The glycosylation of myeloperoxidase.
The enzyme myeloperoxidase (MPO) is an important part of the neutrophil immune reaction and can be found in alfa granula. The presence of MPO can be used to distinguish acute myelogenous leukemia from acute lymphocytic leukemia. However, the methods employed to do so, such as flow cytometry and immunohistochemistry rely on antibody recognition, and therefore the characterization of the mature MPO, including post-translational modifications, must be considered as important as epitope mapping. MPO has 5 N-linked glycosylation sites, occupied by both high mannose and complex glycan structures. In this study we utilize intact glycopeptide MSMS analysis for site specific characterization of the glycan structures of MPO from a cancer patient. The identified glycan structures are compared to those of MPO from healthy donors, in order to probe for any potential differences that may have diagnostic use.
Ravnsborg
Tina
T
Institute of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark.
Houen
Gunnar
G
Højrup
Peter
P
D000595:Amino Acid Sequence; D018604:Epitope Mapping; D005434:Flow Cytometry; D006031:Glycosylation; D006801:Humans; D008214:Lymphocytes / Q000378:metabolism; D008969:Molecular Sequence Data; D009504:Neutrophils / Q000378:metabolism; D009195:Peroxidase / Q000737:chemistry* / Q000302:isolation & purification; D011134:Polysaccharides / Q000032:analysis*; D011499:Protein Processing, Post-Translational; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D011134:Polysaccharides; D009195:Peroxidase