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Formation of disulphide-linked µ2ω2 tetramers in pre-B cells by the 18K ω-immunoglobulin light chain

Abstract

Pre-B cells are precursors of B lymphocytes that contain intracel-lular heavy-chain protein (µ) and are either yet to rearrange their light-chain genes or are in the process of doing so1–4. These cells have traditionally been considered to contain intracellular µ-chain with no associated light chain. We demonstrate here that pre-B lymphoid lines synthesize a protein of relative molecular mass (Mr) 18,000 (18K), which we term ω, which forms disulphide-linked µ2ω2 tetramers. This protein could be immunoprecipitated with µ-chain from pre-B lines, but not from T-cell and fibroblast lines that express transfected µ-genes, nor from a pre-B line that synthesizes a Dµ-protein (which lacks a V domain). We view the ω-chain as being a pre-B specific surrogate light chain that may be essential for the important regulatory function that the µ-protein is believed to have at this stage of differentiation.

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Pillai, S., Baltimore, D. Formation of disulphide-linked µ2ω2 tetramers in pre-B cells by the 18K ω-immunoglobulin light chain. Nature 329, 172–174 (1987). https://doi.org/10.1038/329172a0

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