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FEBS Lett. 2013 Dec 11;587(24):3986-94. doi: 10.1016/j.febslet.2013.10.034. Epub 2013 Nov 5.

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

Author information

1
Institute of Laboratory Animal Science, Chinese Academy of Medical Sciences (CAMS) and Comparative Medicine Center, Peking Union Medical College (PUMC), Key Laboratory of Human Disease Comparative Medicine, Beijing, China.

Abstract

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.

KEYWORDS:

Apoptosis; Binding; CD45; DMEM; Dulbecco’s modified Eagle’s medium; Galectin-3; MW; N-Glycans; O-Glycans; PBST; SDS–PAGE; molecular weight; phosphate buffered saline with Tween 20; sodium dodecyl sulfate–polyacrylamide gel electrophoresis

PMID:
24211831
DOI:
10.1016/j.febslet.2013.10.034
[Indexed for MEDLINE]
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