N-Glycosylation is required for FDNC5 stabilization and irisin secretion
N-Glycosylation is required for FDNC5 stabilization and irisin secretion
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DOI：
10.1042/bcj20170241
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发表时间：
2017-09-15
影响因子：
4.1
通讯作者：
Liu, Dongjun
中科院分区：
文献类型：
--
作者：
Nie, Yongwei;Liu, Dongjun
鸢尾素是一种来源于FNDC 5胞外结构域的肌因子，已显示其介导白色脂肪组织的产热。生物化学数据表明，FNDC 5的N-糖基化不太可能影响鸢尾素的配体或受体活化。FNDC 5的N-糖基化仍然知之甚少。在本研究中，我们分析了FNDC 5的N-糖基化位点，发现两个潜在的N-糖基化位点（Asn（36）和Asn（81））确实可以被N-聚糖占据。此外，我们还发现，N-糖基化的缺乏降低了鸢尾素的分泌，这与FNDC 5的不稳定性和信号肽的切割缺陷有关。我们还发现成肌细胞分化后N-糖基化FNDC 5的表达水平升高。这些发现表明，鸢尾素的分泌是由N-糖基化，这反过来又增强了我们的理解糖基化的鸢尾素的分泌。
Irisin, a myokine derived from the extracellular domain of FNDC5, has been shown to mediate thermogenesis of white adipose tissue. Biochemical data have shown that N-glycosylation of FNDC5 is unlikely to affect ligand or receptor activation of irisin. The N-glycosylation of FNDC5 remains poorly understood. In the present study, we analysed N-glycosylation sites of FNDC5 and found that two potential N-glycosylation sites (Asn(36) and Asn(81)) could indeed be occupied by N-glycan. Furthermore we showed that the lack of N-glycosylation decreases the secretion of irisin, which is relevant to the instability of FNDC5 and the deficiency of cleavage of the signal peptide. We also found that the expression level of N-glycosylated FNDC5 was elevated after myoblast differentiation. These findings show that the secretion of irisin is modulated by N-glycosylation, which in turn enhances our understanding of the secretion of glycosylated irisin.