Identification of two distinct phosphoproteins as components of the human B cell antigen receptor complex

In human B cells, the molecules that, upon receptor occupancy, couple membrane immunoglobulin to intracellular signal transduction pathways have never been identified. We here describe two phosphoproteins as integral parts of the B cell antigen receptor complex. Membrane IgM is non-covalently associ...

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Bibliographic Details
Published inEuropean journal of immunology Vol. 20; no. 12; p. 2789
Main Authors Van Noesel, C J, Borst, J, De Vries, E F, Van Lier, R A
Format Journal Article
LanguageEnglish
Published Germany 01.12.1990
Subjects
B-Lymphocytes - physiology
Chromatography, High Pressure Liquid
Disulfides
Glycoproteins - physiology
Humans
Immunoglobulin M - physiology
Macromolecular Substances
Molecular Weight
Peptide Mapping
Phosphoproteins - chemistry
Phosphoproteins - physiology
Phosphoserine - metabolism
Receptors, Antigen, B-Cell - chemistry
Receptors, Antigen, B-Cell - physiology
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Summary:In human B cells, the molecules that, upon receptor occupancy, couple membrane immunoglobulin to intracellular signal transduction pathways have never been identified. We here describe two phosphoproteins as integral parts of the B cell antigen receptor complex. Membrane IgM is non-covalently associated with a disulfide-linked heterodimer of glycoproteins. These molecules can be demonstrated on B cell lines and freshly isolated polyclonal B cell populations and are subject to phosphorylation at serine residues. Identification of these constituents of the B cell receptor complex opens up the opportunity to study coupling of the B cell antigen receptor to the intracellular signal transduction machinery at the molecular level.
ISSN:0014-2980
DOI:10.1002/eji.1830201238