Biochemistry of antigen receptor signaling in mature and developing B lymphocytes

Critical Reviews in Immunology

Volumn 17, Issue 3-4, 1997, Pages 353-385

  Birkeland, Marian L ^a   Monroe, John G ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Antigen receptor; B cell; Co receptor; Development; Signal transduction

Indexed keywords

LYMPHOCYTE ANTIGEN RECEPTOR; PROTEIN TYROSINE KINASE;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANTIGEN PRESENTATION; ANTIGEN RECOGNITION; B LYMPHOCYTE ACTIVATION; BIOCHEMISTRY; CELL MATURATION; CROSS LINKING; ENZYME REGULATION; IMMUNE RESPONSE; MAJOR HISTOCOMPATIBILITY COMPLEX; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; REVIEW; SIGNAL TRANSDUCTION;

EID: 0031009145     PISSN: 10408401     EISSN: None     Source Type: Journal    
DOI: 10.1615/critrevimmunol.v17.i3-4.50     Document Type: Review

References (228)

1. Hombach, J., Leclerq, L., Radbruch, A., Rajewsky, K., and Reth, M., A novel 34-kd protein co-isolated with the IgM molecule in surface IgM-expressing cells, EMBO J., 7, 3451, 1988.
2. Campbell, K. S. and Cambier, J. C., B lymphocyte antigen receptors (mlg) are noncovalently associated with a disulphide-linked, inducibly phosphorylated glycoprotein complex, EMBO J., 9, 441, 1990.
3. Wienands, J., Hombach, J., Radbruch, A., Riester, C., and Reth, M., Molecular components of the B-cell antigen receptor complex of class IgD differ partly from those of IgM, EMBO J., 9, 449, 1990.
4. Campbell, K. S., Hager, E. J., Friedrich, R. J., and Cambier, J. C., IgM antigen receptor complex contains phosphoprotein products of B29 and mb-1 genes, Proc. Natl. Acad. Sci. U.S.A., 88, 3982, 1991.
5. Hombach, J., Lottspeich, F., and Reth, M., Identification of the genes encoding the IgM-a and IgM-b components of the IgM antigen receptor complex by amino terminal sequencing, Eur. J. Immunol., 20, 2795, 1990.
6. Sakaguchi, N., Kashiwamura, S.-I., Kimoto, M., Thalmann, P., and Melchers, F., B lymphocyte lineage-restricted expression of mb-1, a gene with CD3-like structural properties, EMBO J., 7, 3457, 1988.
7. Hermanson, G. G., Eisenberg, D., Kincade, P. W., and Wall, R., B29: a member of the immunoglobulin gene superfamily exclusively expressed on B-lineage cells, Proc. Natl. Acad. Sci. U.S.A., 85, 6890, 1988.
8. Hombach, J., Tsubata, T., Leclerq, L., Stappert, H., and Reth, M., Molecular components of the B-cell antigen receptor complex of the IgM class, Nature, 343, 760, 1990.
9. Campbell, K. S., Hagner, E. J., and Cambier, J. C., α-Chains of IgM and IgD antigen receptor complexes are differentially N-glycosylated MB-1-related molecules, J. Immunol., 147, 1575, 1991.
10. Friedrich, R. J., Campbell, K. S., and Cambier, J. C., The γ subunit of the B-cell antigen receptor complex is a C-terminally truncated product of the B29 gene, J. Immunol., 150, 2814, 1993.
11. Venkitaraman, A. R., Williams, G. T., Dariavach, P., and Neuberger, M. S., The B-cell antigen receptor of the five immunoglobulin classes, Nature, 352, 777, 1991.
12. Barclay, A. N., Beyers, A. D., Birkeland, M. L., Brown, M. H., Davis, S. J., Somoza, C., and Williams, A. F., The Leucocyte Antigen Factsbook, Academic Press, London, 1992, 1.
13. Reth, M., Antigen receptor tail clue, Nature, 338, 383, 1989.
14. Chan, A. C., Desai, D. M., and Weiss, A., The role of protein tyrosine kinases and protein tyrosine phosphatases in T-cell antigen receptor signal transduction [Review], Annu. Rev. Immunol., 12, 555, 1994.
15. Grupp, S. A., Mitchell, R. N., Schreiber, K. L., McKean, D. J., and Abbas, A. K., Molecular mechanisms that control expression of the B lymphocyte antigen receptor complex, J. Exp. Med., 181, 161, 1995.
16. Grupp, S. A., Campbell, K., Mitchell, R. N., Gambier, J. C., and Abbas, A. K., Signaling-defeclive mutants of the B lymphocyte antigen receptor fail to associate with Ig-alpha and Ig-beta/gamma, J. Biol. Chem., 268, 25776, 1993.
17. Papavasiliou, F., Jankovic, M., Suh, H., and Nussenzweig, M. C., The cytoplasmic domains of immunoglobulin (Ig) α and Igβ can independently induce the precursor B-cell transition and allelic exclusion, J. Exp. Med., 182, 1389, 1995.
18. Papavasiliou, F., Misulovin, Z., Suh, H., and Nussenzweig, M. C., The role of Ig beta in precursor B cell transition and allelic exclusion, Science, 268, 408, 1995.
19. Burkhardt, A. L., Brunswick, M., Bolen, J. B., and Mond, J. J., Anti-immunoglobulin stimulation of B lymphocytes activates src-related protein-tyrosine kinases, Proc. Natl. Acad. Sci. U.S.A., 88, 7410, 1991.
20. Gold, M. R., Law, D. A., and DeFranco, A. L., Stimulation of protein tyrosine phosphorylation by the B-lymphocyte antigen receptor, Nature, 345, 810, 1990.
21. Gold, M. R., Matsuuchi, L., Kelly, R. B., and DeFranco, A. L., Tyrosine phosphorylation of components of the B-cell antigen receptors following cross-linking, Proc. Natl. Acad. Sci. U.S.A., 88, 3436, 1991.
22. Cambier, J. C., Pleiman, C. M., and Clark, M. R., Signal transduction by the B-cell antigen receptor and its coreceptors, Annu. Rev. Immunol., 12, 457, 1994.
23. Clark, M. R., Johnson, S. A., and Cambier, J. C., Analysis of Ig-α tyrosine kinase interaction reveals two levels of binding specificity and tyrosine phosphorylated Ig-α stimulation of Fyn activity, EMBO J., 13, 1911, 1994.
24. Ren, R., Mayer, B. J., Cicchetti, P., and Baltimore, D., Identification of a ten-amino acid proline-rich SH3 binding site, Science, 259, 1157, 1993.
25. Mayer, B. J., Jackson, P. K., and Baltimore, D., The noncatalytic src homology region 2 segment of abl tyrosine kinase binds to tyrosine-phosphorylated cellular proteins with high affinity, Proc. Natl. Acad. Sci. U.S.A., 88, 627, 1991.
