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Journal articles on the topic 'Peroxidasin'

Author: Grafiati

Published: 2 June 2025

Last updated: 31 July 2025

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1

Bathish, Boushra, Martina Paumann-Page, Louise N. Paton, Anthony J. Kettle, and Christine C. Winterbourn. "Peroxidasin mediates bromination of tyrosine residues in the extracellular matrix." Journal of Biological Chemistry 295, no. 36 (2020): 12697–705. http://dx.doi.org/10.1074/jbc.ra120.014504.

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Peroxidasin is a heme peroxidase that oxidizes bromide to hypobromous acid (HOBr), a powerful oxidant that promotes the formation of the sulfilimine crosslink in collagen IV in basement membranes. We investigated whether HOBr released by peroxidasin leads to other oxidative modifications of proteins, particularly bromination of tyrosine residues, in peroxidasin-expressing PFHR9 cells. Using stable isotope dilution LC-MS/MS, we detected the formation of 3-bromotyrosine, a specific biomarker of HOBr-mediated protein modification. The level of 3-bromotyrosine in extracellular matrix proteins from

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2

McCall, A. Scott, Gautam Bhave, Vadim Pedchenko, et al. "Inhibitory Anti-Peroxidasin Antibodies in Pulmonary-Renal Syndromes." Journal of the American Society of Nephrology 29, no. 11 (2018): 2619–25. http://dx.doi.org/10.1681/asn.2018050519.

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BackgroundGoodpasture syndrome (GP) is a pulmonary-renal syndrome characterized by autoantibodies directed against the NC1 domains of collagen IV in the glomerular and alveolar basement membranes. Exposure of the cryptic epitope is thought to occur via disruption of sulfilimine crosslinks in the NC1 domain that are formed by peroxidasin-dependent production of hypobromous acid. Peroxidasin, a heme peroxidase, has significant structural overlap with myeloperoxidase (MPO), and MPO-ANCA is present both before and at GP diagnosis in some patients. We determined whether autoantibodies directed agai

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3

He, Cuiwen, Wenxin Song, Thomas A. Weston, et al. "Peroxidasin-mediated bromine enrichment of basement membranes." Proceedings of the National Academy of Sciences 117, no. 27 (2020): 15827–36. http://dx.doi.org/10.1073/pnas.2007749117.

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Bromine and peroxidasin (an extracellular peroxidase) are essential for generating sulfilimine cross-links between a methionine and a hydroxylysine within collagen IV, a basement membrane protein. The sulfilimine cross-links increase the structural integrity of basement membranes. The formation of sulfilimine cross-links depends on the ability of peroxidasin to use bromide and hydrogen peroxide substrates to produce hypobromous acid (HOBr). Once a sulfilimine cross-link is created, bromide is released into the extracellular space and becomes available for reutilization. Whether the HOBr genera

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4

Kovács, Hajnal A., Enikő Lázár, György Várady, Gábor Sirokmány, and Miklós Geiszt. "Characterization of the Proprotein Convertase-Mediated Processing of Peroxidasin and Peroxidasin-like Protein." Antioxidants 10, no. 10 (2021): 1565. http://dx.doi.org/10.3390/antiox10101565.

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Peroxidasin (PXDN) and peroxidasin-like protein (PXDNL) are members of the peroxidase-cyclooxygenase superfamily. PXDN functions in basement membrane synthesis by forming collagen IV crosslinks, while the function of PXDNL remains practically unknown. In this work, we characterized the post-translational proteolytic processing of PXDN and PXDNL. Using a novel knock-in mouse model, we demonstrate that the proteolytic cleavage of PXDN occurs in vivo. With the help of furin-specific siRNA we also demonstrate that the proprotein-convertase, furin participates in the proteolytic processing of PXDN.

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5

Paumann-Page, Martina, Christian Obinger, Christine C. Winterbourn, and Paul G. Furtmüller. "Peroxidasin Inhibition by Phloroglucinol and Other Peroxidase Inhibitors." Antioxidants 13, no. 1 (2023): 23. http://dx.doi.org/10.3390/antiox13010023.

