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The Journal of Immunology, Vol 149, Issue 9 2841-2850, Copyright © 1992 by American Association of Immunologists


ARTICLES

The CD19/CD21 signal transducing complex of human B lymphocytes includes the target of antiproliferative antibody-1 and Leu-13 molecules

LE Bradbury, GS Kansas, S Levy, RL Evans and TF Tedder
Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, MA 02115-6084.

CD19 is a member of the Ig superfamily expressed on the surface of B lymphocytes that may be involved in the regulation of B cell function. Immunoprecipitation studies with B cell lines solubilized by digitonin have shown CD19 to be part of a multimolecular complex that includes CD21 (CR2) and other unidentified proteins. In this study, two of the CD19-associated proteins were identified as TAPA-1, which is expressed on most cell types, and Leu-13, which is expressed on subsets of lymphoid cells. TAPA-1 and Leu-13 are physically associated in many cell lineages. CD19 and CD21 mAb each specifically coprecipitated proteins of the same size as those precipitated by TAPA-1 and Leu-13 mAb from B cell lines and cDNA-transfected K562 cell lines. Western blot analysis with a TAPA-1 mAb verified the identity of TAPA-1 in CD19 and CD21 immunoprecipitated materials. In addition, when TAPA-1 or Leu- 13 were crosslinked and patched on the cell surface, all of the CD19 comigrated with TAPA-1 and some of the CD19 comigrated with Leu-13. Furthermore, mAb binding to CD19, CD21, TAPA-1, and Leu-13 on B cell lines induced similar biologic responses, including the induction of homotypic adhesion, inhibition of proliferation, and an augmentation of the increase in intracellular [Ca2+] induced by suboptimal cross- linking of surface Ig on B cell lines. Together, these data suggest that TAPA-1 and Leu-13 are broadly expressed members of a signal transduction complex in which lineage-specific proteins, such as CD19 and CD21, provide cell-specific functions.


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J. Weitzman, A Chen, and M. Hemler
Investigation of the role of beta 1 integrins in cell-cell adhesion
J. Cell Sci., January 11, 1995; 108(11): 3635 - 3644.
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J. Biol. Chem.Home page
J. C. Poe, M. Fujimoto, P. J. Jansen, A. S. Miller, and T. F. Tedder
CD22 Forms a Quaternary Complex with SHIP, Grb2, and Shc. A PATHWAY FOR REGULATION OF B LYMPHOCYTE ANTIGEN RECEPTOR-INDUCED CALCIUM FLUX
J. Biol. Chem., June 2, 2000; 275(23): 17420 - 17427.
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J. Biol. Chem.Home page
A.-K. Somani, K. Yuen, F. Xu, J. Zhang, D. R. Branch, and K. A. Siminovitch
The SH2 Domain Containing Tyrosine Phosphatase-1 Down-regulates Activation of Lyn and Lyn-induced Tyrosine Phosphorylation of the CD19 Receptor in B Cells
J. Biol. Chem., January 12, 2001; 276(3): 1938 - 1944.
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J. Biol. Chem.Home page
C. S. Stipp, D. Orlicky, and M. E. Hemler
FPRP, a Major, Highly Stoichiometric, Highly Specific CD81- and CD9-associated Protein
J. Biol. Chem., February 9, 2001; 276(7): 4853 - 4862.
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J. Biol. Chem.Home page
C. S. Stipp, T. V. Kolesnikova, and M. E. Hemler
EWI-2 Is a Major CD9 and CD81 Partner and Member of a Novel Ig Protein Subfamily
J. Biol. Chem., October 26, 2001; 276(44): 40545 - 40554.
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