Title : Heparins increase endothelial nitric oxide bioavailability by liberating vessel-immobilized myeloperoxidase.

Pub. Date : 2006 Apr 18

PMID : 16606792






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Heparins increase endothelial nitric oxide bioavailability by liberating vessel-immobilized myeloperoxidase. Nitric Oxide myeloperoxidase Homo sapiens
2 MPO binds to and transcytoses endothelial cells in a glycosaminoglycan-dependent manner, and MPO binding to the vessel wall is a prerequisite for MPO-dependent oxidation of endothelium-derived nitric oxide (NO) and impairment of endothelial function in animal models. Nitric Oxide myeloperoxidase Homo sapiens
3 MPO binds to and transcytoses endothelial cells in a glycosaminoglycan-dependent manner, and MPO binding to the vessel wall is a prerequisite for MPO-dependent oxidation of endothelium-derived nitric oxide (NO) and impairment of endothelial function in animal models. Nitric Oxide myeloperoxidase Homo sapiens
4 MPO binds to and transcytoses endothelial cells in a glycosaminoglycan-dependent manner, and MPO binding to the vessel wall is a prerequisite for MPO-dependent oxidation of endothelium-derived nitric oxide (NO) and impairment of endothelial function in animal models. Nitric Oxide myeloperoxidase Homo sapiens