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Human peroxidasin (PXDN) is a ubiquitous peroxidase enzyme expressed in most tissues in the body. PXDN represents an interesting therapeutic target for inhibition, as it plays a role in numerous pathologies, including cardiovascular disease, cancer and fibrosis. Like other peroxidases, PXDN generates hypohalous acids and free radical species, thereby facilitating oxidative modifications of numerous biomolecules. We have studied the inhibition of PXDN halogenation and peroxidase activity by phloroglucinol and 14 other peroxidase inhibitors. Although a number of compounds on their own potently i

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6

Arnhold, Jürgen, and Ernst Malle. "Halogenation Activity of Mammalian Heme Peroxidases." Antioxidants 11, no. 5 (2022): 890. http://dx.doi.org/10.3390/antiox11050890.

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Mammalian heme peroxidases are fascinating due to their unique peculiarity of oxidizing (pseudo)halides under physiologically relevant conditions. These proteins are able either to incorporate oxidized halides into substrates adjacent to the active site or to generate different oxidized (pseudo)halogenated species, which can take part in multiple (pseudo)halogenation and oxidation reactions with cell and tissue constituents. The present article reviews basic biochemical and redox mechanisms of (pseudo)halogenation activity as well as the physiological role of heme peroxidases. Thyroid peroxida

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7

Colon, Selene, Haiyan Luan, Yan Liu, Cameron Meyer, Leslie Gewin, and Gautam Bhave. "Peroxidasin and eosinophil peroxidase, but not myeloperoxidase, contribute to renal fibrosis in the murine unilateral ureteral obstruction model." American Journal of Physiology-Renal Physiology 316, no. 2 (2019): F360—F371. http://dx.doi.org/10.1152/ajprenal.00291.2018.

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Renal fibrosis is the pathological hallmark of chronic kidney disease (CKD) and manifests as glomerulosclerosis and tubulointerstitial fibrosis. Reactive oxygen species contribute significantly to renal inflammation and fibrosis, but most research has focused on superoxide and hydrogen peroxide (H2O2). The animal heme peroxidases myeloperoxidase (MPO), eosinophil peroxidase (EPX), and peroxidasin (PXDN) uniquely metabolize H2O2 into highly reactive and destructive hypohalous acids, such as hypobromous and hypochlorous acid. However, the role of these peroxidases and their downstream hypohalous

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8

Péterfi, Zalán, Zsuzsanna E. Tóth, Hajnal A. Kovács, et al. "Peroxidasin-like protein: a novel peroxidase homologue in the human heart." Cardiovascular Research 101, no. 3 (2013): 393–99. http://dx.doi.org/10.1093/cvr/cvt256.

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9

Brandes, R. P. "Vascular peroxidase 1/peroxidasin: a complex protein with a simple function?" Cardiovascular Research 91, no. 1 (2011): 1–2. http://dx.doi.org/10.1093/cvr/cvr120.

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10

Dempsey, Bianca, Litiele Cezar Cruz, Marcela Franco Mineiro, Railmara Pereira da Silva, and Flavia Carla Meotti. "Uric Acid Reacts with Peroxidasin, Decreases Collagen IV Crosslink, Impairs Human Endothelial Cell Migration and Adhesion." Antioxidants 11, no. 6 (2022): 1117. http://dx.doi.org/10.3390/antiox11061117.

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Uric acid is considered the main substrate for peroxidases in plasma. The oxidation of uric acid by human peroxidases generates urate free radical and urate hydroperoxide, which might affect endothelial function and explain, at least in part, the harmful effects of uric acid on the vascular system. Peroxidasin (PXDN), the most recent heme-peroxidase described in humans, catalyzes the formation of hypobromous acid, which mediates collagen IV crosslinks in the extracellular matrix. This enzyme has gained increasing scientific interest since it is associated with cardiovascular disease, cancer, a

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11

Cheng, Guangjie, and Ruizheng Shi. "Mammalian peroxidasin (PXDN): From physiology to pathology." Free Radical Biology and Medicine 182 (March 2022): 100–107. http://dx.doi.org/10.1016/j.freeradbiomed.2022.02.026.

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12

Bathish, Bee, Anthony Kettle, and Christine Winterbourn. "Inhibition of Peroxidasin-Mediated Collagen IV Crosslinking." Free Radical Biology and Medicine 87 (October 2015): S109. http://dx.doi.org/10.1016/j.freeradbiomed.2015.10.286.

