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

0399439 - BFÚ 2014 RIV NL eng J - Journal Article
Kubala, Lukáš - Kolářová, Hana - Víteček, Jan - Kremserová, Silvie - Klinke, A. - Lau, D. - Chapman, A.L.P. - Baldus, S. - Eiserich, J.P.
The potentiation of myeloperoxidase activity by the glycosaminoglycan-dependent binding of myeloperoxidase to proteins of the extracellular matrix.
Biochimica et Biophysica Acta-General Subjects. Roč. 1830, č. 10 (2013), s. 4524-4536. ISSN 0304-4165. E-ISSN 1872-8006
R&D Projects: GA ČR(CZ) GCP305/12/J038
Grant - others:GA MŠk(CZ) ED1.100/02/0123
Institutional research plan: CEZ:AV0Z50040702
Institutional support: RVO:68081707
Keywords : Endothelium * Enzyme activity * Collagen IV
Subject RIV: BO - Biophysics
Impact factor: 3.829, year: 2013

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. observed.
Permanent Link: http://hdl.handle.net/11104/0226771