The Journal of Immunology, Vol 151, Issue 8 4090-4097, Copyright © 1993 by American Association of Immunologists

ARTICLES

The TAPA-1 molecule is associated on the surface of B cells with HLA-DR molecules

MR Schick and S Levy
Department of Medicine, Stanford University Medical Center, CA 94305- 5306.

TAPA-1 is a transmembrane protein that has been shown to be involved in cell growth and cellular adhesion. Our studies were aimed at determining the mechanisms of the biologic phenomena mediated by TAPA- 1, which include the identification of proteins that are associated with it on the surface of lymphocytes. We and others have previously shown that Leu-13, a leukocyte Ag, is one such molecule and that in B cells TAPA-1 is associated with the CD19 Ag. Herein we identify an additional molecule, HLA-DR, that is noncovalently associated on the surface of B cells with TAPA-1. This association was first detected by immunoprecipitation by anti-TAPA-1 and by anti-HLA-DR antibodies in the presence of mild detergents. The initial observation was confirmed by 2- dimensional SDS-PAGE and by direct identification of TAPA-1 in anti-HLA- DR immunoprecipitates by Western blot analysis. The association of the two molecules on the surface of a human B cell line was shown by cocapping experiments. In addition, antibodies to both molecules can induce cellular adhesion and an antiproliferative effect. Because the tissue distribution of these two molecules only partially overlaps, with TAPA-1 being expressed on most cell types and MHC class II expressed on a more restricted group of tissue, it is possible that the TAPA-1 molecule provides a basic function that can augment a cell type specific activity. In B cells the association of TAPA-1 with CD19 and HLA-DR may increase cellular interaction and play a supporting role in the transmission of specific signals.

This article has been cited by other articles:

				R. S. Barsoum Hepatitis C virus: from entry to renal injury--facts and potentials Nephrol. Dial. Transplant., July 1, 2007; 22(7): 1840 - 1848. [Full Text] [PDF]

				J. J. Unternaehrer, A. Chow, M. Pypaert, K. Inaba, and I. Mellman The tetraspanin CD9 mediates lateral association of MHC class II molecules on the dendritic cell surface PNAS, January 2, 2007; 104(1): 234 - 239. [Abstract] [Full Text] [PDF]

				N. J. Poloso, L. K. Denzin, and P. A. Roche CDw78 Defines MHC Class II-Peptide Complexes That Require Ii Chain-Dependent Lysosomal Trafficking, Not Localization to a Specific Tetraspanin Membrane Microdomain J. Immunol., October 15, 2006; 177(8): 5451 - 5458. [Abstract] [Full Text] [PDF]

				D. Rosa, G. Saletti, E. De Gregorio, F. Zorat, C. Comar, U. D'Oro, S. Nuti, M. Houghton, V. Barnaba, G. Pozzato, et al. Activation of naive B lymphocytes via CD81, a pathogenetic mechanism for hepatitis C virus-associated B lymphocyte disorders PNAS, December 20, 2005; 102(51): 18544 - 18549. [Abstract] [Full Text] [PDF]

				K. L. Clark, A. Oelke, M. E. Johnson, K. D. Eilert, P. C. Simpson, and S. C. Todd CD81 Associates with 14-3-3 in a Redox-regulated Palmitoylation-dependent Manner J. Biol. Chem., May 7, 2004; 279(19): 19401 - 19406. [Abstract] [Full Text] [PDF]

				F. Ma, M. Wada, H. Yoshino, Y. Ebihara, T. Ishii, A. Manabe, R. Tanaka, T. Maekawa, M. Ito, H. Mugishima, et al. Development of human lymphohematopoietic stem and progenitor cells defined by expression of CD34 and CD81 Blood, June 15, 2001; 97(12): 3755 - 3762. [Abstract] [Full Text] [PDF]

				F. Berditchevski Complexes of tetraspanins with integrins: more than meets the eye J. Cell Sci., January 12, 2001; 114(23): 4143 - 4151. [Abstract] [Full Text] [PDF]

				K. R. Bobbitt and L. B. Justement Regulation of MHC Class II Signal Transduction by the B Cell Coreceptors CD19 and CD22 J. Immunol., November 15, 2000; 165(10): 5588 - 5596. [Abstract] [Full Text] [PDF]

				J. Deng, V. P. Yeung, D. Tsitoura, R. H. DeKruyff, D. T. Umetsu, and S. Levy Allergen-Induced Airway Hyperreactivity Is Diminished in CD81-Deficient Mice J. Immunol., November 1, 2000; 165(9): 5054 - 5061. [Abstract] [Full Text] [PDF]

				H. M. Munnelly, C. J. Brady, G. M. Hagen, W. F. Wade, D. A. Roess, and B. G. Barisas Rotational and lateral dynamics of I-Ak molecules expressing cytoplasmic truncations Int. Immunol., September 1, 2000; 12(9): 1319 - 1328. [Abstract] [Full Text] [PDF]

				A. Higginbottom, E. R. Quinn, C.-C. Kuo, M. Flint, L. H. Wilson, E. Bianchi, A. Nicosia, P. N. Monk, J. A. McKeating, and S. Levy Identification of Amino Acid Residues in CD81 Critical for Interaction with Hepatitis C Virus Envelope Glycoprotein E2 J. Virol., April 15, 2000; 74(8): 3642 - 3649. [Abstract] [Full Text]

				M. S. Chen, K. S. K. Tung, S. A. Coonrod, Y. Takahashi, D. Bigler, A. Chang, Y. Yamashita, P. W. Kincade, J. C. Herr, and J. M. White Role of the integrin-associated protein CD9 in binding between sperm ADAM 2 and the egg integrin alpha 6beta 1: Implications for murine fertilization PNAS, October 12, 1999; 96(21): 11830 - 11835. [Abstract] [Full Text] [PDF]

				C. Claas, S. Seiter, A. Claas, L. Savelyeva, M. Schwab, and M. Zoller Association Between the Rat Homologue of CO-029, a Metastasis-associated Tetraspanin Molecule and Consumption Coagulopathy J. Cell Biol., April 6, 1998; 141(1): 267 - 280. [Abstract] [Full Text] [PDF]

				E. N. Tsitsikov, J. C. Gutierrez-Ramos, and R. S. Geha Impaired CD19 expression and signaling, enhanced antibody response to type II T independent antigen and reduction of B-1 cells in CD81-deficient mice PNAS, September 30, 1997; 94(20): 10844 - 10849. [Abstract] [Full Text] [PDF]

				P. M. Sincock, G. Mayrhofer, and L. K. Ashman Localization of the Transmembrane 4 Superfamily (TM4SF) Member PETA-3 (CD151) in Normal Human Tissues: Comparison with CD9, CD63, and {alpha}5ss1 Integrin J. Histochem. Cytochem., January 1, 1997; 45(4): 515 - 526. [Abstract] [Full Text] [PDF]

				E. E. Geisert Jr., L. Yang, and M. H. Irwin Astrocyte Growth, Reactivity, and the Target of the Antiproliferative Antibody, TAPA J. Neurosci., September 1, 1996; 16(17): 5478 - 5487. [Abstract] [Full Text] [PDF]

				X.-R. Wu, J. J. Medina, and T.-T. Sun Selective Interactions of UPIa and UPIb, Two Members of the Transmembrane 4 Superfamily, with Distinct Single Transmembrane-domained Proteins in Differentiated Urothelial Cells J. Biol. Chem., December 15, 1995; 270(50): 29752 - 29759. [Abstract] [Full Text] [PDF]

				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. [Abstract] [Full Text] [PDF]

				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. [Abstract] [Full Text] [PDF]