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Mol. Cells 2007; 24(3): 416-423

Published online December 31, 2007

© The Korean Society for Molecular and Cellular Biology

Increased α2,3-Sialylation and Hyperglycosylation of N-Glycans in Embryonic Rat Cortical Neurons During Camptothecin-induced Apoptosis

Sung-Min Kim, Jung-Sun Lee, Yoon-Hee Lee, Woo-Jung Kim, Su-Il Do, Young-Kug Choo and Yong-Il Park

Abstract

Alterations in the glycan chains of cell surface glycoconjugates are frequently involved biological processes such as cell-cell interaction, cell migration, differentiation and development. Cultured embryonic (E18) rat cortical neurons underwent apoptosis in response to camptothecin, and lectin histochemistry showed that binding to apoptotic neurons of FITC-conjugated Maackia amurensis agglutinin (MAA), which is specific for terminal α2,3-sialic acid residues, increased progressively with increasing concentrations of camptothecin. Analysis of the total proteins of apoptotic neurons by SDS-PAGE, and lectin blotting using HRP-labeled MAA, revealed that the expression of terminal α2,3-sialic acid residues on an unknown protein with an apparent molecular mass of 25.6 kDa also increased in apoptotic neurons. NP-HPLC analysis of the total cellular N-glycans of normal and apoptotic neurons demonstrated that the expression of structurally simpler biantennary types of N-glycans fell by 49% during apoptosis whereas the more branched triantennary types of N-glycans with terminal sialic acid residues increased by up to 59%. These results suggest that increased surface expression of α2,3-sialic acid residues and hyperglycosylation of N-glycans is a common feature of cellular responses to changes in cell physiology such as tumorigenesis and apoptosis.

Keywords Apoptosis; Embryonic Rat Cortical Neurons; Hyperglycosylation; N-Glycans; Sialomolecules.

Article

Research Article

Mol. Cells 2007; 24(3): 416-423

Published online December 31, 2007

Copyright © The Korean Society for Molecular and Cellular Biology.

Increased α2,3-Sialylation and Hyperglycosylation of N-Glycans in Embryonic Rat Cortical Neurons During Camptothecin-induced Apoptosis

Sung-Min Kim, Jung-Sun Lee, Yoon-Hee Lee, Woo-Jung Kim, Su-Il Do, Young-Kug Choo and Yong-Il Park

Abstract

Alterations in the glycan chains of cell surface glycoconjugates are frequently involved biological processes such as cell-cell interaction, cell migration, differentiation and development. Cultured embryonic (E18) rat cortical neurons underwent apoptosis in response to camptothecin, and lectin histochemistry showed that binding to apoptotic neurons of FITC-conjugated Maackia amurensis agglutinin (MAA), which is specific for terminal α2,3-sialic acid residues, increased progressively with increasing concentrations of camptothecin. Analysis of the total proteins of apoptotic neurons by SDS-PAGE, and lectin blotting using HRP-labeled MAA, revealed that the expression of terminal α2,3-sialic acid residues on an unknown protein with an apparent molecular mass of 25.6 kDa also increased in apoptotic neurons. NP-HPLC analysis of the total cellular N-glycans of normal and apoptotic neurons demonstrated that the expression of structurally simpler biantennary types of N-glycans fell by 49% during apoptosis whereas the more branched triantennary types of N-glycans with terminal sialic acid residues increased by up to 59%. These results suggest that increased surface expression of α2,3-sialic acid residues and hyperglycosylation of N-glycans is a common feature of cellular responses to changes in cell physiology such as tumorigenesis and apoptosis.

Keywords: Apoptosis, Embryonic Rat Cortical Neurons, Hyperglycosylation, N-Glycans, Sialomolecules.

Mol. Cells
Aug 31, 2022 Vol.45 No.8, pp. 513~602
COVER PICTURE
Cryo-EM structure of human porphyrin transporter ABCB6 (main figure) shows that binding of hemin (inset, magenta) in concert with two glutathione molecules (cyan) primes ABCB6 for high ATP turnover (Kim et al., pp. 575-587).

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