26. Pawson, T., Protein modules and signalling networks, Nature, 373, 573, 1995.
27. Bolen, J. B., Protein tyrosine kinases in the initiation of antigen receptor signaling [Review], Curr. Opin. Immunol, 7, 306, 1995.
28. Carter, R. H. and Fearon, D. T., CD19: lowering the threshold for antigen receptor stimulation of B lymphocytes, Science, 256, 105, 1992.
29. Fearon, D. T. and Carter, R. H., The CD19/CR2/ TAPA-1 complex of B lymphocytes: linking natural to acquired immunity [Review], Annu. Rev. Immunol., 13, 127, 1995.
30. Bradbury, L. E., Kansas, G. S., Levy, S., Evans, R. L., and Tedder, T. F., The CD19/CD21 signal transducing complex of human B lymphocytes includes the target of antiproliferative antibody-1 and Leu-13 molecules, J. Immunol., 149, 2841, 1992.
31. Matsumoto, A. K., Kopicky-Burd, J., Carter, R. H., Tuveson, D. A., Tedder, T. F., and Fearon, D. T., Intersection of the complement and immune systems: a signal transduction complex of the B lymphocyte-containing complement receptor type 2 and CD19, J. Exp. Med., 173, 55, 1991.
32. Chalupny, N. J., Kanner, S. B., Schieven, G. L., Wee, S., Gilliland, L. K., Aruffo, A., and Ledbetter, J. A., Tyrosine phosphorylation of CD 19 in pre-B and mature B cells, EMBO J., 12, 2691, 1993.
33. Uckun, F. M., Burkhardt, A. L., Jarvis, L., Jun, X., Stealey, B., Dibirdik, I., Myers, D. E., Tuel-Ahlgren, L., and Bolen, J. B., Signal transduction through the CD19 receptor during discrete developmental stages of human B-cell ontogeny, J. Biol. Chem., 268, 21172, 1993.
34. Chalupny, N. J., Aruffo, A., Esselstyn, J. M., Chan, P. Y., Bajorath, J., Blake, J., Gilliland, L. K., Ledbetter, J. A., and Tepper, M. A., Specific binding of Fyn and phosphatidylinositol 3-kinase to the B-cell surface glycoprotein CD19 through their src homology 2 domains, Eur. J. Immunol., 25, 2978, 1995.
35. van Noesel, C. J., Lankester, A. C., van Schijndel, G. M., and van Lier, R. A., The CR2/CD19 complex on human B cells contains the src-family kinase Lyn, Int. Immunol., 5, 699, 1993.
36. Fearon, D. T. and Ahearn, J. M., Complement receptor type 1 (C3b/C4b receptor; CD35) and complement receptor type 2 (C3d/Epstein-Barr virus receptor; CD21) [Review], Curr. Top. Micro. Immunol., 153, 83, 1990.
37. Oren, R., Takahashi, S., Doss, C., Levy, R., and Levy, S., TAPA-1, the target of an antiproliferative antibody, defines a new family of transmembrane proteins, Mol. Cell. Biol., 10, 4007, 1990.
38. Levy, S., Nguyen, V. Q., Andria, M. L., and Takahashi, S., Structure and membrane topology of TAPA-1, J. Biol. Chem., 266, 14597, 1991.
39. Takahashi, S., Doss, C., Levy, S., and Levy, R., TAPA-1, the target of an antiproliferative antibody, is associated on the cell surface with the Leu-13 antigen, J. Immunol., 145, 2207, 1990.
40. Schick, M. R. and Levy, S., The TAPA-1 molecule is associated on the surface of B cells with HLA-DR molecules, J. Immunol., 151, 4090, 1993.
41. Angelisova, P., Hilgert, I., and Horejsi, V., Association of four antigens of the tetraspans family (CD37, CD53, TAPA-1, and R2/C33) with MHC class II glycoproteins, Immunogenetics, 39, 249, 1994.
42. Deblandre, G. A., Marinx, O. P., Evans, S. S., Majjaj, S., Leo, O., Caput, D., Huez, G. A., and Wathelet, M. G., Expression cloning of an interferon-inducible 17-kDa membrane protein implicated in the control of cell growth, J. Biol. Chem., 270, 23860, 1995.
43. Kansas, G. S. and Tedder, T. F., Transmembrane signals generated through MHC class II, CD19, CD20, CD39, and CD40 antigens induce LFA-1-dependent and independent adhesion in human B cells through a tyrosine kinase-dependent pathway, J. Immunol., 147, 4094, 1991.
44. Matsumoto, A. K., Martin, D. R., Carter, R. H., Klickstein, L. B., Ahearn, J. M., and Fearon, D. T., Functional dissection of the CD21/CD19/TAPA-1/ Leu-13 complex of B lymphocytes, J. Exp. Med., 178, 1407, 1993.
45. Tuveson, D. A., Carter, R. H., Soltoff, S. P., and Fearon, D. T., CD19 of B cells as a surrogate kinase insert region to bind phosphatidylinositol 3-kinase, Science, 260, 986, 1993.
46. Esselstyn, J. M., Chalupny, N. J., Aruffo, A., Gilliland, L. K., Ledbetter, J. A., and Tepper, M. A., Specific binding of Fyn and phosphatidylinositol 3-kinase to the B-cell surface glycoprotein CD19 through their src homology 2 domains, Eur. J. Immunol., 25, 2978, 1995.
47. Roifman, C. M. and Ke, S., CD19 is a substrate of the antigen receptor-associated protein tyrosine kinase in human B cells, Biochem. Biophys. Res. Comm., 194, 222, 1993.
48. Nagai, K., Takata, M., Yamamura, H., and Kurosaki, T., Tyrosine phosphorylation of She is mediated through Lyn and Syk in B-cell receptor signaling, J. Biol. Chem., 270, 6824, 1995.
49. Nishizumi, H., Yaniuchi, I., Yamanashi, Y., Kitamura, D., Ilic, D., Mori, S., Watanabe, T., and Yamamoto, T., Impaired proliferation of peripheral B cells and indication of autoimmune disease in lyn-deficient mice, Immunity, 3, 549, 1995.
50. Hibbs, M. L., Tarinton, D. M., Armes, J., Grail, D., Hodgson, G., Maglitto, R., Stacker, S. A., and Dunn, A. R., Multiple defection in the immune system of Lyn-deficient mice, culminating in autoimmune disease, Cell, 83, 301, 1995.
51. Dempsey, P. W., Allison, M. E., Akkaraju, S., Goodnow, C. C., and Fearon, D. T., C3d of complement as a molecular adjuvant: bridging innate and acquired immunity, Science, 271, 348, 1996.
52. Ahearn, J. M., Fischer, M. B., Croix, D., Goerg, S., Ma, M., Xia, J., Zhou, X., Howard, R. G., Rothstein, T. L., and Carroll, M. C., Disruption of the Cr2 locus results in a reduction in B-1a cells and in an impaired B-cell response to T-dependent antigen, Immunity, 4, 251, 1996.
53. Riekert, R. C., Rajewsky, K., and Roes, J., Impairment of T-cell-dependent B-cell responses and B-1 cell development in CD 19-deficient mice, Nature, 376, 352, 1995.
