Myeloperoxidase (MPO; non recombinant)
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Idiopathic Crescentic Glomerulonephritis
Classic Panarteritis Nodosa
Myeloperoxidase (MPO) is an enzyme from the granula of neutrophil granulocytes. A complicated sequence of processing steps (which preclude recombinant production) converts a 80 kDa initial translation product to the mature enzyme which consists of two 64 kDa heavy chains and two 13 kDa light chains. MPO derives its characteristic green color from a unique "green heme" cofactor. The peroxidase activity of MPO generates hypochlorite which acts to kill microbes and to inactivate inhibitors of lytic enzymes which the neutrophil leukocytes releases to degrade material in their vicinity.
MPO is an autoantigen in a number of vasculitides, inflammatory autoimmune diseases of the vasculature, which can be classified depending on the affected type of blood vessel. Vasculitides showing high prevalences and clinical association with anti-MPO autoantibodies are microscopic polyangiitis, Churg-Strauss syndrome, classic panarteriitis nodosa, or idiopathic crescentic glomerulonephritis. Immunofluorescence on fixed neutrophils classically detects anti-MPO autoantibodies by a so-called p-ANCA staining pattern. With the availability of purified MPO antigen ELISA, line or multiplex assays offer diagnostic alternatives to the demanding immunofluorescence approach.
Human native myeloperoxidase is purified from DIARECT from polymorphonuclear leukocytes of peripheral human blood