Myeloperoxidase (MPO) is a heme protein synthesized during myeloid differentiation that constitutes the major component of neutrophil azurophilic granules. Produced as a single chain precursor, myeloperoxidase is subsequently cleaved into a light and heavy chain. The mature myeloperoxidase is a tetramer composed of 2 light chains and 2 heavy chains. This enzyme produces hypohalous acids central to the microbicidal activity of neutrophils. [provided by RefSeq, Nov 2014]
Forensic Context
A study in mice demonstrated that the biomarker MPO, a neutrophil marker, was used in a double immunofluorescent procedure to co-localize with the MPO in contused skeletal muscle, identifying HIPK2+/MPO+ cells with the average ratio of these cells peaking at 1 day post-injury [Zhang et al. DOI:10.14670/HH-18-072]. A study in humans demonstrated that the MPO is a crucial prerequisite for structural remodeling of the myocardium and can contribute to atrial fibrillation development [Liu et al. DOI:10.1371/journal.pone.0044906].