54. Sato, S., Steeber, D. A., and Tedder, T. F., The CD 19 signal transduction molecule is a response regulator of B-lymphocyte differentiation, Proc. Natl. Acad. Sci. U.S.A., 92, 11558, 1995.
55. Engel, P., Zhou, L. J., Ord, D. C., Sato, S., Koller, B., and Tedder, T. F., Abnormal B lymphocyte development, activation, and differentiation in mice that lack or overexpress the CD19 signal transduction molecule, Immunity, 3, 39, 1995.
56. Leprince, C., Draves, K. E., Geahlen, R. L., Ledbetter, J. A., and Clark, E. A., CD22 associates with the human surface IgM-B-cell antigen receptor complex, Proc. Natl. Acad. Sci. U.S.A., 90, 3236, 1993.
57. Peaker, C. J. and Neuberger, M. S., Association of CD22 with the B-cell antigen receptor, Eur. J. Immunol., 23, 1358, 1993.
58. Schulte, R. J., Campbell, M. A., Fischer, W. H., and Sefton, B. M., Tyrosine phosphorylation of CD22 during B-cell activation, Science, 258, 1001, 1992.
59. Engel, P., Wagner, N., Miller, A. S., and Tedder, T. F., Identification of the ligand-binding domains of CD22, a member of the immunoglobulin superfamily that uniquely binds a sialic acid-dependent ligand, J. Exp. Med., 181, 1581, 1995.
60. Campbell, M. A. and Klinman, N. R., Phosphotyrosine-dependent association between CD22 and protein tyrosine phosphatase 1C, Eur. J. Immunol., 25, 1573, 1995.
61. Doody, G. M., Justement, L. B., Delibrias, C. C., Matthews, R. J., Lin, J., Thomas, M. L., and Fearon, D. T., A role in B-cell activation for CD22 and the protein tyrosine phosphatase SHP, Science, 269, 242, 1995.
62. Law, C. L., Sidorenko, S. P., Chandran, K. A., Zhao, A., Shen, S. H., Fischer, E. H., and Clark, E. A., CD22 associates with protein tyrosine phosphatase 1C, Syk, and phospholipase C-γ1 upon B-cell activation, J. Exp. Med., 183, 547, 1996.
63. Thomas, M. L., The leukocyte common antigen family [Review], Annu. Rev. Immunol., 1, 339, 1989.
64. Trowbridge, I. S. and Thomas, M. L., CD45: an emerging role as a protein tyrosine phosphatase required for lymphocyte activation and development [Review], Annu. Rev. Immunol., 12, 85, 1994.
65. Charbonneau, H., Tonks, N. K., Kumar, S., Diltz, C. D., Harrylock, M., Cool, D. E., Krebs, E. G., Fischer, E. H., and Walsh, K. A., Human placenta protein-tyrosine-phosphatase: amino acid sequence and relationship to a family of receptor-like proteins, Proc. Natl. Acad. Sci. U.S.A., 86, 5252, 1989.
66. Charbonneau, H., Tonks, N. K., Walsh, K. A., and Fischer, E. H.,The leukocyte common antigen (CD45): a putative receptor-linked protein tyrosine phosphatase, Proc. Natl. Acad. Sci. U.S.A., 85, 7182, 1988.
67. Justement, L. B., Campbell, K. S., Chien, N., and Cambier, J. C., Regulation of B-cell antigen receptor signal transduction and phosphorylation by CD45, Science, 252, 1839, 1991.
68. Pingel, J. T. and Thomas, M. L., Evidence that the leukocyte-common antigen is required for antigen-induced T-lymphocyte proliferation. Cell, 58, 1055, 1989.
69. Kishihara, K., Penninger, J., Wallace, V. A., Kundig, T. M., Kawai, K., Wakeham, A., Timms, E., Pfeffer, K., Ohashi, P. S., Thomas, M. L., Furlonger, C., Paige, C. J., and Mak, T. W., Normal B-lymphocyte development but impaired T-cell maturation in CD45-exon6 protein tyrosine phosphatase-deficient mice, Cell, 74, 143, 1993.
70. Benatar, T., Carsetti, R., Furlonger, C., Kamalia, N., Mak, T., and Paige, C. J., Immunoglobulin-mediated signal transduction in B cells from CD45-deficient mice, J. Exp. Med., 183, 329, 1996.
71. Hovis, R. R., Donovan, J. A., Musci, M. M., Motto, D. G., Goldman, F. D., Ross, S. E., and Koretzky, G. A., Rescue of signaling by a chimeric protein containing the cytoplasmic domain of CD45, Science, 260, 544, 1993.
72. 2+ oscillations, J. Exp. Med., 176, 835, 1992.
73. Howard, M., Grimaldi, J. C., Bazan, J. F., Lund, F. E., Santos-Argumedo, L., Parkhouse, R. M., Walseth, T. F., and Lee, H. C., Formation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38, Science, 262, 1056, 1993.
74. Lund, F., Solvason, N., Grimaldi, J. C., Parkhouse, R. M., and Howard, M., Murine CD38: an immunoregulatory ectoenzyme [Review], Immunol. Today, 16, 469, 1995.
75. Kikuchi, Y., Yasue, T., Miyake, K., Kimoto, M., and Takatsu, K., CD38 ligation induces tyrosine phosphorylation of Bruton tyrosine kinase and enhanced expression of interleukin 5-receptor alpha chain: synergistic effects with interleukin 5, Proc. Natl. Acad. Sci. U.S.A., 92, 11814, 1995.
76. Lund, F. E., Solvason, N. W., Cooke, M. P., Heath, A. W., Grimaldi, J. C., Parkhouse, R. M. E., Goodnow, C. C., and Howard, M. C., Signaling through murine CD38 is impaired in antigen receptor-unresponsive B cells, Eur. J. Immunol., 25, 1338, 1995.
77. Santos-Argumedo, L., Lund, F. E., Heath, A. W., Solvason, N., Wu, W. W., Grimaldi, J. C., Parkhouse, R. M., and Howard, M., CD38 unresponsiveness of xid B cells implicates Bruton's tyrosine kinase (btk) as a regular of CD38-induced signal transduction, Int. Immunol., 7, 163, 1995.
78. Lund, F. E., Naixuan, Y., Kim, K.-M., Reth, M., and Howard, M. C., Signaling through CD38 augments B-cell antigen receptor (BCR) responses and is dependent on BCR expression, J. Immunol., 157, 1455, 1996.
79. Parker, D. C., Induction and suppression of polyclonal antibody responses by anti-Ig reagents and antigen-nonspecific helper factors: a comparison of the effects of anti-Fab, anti-IgM, and anti-IgD on murine B cells [Review], Immunol. Rev., 52, 115, 1980.
80. Bijsterbosch, M. K. and Klaus, G. G. B., Cross-linking of surface immunoglobulin and Fc receptors on B lymphocytes inhibits stimulation of inositol phospholipid breakdown via the antigen receptors, J. Exp. Med., 162, 1825, 1985.
