Peroxidasin protein expression and enzymatic activity in metastatic melanoma cell lines are associated with invasive potential
Peroxidasin, a heme peroxidase, has been shown to play a role in cancer progression. mRNA expression has been reported to be upregulated in metastatic melanoma cell lines and connected to the invasive phenotype, but little is known about how peroxidasin acts in cancer cells. We have analyzed peroxid...
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doaj-ecab46f1afd042139dc822be8320f9652021-09-21T04:09:20ZengElsevierRedox Biology2213-23172021-10-0146102090Peroxidasin protein expression and enzymatic activity in metastatic melanoma cell lines are associated with invasive potentialMartina Paumann-Page0Nikolaus F. Kienzl1Jyoti Motwani2Boushra Bathish3Louise N. Paton4Nicholas J. Magon5Benjamin Sevcnikar6Paul G. Furtmüller7Michael W. Traxlmayr8Christian Obinger9Mike R. Eccles10Christine C. Winterbourn11Centre for Free Radical Research, Department of Pathology and Biomedical Science, University of Otago Christchurch, P.O. Box 4345, Christchurch, New Zealand; Corresponding author.Department of Chemistry, Institute of Biochemistry, University of Natural Resources and Life Sciences, 1190, Vienna, AustriaDepartment of Pathology, Dunedin School of Medicine, University of Otago, 270 Great King Street, Dunedin, 9054, New ZealandCentre for Free Radical Research, Department of Pathology and Biomedical Science, University of Otago Christchurch, P.O. Box 4345, Christchurch, New ZealandCentre for Free Radical Research, Department of Pathology and Biomedical Science, University of Otago Christchurch, P.O. Box 4345, Christchurch, New ZealandCentre for Free Radical Research, Department of Pathology and Biomedical Science, University of Otago Christchurch, P.O. Box 4345, Christchurch, New ZealandDepartment of Chemistry, Institute of Biochemistry, University of Natural Resources and Life Sciences, 1190, Vienna, AustriaDepartment of Chemistry, Institute of Biochemistry, University of Natural Resources and Life Sciences, 1190, Vienna, AustriaDepartment of Chemistry, Institute of Biochemistry, University of Natural Resources and Life Sciences, 1190, Vienna, AustriaDepartment of Chemistry, Institute of Biochemistry, University of Natural Resources and Life Sciences, 1190, Vienna, AustriaDepartment of Pathology, Dunedin School of Medicine, University of Otago, 270 Great King Street, Dunedin, 9054, New ZealandCentre for Free Radical Research, Department of Pathology and Biomedical Science, University of Otago Christchurch, P.O. Box 4345, Christchurch, New ZealandPeroxidasin, a heme peroxidase, has been shown to play a role in cancer progression. mRNA expression has been reported to be upregulated in metastatic melanoma cell lines and connected to the invasive phenotype, but little is known about how peroxidasin acts in cancer cells. We have analyzed peroxidasin protein expression and activity in eight metastatic melanoma cell lines using an ELISA developed with an in-house peroxidasin binding protein. RNAseq data analysis confirmed high peroxidasin mRNA expression in the five cell lines classified as invasive and low expression in the three non-invasive cell lines. Protein levels of peroxidasin were higher in the cell lines with an invasive phenotype. Active peroxidasin was secreted to the cell culture medium, where it accumulated over time, and peroxidasin protein levels in the medium were also much higher in invasive than non-invasive cell lines. The only well-established physiological role of peroxidasin is in the formation of a sulfilimine bond, which cross-links collagen IV in basement membranes via catalyzed oxidation of bromide to hypobromous acid. We found that peroxidasin secreted from melanoma cells formed sulfilimine bonds in uncross-linked collagen IV, confirming peroxidasin activity and hypobromous acid formation. Moreover, 3-bromotyrosine, a stable product of hypobromous acid reacting with tyrosine residues, was detected in invasive melanoma cells, substantiating that their expression of peroxidasin generates hypobromous acid, and showing that it does not exclusively react with collagen IV, but also with other biomolecules.http://www.sciencedirect.com/science/article/pii/S2213231721002494PeroxidasinMetastatic melanomaHypobromous acidBromotyrosineCollagen IV cross-linking |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Martina Paumann-Page Nikolaus F. Kienzl Jyoti Motwani Boushra Bathish Louise N. Paton Nicholas J. Magon Benjamin Sevcnikar Paul G. Furtmüller Michael W. Traxlmayr Christian Obinger Mike R. Eccles Christine C. Winterbourn |
