Regulation of galectin‐3‐induced apoptosis of Jurkat cells by both O‐glycans and N‐glycans on CD45
pmid: 24211831
Regulation of galectin‐3‐induced apoptosis of Jurkat cells by both O‐glycans and N‐glycans on CD45
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.
- Institute of Laboratory Animal Science China (People's Republic of)
- PEKING UNION MEDICAL COLLEGE China (People's Republic of)
- Chinese Academy of Medical Sciences & Peking Union Medical College China (People's Republic of)
Glycosylation, Galectin 3, Molecular Sequence Data, Apoptosis, Binding, N-Glycans, Jurkat Cells, HEK293 Cells, O-Glycans, Polysaccharides, Mutagenesis, Site-Directed, Tumor Cells, Cultured, Galectin-3, Humans, Leukocyte Common Antigens, CD45, Amino Acid Sequence, Protein Binding
Glycosylation, Galectin 3, Molecular Sequence Data, Apoptosis, Binding, N-Glycans, Jurkat Cells, HEK293 Cells, O-Glycans, Polysaccharides, Mutagenesis, Site-Directed, Tumor Cells, Cultured, Galectin-3, Humans, Leukocyte Common Antigens, CD45, Amino Acid Sequence, Protein Binding
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