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PMID: 2303036 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Molecular components of the B cell antigen receptor complex of class IgD differ partly from those of IgM.

The EMBO journal ·Vol. 9 ·No. 2 ·1990-02-00 ·Pages 449-55

Wienands J, Hombach J, Radbruch A, Riesterer C, Reth M

Abstract

Two classes of immunoglobulin, IgM and IgD, are present as antigen receptors on the surface of mature B lymphocytes. We show here that IgD molecules are noncovalently associated in the B cell membrane with a heterodimer consisting of two proteins of 35 kd (IgD-alpha) and 39 kd (Ig-beta), respectively. The two novel proteins are not found in the IgD-expressing myeloma J558L delta m, which fails to bring IgD antigen receptor onto the cell surface. In a surface IgD positive variant line of this myeloma, however, membrane-bound IgD molecules are associated with the heterodimer, suggesting that the formation of an antigen receptor complex is required for surface IgD expression. We further demonstrate that the IgD-associated heterodimer differs partly from that of the IgM antigen receptor and that its binding to the heavy chain only requires the presence of the last constant domain and the transmembrane part of the delta m chain.

MeSH Terms
Animals B-Lymphocytes/immunology Cell Line Gene Expression Genes, Immunoglobulin Genetic Vectors Immunoglobulin D/genetics,isolation & purification Immunoglobulin M/isolation & purification Macromolecular Substances Receptors, Antigen, B-Cell/genetics,isolation & purification Transfection
Chemicals
Immunoglobulin D Immunoglobulin M Macromolecular Substances Receptors, Antigen, B-Cell
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Wienands J
Max-Planck-Institut für Immunbiologie, Freiburg, FRG.
Hombach J
Radbruch A
Riesterer C
Reth M
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1990-02-00
Pages
449-55
Language
English
Region
England
NLM ID
8208664
PMCID
PMC551686
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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