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The potentiation of myeloperoxidase activity by the glycosaminoglycan-dependent binding of myeloperoxidase to proteins of the extracellular matrix

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The potentiation of myeloperoxidase activity by the glycosaminoglycan-dependent binding of myeloperoxidase to proteins of the extracellular matrix. / Kubala, Lukáš; Kolářová, Hana; Víteček, Jan; Kremserová, Silvie; Klinke, Anna; Lau, Denise; Chapman, Anna L P; Baldus, Stephan; Eiserich, Jason P.

In: Biochim Biophys Acta, Vol. 1830, No. 10, 10.2013, p. 4524-4536.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Kubala, L, Kolářová, H, Víteček, J, Kremserová, S, Klinke, A, Lau, D, Chapman, ALP, Baldus, S & Eiserich, JP 2013, 'The potentiation of myeloperoxidase activity by the glycosaminoglycan-dependent binding of myeloperoxidase to proteins of the extracellular matrix', Biochim Biophys Acta, vol. 1830, no. 10, pp. 4524-4536. https://doi.org/10.1016/j.bbagen.2013.05.024

APA

Kubala, L., Kolářová, H., Víteček, J., Kremserová, S., Klinke, A., Lau, D., Chapman, A. L. P., Baldus, S., & Eiserich, J. P. (2013). The potentiation of myeloperoxidase activity by the glycosaminoglycan-dependent binding of myeloperoxidase to proteins of the extracellular matrix. Biochim Biophys Acta, 1830(10), 4524-4536. https://doi.org/10.1016/j.bbagen.2013.05.024

Vancouver

Kubala L, Kolářová H, Víteček J, Kremserová S, Klinke A, Lau D et al. The potentiation of myeloperoxidase activity by the glycosaminoglycan-dependent binding of myeloperoxidase to proteins of the extracellular matrix. Biochim Biophys Acta. 2013 Oct;1830(10):4524-4536. https://doi.org/10.1016/j.bbagen.2013.05.024

Bibtex

@article{d2fa6207911245018b0f4bc1c5ea9732,
title = "The potentiation of myeloperoxidase activity by the glycosaminoglycan-dependent binding of myeloperoxidase to proteins of the extracellular matrix",
abstract = "BACKGROUND: Myeloperoxidase (MPO) is an abundant hemoprotein expressed by neutrophil granulocytes that is recognized to play an important role in the development of vascular diseases. Upon degranulation from circulating neutrophil granulocytes, MPO binds to the surface of endothelial cells in an electrostatic-dependent manner and undergoes transcytotic migration to the underlying extracellular matrix (ECM). However, the mechanisms governing the binding of MPO to subendothelial ECM proteins, and whether this binding modulates its enzymatic functions are not well understood.METHODS: We investigated MPO binding to ECM derived from aortic endothelial cells, aortic smooth muscle cells, and fibroblasts, and to purified ECM proteins, and the modulation of these associations by glycosaminoglycans. The oxidizing and chlorinating potential of MPO upon binding to ECM proteins was tested.RESULTS: MPO binds to the ECM proteins collagen IV and fibronectin, and this association is enhanced by the pre-incubation of these proteins with glycosaminoglycans. Correspondingly, an excess of glycosaminoglycans in solution during incubation inhibits the binding of MPO to collagen IV and fibronectin. These observations were confirmed with cell-derived ECM. The oxidizing and chlorinating potential of MPO was preserved upon binding to collagen IV and fibronectin; even the potentiation of MPO activity in the presence of collagen IV and fibronectin was observed.CONCLUSIONS: Collectively, the data reveal that MPO binds to ECM proteins on the basis of electrostatic interactions, and MPO chlorinating and oxidizing activity is potentiated upon association with these proteins.GENERAL SIGNIFICANCE: Our findings provide new insights into the molecular mechanisms underlying the interaction of MPO with ECM proteins.",
keywords = "Cells, Cultured, Collagen Type IV/metabolism, Dimerization, Endothelium, Vascular/cytology, Extracellular Matrix Proteins/chemistry, Fibronectins/metabolism, Glycosaminoglycans/metabolism, Humans, Nitrates/metabolism, Oxidative Stress, Peroxidase/metabolism, Protein Binding, Tyrosine/metabolism",
author = "Luk{\'a}{\v s} Kubala and Hana Kol{\'a}{\v r}ov{\'a} and Jan V{\'i}te{\v c}ek and Silvie Kremserov{\'a} and Anna Klinke and Denise Lau and Chapman, {Anna L P} and Stephan Baldus and Eiserich, {Jason P}",
note = "Copyright {\textcopyright} 2013 Elsevier B.V. All rights reserved.",
year = "2013",
month = oct,
doi = "10.1016/j.bbagen.2013.05.024",
language = "English",
volume = "1830",
pages = "4524--4536",
journal = "Biochim Biophys Acta",
issn = "0006-3002",
number = "10",

}

RIS

TY - JOUR

T1 - The potentiation of myeloperoxidase activity by the glycosaminoglycan-dependent binding of myeloperoxidase to proteins of the extracellular matrix

AU - Kubala, Lukáš

AU - Kolářová, Hana

AU - Víteček, Jan

AU - Kremserová, Silvie

AU - Klinke, Anna

AU - Lau, Denise

AU - Chapman, Anna L P

AU - Baldus, Stephan

AU - Eiserich, Jason P

N1 - Copyright © 2013 Elsevier B.V. All rights reserved.

