Biosynthesis of membrane and secreted ε{lunate}-chains during lipopolysaccharideinduced differentiation of an IgE+ murine B-lymphoma

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Abstract

A switch variant of the 1.29 murine B-cell lymphoma expressing membrane IgE and inducible by lipopolysaccharide (LPS) to increase the rate of IgE secretion was characterized. The cells (1.29 ε{lunate}+2) express membrane-bound IgE, and also secrete considerable amounts of IgE when grown in regular culture medium. Membrane and secreted IgE contain structurally different heavy chains. The former is constituted by a 93-kd molecule (ε{lunate}m), while secretory chains (ε{lunate}s) have an apparent mol. wt of 86,000. Both ε{lunate}m and ε{lunate}s are heavily glycosylated: in the presence of tunicamycin their apparent mol. wt is reduced by approx. 35% (61 kd for ε{lunate}m and 56 kd for ε{lunate}s). Glycosylation is necessary for membrane expression and for secretion of IgE molecules. Stimulation with LPS leads to the disappearance of IgE molecules from the cell surface (determined by radioiodination) although ε{lunate}m-chains are still synthesized, suggesting a defective transport of membrane IgE in LPS-treated cells. The ε{lunate}m:ε{lunate}s ratio decreases upon LPS stimulation. A similar change can be observed in the messenger RNAs specific for ε{lunate}m and ε{lunate}s, possibly suggesting a major pretranslational control for ε{lunate}m and ε{lunate}s biosynthesis.

Original languageEnglish
Pages (from-to)1289-1296
Number of pages8
JournalMolecular Immunology
Volume22
Issue number11
DOIs
Publication statusPublished - 1985

ASJC Scopus subject areas

  • Molecular Biology
  • Immunology

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