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Peroxidasin forms sulfilimine chemical bonds using hypohalous acids in tissue genesis
- Source :
- Nature Chemical Biology. 8:784-790
- Publication Year :
- 2012
- Publisher :
- Springer Science and Business Media LLC, 2012.
-
Abstract
- Collagen IV comprises the predominant protein network of basement membranes, a specialized extracellular matrix, which underlie epithelia and endothelia. These networks assemble through oligomerization and covalent crosslinking to endow mechanical strength and shape cell behavior through interactions with cell-surface receptors. A recently discovered sulfilimine (S=N) bond between a methionine sulfur and hydroxylysine nitrogen reinforces the collagen IV network. We demonstrate that peroxidasin, an enzyme found in basement membranes, catalyzes formation of the sulfilimine bond. Drosophila peroxidasin mutants have disorganized collagen IV networks and torn visceral muscle basement membranes, pointing to a critical role for the enzyme in tissue biogenesis. Peroxidasin generates hypohalous acids as reaction intermediates, suggesting a paradoxically anabolic role for these usually destructive oxidants. This work highlights sulfilimine bond formation as what is to our knowledge the first known physiologic function for peroxidasin, a role for hypohalous oxidants in tissue biogenesis, and a possible role for peroxidasin in inflammatory diseases.
- Subjects :
- Collagen Type IV
chemistry.chemical_classification
Extracellular Matrix Proteins
Cell Biology
Sulfilimine
Biology
Catalysis
Article
Extracellular matrix
Hydroxylysine
chemistry.chemical_compound
Membrane
Enzyme
chemistry
Biochemistry
Covalent bond
Animals
Drosophila
Imines
Acids
Molecular Biology
Biogenesis
Function (biology)
Peroxidase
Subjects
Details
- ISSN :
- 15524469 and 15524450
- Volume :
- 8
- Database :
- OpenAIRE
- Journal :
- Nature Chemical Biology
- Accession number :
- edsair.doi.dedup.....13fcd3e5ca8a499f5ce703c69a5954c7