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 - Článek v odborném periodiku
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
Grant CEP: GA ČR(CZ) GCP305/12/J038
Grant ostatní: GA MŠk(CZ) ED1.100/02/0123
Výzkumný záměr: CEZ:AV0Z50040702
Institucionální podpora: RVO:68081707
Klíčová slova: Endothelium * Enzyme activity * Collagen IV
Kód oboru RIV: BO - Biofyzika
Impakt faktor: 3.829, rok: 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.
Trvalý link: http://hdl.handle.net/11104/0226771