PY - 2013/10

Y1 - 2013/10

N2 - BACKGROUND: Myeloperoxidase (MPO) is an abundant hemoprotein expressed by neutrophil granulocytes that is recognized to play an important role in the development of vascular diseases. Upon degranulation from circulating neutrophil granulocytes, MPO binds to the surface of endothelial cells in an electrostatic-dependent manner and undergoes transcytotic migration to the underlying extracellular matrix (ECM). However, the mechanisms governing the binding of MPO to subendothelial ECM proteins, and whether this binding modulates its enzymatic functions are not well understood.METHODS: We investigated MPO binding to ECM derived from aortic endothelial cells, aortic smooth muscle cells, and fibroblasts, and to purified ECM proteins, and the modulation of these associations by glycosaminoglycans. The oxidizing and chlorinating potential of MPO upon binding to ECM proteins was tested.RESULTS: MPO binds to the ECM proteins collagen IV and fibronectin, and this association is enhanced by the pre-incubation of these proteins with glycosaminoglycans. Correspondingly, an excess of glycosaminoglycans in solution during incubation inhibits the binding of MPO to collagen IV and fibronectin. These observations were confirmed with cell-derived ECM. The oxidizing and chlorinating potential of MPO was preserved upon binding to collagen IV and fibronectin; even the potentiation of MPO activity in the presence of collagen IV and fibronectin was observed.CONCLUSIONS: Collectively, the data reveal that MPO binds to ECM proteins on the basis of electrostatic interactions, and MPO chlorinating and oxidizing activity is potentiated upon association with these proteins.GENERAL SIGNIFICANCE: Our findings provide new insights into the molecular mechanisms underlying the interaction of MPO with ECM proteins.

AB - BACKGROUND: Myeloperoxidase (MPO) is an abundant hemoprotein expressed by neutrophil granulocytes that is recognized to play an important role in the development of vascular diseases. Upon degranulation from circulating neutrophil granulocytes, MPO binds to the surface of endothelial cells in an electrostatic-dependent manner and undergoes transcytotic migration to the underlying extracellular matrix (ECM). However, the mechanisms governing the binding of MPO to subendothelial ECM proteins, and whether this binding modulates its enzymatic functions are not well understood.METHODS: We investigated MPO binding to ECM derived from aortic endothelial cells, aortic smooth muscle cells, and fibroblasts, and to purified ECM proteins, and the modulation of these associations by glycosaminoglycans. The oxidizing and chlorinating potential of MPO upon binding to ECM proteins was tested.RESULTS: MPO binds to the ECM proteins collagen IV and fibronectin, and this association is enhanced by the pre-incubation of these proteins with glycosaminoglycans. Correspondingly, an excess of glycosaminoglycans in solution during incubation inhibits the binding of MPO to collagen IV and fibronectin. These observations were confirmed with cell-derived ECM. The oxidizing and chlorinating potential of MPO was preserved upon binding to collagen IV and fibronectin; even the potentiation of MPO activity in the presence of collagen IV and fibronectin was observed.CONCLUSIONS: Collectively, the data reveal that MPO binds to ECM proteins on the basis of electrostatic interactions, and MPO chlorinating and oxidizing activity is potentiated upon association with these proteins.GENERAL SIGNIFICANCE: Our findings provide new insights into the molecular mechanisms underlying the interaction of MPO with ECM proteins.

KW - Cells, Cultured

KW - Collagen Type IV/metabolism

KW - Dimerization

KW - Endothelium, Vascular/cytology

KW - Extracellular Matrix Proteins/chemistry

KW - Fibronectins/metabolism

KW - Glycosaminoglycans/metabolism

KW - Humans

KW - Nitrates/metabolism

KW - Oxidative Stress

KW - Peroxidase/metabolism

KW - Protein Binding

KW - Tyrosine/metabolism

U2 - 10.1016/j.bbagen.2013.05.024

DO - 10.1016/j.bbagen.2013.05.024

M3 - SCORING: Journal article

C2 - 23707661

VL - 1830

SP - 4524

EP - 4536

JO - Biochim Biophys Acta

JF - Biochim Biophys Acta

SN - 0006-3002

IS - 10

ER -