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13

Soudi, Monika, Martina Paumann-Page, Cedric Delporte, et al. "Multidomain Human Peroxidasin 1 Is a Highly Glycosylated and Stable Homotrimeric High Spin Ferric Peroxidase." Journal of Biological Chemistry 290, no. 17 (2015): 10876–90. http://dx.doi.org/10.1074/jbc.m114.632273.

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14

McAdoo, Stephen P., and Charles D. Pusey. "Peroxidasin—a Novel Autoantigen in Anti-GBM Disease?" Journal of the American Society of Nephrology 29, no. 11 (2018): 2605.2–2607. http://dx.doi.org/10.1681/asn.2018090946.

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15

Papageorgiou, A. P., and S. Heymans. "Peroxidasin-like protein: expanding the horizons of matrix biology." Cardiovascular Research 101, no. 3 (2014): 342–43. http://dx.doi.org/10.1093/cvr/cvu017.

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16

Yan, Xiaohe, Sibylle Sabrautzki, Marion Horsch, et al. "Peroxidasin is essential for eye development in the mouse." Human Molecular Genetics 23, no. 21 (2014): 5597–614. http://dx.doi.org/10.1093/hmg/ddu274.

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17

Nelson, R. E., L. I. Fessler, Y. Takagi, et al. "Peroxidasin: a novel enzyme-matrix protein of Drosophila development." EMBO Journal 13, no. 15 (1994): 3438–47. http://dx.doi.org/10.1002/j.1460-2075.1994.tb06649.x.

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18

Bhave, Gautam, Selene Colon, and Nicholas Ferrell. "The sulfilimine cross-link of collagen IV contributes to kidney tubular basement membrane stiffness." American Journal of Physiology-Renal Physiology 313, no. 3 (2017): F596—F602. http://dx.doi.org/10.1152/ajprenal.00096.2017.

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Basement membranes (BMs), a specialized form of extracellular matrix, underlie nearly all cell layers and provide structural support for tissues and interact with cell surface receptors to determine cell behavior. Both macromolecular composition and stiffness of the BM influence cell-BM interactions. Collagen IV is a major constituent of the BM that forms an extensively cross-linked oligomeric network. Its deficiency leads to BM mechanical instability, as observed with glomerular BM in Alport syndrome. These findings have led to the hypothesis that collagen IV and its cross-links determine BM

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19

Colon, Selene, and Gautam Bhave. "Proprotein Convertase Processing Enhances Peroxidasin Activity to Reinforce Collagen IV." Journal of Biological Chemistry 291, no. 46 (2016): 24009–16. http://dx.doi.org/10.1074/jbc.m116.745935.

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20

Bathish, Bee, Rufus Turner, Tony Kettle, and Christine Winterbourn. "Peroxidasin-Catalysed Oxidative Modifications of Proteins in the Extracellular Matrix." Free Radical Biology and Medicine 100 (November 2016): S19—S20. http://dx.doi.org/10.1016/j.freeradbiomed.2016.10.044.

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21

Costa, Lyndon H., Amrita Dhutia, Charles D. Pusey, Stephen P. McAdoo, and Maria Prendecki. "Identification of Anti-Peroxidasin Antibodies in Human and Experimental Glomerulonephritis." Journal of the American Society of Nephrology 34, no. 11S (2023): 960. http://dx.doi.org/10.1681/asn.20233411s1960c.

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22

Manral, Pallavi, Selene Colon, Gautam Bhave, Ming-Hui Zhao, Sanjay Jain, and Dorin-Bogdan Borza. "Peroxidasin Is a Novel Target of Autoantibodies in Lupus Nephritis." Kidney International Reports 4, no. 7 (2019): 1004–6. http://dx.doi.org/10.1016/j.ekir.2019.04.009.

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23

van der Vliet, Albert, Aida Habibovic, Litiele C. da Cruz, Miklos Geiszt, Vikas Anathy, and Yvonne M. W. Janssen-Heininger. "Oxidative mechanisms in fibrotic disease: From NADPH oxidases to peroxidasin." Free Radical Biology and Medicine 233 (June 2025): S8. https://doi.org/10.1016/j.freeradbiomed.2025.05.032.

