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

Varování

Publikace nespadá pod Lékařskou fakultu, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.

Autoři	KUBALA Lukáš KOLÁŘOVÁ Hana VÍTEČEK Jan KREMSEROVÁ Silvie KLINKE Anna LAU Denise CHAPMAN Anna L P BALDUS Stephan EISERICH Jason P
Rok publikování	2013
Druh	Článek v odborném periodiku
Časopis / Zdroj	BBA : Biochimica et biophysica acta : international journal of biochemistry and biophysics.
Fakulta / Pracoviště MU	Přírodovědecká fakulta
Citace
Doi	http://dx.doi.org/10.1016/j.bbagen.2013.05.024
Obor	Genetika a molekulární biologie
Klíčová slova	Endothelium; Enzyme activity; Collagen IV; Fibronectin; Inflammation; Cardiovascular disease
Přiložené soubory	Kubala_BBA_2013.pdf
Popis	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.