase 2, Amino Acid Sequence, Animals, Cloning, Molecular, Extracellular Matrix, Flavoproteins, Humans, Membrane Glycoproteins, Models, Biological, Models, Molecular, Molecular Sequence Data, Phagocytes, Tissue Distribution, Mutagenesis, Caenorhabditis elegans, Sequence Homology, Amino Acid, Protein Structure, Tertiary, DNA, Complementary, NADPH Oxidases
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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