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Chemical and serologic characterization of human lambda VIII light chains

A Solomon1, D T Weiss, C Murphy

  • 1Department of Medicine, University of Tennessee Medical Center/Graduate School of Medicine, Knoxville 37920.

Journal of Immunology (Baltimore, Md. : 1950)
|August 15, 1994
PubMed
Summary

Researchers identified a new human lambda light chain subgroup, V lambda VIII, with unique structural features. This subgroup is found in normal individuals and is prevalent in rheumatoid arthritis patients with IgM lambda rheumatoid factors.

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Area of Science:

  • Immunology and Molecular Biology: Focus on immunoglobulin light chain structure and function.

Background:

  • Human immunoglobulin lambda (Ig lambda) light chains exhibit diverse variable (V) region subgroups.
  • Previous classifications recognized several V lambda subgroups, but a distinct V lambda VIII subgroup was newly identified.

Purpose of the Study:

  • To elucidate the structural and serologic properties of the newly identified human V lambda VIII light chain subgroup.
  • To investigate the prevalence and potential functional significance of V lambda VIII in normal and pathological conditions, particularly rheumatoid arthritis.

Main Methods:

  • Analysis of amino acid sequences of two monoclonal lambda light chains (Bence Jones proteins HAG and BIV) and a prototypic cDNA (Humla8f10).
  • Comparison of V lambda VIII sequences with other known V lambda subgroups to identify distinguishing features.

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  • Development of anti-V lambda VIII subgroup-specific antibodies for quantification in various biological samples.

    • Main Results:

    • Proteins HAG and BIV were classified as V lambda VIII subgroup members, distinct from other V lambda subgroups based on amino acid sequences.
    • V lambda VIII chains possess an elongated second complementarity-determining region (CDR2) of 11 residues, differing from the typical seven residues in other subgroups.
    • Approximately 3% of Ig lambda in normal serum contain V lambda VIII L chains; this frequency rises to 19% in monoclonal IgM lambda rheumatoid factors from rheumatoid arthritis patients.

    Conclusions:

    • The human V lambda VIII subgroup has unique structural characteristics, notably an extended CDR2, potentially influencing ligand-binding specificity.
    • V lambda VIII L chains are present in normal individuals and are significantly enriched in specific autoimmune conditions like rheumatoid arthritis.
    • These findings contribute to understanding the structural diversity and functional roles of human immunoglobulin light chain subgroups.