PMID: PMC4084840-2

 

    Legend: Gene, Sites

Title : ITIH4 is a secreted glycoprotein that is up-regulated by IL-6 aspart of the acute phase response to turpentine-induced inflammationin rats and in response to infection in humans

Abstract :

1. Glycosylation of ITIH4 is of considerableinterest due to the biomarker potential of its proteolytic productsand glycoforms in several forms of cancer, the involvement of ITIH4in liver development and stabilization of the ECM , and observed changesin ITIH4 expression and glycosylation in ovarian and other cancers
2. Glycosylation can mediate protein interactions, influence protein stability, and impact proteinfunction
3. Our results confirm previous reports that ITIH4 is heavilyglycosylated; it is therefore plausible that glycosylation modifies ITIH4 structure and function
4. While microheterogeneity of glycoformsdiffers between ITIH4 protein expressed in HEK293 cells and proteinisolated from serum, occupancy of N-glycosylation sites does not differ
5. However, utilization of O-glycosylation sites differs between thecell line and serum

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

• 0. glycoprotein, , ITIH4, -, -
• 0. glycoprotein, , glycoprotein, -, -
• 1. Glycosylation, , ITIH4, -, -
• 3. heavilyglycosylated, , ITIH4, -, -
• 4. N-glycosylation, , -, -, sites
• 4. occupancy, , -, -, sites
• 5. O-glycosylation, , -, -, sites

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

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

 

Protein	NCBI ID	SENTENCE INDEX