The Relationship of Secretion and Activity of Recombinant Factor IX with N-Glycosylation

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Khalilzadeh Samira; VATANDOOST JAFAR

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Journal Paper

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Journal: Research in Molecular Medicine Year:2020 | Volume:8 | Issue:1 Page(s): 31-36

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Title

The Relationship of Secretion and Activity of Recombinant Factor IX with N-Glycosylation

Author(s)

Khalilzadeh Samira | VATANDOOST JAFAR | Issue Writer Certificate

Keywords

Blood Coagulation Factor IX

N-glycosylation

Tunicamycin

Protein folding

Abstract

Background: Human coagulation factor IX (hFIX) is a glycoprotein with two N-glycosylation sites at the activation peptide. Since the activation peptide is removed in mature hFIX, the exact role of N-glycosylation is unclear. To investigate the role of N-glycosylation in the secretion and activity of hFIX, we inhibited N-glycosylation by Tunicamycin in the stable Human Embryonic Kidney (HEK)coagulation Factor IX (FIX) cells. Materials and Methods: After the treatment of stable FIX-expressing HEK cells in the presence or absence of Tunicamycin, the expression and activity of the recombinant FIX (rFIX) were determined in culture medium and cell lysate with enzyme-linked immunosorbent assay and clotting test, respectively. Results: Based on the data analysis, total concentrations of FIX in stable HEK-FIX was the same in the media with and without Tunicamycin. But throughout the post-induction period, the intracellular and secreted levels of FIX in Tunicamycin-treated HEK-FIX cells increased and decreased, respectively, compared with those of control HEK-FIX cells, though the results were not significant. These results indicate that disrupting the synthetic process may slightly reduce the FIX levels secreted in HEK-FIX cells. Conclusion: Although glycosylation plays a vital role in the folding and secretion of the proteins, it does not affect the secretion of FIX. Besides, the N-glycosylation of the produced FIX failed to play a significant role in its activity.

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APA: Copy

Khalilzadeh, Samira, & VATANDOOST, JAFAR. (2020). The Relationship of Secretion and Activity of Recombinant Factor IX with N-Glycosylation. RESEARCH IN MOLECULAR MEDICINE, 8(1), 31-36. SID. https://sid.ir/paper/687362/en

Vancouver: Copy

Khalilzadeh Samira, VATANDOOST JAFAR. The Relationship of Secretion and Activity of Recombinant Factor IX with N-Glycosylation. RESEARCH IN MOLECULAR MEDICINE[Internet]. 2020;8(1):31-36. Available from: https://sid.ir/paper/687362/en

IEEE: Copy

Samira Khalilzadeh, and JAFAR VATANDOOST, “The Relationship of Secretion and Activity of Recombinant Factor IX with N-Glycosylation,” RESEARCH IN MOLECULAR MEDICINE, vol. 8, no. 1, pp. 31–36, 2020, [Online]. Available: https://sid.ir/paper/687362/en

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