Title : Glycoproteomic analysis of human
fibrinogen reveals novel
regions of O-glycosylation
Abstract :
- Human fibrinogen is a 340 kDa, soluble plasma glycoprotein composed of paired sets of three subunits (α, β, γ)
- The protein plays a crucial role in protecting the vascular network against the loss of blood after tissue injury
- The beta and gamma subunits each contain one N-glycosylation site , each of which is occupied by a biantennary N-glycan
- So far O-linked oligosaccharides have rarely been described
- Here, we make use of tryptic- and proteinase K-generated fibrinogen glycopeptides for the detailed analysis of the protein's O-glycosylation by combining information obtained from both one- and two-dimensional nanoLC- ESI-ion trap (IT)-MS approaches
- Glycopeptides were analyzed by ion trap-MS/MS which displayed fragmentations of glycosidic linkages and some peptide backbone cleavages
- MS3 spectra of the generated O-glycopeptides showed cleavages of the peptide backbone and provided essential information on the peptide sequence
- The previously reported N-glycan attachment sites of human fibrinogen could be confirmed
- Moreover, we describe seven novel O-glycosylation regions in human fibrinogen , all occupied by a monosialylated T-antigen
- Our findings may help to improve the general understanding of human fibrinogen in the blood clotting process
Output (sent_index, trigger,
protein,
sugar,
site):
- 1. glycoprotein, , Human fibrinogen, -, -
- 1. glycoprotein, , glycoprotein, -, -
- 3. N-glycosylation, , -, -, site
- 3. occupied, , -, -, site
- 5. glycopeptides, , -, -, glycopeptides
- 7. O-glycopeptides, , -, -, O-glycopeptides
- 8. fibrinogen, , fibrinogen, The previously reported N-glycan attachment sites, -
Output(Part-Of) (sent_index,
protein,
site):
- 3. subunits, site
- 5. proteinase K-generated fibrinogen, glycopeptides
- 9. fibrinogen, regions
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):