Differences in glycoprotein complexes associated with IgM and IgD on normal murine B cells potentially enable transduction of different signals

EMBO J. 1990 Jul;9(7):2117-24. doi: 10.1002/j.1460-2075.1990.tb07380.x.

Abstract

Studies presented here demonstrate that IgM and IgD molecules on normal murine B lymphocytes exist in different, noncovalently associated molecular complexes containing distinct but potentially related glycoproteins. The glycoproteins in these complexes, particularly those associated with IgD, show striking differences in various lymphoid organs and in X-linked immunodeficient (Xid) mice. These differences are due in part to post-translational processing. They apparently reflect the differential expression of the Ig-associated glycoproteins in the various B cell subpopulations and lineages and the differential distribution of the subpopulations and lineages in the various lymphoid organs. In addition, they reflect structural differences in the IgM and IgD complexes which, we suggest, permit differential signal transduction by IgM and IgD on the same B cell.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • B-Lymphocytes / immunology*
  • Electrophoresis, Polyacrylamide Gel
  • Immunoglobulin D / isolation & purification
  • Immunoglobulin D / physiology*
  • Immunoglobulin M / isolation & purification
  • Immunoglobulin M / physiology*
  • Lymph Nodes / immunology
  • Membrane Glycoproteins / isolation & purification
  • Membrane Glycoproteins / physiology*
  • Mice
  • Mice, Inbred BALB C
  • Mice, Inbred CBA
  • Molecular Weight
  • Peritoneal Cavity / cytology
  • Protein Binding
  • Receptors, Antigen, B-Cell / isolation & purification
  • Receptors, Antigen, B-Cell / physiology*
  • Signal Transduction*
  • Spleen / immunology

Substances

  • Immunoglobulin D
  • Immunoglobulin M
  • Membrane Glycoproteins
  • Receptors, Antigen, B-Cell