Neutrophil myeloperoxidase harbors distinct site-specific peculiarities in its glycosylation.
MPO
anti-neutrophil cytoplasmic autoantibody (ANCA)
autoimmune disease
glycoproteomics
glycosylation
mannose-6-phosphate (M6P)
mass spectrometry (MS)
myeloperoxidase
neutrophil
paucimannose
phosphomannose
self-antigen
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
27 12 2019
27 12 2019
Historique:
received:
18
09
2019
revised:
08
11
2019
pubmed:
14
11
2019
medline:
23
6
2020
entrez:
14
11
2019
Statut:
ppublish
Résumé
Anti-neutrophil cytoplasmic autoantibodies (ANCAs) are directed against lysosomal components of neutrophils. ANCAs directed to proteinase 3 and myeloperoxidase (MPO) in particular are associated with distinct forms of small vessel vasculitides. MPO is an abundant neutrophil-derived heme protein that is part of the antimicrobial defense system. The protein is typically present in the azurophilic granules of neutrophils, but a large portion may also enter the extracellular space. It remains unclear why MPO is frequently the target of antibody-mediated autoimmune responses. MPO is a homodimeric glycoprotein, posttranslationally modified with complex sugars at specific sites. Glycosylation can strongly influence protein function, affecting its folding, receptor interaction, and backbone accessibility. MPO potentially can be heavily modified as it harbors 5 putative
Identifiants
pubmed: 31719144
pii: S0021-9258(20)30039-9
doi: 10.1074/jbc.RA119.011098
pmc: PMC6937560
doi:
Substances chimiques
Glycopeptides
0
Polysaccharides
0
Peroxidase
EC 1.11.1.7
Mannose
PHA4727WTP
Banques de données
PDB
['1CXP']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
20233-20245Informations de copyright
© 2019 Reiding et al.
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