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Related Experiment Videos

Human T-lymphocyte activation is associated with changes in O-glycan biosynthesis.

F Piller1, V Piller, R I Fox

  • 1Cancer Research Center, La Jolla Cancer Research Foundation, California.

The Journal of Biological Chemistry
|October 15, 1988
PubMed
Summary

Human T-lymphocyte activation alters the carbohydrate structures of the cell-surface glycoprotein leukosialin. This shift is driven by changes in key enzyme activities, impacting T-cell function.

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Area of Science:

  • Immunology
  • Glycobiology
  • Cell Biology

Background:

  • T-lymphocytes play a crucial role in the immune response.
  • Cell surface glycoproteins are vital for cell communication and function.
  • Leukosialin (CD43) is a major sialoglycoprotein on T-lymphocytes with poorly understood activation-dependent modifications.

Purpose of the Study:

  • To investigate the changes in the major cell-surface sialoglycoprotein of human T-lymphocytes upon activation.
  • To identify the specific structural alterations in the carbohydrate chains of leukosialin during T-cell activation.
  • To elucidate the enzymatic mechanisms responsible for these glycan modifications.

Main Methods:

  • Activation of human T-lymphocytes using anti-CD3 antibodies and interleukin-2.

Related Experiment Videos

  • Analysis of the apparent molecular weight of the major cell-surface sialoglycoprotein.
  • Identification of the sialoglycoprotein as leukosialin using monospecific antiserum.
  • Detailed structural analysis of the O-glycans on leukosialin from resting and activated T-lymphocytes.

    • Main Results:

    • T-lymphocyte activation significantly increased the apparent molecular weight of leukosialin.
    • Resting T-lymphocytes express disialotetrasaccharides on leukosialin.
    • Activated T-cells display more complex O-glycans, including a beta 1----6GlcNAc linkage, on leukosialin.
    • These structural changes are attributed to decreased alpha 2----6 sialyltransferase activity and increased beta 1----6GlcNAc-transferase activity.

    Conclusions:

    • T-lymphocyte activation induces a profound remodeling of leukosialin's O-glycan structures.
    • The observed glycan shift is mediated by coordinated changes in specific glycosyltransferase activities.
    • These findings highlight the dynamic nature of cell surface glycans in regulating T-cell activation and function.