81. D'Ambrosio, D., Hippen, K. L., Minskoff, S. A., Mellman, I., Pani, G., Siminovitch, K. A., and Gambier, J. C., Recruitment and activation of PTP1C in negative regulation of antigen receptor signaling by FcγRIIB1, Science, 268, 293, 1995.
82. Muta, T., Kurosaki, T., Misulovin, Z., Sanchez, M., Nussenzweig, M. C., and Ravetch, J. V., A 13-amino-acid motif in the cytoplasmic domain of FcγRIIB modulates B-cell receptor signaling, Nature, 368, 70, 1994.
83. Ravetch, J. V. and Kinet, J. P., Fc receptors [Review], Annu. Rev. Immunol., 9, 457, 1991.
84. Saouaf, S. J., Mahajan, S., Rowley, R. B., Kut, S. A., Fargnoli, J., Burkhardt, A. L., Tsukada, S., Witte, O. N., and Bolen, J. B., Temporal differences in the activation of three classes of non-transmembrane protein tyrosine kinases following B-cell antigen receptor surface engagement, Proc. Natl. Acad. Sci. U.S.A., 91, 9524, 1994.
85. Rawlings, D. J. and Witte, O. N., Bruton's tyrosine kinase is a key regulator in B-cell development [Review], Immunol. Rev., 138, 105, 1994.
86. Conley, M. E., Parolini, O., Rohrer, J., and Campana, D., X-linked agammaglobulinemia: new approaches to old questions based on the identification of the defective gene [Review], Immunol. Rev., 138, 5, 1994.
87. Mayer, B. J., Ren, R., Clark, K. L., and Baltimore, D., A putative modular domain present in diverse signaling proteins [letter], Cell, 73, 629, 1993.
88. Yao, L., Kawakami, Y., and Kawakami, T., The pleckstrin homology domain of Bruton tyrosine kinase interacts with protein kinase C, Proc. Natl. Acad. Sci. U.S.A., 91, 9175, 1994.
89. Hyvonen, M., Macias, M. J., Nilges, M., Oschkinat, H., Saraste, M., and Wilmanns, M., Structure of the binding site for inositol phosphates in a PH domain, EMBO J., 14, 4676, 1995.
90. Cheng, G., Ye, Z. S., and Baltimore, D., Binding of Bruton's tyrosine kinase to Fyn, Lyn, or Hck through a Src homology 3 domain-mediated interaction, Proc. Natl. Acad. Sci. U.S.A., 91, 8152, 1994.
91. Aoki, Y., Isselbacher, K. J., and Pillai, S., Bruton tyrosine kinase is tyrosine phosphorylated and activated in pre-B lymphocytes and receptor-ligated B cells, Proc. Natl. Acad. Sci. U.S.A., 91, 10606, 1994.
92. Hutchcroft, J. E., Harrison, M. L., and Geahlen, R. L., Association of the 72-kDa protein-tyrosine kinase PTK72 with the B-cell antigen receptor, J. Biol. Chem., 267, 8613, 1992.
93. Chow, L. M., Fournel, M., Davidson, D., and Veillette, A., Negative regulation of T-cell receptor signalling by tyrosine protein kinase p50csk, Nature, 365, 156, 1993.
94. Sabe, H., Okada, M., Nakagawa, H., and Hanafusa, H., Activation of c-Src in cells bearing v-Crk and its suppression by Csk, Mol. Cell. Biol., 12, 4706, 1992.
95. fgr is expressed in murine splenic B cells and is activated in response to antigen receptor crosslinking, J. Immunol., 154, 3234, 1995.
96. fgr, J. Immunol., 154, 1919, 1995.
97. Wasserman, R., Li, V.-S., and Hardy, R. R., Differential expression of the Blk and Ret tyrosine kinases during B lineage development is dependent on Ig rearrangement, J. Immunol., 155, 644, 1995.
98. Weng, W. K., Jarvis, L., and LeBien, T. W., Signaling through CD19 activates Vav/mitogen-activated protein kinase pathway and induces formation of a CD19/Vav/phosphatidylinositol 3-kinase complex in human B-cell precursors, J. Biol. Chem., 269, 32514, 1994.
99. Turner, M., Mee, P. J., Costello, P. S., Williams, O., Price, A. A., Duddy, L. P., Furlong, M. T., Geahlen, R. L., and Tybulewicz, V. L., Perinatal lethality and blocked B-cell development in mice lacking the tyrosine kinase Syk, Nature, 378, 298, 1995.
100. Cheng, A. M., Rowley, B., Pao, W., Hayday, A., Bolen, J. B., and Pawson, T., Syk tyrosine kinase required for mouse viability and B-cell development, Nature, 378, 303, 1995.
101. 2+ mobilization through distinct pathways, EMBO J., 13, 1341, 1994.
102. Kurosaki, T., Takata, M., Yamanashi, Y., Inazu, T., Taniguchi, T., Yamamoto, T., and Yamamura, H., Syk activation by the Src-family tyrosine kinase in the B-cell receptor signaling, J. Exp. Med., 179, 1725, 1994.
103. Kurosaki, T., Johnson, S. A., Pao, L., Sada, K., Yamamura, H., and Cambier, J. C., Role of the syk autophosphorylation site and SH2 domains in B-cell antigen receptor signaling, J. Exp. Med., 182, 1815, 1995.
104. Rowley, R. B., Burkhardt, A. L., Chao, H.-G., Matsueda, G. R., and Bolen, J. R., Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Igα/Igβ immunoreceptor tyrosine activation motif binding and autophosphorylation, J. Biol. Chem., 19, 11590, 1995.
105. Johnson, S. A., Pleiman, C. M., Pao, L., Schneringer, J., Hippen, K., and Cambier, J. C., Phosphorylated immunoreceptor signaling motifs (ITAMS) exhibit unique abilities to bind and activate lyn and syk tyrosine kinases, J. Immunol, 155, 4596, 1995.
106. Sillman, A. L. and Monroe, J. G., Association of p72syk with the src homology-2 (SH2) domains of PLCγ1 in B lymphocytes, J. Biol. Chem., 270, 11806, 1995.
107. Hata, A., Sabe, H., Kurosaki, T., Takata, M., and Hanafusa, H., Functional analysis of csk in signal transduction through the B-cell antigen receptor, Mol. Cell. Biol, 14, 7306, 1994.
108. Rawlings, D. J., Saffran, D. C., Tsukada, S., Largaespada, D. A., Grimaldi, J. C., Cohen, L., Mohr, R. N., Bazan, J. F., Howard, M., Copeland, N. G., Jenkins, N. A., and Witte, O. N., Mutation of unique region of Bruton's tyrosine kinase in immunodeficient XID mice, Science, 261, 358, 1993.
109. Thomas, J. D., Sideras, P., Smith, C. I., Vorechovsky, I., Chapman, V., and Paul, W. E., Colocalization of X-linked agammaglobulinemia and X-linked immunodeficiency genes, Science, 261, 355, 1993.