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24

Svensson, B. E. "Abilities of peroxidases to catalyse peroxidase-oxidase oxidation of thiols." Biochemical Journal 256, no. 3 (1988): 757–62. http://dx.doi.org/10.1042/bj2560757.

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The abilities of various peroxidases to catalyse the peroxidase-oxidase oxidation of seven aminothiols were studied. Cysteamine and cysteine esters were found to be peroxidase-oxidase substrates for eosinophil peroxidase and myeloperoxidase, whereas other thiols tested were inactive or poorly active with these peroxidases. With lactoperoxidase and horseradish peroxidase, all the tested thiols were inactive or poorly active as peroxidase-oxidase substrates. These studies suggest that a main reason for thiols being poor peroxidase-oxidase substrates is because these thiols are poor peroxidatic s

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25

Sirokmány, Gábor, Hajnal A. Kovács, Enikő Lázár, et al. "Peroxidasin-mediated crosslinking of collagen IV is independent of NADPH oxidases." Redox Biology 16 (June 2018): 314–21. http://dx.doi.org/10.1016/j.redox.2018.03.009.

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26

Bhave, Gautam, Christopher F. Cummings, Roberto M. Vanacore, et al. "Peroxidasin forms sulfilimine chemical bonds using hypohalous acids in tissue genesis." Nature Chemical Biology 8, no. 9 (2012): 784–90. http://dx.doi.org/10.1038/nchembio.1038.

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27

Ma, Chun‐Ping, Zi‐Mu Guo, Feng‐Li Zhang, and Jian‐Ya Su. "Molecular identification, expression and function analysis of peroxidasin in Chilo suppressalis." Insect Science 27, no. 6 (2020): 1173–85. http://dx.doi.org/10.1111/1744-7917.12743.

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28

Paumann-Page, Martina, Rupert Tscheliessnig, Benjamin Sevcnikar, et al. "Monomeric and homotrimeric solution structures of truncated human peroxidasin 1 variants." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1868, no. 1 (2020): 140249. http://dx.doi.org/10.1016/j.bbapap.2019.07.002.

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29

Dougan, Hawsawi, Burton, et al. "Proteomics-Metabolomics Combined Approach Identifies Peroxidasin as a Protector against Metabolic and Oxidative Stress in Prostate Cancer." International Journal of Molecular Sciences 20, no. 12 (2019): 3046. http://dx.doi.org/10.3390/ijms20123046.

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: Peroxidasin (PXDN), a human homolog of Drosophila PXDN, belongs to the family of heme peroxidases and has been found to promote oxidative stress in cardiovascular tissue, however, its role in prostate cancer has not been previously elucidated. We hypothesized that PXDN promotes prostate cancer progression via regulation of metabolic and oxidative stress pathways. We analyzed PXDN expression in prostate tissue by immunohistochemistry and found increased PXDN expression with prostate cancer progression as compared to normal tissue or cells. PXDN knockdown followed by proteomic analysis reveale

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30

Medfai, Hayfa, Alia Khalil, Alexandre Rousseau, et al. "Human peroxidasin 1 promotes angiogenesis through ERK1/2, Akt, and FAK pathways." Cardiovascular Research 115, no. 2 (2018): 463–75. http://dx.doi.org/10.1093/cvr/cvy179.

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31

YAN, X., and J. GRAW. "A mutation in peroxidasin causes microphalmia and anterior segment dysgenesis in mice." Acta Ophthalmologica 90 (August 6, 2012): 0. http://dx.doi.org/10.1111/j.1755-3768.2012.2464.x.

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32

Sitole, Boitumelo Nonhlanhla, and Demetra Mavri-Damelin. "Peroxidasin is regulated by the epithelial-mesenchymal transition master transcription factor Snai1." Gene 646 (March 2018): 195–202. http://dx.doi.org/10.1016/j.gene.2018.01.011.

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33

Hanmer, Kerry L., and Demetra Mavri-Damelin. "Peroxidasin is a novel target of the redox-sensitive transcription factor Nrf2." Gene 674 (October 2018): 104–14. http://dx.doi.org/10.1016/j.gene.2018.06.076.

