75
Views
127
CrossRef citations to date
0
Altmetric
Cell Growth and Development

Impaired Immune Responses and B-Cell Proliferation in Mice Lacking the Id3 Gene

, , , &
Pages 5969-5980 | Received 26 Feb 1999, Accepted 08 Jun 1999, Published online: 27 Mar 2023

REFERENCES

  • Atherton, G. T., H. Travers, R. Deed, and J. Norton 1996. Regulation of cell differentiation in C2C12 myoblasts by the Id3 helix-loop-helix protein. Cell Growth Differ. 7:1059–1066.
  • Bain, G., E. C. Robanus Maandag, H. P. te Riele, A. J. Feeney, A. Sheehy, M. Schlissel, S. A. Shinton, R. R. Hardy, and J. Murre 1997. Both E12 and E47 allow commitment to the B cell lineage. Immunity 6:145–154.
  • Bain, G., E. C. Maandag, D. J. Izon, D. Amsen, A. M. Kruisbeek, B. C. Weintraub, I. Krop, M. S. Schlissel, A. J. Feeney, M. van Roon, M. van der Valk, H. P. J. te Riele, A. Berns, and J. Murre 1994. E2A proteins are required for proper B cell development and initiation of immunoglobulin gene rearrangements. Cell 79:885–892.
  • Barone, M. V., R. Pepperkok, F. A. Peverali, and J. Philipson 1994. Id proteins control growth induction in mammalian cells. Proc. Natl. Acad. Sci. USA 91:4985–4988.
  • Benezra, R. 1994. An intermolecular disulfide bond stabilizes E2A homodimers and is required for DNA binding at physiological temperatures. Cell 79:1057–1067.
  • Benezra, R., R. L. Davis, D. Lockshon, D. L. Turner, and J. Weintraub 1990. The protein Id: a negative regulator of helix-loop-helix DNA binding proteins. Cell 61:49–59.
  • Biggs, J., E. V. Murphy, and J. Israel 1992. A human Id-like helix-loop-helix protein expressed during early development. Proc. Natl. Acad. Sci. USA 89:1512–1516.
  • Blanchard, D. A., M. T. Affredou, and J. Vazquez 1997. Modulation of the p27kip1 cyclin-dependent kinase inhibitor expression during IL-4 mediated human B cell activation. J. Immunol. 158:3054–3061.
  • Carter, R. H., and J. Fearon 1992. CD19: lowering the threshold for antigen receptor stimulation of B lymphocytes. Science 256:105–107.
  • Choi, J. K., C. P. Shen, H. S. Radomska, L. A. Eckhardt, and J. Kadesch 1997. E47 activates the Ig-heavy chain and TdT loci in non-B cells. EMBO J. 15:5014–5021.
  • Christy, B. A., L. K. Sanders, L. F. Lau, N. G. Copeland, N. A. Jenkins, and J. Nathans 1991. An Id-related helix-loop-helix protein encoded by a growth factor-inducible gene. Proc. Natl. Acad. Sci. USA 88:1815–1819.
  • Coffman, R. L., D. A. Lebman, and J. Rothman 1993. Mechanism and regulation of immunoglobulin isotype switching. Adv. Immunol. 54:229–270.
  • Cogne, M., R. Lansford, A. Bottaro, J. Zhang, J. Gorman, F. Young, H. L. Cheng, and J. Alt 1994. A class switch control region at the 3′ end of the immunoglobulin heavy chain locus. Cell 77:737–747.
  • Coligan J. E., A. M. Kruisbeek, D. H. Margulies, E. M. Shevach, W. Strober 1990. Current protocols in immunology, p. 5.51–5.53 Wiley Interscience, New York, N.Y.
  • Collins, J. T., and J. Dunnick 1993. Germline transcripts of the murine immunoglobulin gamma 2a gene: structure and induction by IFN-gamma. Int. Immunol. 5:885–891.
  • Datto, M. B., J. P. Frederick, L. Pan, A. J. Borton, Y. Zhuang, and J. Wang 1999. Targeted disruption of Smad3 reveals an essential role in transforming growth factor beta-mediated signal transduction. Mol Cell. Biol. 19:2495–2504.