110. Tsukada, S., Saffran, D. C., Rawlings, D. J., Parolini, O., Allen, R. C., Klisak, I., Sparkles, R. S., Kubagawa, H., Mohandas, T., Quan, S., Belmont, J. W., Cooper, M. D., Conley, M. E., and Witte, O. N., Deficient expression of a B-cell cytoplasmic tyrosine kinase in human X-linked agammaglobulinemia, Cell, 72, 279, 1993.
111. Vetrie, D., Vorechovsky, I., Sideras, P., Holland, J., Davies, A., Flinter, F., Hammarstrom, L., Kinnon, C., Levinsky, R., Bobrow, M., Smith, C. I. E., and Bentley, D. R., The gene involved in X-linked agammaglobulinaemia is a member of the src family of protein-tyrosine kinases [published erratum appears in Nature, 364(6435), 362, 1993] [see comments], Nature, 361, 226, 1993.
112. Lemmon, M. A., Ferguson, K. M., and Schlessinger, J., PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surface, Cell, 85, 621, 1996.
113. 1 transition of resting B lymphocytes, J. Immunol., 135, 1674, 1985.
114. Klaus, G. G. B., O'Garra, A., Bijsterbosch, M. K., and Holman, M., Induction of DNA synthesis in B cells by a combination of Ca2+ ionophores and phorbol myristic acetate, Eur. J. Immunol., 16, 92, 1985.
115. Kim, T. J., Kim, Y. T., and Pillai, S., Association of activated phosphatidylinositol 3-kinase with p120cbl in antigen receptor-ligated B cells, J. Biol. Chem., 270, 27504, 1995.
116. cbl is a major substrate of tyrosine phosphorylation upon B-cell antigen receptor stimulation and interacts in vivo with Fyn and Syk tyrosine kinases, Grb2 and She adaptors, and the p85 subunit of phosphatidylinositol 3-kinase, J. Biol. Chem., 271, 3187, 1996.
117. Pleiman, C. M., Hertz, W. M., and Cambier, J. C., Activation of phosphatidylinositol-3′ kinase by Src-family kinase SH3 binding to the p85 subunit, Science, 263, 1609, 1994.
118. Yamanashi, Y., Fukui, Y., Wongsasant, W., Kinoshita, Y., Ichimoiri, Y., Yoyoshima, Y., and Yamamoto, T., Activation of Src-like protein tyrosine kinase lyn and its association with phosphatidyl-inositol 3-kinase upon B-cell antigen receptor-mediated signaling, Proc. Natl. Acad. Sci. U.S.A., 89, 1118, 1992.
119. Kapeller, R. and Cantley, L. C., Phosphatidylinositol 3-kinase [Review], Bioessays, 16, 565, 1994.
120. Ward, S. G., June, C. H., and Olive, D., PI 3-kinase: a pivotal pathway in T-cell activation?, Immunol. Today, 17, 187, 1996.
121. Gold, M. R., Chan, V. W. F., Turck, C. W., and DeFranco, A. L., Membrane Ig crosslinking regulates phosphatidylinositol 3 kinase in B lymphocytes, J. Immunol., 148, 2012, 1992.
122. Gold, M. R. and Aebersold, R., Both phosphatidylinositol 3-kinase and phosphatidylinositol 4-kinase products are increased by antigen receptor signaling in B cells, J. Immunol., 152, 42, 1994.
123. Nakanishi, H., Brewer, K. A., and Exton, J. H., Activation of the ζ isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate, J. Biol. Chem., 268, 13, 1993.
124. Bos, J. L., A target for phosphoinositide 3-kinase: Akt/ PKB [Review], Trends Biochem. Sci., 20, 441, 1995.
125. Burgering, B. M. and Coffer, P. J., Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction [see comments], Nature, 376, 599, 1995.
126. Franke, T. F., Yang, S. I., Chan, T. O., Datta, K., Kazlauskas, A., Morrison, D. K., Kaplan, D. R., and Tsichlis, P. N., The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase, Cell, 81, 727, 1995.
127. Petritsch, C., Woscholski, R., Edelmann, H. M., Parker, P. J., and Ballou, L. M., Selective inhibition of p70 S6 kinase activation by phosphatidylinositol 3-kinase inhibitors, Eur. J. Biochem., 230, 431, 1995.
128. Weng, Q. P., Andrabi, K., Klippel, A., Kozlowski, M. T., Williams, L. T., and Avruch, J., Phosphatidylinositol 3-kinase signals activation of p70 S6 kinase in situ through site-specific p70 phosphorylation, Proc. Natl. Acad. Sci. U.S.A., 92, 5744, 1995.
129. Karnitz, L. M., Burns, L. A., Sutor, S. L., Blenis, J., and Abraham, R. T., Interleukin-2 triggers a novel phosphatidylinositol 3-kinase-dependent MEK activation pathway, Mol. Cell. Biol., 15, 3049, 1995.
130. Dhand, R., Hiles, I., Panayotou, G., Roche, S., Fry, M. J., Gout, I., Totty, N. F., Truong, O., Vicendo, P., Yonezawa, K., Kasuga, M., Courtneige, S. A., and Waterfield, M. D., PI 3-kinase is a dual specificity enzyme: autoregulation by an intrinsic protein-serine kinase activity, EMBO J., 13, 522, 1994.
131. Gold, M. R., Crowley, M. T., Martin, G. A., McCormick, F., and DeFranco, A. L., Targets of B lymphocyte antigen receptor signal transduction include the p21ras GTPase-activating protein (GAP) and two GAP-associated proteins, J. Immunol., 150, 377, 1993.
132. Saxton, T. M., vacOostveen, I., Bowtell, D., Aebersold, R., and Gold, M. R., B-cell antigen receptor cross-linking induces phosphorylation of the p21ras oncoprotein activators SHC and mSOS1 as well as assembly of complexes containing SHC, GRB-2, mSOS1, and a 145-kDa tyrosine-phosphorylated protein, J. Immunol., 153, 623, 1994.
133. Boyer, M. J., Gutmann, D. H., Collins, F. S., and Bar-Sagi, D., Crosslinking of the surface immunoglobulin receptor in B lymphocytes induces a redistribution of neurofibromin but not p 120-GAP, Oncogene, 9, 349, 1994.
134. Boguski, M. S. and McCormick, F., Proteins regulating ras and its relatives, Nature, 366, 643, 1993.
135. Egan, S. E., Giddings, B. W., Brooks, M. W., Buday, L., Sizeland, A. M., and Weinberg, R. A., Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation [see comments], Nature, 363, 45, 1993.
136. Lowenstein, E. J., Daly, R. J., Batzer, A. G., Li, W., Margolis, B., Lammers, R., Ullrich, A., Skolnik, E. Y., Bar-Sagi, D., and Schlessinger, J., The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling, Cell, 70, 431, 1992.
