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PMID: 8475064 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

CD22 associates with the human surface IgM-B-cell antigen receptor complex.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 90 ·No. 8 ·1993-04-15 ·Pages 3236-40

Leprince C, Draves KE, Geahlen RL, Ledbetter JA, Clark EA

Abstract

The B-cell surface molecule CD22, when cross-linked, modulates signaling through the surface IgM (sIgM)-B-cell receptor (BCR) complex. Here we analyzed the basis of this interaction between CD22 and the human sIgM complex. After lysis of B cells or B-cell lines in digitonin, CD22 coimmunoprecipitated a kinase activity that in vitro-phosphorylated two polypeptides of 150 and 130 kDa on tyrosine residues. By immunoblot analysis with a rabbit anti-serum specific for a synthetic peptide of CD22, we found these proteins to be CD22 itself. Furthermore, the phosphorylated 150-kDa CD22 was found in the sIgM-BCR complex maintained by digitonin, along with Ig alpha/mb-1, Ig beta/B29, and a 75-kDa polypeptide precipitated by an antiserum specific to protein-tyrosine kinase PTK72. CD22 is likely to be an important signaling partner in the sIgM-BCR complex since it is very rapidly and strikingly phosphorylated after sIgM is cross-linked and since it contains the antigen recognition homology I (ARHI) motif, present in other antigen receptor molecules.

MeSH Terms
Amino Acid Sequence Animals Antigens, CD/genetics,isolation & purification,metabolism Antigens, Differentiation, B-Lymphocyte/genetics,isolation & purification,metabolism B-Lymphocytes/immunology,metabolism Burkitt Lymphoma Cell Adhesion Molecules/isolation & purification,metabolism Cell Membrane/immunology,metabolism Cells, Cultured Electrophoresis, Polyacrylamide Gel Humans Immunoglobulin M/isolation & purification,metabolism Lectins Mice Molecular Sequence Data Molecular Weight Palatine Tonsil/immunology Protein Kinases/isolation & purification,metabolism Receptors, Antigen, B-Cell/isolation & purification,metabolism Sequence Homology, Amino Acid Sialic Acid Binding Ig-like Lectin 2 Tumor Cells, Cultured
Chemicals
Antigens, CD Antigens, Differentiation, B-Lymphocyte CD22 protein, human Cd22 protein, mouse Cell Adhesion Molecules Immunoglobulin M Lectins Receptors, Antigen, B-Cell Sialic Acid Binding Ig-like Lectin 2 Protein Kinases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Leprince C
Department of Microbiology, University of Washington, Seattle 98195.
Draves K E
Geahlen R L
Ledbetter J A
Clark E A
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43 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.90.8.3236
Published
1993-04-15
Pages
3236-40
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC46274
Subset
IM
Grants
NCI NIH HHS · CA37372 · United States
NIGMS NIH HHS · GM37905 · United States
NIGMS NIH HHS · GM42508 · United States
External Links
PubMed source DOI: 10.1073/pnas.90.8.3236 PMC Full Text View journal details
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