Myeloperoxidase fragments reacting with serum from a patient with myeloperoxidase-anti-neutrophil cytoplasmic antibody-positive glomerulonephritis
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Myeloperoxidase (MPO) participates in the protection against bacterial infections. This molecule is recognized with an autoantibody, P-ANCA (antineutrophil cytoplasmic antibody with a perinuclear staining pattern). It has been widely detected in certain diseases including vasculitis and crescentic glomerulonephritis. We describe the epitope of MPO recognized by the antibody. Four sera, which were selected from 75 MPO-ANCA positive sera, reacted with the large 59-kDa subunit of MPO, but not with the small 14-kDa subunit. One of the 4 sera reacted with 55-kDa, 34-kDa and 19-kDa deglycosylated forms derived from the 59-kDa large subunit of MPO by treatment with endoglycosidase-H (Endo-H). This serum did not react with 38-kDa or 23-kDa peptides from the large subunit which had not undergone Endo-H treatment, whereas 42-kDa and 40-kDa peptides treated with or without Endo-H, or with heat and nagase, weakly reacted with the serum. These results suggest that the recognition site in the MPO molecule by an anti-MPO serum is adjacent to sites of sugar attachment, which are located on the periphery in the upstream of Mef409 of the large MPO subunit.
Key wordsneutrophils myeloperoxidase autoantibodies to neutrophil glomerulonephritis chronic rheumatoid arthritis
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