spellingShingle |
Martina Paumann-Page Nikolaus F. Kienzl Jyoti Motwani Boushra Bathish Louise N. Paton Nicholas J. Magon Benjamin Sevcnikar Paul G. Furtmüller Michael W. Traxlmayr Christian Obinger Mike R. Eccles Christine C. Winterbourn Peroxidasin protein expression and enzymatic activity in metastatic melanoma cell lines are associated with invasive potential Redox Biology Peroxidasin Metastatic melanoma Hypobromous acid Bromotyrosine Collagen IV cross-linking |
author_facet |
Martina Paumann-Page Nikolaus F. Kienzl Jyoti Motwani Boushra Bathish Louise N. Paton Nicholas J. Magon Benjamin Sevcnikar Paul G. Furtmüller Michael W. Traxlmayr Christian Obinger Mike R. Eccles Christine C. Winterbourn |
author_sort |
Martina Paumann-Page |
title |
Peroxidasin protein expression and enzymatic activity in metastatic melanoma cell lines are associated with invasive potential |
title_short |
Peroxidasin protein expression and enzymatic activity in metastatic melanoma cell lines are associated with invasive potential |
title_full |
Peroxidasin protein expression and enzymatic activity in metastatic melanoma cell lines are associated with invasive potential |
title_fullStr |
Peroxidasin protein expression and enzymatic activity in metastatic melanoma cell lines are associated with invasive potential |
title_full_unstemmed |
Peroxidasin protein expression and enzymatic activity in metastatic melanoma cell lines are associated with invasive potential |
title_sort |
peroxidasin protein expression and enzymatic activity in metastatic melanoma cell lines are associated with invasive potential |
publisher |
Elsevier |
series |
Redox Biology |
issn |
2213-2317 |
publishDate |
2021-10-01 |
description |
Peroxidasin, a heme peroxidase, has been shown to play a role in cancer progression. mRNA expression has been reported to be upregulated in metastatic melanoma cell lines and connected to the invasive phenotype, but little is known about how peroxidasin acts in cancer cells. We have analyzed peroxidasin protein expression and activity in eight metastatic melanoma cell lines using an ELISA developed with an in-house peroxidasin binding protein. RNAseq data analysis confirmed high peroxidasin mRNA expression in the five cell lines classified as invasive and low expression in the three non-invasive cell lines. Protein levels of peroxidasin were higher in the cell lines with an invasive phenotype. Active peroxidasin was secreted to the cell culture medium, where it accumulated over time, and peroxidasin protein levels in the medium were also much higher in invasive than non-invasive cell lines. The only well-established physiological role of peroxidasin is in the formation of a sulfilimine bond, which cross-links collagen IV in basement membranes via catalyzed oxidation of bromide to hypobromous acid. We found that peroxidasin secreted from melanoma cells formed sulfilimine bonds in uncross-linked collagen IV, confirming peroxidasin activity and hypobromous acid formation. Moreover, 3-bromotyrosine, a stable product of hypobromous acid reacting with tyrosine residues, was detected in invasive melanoma cells, substantiating that their expression of peroxidasin generates hypobromous acid, and showing that it does not exclusively react with collagen IV, but also with other biomolecules. |
topic |
Peroxidasin Metastatic melanoma Hypobromous acid Bromotyrosine Collagen IV cross-linking |
url |
http://www.sciencedirect.com/science/article/pii/S2213231721002494 |
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