  • Deed, R. W., S. M. Bianchi, G. T. Atherton, D. Johnston, M. Santibanez-Koref, J. J. Murphy, and J. Norton 1993. An immediate early human gene encodes an Id-like helix-loop-helix protein and is regulated by protein kinase C activation in diverse cell types. Oncogene 8:599–607.
  • Deed, R. W., E. Hara, G. T. Atherton, G. Peters, and J. Norton 1997. Regulation of Id3 cell cycle function by Cdk-2-dependent phosphorylation. Mol. Cell. Biol. 17:6815–6821.
  • Desprez, P. Y., E. Hara, M. J. Bissell, and J. Campisi 1995. Suppression of mammary epithelial cell differentiation by the helix-loop-helix protein Id-1. Mol. Cell. Biol. 15:3398–3404.
  • Edmondson, D. G., and J. Olson 1993. Helix-loop-helix proteins as regulators of muscle-specific transcription. J. Biol. Chem. 268:755–758.
  • Ellis, H. M., D. R. Spann, and J. Posakony 1990. Extramacrochaetae, a negative regulator of sensory organ development in Drosophila, defines a new class of helix-loop-helix proteins. Cell 61:27–38.
  • Ellmeier, W., A. Aguzzi, E. Kleiner, R. Kurzbauer, and J. Weith 1992. Mutually exclusive expression of a helix-loop-helix gene and N-myc in human neuroblastomas and in normal development. EMBO J. 11:2563–2571.
  • Engel, P., L.-J. Zhou, D. C. Ord, S. Sato, B. Koller, and J. Tedder 1995. Abnormal B lymphocyte development, activation and differentiation in mice that lack or overexpress the CD19 signal transduction molecule. Immunity 3:39–50.
  • Esser, C., and J. Radbruch 1990. Immunoglobulin class switching: molecular and cellular analysis. Annu. Rev. Immunol. 8:717–735.
  • Finkelman, F. D., J. Holmes, I. M. Katona, J. F. Jr. Urban, M. P. Beckmann, L. S. Park, K. A. Schooley, R. L. Coffman, T. R. Mosmann, and J. Paul 1990. Lymphokine control of in vivo immunoglobulin isotype selection. Annu. Rev. Immunol. 8:303–333.
  • Garrell, J., and J. Modolell 1990. The Drosophila extramacrochaetae locus, an antagonist of proneural genes that, like these genes, encodes a helix-loop-helix protein. Cell 61:39–48.
  • Goldfarb, A. N., J. P. Flores, and J. Lewandowska 1997. Involvement of the E2A basic helix-loop-helix protein in immunoglobulin heavy chain class switching. Mol. Immunol. 33:947–956.
  • Hara, E., M. Hall, and J. Peters 1997. Cdk2-dependent phosphorylation of Id2 modulates activity of E2A-related transcription factors. EMBO J. 16:332–342.
  • Hara, E., T. Yamaguchi, H. Nojima, T. Ide, J. Campisi, H. Okayama, and J. Oda 1994. Id-related genes encoding helix-loop-helix proteins are required for G1 progression and are repressed in senescent human fibroblasts. J. Biol. Chem. 269:2139–2145.
  • Heemskerk, M. H., B. Blom, G. Nolan, A. P. Stegmann, A. Q. Bakker, K. Weijer, P. C. Res, and J. Spits 1998. Inhibition of T cell and promotion of natural killer cell development by the dominant negative helix loop helix factor Id3. J. Exp. Med. 186:1597–1602.
  • Jan, Y. N., and J. Jan 1993. HLH proteins, fly neurogenesis, and vertebrate myogenesis. Cell 75:827–830.
  • Jen, Y., H. Weintraub, and J. Benezra 1992. Overexpression of Id protein inhibits the muscle differentiation program: in vivo association of Id with E2A proteins. Genes Dev. 6:1466–1479.
  • Johnson, J. E., S. J. Birren, and J. Anderson 1990. Two rat homologues of Drosophila achaete-scute specifically expressed in neuronal precursors. Nature 346:858–861.
  • Kelly, K., B. H. Cochran, C. D. Stiles, and J. Leder 1983. Cell-specific regulation of the c-myc gene by lymphocyte mitogens and platelet-derived growth factor. Cell 35:603–610.
  • Lau, L. F., and J. Nathans 1987. Expression of a set of growth-related immediate early genes in BALB/c 3T3 cells: coordinate regulation with c-fos or c-myc. Proc. Natl. Acad. Sci. USA 84:1182–1186.
