Publication details
The potentiation of myeloperoxidase activity by the glycosaminoglycan-dependent binding of myeloperoxidase to proteins of the extracellular matrix
| Authors | |
|---|---|
| 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 | |
| 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. |