Title : Myeloperoxidase mediated alteration of endothelial function is dependent on its cationic charge.

Pub. Date : 2021 Jan

PMID : 33271281






4 Functional Relationships(s)
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1 Moreover, interaction of MPO, which is carrying a cationic charge, with anionic glycosaminoglycans (GAGs) resulted in reduction of their relative charge. Glycosaminoglycans myeloperoxidase Homo sapiens
2 Moreover, interaction of MPO, which is carrying a cationic charge, with anionic glycosaminoglycans (GAGs) resulted in reduction of their relative charge. Glycosaminoglycans myeloperoxidase Homo sapiens
3 By means of micro-viscometry and atomic force microscopy, we disclosed that MPO can crosslink GAG chains. Glycosaminoglycans myeloperoxidase Homo sapiens
4 Altogether, these findings provide evidence that MPO through interaction with GAGs modulates overall charge of the GLX, causing modification of its structure and thus affecting EC function. Glycosaminoglycans myeloperoxidase Homo sapiens