  • Loveys, D. A., M. B. Streiff, and J. Kato 1996. E2A basic-helix-loop-Helix transcription factors are negatively regulated by serum growth factors and by the Id3 proteins. Nucleic Acids Res. 24:2813–2820.
  • Ma, L., B. Hu, and J. Kenter 1997. Ig S gamma-specific DNA binding protein SNAP is related to the helix-loop-helix transcription factor E47. Int. Immunol. 9:1021–1029.
  • Massari, M. E., R. R. Rivera, J. R. Voland, M. W. Quong, T. M. Breit, J. J. M. van Dongen, O. D. de Smit, and J. Murre 1998. Characterization of ABF-1, a novel basic helix-loop-helix transcription factor expressed in activated B lymphocytes. Mol. Cell. Biol. 18:3130–3139.
  • Mellentin, J. D., S. D. Smith, and J. Cleary 1989. Lyl-1, a novel gene altered by chromosomal translocation in T cell leukemia, codes for a protein with a helix-loop-helix DNA binding motif. Cell 58:77–83.
  • Melnikova, I. N., and J. Christy 1996. Muscle cell differentiation is inhibited by the helix-loop-helix protein Id3. Cell Growth Differ. 7:1067–1079.
  • Meyer, K. B., M. Skogberg, C. Margenfeld, J. Ireland, and J. Pettersson 1995. Repression of the immunoglobulin heavy chain 3′ enhancer by helix-loop-helix protein Id3 via a functionally important E47/E12 binding site: implications for developmental control of enhancer function. Eur. J. Immunol. 25:1770–1777.
  • Moldes, M., F. Lasnier, B. Feve, J. Pairault, and J. Djian 1997. Id3 prevents differentiation of preadipose cells. Mol. Cell. Biol. 17:1796–1804.
  • Mond, J. J., A. Lees, and J. Snapper 1995. T cell-independent antigens type 2. Annu. Rev. Immunol. 13:655–692.
  • Murphy, J. J., and J. Norton 1990. Cell-type-specific early response gene expression during plasmacytoid differentiation of human B lymphocytic leukemia cells. Biochim. Biophys. Acta 1049:261–271.
  • Murre, C., P. S. McCaw, and J. Baltimore 1989. A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins. Cell 56:777–783.
  • Murre, C., P. S. McCaw, H. Vaessin, M. Caudy, L. Y. Jan, Y. N. Jan, C. V. Cabrera, J. N. Buskin, S. D. Hauschka, A. B. Lassar, H. Weintraub, and J. Baltimore 1989. Interactions between heterodimeric helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence. Cell 58:537–544.
  • Prabhu, S., A. Ignatova, S. T. Park, and J. Sun 1997. Regulation of the expression of cyclin-dependent kinase inhibitor p21 by E2A and Id proteins. Mol. Cell. Biol. 17:5888–5896.
  • Riechmann, V., I. van Cruchten, and J. Sablitzky 1994. The expression pattern of Id4, a novel dominant negative helix-loop-helix protein, is distinct from Id1, Id2 and Id3. Nucleic Acids Res. 22:749–755.
  • Roberts, V. J., R. Steenbergen, and J. Murre 1993. Localization of E2A mRNA expression in developing and adult rat tissues. Proc. Natl. Acad. Sci. USA 90:7583–7587.
  • Rupp, R. A., and J. Weintraub 1991. Ubiquitous MyoD transcription at the midblastula transition precedes induction-dependent MyoD expression in presumptive mesoderm of X. laevis. Cell 65:927–937.
  • Sato, S., N. Ono, D. Steeber, D. Pisetsky, and J. Tedder 1996. CD19 regulates B lymphocyte signaling thresholds critical for the development of B-1 lineage cells and autoimmunity. J. Immunol. 157:4371–4378.
  • Schlissel, M., A. Voronova, and J. Baltimore 1991. Helix-loop-helix transcription factor E47 activates germ-line immunoglobulin heavy-chain gene transcription and rearrangement in a pre-T-cell line. Genes Dev. 5:1367–1376.
  • Severinson, E., C. Fernandez, and J. Stavnezer 1990. Induction of germ-line immunoglobulin heavy chain transcripts by mitogens and interleukins prior to switch recombination. Eur. J. Immunol. 20:1079–1084.
