PMID: PMC4256492-2-3

 

    Legend: Gene, Sites

Title : Concluding Remarks

Abstract :

1. The mass spectrometric site-specific glycopeptide characterization performed in this study mapped the glycosylation profile of lubricin within the STP-rich region and indicates that lubricin glycosylation displays both micro- and macroheterogeneity
2. The presence of two adjacent simultaneously glycosylated Thr residues in the consensus repeat unit EPAPTTPK indicated that there are regions within the lubricin domain that are highly glycosylated
3. The data presented here redefine an extended STP-rich region relative to the mucin domain previously defined by UniProt
4. Screening of ppGalNAc Ts from primary FLSs showed high expression of the less understood GALNT15 and GALNT5 genes, indicating that lubricin glycosylation is unique
5. Overall, this study showed that heavy glycosylation, particularly sialylation, is essential for creating the amphoteric nature of lubricin , a property that may facilitate its efficient biolubrication function

Output (sent_index, trigger, protein, sugar, site):

• 1. glycopeptide, , -, -, glycopeptide
• 1. glycosylation, , lubricin, -, -
• 2. glycosylated, , -, -, Thr residues
• 2. glycosylated, , -, -, regions

Output(Part-Of) (sent_index, protein, site):

• 1. STP, region
• 2. lubricin, domain
• 3. STP, region

*Output_Site_Fusion* (sent_index, protein, sugar, site):

 

Protein	NCBI ID	SENTENCE INDEX