137. Smit, L., de Vries-Smits, A. M., Bos, J. L., and Borst, J., B-cell antigen receptor stimulation induces formation of a Shc-Grb2 complex containing multiple tyrosine-phosphorylated proteins, J. Biol. Chem., 269, 20209, 1994.
138. Bustelo, X. R., Ledbetter, J. A., and Barbacid, M., Product of vav proto-oncogene defines a new class of tyrosine protein kinase substrates [see comments], Nature, 356, 68, 1992.
139. Margolis, B., Hu, P., Katzav, S., Li, W., Oliver, J. M., Ullrich, A., Weiss, A., and Schlessinger, J., Tyrosine phosphorylation of vav proto-oncogene product containing SH2 domain and transcription factor motifs [see comments]. Nature, 356, 71, 1992.
140. Bustelo, X. R. and Barbacid, M., Tyrosine phosphorylation of the vav proto-oncogene product in activated B cells, Science, 256, 1196, 1992.
141. 1, J. Immunol., 152, 2123, 1994.
142. Tarakhovsky, A., Turner, M., Schaal, S., Mee, P. J., Duddy, L. P., Rajewsky, K., and Tybulewicz, V. L. J., Defective antigen receptor-mediated proliferation of B and T cells in the absence of Vav, Nature, 374, 467, 1995.
143. Zhang, R., Alt, F. W., Davidson, L., Orkin, S. H., and Swat, W., Defective signalling through the T-and B-cell antigen receptors in lymphoid cells lacking the vav proto-oncogene, Nature, 374, 470, 1995.
144. Lankester, A. C., van Schijndel, G. M., Rood, P. M., Verhoeven, A. J., and van Lier, R. A., B-cell antigen receptor cross-linking induces tyrosine phosphorylation and membrane translocation of a multimeric She complex that is augmented by CD19 co-ligation, Eur. J. Immunol., 24, 2818, 1994.
145. Crowley, M. T., Harmer, S. L., and DeFranco, A. L., Activation-induced association of a 145-kDa tyrosine-phosphorylated protein with She and Syk in B lymphocytes and macrophages, J. Biol. Chem., 271, 1145, 1996.
146. Blake, T. J., Shapiro, M., Morse, H. III, and Langdon, W. Y., The sequences of the human and mouse c-cbl proto-oncogenes show v-cbl was generated by a large truncation encompassing a proline-rich domain and a leucine zipper-like motif, Oncogene, 6, 653, 1991.
147. Taniuchi, I., Kitamura, D., Maekawa, Y., Fukuda, T., Kishi, H., and Watanabe, T., Antigen-receptor induced clonal expansion and deletion of lymphocytes are impaired in mice lacking HS1 protein, a substrate of the antigen-receptor-coupled tyrosine kinases, EMBO J., 14, 3664, 1995.
148. Langdon, W. Y. and Blake, T. J., The human CBL oncogene, Curr. Top. Microbiol. Immunol., 166, 159, 1990.
149. Tezuka, T., Umemori, H., Fusaki, N., Yagi, T., Takata, M., Kurosaki, T., and Yamamoto, T., Physical and functional association of the cbl protooncogene product with an Src-family protein tyrosine kinase, p53/56lyn, in the B-cell antigen receptor-mediated signaling, J. Exp. Med., 183, 675, 1996.
150. Yoon, C. H., Lee, J., Jongeward, G. D., and Sternberg, P. W., Similarity of sli-1, a regulator of vulval development in C. elegans, to the mammalian proto-oncogene c-cbl, Science, 269, 1102, 1995.
151. Yamanashi, Y., Okada, M., Semba, T., Yamori, T., Umemori, H., Tsunasawa, S., Toyoshima, K., Kitamura, D., Watanabe, T., and Yamamoto, T., Identification of HS1 protein as a major substrate of protein-tyrosine kinase(s) upon B-cell antigen receptor-mediated signaling, Proc. Natl. Acad. Sci. U.S.A., 90, 3631, 1993.
152. Baumann, G., Maier, D., Freuler, F., Tschopp, C., Baudisch, K., and Wienands, J., In vitro characterization of major ligands for Src homology 2 domains derived from protein tyrosine kinases, from the adaptor protein SHC and from GTPase-activating protein in Ramos B cells, Eur. J. Immunol., 24, 1799, 1994.
153. Fukuda, T., Kitamura, D., Taniuchi, I., Maekawa, Y., Benhamou, L. E., Sarthou, P., and Watanabe, T., Restoration of surface IgM-mediated apoptosis in an anti-IgM-resistant variant of WEHI-231 lymphoma cells by HS1, a protein-tyrosine kinase substrate, Proc. Natl. Acad. Sci. U.S.A., 92, 7302, 1995.
154. Wicker, L. S., Boltz, R., Jr., Matt, V., Nichols, E. A., Peterson, L. B., and Sigal, N. H., Suppression of B-cell activation by cyclosporin A, FK506 and rapamycin, Eur. J. Immunol., 20, 2277, 1990.
155. Shaw, J. P., Utz, P. J., Durand, D. B., Toole, J. J., Emmel, E. A., and Crabtree, G. R., Identification of a putative regulator of early T-cell activation genes, Science, 241, 202, 1988.
156. Rao, A., NF-ATp: a transcription factor required for the co-ordinate induction of several cytokine genes [Review], Immunol. Today, 15, 274, 1994.
157. Choi, M. S. K., Brines, R. D., Holman, M. J., and Klaus, G. G. B., Induction of NF-AT in normal B lymphocytes by anti-immunoglobulin or CD40 ligand in conjunction with IL-4, Immunity, 1, 179, 1994.
158. Yaseen, N. R., Maizel, A. L., Wang, F., and Sharma, S., Comparative analysis of NFAT (nuclear factor of activated T cells) complex in human T and B lymphocytes, J. Biol. Chem., 268, 14285, 1993.
159. Venkataraman, L., Francis, D. A., Wang, Z., Liu, J., Rothstein, T. L., and Sen, R., Cyclosporin-A sensitive induction of NF-AT in murine B cells, Immunity, 1, 189, 1994.
160. Rao, A., NFATp, a cyclosporin-sensitive transcription factor implicated in cytokine gene induction [Review], J. Leukocyte Biol., 57, 536, 1995.
161. Goldfeld, A. E., Flemington, E. K., Boussiotis, V. A., Theodos, C. M., Titus, R. G., Strominger, J. L., and Speck, S. H., Transcription of the tumor necrosis factor alpha gene is rapidly induced by anti-immunoglobulin and blocked by cyclosporin A and FK506 in human B cells, Proc. Natl. Acad. Sci. U.S.A., 89, 12198, 1992.
162. Jain, J., McCaffrey, P. G., Valge-Archer, V. E., and Rao, A., Nuclear factor of activated T cells contains Fos and Jun, Nature, 356, 801, 1992.
163. Monroe, J. G., Up-regulation of c-fos expression is a component of the mlg signal transduction mechanism but is not indicative of competence for proliferation, J. Immunol., 140, 1454, 1988.
