Article
Genotype-dependent N-glycosylation and newly exposed O-glycosylation affect plasmin-induced cleavage of histidine-rich glycoprotein (HRG).
The Journal of biological chemistry - 1 Mar 2024
Zou Yang, Pronker Matti F, Damen J Mirjam A, Heck Albert J R, Reiding Karli R
Abstract excerpt
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...
Topics
- Animals
- Cricetinae
- Humans
- CHO Cells
- Cricetulus
- Fibrinolysin
- Genotype
- Glycosylation
- Polysaccharides
- Protein Isoforms
- Proteins
- Tandem Mass Spectrometry
- Chromatography, High Pressure Liquid
- Histidine-Rich Glycoprotein