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Related Experiment Videos

Human Ia alpha- and beta-chains are sulfated.

A J Sant1, M Zacheis, T Rumbarger

  • 1Department of Microbiology and Immunology, Washington University School of Medicine, St. Louis, MO 63110.

Journal of Immunology (Baltimore, Md. : 1950)
|January 1, 1988
PubMed
Summary

Human Ia antigens (HLA-DR, HLA-DQ, HLA-DP) alpha, beta, and invariant chains can be sulfated. This post-translational modification suggests a potential role for sulfation in the function of these crucial immune molecules.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • Human Ia antigens (HLA-DR, HLA-DQ, HLA-DP) are critical immune molecules.
  • These antigens are heterodimers composed of alpha and beta glycoprotein chains.
  • Previous research identified a sulfated proteoglycan associated with Ia antigens.

Purpose of the Study:

  • To investigate the presence and nature of non-proteoglycan sulfated components associated with human Ia antigens.
  • To determine if the alpha, beta, and invariant chains of Ia molecules undergo sulfation.

Main Methods:

  • Immunoprecipitation of Ia antigens (DR and DQ) from human cells.
  • Analysis of immunoprecipitated components using one-dimensional and two-dimensional sodium dodecyl sulfate-gel electrophoresis.

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  • Treatment with endoglycosidase F to assess the site of sulfation.

    • Main Results:

    • Non-proteoglycan sulfated components were detected in Ia immunoprecipitates.
    • These sulfated components exhibited molecular weights indistinguishable from Ia alpha and beta glycoproteins.
    • Two-dimensional gel analysis confirmed sulfation of Ia alpha, beta, and invariant chains.
    • Sulfation was localized to the protein portion, as it was resistant to endoglycosidase F treatment.

    Conclusions:

    • Human Ia antigen alpha, beta, and invariant chains are subject to sulfation.
    • This post-translational modification suggests sulfation may play a significant role in the physiology and function of Ia molecules.
    • Further research is warranted to elucidate the specific functional implications of Ia chain sulfation.