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Regulation of galectin-3-induced apoptosis of Jurkat cells by both O-glycans and N-glycans on CD45

机译:O-聚糖和N-聚糖对半乳糖凝集素3诱导Jurkat细胞凋亡的调节作用

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Galectin-3 has been reported to induce apoptosis of Jurkat cells through binding receptors such as CD45. CD45RABC is heavily O-glycosylated and N-glycosylated, while CD45RO is only N-glycosylated. In this study, no apoptosis induced by galectin-3 was detected in CD45RO-transfected cells, whereas apoptosis of CD45RABC-transfected cells was observed, implying that O-glycans on CD45 might play roles in galectin-3-induced apoptosis. O-Glycosylation inhibition assay further suggests the role of O-glycans on CD45 in regulation of galectin-3-induced apoptosis. We also found that deglycosylation at N327 of CD45RO resulted in increased binding to galectin-3 without affecting apoptosis, while deglycosylation at N36 or N109 of CD45RO enhanced galectin-3-induced apoptosis. These data demonstrate that galectin-3-induced apoptosis of Jurkat cells is regulated by both O-glycans and N-glycans on CD45.
机译:据报道,Galectin-3通过结合受体如CD45诱导Jurkat细胞凋亡。 CD45RABC被严重O-糖基化和N-糖基化,而CD45RO仅被N-糖基化。在这项研究中,在CD45RO转染的细胞中未检测到由Galectin-3诱导的凋亡,而未观察到CD45RABC转染的细胞凋亡,这表明CD45上的O-聚糖可能在Galectin-3诱导的凋亡中起作用。 O-糖基化抑制试验进一步表明,O-聚糖在CD45上对Galectin-3诱导的细胞凋亡的调节作用。我们还发现,CD45RO的N327的去糖基化导致与galectin-3的结合增加,而不影响细胞凋亡,而CD45RO的N36或N109的去糖基化增强了galectin-3诱导的凋亡。这些数据表明,galectin-3诱导的Jurkat细胞凋亡受到CD45上O聚糖和N聚糖的调节。

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