Title : Fibrinogen α and β Chain
Abstract :
- The blood clotting protein fibrinogen is known to be N-glycosylated at the β- and γ-chain
- Interestingly, a recent study by Zauner et al. could also show O-glycosylated sites and regions, seven in total, within the molecule (51)
- In the present study O-glycosylation of the fibrinogen alpha region aa524–528 could be confirmed; pinpointing the exact O-glycosylation site was not possible, though (supplemental Fig
- S5, 524GKFPG531, m/z 725.782+)
- Nevertheless, O-glycosylation within the fibrinogen beta region aa58–67 could be confirmed and pinpointed
- Here, the presence of the ETD fragment ions m/z 931.541+, 1300.541+, and 1915.501+, corresponding to z+19, c6, and c12 ions (supplemental Fig
- S6), 54EEAPLRPAPPPIS67, m/z 706.273+) indicates O-glycosylation at the site Ser58
- This contrasts recent findings by Bai et al. who reported the site Ser67 to be O-glycosylated, but not the site Ser58 (76)
- In agreement with previous findings, both fibrinogen O-glycopeptides (524GKFPG531, m/z 725.782+, 54EEAPLRPAPPPIS67, m/z 706.273+), detected in the present study, were found to be decorated with monosialylated T-antigens
- Interestingly, the peptide 54EEAPLRPAPPPIS67 was also found in its nonglycosylated form (HILIC fractions #12-#15, CID, see supplemental Table S2), which suggests only a partial occupation of the O-glycosylation site Ser58
Output (sent_index, trigger,
protein,
sugar,
site):
- 10. O-glycosylation, , -, -, site Ser58
- 2. O-glycosylated, , -, -, sites
- 3. O-glycosylation, , -, -, site
- 7. O-glycosylation, , -, -, Ser58
- 8. O-glycosylated, , -, -, Ser67
- 9. O-glycopeptides, , -, -, O-glycopeptides
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):
- 10. -, -, site Ser58
- 7. -, -, Ser58
- 8. -, -, Ser67