164. Hibi, M., Lin, A., Smeal, T., Minden, A., and Karin, M., Identification of an oncoprotein-and UV-responsive protein kinase that binds and potentiates the c-jun activation domain, Genes Dev., 1, 2135, 1993.
165. Derijard, B., Hibi, M., Wu, I.-H., Barrett, T., Su, B., Deng, T., Karin, M., and Davis, R. J., JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain, Cell, 76, 1025, 1994.
166. Fisher, C. L., Ghysdael, J., and Cambier, J. C., Ligation of membrane Ig leads to calcium-mediated phosphorylation of the proto-oncogene product, Ets-1, J. Immunol., 146, 1743, 1991.
167. Liu, J., Chiles, T. C., Sen, R., and Rothstein, T. L., Inducible nuclear expression of NF-κB in primary B cells stimulated through the surface Ig receptor, J. Immunol., 146, 1685, 1991.
168. Xie, H., Chiles, T. C., and Rothstein, T. L., Indue tion of CREB activity via the surface Ig receptor of B cells, J. Immunol., 151, 880, 1993.
169. McMahon, S. B. and Monroe, J. G., Role of primary response genes in generating cellular responses to growth factors, FASEB J., 6, 2707, 1992.
170. Snow, E. C., Fetherston, J. D., and Zimmer, S., Induction of the c-myc protooncogene after antigen binding to hapten-specific B cells, J. Exp. Med., 164, 944, 1986.
171. McCormack, J. E., Pepe, V. H., Kent, R. B., Deans, M., Marshak-Rothstein, A., and Sonenshein, G. E., Specific regulation of c-myc oncogene expression in a murine B-cell lymphoma, Proc. Natl. Acad. Sci. U.S.A., 81, 5546, 1984.
172. Lacy, J., Summers, W. C., and Sarkar, S. N., Induction of c-myc expression in human B lymphocytes by B-cell growth factor and anti-immunoglobulin, Proc. Natl. Acad. Sci. U.S.A., 83, 1458, 1986.
173. Chiles, T. C. and Rothstein, T. L., Surface Ig receptor-induced nuclear AP-1-dependent gene expression in B lymphocytes, J. Immunol., 149, 825, 1992.
174. Cao, X. M., Koski, R. A., Gashler, A., McKiernan, M., Morris, C. F., Gaffney, R., Hay, R. V., and Sukhatme, V. P., Identification and characterization of the Egr-1 gene product, a DNA-binding zinc finger protein induced by differentiation and growth signals, Mol. Cell. Biol., 10, 1931, 1990.
175. Christy, B. and Nathans, D., DNA binding site of the growth factor-inducible protein Zif268, Proc. Natl. Acad. Sci. U.S.A., 86, 8737, 1989.
176. Lemaire, P., Vesque, C., Schmitt, J., Stunnenberg, H., Frank, R., and Charnay, P., The serum-inducible mouse gene Krox-24 encodes a sequence-specific transcriptional activator, Mol. Cell. Biol., 10, 3456, 1990.
177. 1 transition of the cell cycle, Mol. Cell. Biol., 14, 5242, 1994.
178. McMahon, S. B. and Monroe, J. G., Activation of the p21ras pathway couples antigen receptor stimulation to induction of the primary response gene egr-1 in B lymphocytes, J. Exp. Med., 181, 417, 1995.
179. Derijard, B., Raingeaud, J., Barrett, T., Wu, I.-H., Han, J., Ulevitch, R. J., and Davis, R. J., Independent human MAP kinase signal transduction pathways defined by MEK and MKK isoforms, Science, 267, 682, 1995.
180. Treisman, R., Transient accumulation of c-fos RNA following serum stimulation requires a conserved 5′ element and c-fos 3′ sequences, Cell, 42, 889, 1985.
181. Treisman, R., Identification of a protein-binding site that mediates transcriptional response of the c-fos gene to serum factors, Cell, 46, 567, 1986.
182. Treisman, R., Ternary complex factors: growth factor regulated transcriptional activators, Curr. Opin. Genet. Dev., 4, 96, 1994.
183. McMahon, S. B. and Monroe, J. G., A ternary complex factor-dependent mechanism mediates induction of egr-1 through selective serum response elements following antigen receptor cross-linking in B lymphocytes, Mol. Cell. Biol., 15, 1086, 1995.
184. Whitmarsh, A. J., Shore, P., Sharrocks, A.D., and Davis, R. J., Integration of MAP kinase signal transduction pathways at the serum response element, Science, 269, 403, 1995.
185. Janknecht, R., Ernst, W. H., Pingoud, V., and Nordheim, A., Activation of ternary complex factor Elk-1 by MAP kinases, EMBO J., 12, 5097, 1993.
186. Gille, H., Kortenjann, M., Thomae, O., Moomaw, C., Slaughter, C., Cobb, M. H., and Shaw, P. E., ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation, EMBO J., 14, 951, 1995.
187. Gold, M. R., Sanghera, J. S., Stewart, J., and Pelech, S. L., Selective activation of p42 mitogen-activated protein (MAP) kinase in murine B-lymphoma cell lines by membrane immunoglobulin cross-linking, Biochem. J., 287, 269, 1992.
188. Monroe, J. G., Yellen-Shaw, A. J., and Seyfert, V. L., Molecular basis for unresponsiveness and tolerance induction in immature stage B lymphocytes, Adv. Mol. Cell. Immunol, 1, 1, 1993.
189. Perez-Castillo, A., Pipaon, C., Garcia, I., and Alemany, S., NGFI-A gene expression is necessary for T-lymphocyte proliferation, J. Biol. Chem., 268, 19445, 1993.
190. Nguyen, H., Hoffman-Liebermann, B., and Liebermann, D., The zinc finger transcription factor egr-1 is essential for and restricts differentiation along the macrophage lineage, Cell, 72, 197, 1993.
191. Maltzman, J. S., Carman, J. A., and Monroe, J. G., Transcriptional regulation of the Icam-1 gene in antigen receptor and phorbol ester stimulated B lymphocytes: role for transcription factor EGR1, J. Exp. Med., 1747, 1996.
192. Maltzman, J. S., Carman, J. A., and Monroe, J. G., Role of EGR-1 in regulation of stimulus-dependent CD44 transcription in B lymphocytes, Mol. Cell. Biol., 16, 2283, 1996.
193. Rolink, A. and Melchers, F., B lymphopoiesis in the mouse [Review], Adv. Immunol., 53, 123, 1993.
194. Melchers, F., Karasuyama, H., Haasner, D., Bauer, S., Kudo, A., Sakaguchi, N., Jameson, B., and Rolink, A., The surrogate light chain in B-cell development, Immunol. Today, 14, 60, 1993.
195. Melchers, F., Haasner, D., Grawunder, U., Kalberer, C., Karasuyama, H., Winkler, T., and Rolink, A. G., Roles of IgH and L chains and of surrogate H and L chains in the development of cells of the B-lymphocyte lineage, Annu. Rev. Immunol., 12, 209, 1994.
