重组因子IX的分泌和活性与n -糖基化的关系

Research in Molecular Medicine Pub Date : 2020-02-10 DOI:10.32598/RMM.8.1.31

S. Khalilzadeh, J. Vatandoost

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引用次数: 0

摘要

背景：人凝血因子IX（hFIX）是一种在激活肽上具有两个N-糖基化位点的糖蛋白。由于激活肽在成熟hFIX中被去除，N-糖基化的确切作用尚不清楚。为了研究N-糖基化在hFIX分泌和活性中的作用，我们在稳定的人胚胎肾（HEK）凝血因子IX（FIX）细胞中抑制了衣霉素的N-糖基化度。

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

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.

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Research in Molecular Medicine

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审稿时长

21 weeks