Publication details

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

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
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.

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