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34

Ivanov, Sergey V., Kristie L. Rose, Selene Colon, et al. "Identification of brominated proteins in renal extracellular matrix: Potential interactions with peroxidasin." Biochemical and Biophysical Research Communications 681 (November 2023): 152–56. http://dx.doi.org/10.1016/j.bbrc.2023.09.063.

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35

Colon, Selene, and Gautam B. Bhave. "The Loss of Peroxidasin Causes a Sex-Dependent Susceptibility to Vascular Mechanical Injury." Journal of the American Society of Nephrology 33, no. 11S (2022): 164. http://dx.doi.org/10.1681/asn.20223311s1164c.

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36

Sigurdardottir, Anna Karen, Arna Steinunn Jonasdottir, Arni Asbjarnarson, Hildur Run Helgudottir, Thorarinn Gudjonsson, and Gunnhildur Asta Traustadottir. "Peroxidasin Enhances Basal Phenotype and Inhibits Branching Morphogenesis in Breast Epithelial Progenitor Cell Line D492." Journal of Mammary Gland Biology and Neoplasia 26, no. 4 (2021): 321–38. http://dx.doi.org/10.1007/s10911-021-09507-1.

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AbstractThe human breast is composed of terminal duct lobular units (TDLUs) that are surrounded by stroma. In the TDLUs, basement membrane separates the stroma from the epithelial compartment, which is divided into an inner layer of luminal epithelial cells and an outer layer of myoepithelial cells. Stem cells and progenitor cells also reside within the epithelium and drive a continuous cycle of gland remodelling that occurs throughout the reproductive period. D492 is an epithelial cell line originally isolated from the stem cell population of the breast and generates both luminal and myoepith

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37

Kim, Hyun-Kyung, Kyung A. Ham, Seung-Woo Lee, et al. "Biallelic Deletion of Pxdn in Mice Leads to Anophthalmia and Severe Eye Malformation." International Journal of Molecular Sciences 20, no. 24 (2019): 6144. http://dx.doi.org/10.3390/ijms20246144.

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Peroxidasin (PXDN) is a unique peroxidase containing extracellular matrix motifs and stabilizes collagen IV networks by forming sulfilimine crosslinks. PXDN gene knockout in Caenorhabditis elegans (C. elegans) and Drosophila results in the demise at the embryonic and larval stages. PXDN mutations lead to severe eye disorders, including microphthalmia, cataract, glaucoma, and anterior segment dysgenesis in humans and mice. To investigate how PXDN loss of function affects organ development, we generated Pxdn knockout mice by deletion of exon 1 and its 5′ upstream sequences of the Pxdn gene using

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38

Péterfi, Zalán, Ágnes Donkó, Anna Orient, et al. "Peroxidasin Is Secreted and Incorporated into the Extracellular Matrix of Myofibroblasts and Fibrotic Kidney." American Journal of Pathology 175, no. 2 (2009): 725–35. http://dx.doi.org/10.2353/ajpath.2009.080693.

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39

GRAW, J., S. WAGNER, H. FUCHS, and M. HRABE DE ANGELIS. "Mutation in Pxdn encoding peroxidasin causes small lenses and kinky tails in the mouse." Acta Ophthalmologica 89, s248 (2011): 0. http://dx.doi.org/10.1111/j.1755-3768.2011.2221.x.

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40

Li, Yanqing, Yan Jiao, Zhangping Luo, Yang Li, and Yanan Liu. "High peroxidasin-like expression is a potential and independent prognostic biomarker in breast cancer." Medicine 98, no. 44 (2019): e17703. http://dx.doi.org/10.1097/md.0000000000017703.

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41

Sevcnikar, Benjamin, Martina Paumann-Page, Stefan Hofbauer, Vera Pfanzagl, Paul G. Furtmüller, and Christian Obinger. "Reaction of human peroxidasin 1 compound I and compound II with one-electron donors." Archives of Biochemistry and Biophysics 681 (March 2020): 108267. http://dx.doi.org/10.1016/j.abb.2020.108267.

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42

Tindall, Andrew J., Mary Elizabeth Pownall, Ian D. Morris, and Harry V. Isaacs. "Xenopus tropicalis peroxidasin gene is expressed within the developing neural tube and pronephric kidney." Developmental Dynamics 232, no. 2 (2005): 377–84. http://dx.doi.org/10.1002/dvdy.20226.

