Background
Myeloperoxidase (MPO) is a hemecontaining enzyme belonging to the XPO subfamily of peroxidases. It is an abundant neutrophil and monocyte glycoprotein that catalyzes the hydrogen peroxidedependent conversion of chloride, bromide, and iodide to multiple reactive species. MPO activity results in protein nitrosylation and the formation of 3-chlorotyrosine and dityrosine crosslinks. Modification of ApoB100, as well as the lipid and cholesterol components of LDL and HDL, promotes the development of atherosclerosis. MPO is also associated with a variety of other diseases, and inhibits vasodilation in inflammation by depleting the levels of NO. Serum albumin functions as a carrier protein during MPO movement to the basolateral side of epithelial cells. MPO is stored in neutrophil azurophilic granules. Upon cellular activation, it is deposited into pathogencontaining phagosomes. While mice lacking MPO are impaired in clearing select microbial infections,MPO deficiency in humans does not necessarily result in heightened susceptibility to infections.
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