ArticleMatrix biology : journal of the International Society for Matrix Biology2010
Myeloperoxidase-derived oxidants selectively disrupt the protein core of the heparan sulfate proteoglycan perlecan.
Article in Matrix biology : journal of the International Society for Matrix Biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 64 citations in OpenAlex.
- Nox4 and circulating free MPO synergistically promote aortic aneurysm formation.Scientific reports · 2026Article
- Isoform-specific oxidative modifications of tropoelastin by HOCl and MPO alter protein self-assembly.Redox report : communications in free radical research · 2025Article
- Intercellular communication from myotubes to fibroblasts is differentially impacted by mineralocorticoid receptor signaling and muscular dystrophy.Cell communication and signaling : CCS · 2025Article
- Oxidative stress: fundamentals and advances in quantification techniques.Frontiers in chemistry · 2024Review
- Mechanism of peroxidasin inactivation in hyperglycemia: Heme damage by reactive oxygen species.Biochemical and biophysical research communications · 2023Article
- Hypochlorous Acid and Chloramines Induce Specific Fragmentation and Cross-Linking of the G1-IGD-G2 Domains of Recombinant Human Aggrecan, and Inhibit ADAMTS1 Activity.Antioxidants (Basel, Switzerland) · 2023Article
- Activation and Inhibition of Human Matrix Metalloproteinase-9 (MMP9) by HOCl, Myeloperoxidase and Chloramines.Antioxidants (Basel, Switzerland) · 2022Article
- Halogenation Activity of Mammalian Heme Peroxidases.Antioxidants (Basel, Switzerland) · 2022Review
- Sirtuins and Sepsis: Cross Talk between Redox and Epigenetic Pathways.Antioxidants (Basel, Switzerland) · 2021Review
- Article
- Modification of gingival proteoglycans by reactive oxygen species: potential mechanism of proteoglycan degradation during periodontal diseases.Free radical research · 2021Article
- The Dual Role of Myeloperoxidase in Immune Response.International journal of molecular sciences · 2020Review
- Myeloperoxidase-derived damage to human plasma fibronectin: Modulation by protein binding and thiocyanate ions (SCNRedox biology · 2020Article
- Binding of myeloperoxidase to the extracellular matrix of smooth muscle cells and subsequent matrix modification.Scientific reports · 2020Article
- Analysis of protein chlorination by mass spectrometry.Redox biology · 2019Article
- Chlorination and oxidation of the extracellular matrix protein laminin and basement membrane extracts by hypochlorous acid and myeloperoxidase.Redox biology · 2019Article
- Chlorination and oxidation of human plasma fibronectin by myeloperoxidase-derived oxidants, and its consequences for smooth muscle cell function.Redox biology · 2018Article
- Role of Hypohalous Acids in Basement Membrane Homeostasis.Antioxidants & redox signaling · 2017Review
- Inhibition of myeloperoxidase at the peak of experimental autoimmune encephalomyelitis restores blood-brain barrier integrity and ameliorates disease severity.Journal of neurochemistry · 2016Article
- The Ancient Immunoglobulin Domains of Peroxidasin Are Required to Form Sulfilimine Cross-links in Collagen IV.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 3 countries.
Funding
Abstract
The potent oxidants hypochlorous acid (HOCl) and hypobromous acid (HOBr) are produced extracellularly by myeloperoxidase, following release of this enzyme from activated leukocytes. The subendothelial extracellular matrix is a key site for deposition of myeloperoxidase and damage by myeloperoxidase-derived oxidants, with this damage implicated in the impairment of vascular cell function during acute inflammatory responses and chronic inflammatory diseases such as atherosclerosis. The heparan sulfate proteoglycan perlecan, a key component of the subendothelial extracellular matrix, regulates important cellular processes and is a potential target for HOCl and HOBr. It is shown here that perlecan binds myeloperoxidase via its heparan sulfate side chains and that this enhances oxidative damage by myeloperoxidase-derived HOCl and HOBr. This damage involved selective degradation of the perlecan protein core without detectable alteration of its heparan sulfate side chains, despite the presence of reactive GlcNH(2) residing within this glycosaminoglycan. Modification of the protein core by HOCl and HOBr (measured by loss of immunological recognition of native protein epitopes and the appearance of oxidatively-modified protein epitopes) was associated with an impairment of its ability to support endothelial cell adhesion, with this observed at a pathologically-achievable oxidant dose of 425nmol oxidant/mg protein. In contrast, the heparan sulfate chains of HOCl/HOBr-modified perlecan retained their ability to bind FGF-2 and collagen V and were able to promote FGF-2-dependent cellular proliferation. Collectively, these data highlight the potential role of perlecan oxidation, and consequent deregulation of cell function, in vascular injuries by myeloperoxidase-derived HOCl and HOBr.
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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.