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43

Lázár, Enikő, Zalán Péterfi, Gábor Sirokmány, et al. "Structure–function analysis of peroxidasin provides insight into the mechanism of collagen IV crosslinking." Free Radical Biology and Medicine 83 (June 2015): 273–82. http://dx.doi.org/10.1016/j.freeradbiomed.2015.02.015.

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44

Thawornkuno, Charin, Kathyleen Nogrado, Poom Adisakwattana, Tipparat Thiangtrongjit, and Onrapak Reamtong. "Identification and profiling of Trichinella spiralis circulating antigens and proteins in sera of mice with trichinellosis." PLOS ONE 17, no. 3 (2022): e0265013. http://dx.doi.org/10.1371/journal.pone.0265013.

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Trichinellosis is a zoonotic disease caused by the ingestion of the Trichinella nematode. With a worldwide incidence of approximately 10,000 cases per year, Trichinella spiralis is responsible for most human infections. There are no specific signs or symptoms of this parasitic infection. Muscle biopsy is the gold diagnostic standard for trichinellosis, but the technique is invasive and unable to detect the early stage of infection. Although immunodiagnostics are also available, antibody detection usually occurs after 3 weeks and prolonged up to 19 years after the acute phase. Therefore, additi

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Sojoodi, Mozhdeh, Derek J. Erstad, Stephen Barrett, et al. "Peroxidasin deficiency re-programs macrophages toward pro-fibrolysis function and promotes collagen resolution in liver." Journal of Hepatology 77 (July 2022): S36. http://dx.doi.org/10.1016/s0168-8278(22)00483-4.

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46

Sojoodi, Mozhdeh, Derek J. Erstad, Stephen C. Barrett, et al. "Peroxidasin Deficiency Re-programs Macrophages Toward Pro-fibrolysis Function and Promotes Collagen Resolution in Liver." Cellular and Molecular Gastroenterology and Hepatology 13, no. 5 (2022): 1483–509. http://dx.doi.org/10.1016/j.jcmgh.2022.01.015.

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47

Shi, Ruizheng, Zehong Cao, Hong Li, et al. "Peroxidasin contributes to lung host defense by direct binding and killing of gram-negative bacteria." PLOS Pathogens 14, no. 5 (2018): e1007026. http://dx.doi.org/10.1371/journal.ppat.1007026.

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48

Bathish, Boushra, Rufus Turner, Martina Paumann-Page, Anthony J. Kettle, and Christine C. Winterbourn. "Characterisation of peroxidasin activity in isolated extracellular matrix and direct detection of hypobromous acid formation." Archives of Biochemistry and Biophysics 646 (May 2018): 120–27. http://dx.doi.org/10.1016/j.abb.2018.03.038.

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49

Cruz, Litiele, Bianca Dempsey, Railmara Silva, and Flavia Meotti. "Laminin is the main brominated protein by hypobromous acid and Peroxidasin in the extracellular matrix." Free Radical Biology and Medicine 192 (November 2022): 120–21. http://dx.doi.org/10.1016/j.freeradbiomed.2022.10.221.

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50

Sojoodi, Mozhdeh, Stephen C. Barrett, Derek J. Erstad, et al. "Abstract 255: Peroxidasin deficiency recruits pro-healing macrophages into the liver and inhibits NAFLD progression to HCC." Cancer Research 82, no. 12_Supplement (2022): 255. http://dx.doi.org/10.1158/1538-7445.am2022-255.

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Abstract Introduction: During liver fibrosis, tissue repair mechanisms replace necrotic tissue with highly stabilized extracellular matrix (ECM) proteins. ECM stabilization influences the speed of tissue recovery. Here, we used a mouse model of nonalcoholic fatty liver disease (NAFLD) to study the function of peroxidasin (PXDN), a peroxidase that uses H2O2 to cross-link collagen IV, during liver fibrosis progression to hepatocellular carcinoma (HCC). Method: Pxdn-/- and Pxdn+/+ mice were fed with a choline-deficient L-amino acid-defined high-fat diet (CDAHFD) for 16 weeks to create a NAFLD-HCC

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