Background
Myeloperoxidase (MPO) is a heme-containing
enzyme belonging to the XPO subfamily of peroxidases. It is an abundant neutrophil and monocyte glycoprotein that
catalyzes the hydrogen peroxide-dependent
conversion of chloride, bromide, and iodide to multiple reactive species. Post-translational
processing of MPO involves
the insertion of a heme moiety and the proteolytic removal of both a propeptide and a 6 aa internal peptide. This results in a disulfide-linked
dimer composed of a
60 kDa heavy and 12 kDa light chain that associate into a 150 kDa enzymatically active tetramer. The tetramer contains two heme groups and one disulfide bond
between the heavy chains. Alternate splicing generates two additional isoforms of MPO, one with a 32 aa insertion in the light chain, and another with a deletion of
the signal sequence and part of the propeptide. Human and mouse MPO share 87% aa sequence identity. MPO activity results in protein nitrosylation and the
formation of 3-chlorotyrosine
and dityrosine crosslinks. 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 pathogen-containing
phagosomes.
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