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Overview
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Recognizes human myeloperoxidase (MPO), an ~135 glycoprotein expressed in all cells ofthe myeloid linage. MPO functions as an alpha 2 beta 2 heteromultimer consisting of two heavy (alpha ) and two light(beta ) chains of 55 and 15 kDa respectively. MPO is abundantly present in azurophilic granules ofpolymorphonuclear neutrophils (PMNs). It is an important enzyme used during phagocytic lysis ofengulfed foreign particles which takes part in the defense of the organism through production ofhypochlorous acid (HOCl), a potent oxidant. In the stimulated PMN, MPO catalyzes the production ofhypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediatesthat greatly enhance PMN microbicidal activity. Upon activation of neutrophils, MPO can be rapidlyreleased and as such useful in body fluids as marker for inflammatory status. Involvement of MPO hasbeen described in numerous diseases such as atherosclerosis, lung cancer, Alzheimer's disease, inflammatory bowel disease and multiple sclerosis. Autoimmune antibodies to MPO (so called ANCA)are involved in Wegener's disease. Since the discovery of MPO deficiency, initially regarded as rare andrestricted to patients suffering from severe infections, MPO has attracted more clinical attention.
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