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Membrane-bound and secreted IgA contain structurally different alpha-chains.

R Sitia, H Kikutani, A Rubartelli

    Journal of Immunology (Baltimore, Md. : 1950)
    |February 1, 1982
    PubMed
    Summary
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    Murine B lymphoma cell lines synthesize three distinct alpha-chain forms: membrane-bound (αm), secreted (αs), and intracellular (αic). Differences in size and charge are due to primary amino acid structure, not glycosylation.

    Area of Science:

    • Immunology
    • Molecular Biology
    • Cell Biology

    Background:

    • Murine B lymphoma cell lines BF0.3 and 615.2, derived from 1.29, synthesize alpha-chains.
    • Three distinct forms of alpha-chains have been identified, differing in size, pI, cellular location, and turnover rate.

    Purpose of the Study:

    • To characterize the different forms of alpha-chains synthesized by cloned murine B lymphoma cell lines.
    • To elucidate the structural basis for the observed differences between membrane-bound, secreted, and intracellular alpha-chains.

    Main Methods:

    • Lactoperoxidase-catalyzed radioiodination
    • Internal 14C or 35S labeling
    • Immunofluorescence techniques
    • Biosynthetic labeling in the presence and absence of tunicamycin

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    Main Results:

    • Identified three alpha-chain forms: membrane-bound (αm), secreted (αs), and intracellular (αic).
    • Confirmed assignments by comparing immunoglobulin products with a hybridoma cell line (Id 150).
    • Differences in molecular weight and charge between αm and αs are attributed to primary amino acid structure, not glycosylation.

    Conclusions:

    • BF0.3 and 615.2 cell lines produce distinct alpha-chain variants.
    • The structural variations in alpha-chains are primarily due to differences in amino acid sequence, impacting their function and localization.