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

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Authors	KUBALA Lukáš KOLÁŘOVÁ Hana VÍTEČEK Jan KREMSEROVÁ Silvie KLINKE Anna LAU Denise CHAPMAN Anna L P BALDUS Stephan EISERICH Jason P
Year of publication	2013
Type	Article in Periodical
Magazine / Source	BBA : Biochimica et biophysica acta : international journal of biochemistry and biophysics.
MU Faculty or unit	Faculty of Science
Citation
Doi	http://dx.doi.org/10.1016/j.bbagen.2013.05.024
Field	Genetics and molecular biology
Keywords	Endothelium; Enzyme activity; Collagen IV; Fibronectin; Inflammation; Cardiovascular disease
Attached files	Kubala_BBA_2013.pdf
Description	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.