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The potentiation of myeloperoxidase activity by the glycosaminoglycan-dependent binding of myeloperoxidase to proteins of the extracellular matrix
Autoři | |
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Rok publikování | 2013 |
Druh | Článek v odborném periodiku |
Časopis / Zdroj | BBA : Biochimica et biophysica acta : international journal of biochemistry and biophysics. |
Fakulta / Pracoviště MU | |
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 | |
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. |