Differential sialylation of cell surface glycoconjugates in a human B lymphoma cell line regulates susceptibility for CD95 (APO-1/Fas)-mediated apoptosis and for infection by a lymphotropic virus.

@article{Keppler1999DifferentialSO,
  title={Differential sialylation of cell surface glycoconjugates in a human B lymphoma cell line regulates susceptibility for CD95 (APO-1/Fas)-mediated apoptosis and for infection by a lymphotropic virus.},
  author={Oliver T. Keppler and Marcus E Peter and Stephan Hinderlich and Gerhard Moldenhauer and Peer Stehling and Ingo Schmitz and Reinhard Schwartz-Albiez and Werner Reutter and Michael Pawlita},
  journal={Glycobiology},
  year={1999},
  volume={9 6},
  pages={557-69}
}
Sialic acid, as a terminal saccharide residue on cell surface glycoconjugates, plays an important role in a variety of biological processes. In this study, we investigated subclones of the human B lymphoma cell line BJA-B for differences in the glycosylation of cell surface glycoconjugates, and studied the functional implications of such differences. With respect to the expression level of most of the tested B cell-associated antigens, as well as the presence of penultimate saccharide moieties… CONTINUE READING
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