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Related Experiment Videos

Decrease in cell surface sialic acid in etoposide-treated Jurkat cells and the role of cell surface sialidase.

Y Azuma1, A Taniguchi, K Matsumoto

  • 1Department of Clinical Chemistry, School of Pharmaceutical Sciences, Toho University, Funabashi, Chiba, Japan. yutaro@phar.toho-u.ac.jp

Glycoconjugate Journal
|March 23, 2001
PubMed
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Etoposide treatment rapidly alters Jurkat cell surface glycans, decreasing sialic acids and increasing galactose. This desialylation is primarily caused by increased cell surface sialidase activity during etoposide-induced apoptosis.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Glycobiology

Background:

  • Cell surface glycans play crucial roles in cellular processes.
  • Apoptosis induction can lead to significant changes in cell surface glycoproteins.
  • Understanding glycan alterations during apoptosis is vital for cell signaling research.

Purpose of the Study:

  • To investigate the mechanism of cell surface sugar chain alterations during etoposide-induced apoptosis in Jurkat cells.
  • To identify the key enzymes and pathways involved in these glycan changes.
  • To elucidate the role of sialic acid reduction in etoposide-induced apoptosis.

Main Methods:

  • Flow cytometry using specific lectins (Maackia amurensis agglutinin and Ricinus communis agglutinin).
  • Analysis of alpha2,3-sialyltransferase (hST3Gal III and hST3Gal IV) mRNA expression.

Related Experiment Videos

  • Measurement of cell surface sialidase activity.
  • Inhibition studies using 2,3-dehydro-2-deoxy-N-acetylneuraminic acid.

    • Main Results:

    • Etoposide treatment decreased alpha2,3-linked sialic acids and increased galactose on Jurkat cell surfaces within 3 hours.
    • Down-regulation of hST3Gal III and hST3Gal IV mRNA expression was observed.
    • Cell surface sialidase activity increased threefold within 2 hours of etoposide treatment.
    • Sialidase inhibition significantly suppressed the decrease in alpha2,3-linked sialic acids.

    Conclusions:

    • Etoposide-induced apoptosis triggers rapid desialylation of Jurkat cell surface glycans.
    • Increased cell surface sialidase activity is the primary mechanism responsible for the reduction in sialic acids.
    • These findings highlight the dynamic changes in cell surface glycosylation during apoptosis.