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Genotype-dependent N-glycosylation and newly exposed O-glycosylation affect plasmin-induced cleavage of histidine-rich glycoprotein (HRG)

The Journal of biological chemistry, 2024-03, Vol.300 (3), p.105683-105683, Article 105683 [Peer Reviewed Journal]

2024 The Authors ;Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved. ;2024 The Authors 2024 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1016/j.jbc.2024.105683 ;PMID: 38272220

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  • Title:
    Genotype-dependent N-glycosylation and newly exposed O-glycosylation affect plasmin-induced cleavage of histidine-rich glycoprotein (HRG)
  • Author: Zou, Yang ; Pronker, Matti F. ; Damen, J. Mirjam A. ; Heck, Albert J.R. ; Reiding, Karli R.
  • Subjects: Animals ; CHO Cells ; Chromatography, High Pressure Liquid ; Cricetinae ; Cricetulus ; Fibrinolysin - chemistry ; Genotype ; glycoproteomics ; Glycosylation ; HEK293 cells ; histidine-rich glycoprotein ; human plasma ; Humans ; N-glycosylation ; O-glycosylation ; plasmin-induced cleavage ; Polysaccharides - chemistry ; Protein Isoforms ; Proteins ; Tandem Mass Spectrometry
  • Is Part Of: The Journal of biological chemistry, 2024-03, Vol.300 (3), p.105683-105683, Article 105683
  • Description: Histidine-rich glycoprotein (HRG) is an abundant plasma protein harboring at least three N-glycosylation sites. HRG integrates many biological processes, such as coagulation, antiangiogenic activity, and pathogen clearance. Importantly, HRG is known to exhibit five genetic variants with minor allele frequencies of more than 10%. Among them, Pro204Ser can induce a fourth N-glycosylation site (Asn202). Considerable efforts have been made to reveal the biological function of HRG, whereas data on HRG glycosylation are scarcer. To close this knowledge gap, we used C18-based LC–MS/MS to study the glycosylation characteristics of six HRG samples from different sources. We used endogenous HRG purified from human plasma and compared its glycosylation to that of the recombinant HRG produced in Chinese hamster ovary cells or human embryonic kidney 293 cells, targeting distinct genotypic isoforms. In endogenous plasma HRG, every N-glycosylation site was occupied predominantly with a sialylated diantennary complex–type glycan. In contrast, in the recombinant HRGs, all glycans showed different antennarities, sialylation, and core fucosylation, as well as the presence of oligomannose glycans, LacdiNAcs, and antennary fucosylation. Furthermore, we observed two previously unreported O-glycosylation sites in HRG on residues Thr273 and Thr274. These sites together showed more than 90% glycan occupancy in all HRG samples studied. To investigate the potential relevance of HRG glycosylation, we assessed the plasmin-induced cleavage of HRG under various conditions. These analyses revealed that the sialylation of the N- and O-glycans as well as the genotype-dependent N-glycosylation significantly influenced the kinetics and specificity of plasmin-induced cleavage of HRG.
  • Publisher: United States: Elsevier Inc
  • Language: English
  • Identifier: ISSN: 0021-9258
    EISSN: 1083-351X
    DOI: 10.1016/j.jbc.2024.105683
    PMID: 38272220
  • Source: MEDLINE
    PubMed Central
    Alma/SFX Local Collection
    DOAJ Directory of Open Access Journals
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