196. Kitamura, D., Roes, J., Kuhn, R., and Rajewsky, K., A B-cell deficient mouse by targeted disruption of the membrane exon of the immunoglobulin μ chain gene, Nature, 350, 423, 1991.
197. Gong, S. and Nussenzweig, M. C., Regulation of an early developmental checkpoint in the B-cell pathway by Igβ, Science, 272, 411, 1996.
198. Pillai, S. and Baltimore, D., Formation of disulphide-linked μ2w2 tetramers in pre-B cells by the 18K w-immunoglobulin light chain, Nature, 329, 172, 1987.
199. Pillai, S. and Baltimore, D., The omega and iota surrogate immunoglobulin light chains, Curr. Top. Microbiol. Immunol., 137, 136, 1988.
200. Kerr, W. G., Cooper, M. D., Feng, L., Burrows, P. D., and Hendershot, L. M., Mu heavy chain can associate with a pseudo-light chain complex (jL) in human pre-B cells, Int. Immunol., 1, 355, 1989.
201. Loffert, D., Ehlich, A., Muller, W., and Rajewsky, K., Surrogate light chain expression is required to establish immunoglobulin heavy chain allelic exclusion during early B-cell development, Immunity, 4, 133, 1996.
202. Kitamura, D., Kudo, A., Schaal, S., Muller, W., Melchers, F., and Rajewsky, K., A critical role of lambda 5 protein in B-cell development, Cell, 69, 823, 1992.
203. Ehlich, A., Schaal, S., Gu, H., Kitamura, D., Muller, W., and Rajewsky, K., Immunoglobulin heavy and light chain genes rearrange independently at early stages of B-cell development. Cell, 72, 695, 1993.
204. Karasuyama, H., Rolink, A., Shinkai, Y., Young, F., Alt, F. W., and Melchers, F., The expression of Vpre-B/lambda 5 surrogate light chain in early bone marrow precursor B cells of normal and B-cell deficient mutant mice, Cell, 77, 133, 1994.
205. Winkler, T. H., Relink, A., Melchers, F., and Karasuyama, H., Precursor B cells of mouse bone marrow express two different complexes with the surrogate light chain on the surface, Eur. J. Immunol., 25, 446, 1995.
206. Misener, V., Downey, G. P., and Jongstra, J., The immunoglobulin light chain related protein lambda 5 is expressed on the surface of mouse pre-B cell lines and can function as a signal transducing molecule, Int. Immunol., 3, 1129, 1991.
207. Metcalf, E. S. and Klinman, N. R., In vitro tolerance induction of neonatal murine B cells, J. Exp. Med., 143, 1327, 1976.
208. Metcalf, E. S. and Klinman, N. R., In vitro tolerance induction of bone marrow cells: a marker for B-cell maturation, J. Immunol., 118, 2111, 1977.
209. Nossal, G. J. V. and Pike, B. L., Evidence for the clonal abortion theory of B-lymphocyte tolerance, J. Exp. Med., 141, 904, 1975.
210. Nossal, G. J. V., Cellular mechanisms of immunologic tolerance, Annu. Rev. Immunol., 1, 33, 1983.
211. Norvell, A., Mandik, L., and Monroe, J. G., Engagement of the antigen-receptor on immature murine B lymphocytes results in death by apoptosis, J. Immunol., 154, 4404, 1995.
212. Brown, D. M., Warner, G. L., Ales-Martinez, J. E., Scott, D. W., and Phipps, R. W., Prostaglandin E2 induces apoptosis in immature normal and malignant B lymphocytes, Clin. Immunol. Immunopathol., 63, 221, 1992.
213. Monroe, J. G., Tolerance sensitivity of immature stage B cells: can developmentally regulated B-cell antigen receptor (BCR) signal transduction play a role?, J. Immunol., 156, 2657, 1996.
214. Yellen, A. J., Glenn, W., Sukhatme, V. P., Cao, X., and Monroe, J. G., Signaling through surface IgM in tolerance-susceptible immature murine B lymphocytes, J. Immunol., 146, 1446, 1991.
215. Norvell, A., Birkeland, M. L., Carman, J., Sillman, A. L., Wechsler-Reya, R., and Monroe, J. G., Use of isolated immature-stage B cells to understand negative selection and tolerance induction at the molecular level, Immunol. Res., 15, 191, 1996.
216. Carsetti, R., Kohler, G., and Lamers, M. C., Transitional B cells are the target of negative selection in the B-cell compartment, J. Exp. Med., 181, 2129, 1995.
217. Allman, D. M., Ferguson, S. E., Lentz, V. M., and Cancro, M. P., Peripheral B-cell maturation. II. Heat-stable antigen hi splenic B cells are an immature developmental intermediate in the production of long-lived marrow-derived B cells, J. Immunol., 151, 4431, 1993.
218. Norvell, A. and Monroe, J. G., Acquisition of surface IgD fails to protect from tolerance-induction. Both surface IgM-and surface IgD-mediated signals induce apoptosis of immature murine B lymphocytes, J. Immunol, 156, 1328, 1996.
219. Carman, J. A., Wechsler-Reya, R. J., and Monroe, J. G., Immature stage B cells enter but do not progress beyond the early Gl phase of the cell cycle in response to antigen receptor signaling, J. Immunol., 156, 4562, 1996.
220. Gilbert, J. J., Stewart, A., Courtney, C.-A., Fleming, M.-C., Reid, P., Jackson, C. G., Wise, A., Wakelam, M. J. O., and Harnett, M. M., Antigen receptors on immature, but not mature, B and T cells are coupled to cytosolic phospholipase A2 activation, J. Immunol., 156, 2054, 1996.
221. Yellen-Shaw, A. J. and Monroe, J. G., Developmentally regulated association of a 56-kD member of the surface immunoglobulin M receptor complex, J. Exp. Med., 176, 129, 1992.
222. MacLennan, I. C. M., Germinal centers, Annu. Rev. Immunol., 12, 117, 1994.
223. Kelsoe, G., Life and death in germinal centers (redux), Immunity, 4, 107, 1996.
224. Liu, Y. J., Joshua, D. E., Williams, G. T., Smith, C. A., Gordon, J., and MacLennan, I. C., Mechanism of antigen-driven selection in germinal centres, Nature, 342, 929, 1989.
225. Pulendran, B., Kannourakis, G., Nouri, S., and Smith, K. G. C., Soluble antigen can cause enhanced apoptosis of germinal-centre B cells, Nature, 375, 331, 1995.
226. Shokat, K. M. and Goodnow, C. C., Antigen-induced B-cell death and elimination during germinal-centre immune responses, Nature, 375, 334, 1995.
227. Reed, J. C., Bcl-2 and the regulation of programmed cell death [Review], J. Cell. Biol., 124, 1, 1994.
228. Rothstein, T. L., Wang, J. K. M., Panka, D. J., Foote, L. C., Wang, Z., Stanger, B., Cul, H., Ju, S.-T., and Marshak-Rothstein, A., Protection against Fas-dependent Thl-mediated apoptosis by antigen receptor engagement in B cells, Nature, 374, 163, 1995.