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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ledbetter, J. A. Draves, K. E. Clark, E. A. Geahlen, R. L. Leprince, C. |
| Description | Author Affiliation: Leprince C ( Department of Microbiology, University of Washington, Seattle 98195.); |
| 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. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 8 |
| Volume Number | 90 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1993-05-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Antigens, CD Metabolism Antigens, Differentiation, B-Lymphocyte B-Lymphocytes Immunology Cell Adhesion Molecules Immunoglobulin M Lectins Protein Kinases Receptors, Antigen, B-Cell Amino Acid Sequence Animals Genetics Isolation & Purification Burkitt Lymphoma Cell Membrane Cells, Cultured Electrophoresis, Polyacrylamide Gel Mice Molecular Sequence Data Molecular Weight Palatine Tonsil Sequence Homology, Amino Acid Sialic Acid Binding Ig-like Lectin 2 Tumor Cells, Cultured Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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