Developmental regulation of IgM secretion: the role of the carboxy-terminal cysteine

Cell. 1990 Mar 9;60(5):781-90. doi: 10.1016/0092-8674(90)90092-s.


B lymphocytes do not secrete IgM, and plasma cells only secrete IgM polymers. Here we show that both events are attributable to the tailpiece found at the carboxyl terminus of mus chains, and we specifically implicate Cys-575. Thus, if Cys-575 was mutated, IgM was secreted by B cells. Similarly, a mutant IgG containing a mus tailpiece became largely retained within the cell; secretion was restored upon mutation of the tailpiece cysteine. Removal of Cys-575 also allowed hypersecretion of monomeric IgM by plasmacytoma cells. Following further removal of Cmu1, heavy chains were secreted in the absence of light chains. Thus, in B and plasma cells, Cys-575 is involved both in the polymerization of IgM and in intracellular retention of unpolymerized intermediates.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • B-Lymphocytes / immunology*
  • Base Sequence
  • Cell Line
  • Cysteine
  • Humans
  • Immunoglobulin M / biosynthesis*
  • Immunoglobulin M / genetics
  • Immunoglobulin mu-Chains / genetics*
  • Molecular Sequence Data
  • Mutation
  • Oligonucleotide Probes
  • Transfection


  • Immunoglobulin M
  • Immunoglobulin mu-Chains
  • Oligonucleotide Probes
  • Cysteine