  • Shen, C.-P., and J. Kadesch 1995. B-cell-specific DNA binding by an E47 homodimer. Mol. Cell. Biol. 15:4518–4524.
  • Shoji, W., T. Yamamoto, and J. Obinata 1994. The helix-loop-helix protein Id inhibits differentiation of murine erythroleukemia cells. J. Biol. Chem. 269:5078–5084.
  • Snapper, C. M., and J. Paul 1987. Interferon-gamma and B cell stimulatory factor-1 reciprocally regulate Ig isotype production. Science 236:944–947.
  • Solvason, N., W. W. Wu, N. Kabra, X. Wu, E. Lees, and J. Howard 1997. Induction of cell cycle regulatory proteins in anti-immunoglobulin-stimutated mature B lymphocytes. J. Exp. Med. 184:407–417.
  • Stanton, L. W., P. D. Fahrlander, P. M. Tesser, and J. Marcu 1984. Nucleotide sequence comparison of normal and translocated murine c-myc genes. Nature 310:423–425.
  • Sun, X. H. 1994. Constitutive expression of the Id1 gene impairs mouse B cell development. Cell 79:893–900.
  • Sun, X. H., N. G. Copeland, N. A. Jenkins, and J. Baltimore 1991. Id proteins Id1 and Id2 selectively inhibit DNA binding by one class of helix-loop-helix proteins. Mol. Cell. Biol. 11:5603–5611.
  • Swat, W., M. Dessing, H. von Boehmer, and J. Kisielow 1993. CD69 expression during selection and maturation of CD4+8+ thymocytes. Eur. J. Immunol. 23:739–746.
  • Testi, R., J. H. Phillips, and J. Lanier 1989. Leu 23 induction as an early marker of functional CD3/T cell antigen receptor triggering. Requirement for receptor cross-linking, prolonged elevation of intracellular [Ca++] and stimulation of protein kinase C. J. Immunol. 142:1854–1860.
  • Voronova, A., and J. Baltimore 1990. Mutations that disrupt DNA binding and dimer formation in the E47 helix-loop-helix protein map to distinct domains. Proc. Natl. Acad. Sci. USA 87:4722–4726.
  • Weintraub, H. 1993. The MyoD family and myogenesis: redundancy, networks, and thresholds. Cell 75:1241–1244.
  • White, P. S., J. M. Maris, C. Beltinger, E. Sulman, H. N. Marshall, M. Fujimori, B. A. Kaufman, J. A. Biegel, C. Allen, C. Hilliard, M. B. Valentine, A. T. look, H. Enomoto, S. Sakiyama, and J. Brodeur 1995. A region of consistent deletion in neuroblastoma maps within human chromosome 1p36.2-36.3. Proc. Natl. Acad. Sci. USA 92:5520–5524.
  • Wilson, R. B., M. Kiledjian, C. P. Shen, R. Benezra, P. Zwollo, S. M. Dymecki, S. V. Desiderio, and J. Kadesch 1991. Repression of immunoglobulin enhancers by the helix-loop-helix protein Id: implications for B-lymphoid-cell development. Mol. Cell. Biol. 11:6185–6191.
  • Xin, X. Q., C. Nelson, L. Collins, and J. Dorshkind 1994. Kinetics of E2A basic helix-loop-helix-protein expression during myelopoiesis and primary B cell differentiation. J. Immunol. 151:5398–5407.
  • Yan, W., A. Z. Young, V. C. Soares, R. Kelley, R. Benezra, and J. Zhuang 1997. High incidence of acute T-cell tumors in E2A-null mice and E2A/Id1 double knockout mice. Mol. Cell. Biol. 17:7317–7327.
  • Zelazowski, P., J. T. Collins, W. Dunnick, and J. Snapper 1995. Antigen receptor cross-linking differentially regulates germ-line CH ribonucleic acid expression in murine B cells. J. Immunol. 154:1223–1231.
  • Zhuang, Y., R. J. Bardnt, L. Pan, R. Kelley, and J. Dai 1998. Functional replacement of the mouse E2A gene with a human HEB cDNA. Mol. Cell. Biol. 18:3340–3349.
  • Zhuang, Y., P. Cheng, and J. Weintraub 1996. B-lymphocyte development is regulated by the combined dosage of three basic helix-loop-helix genes, E2A, E2-2, and HEB. Mol. Cell. Biol. 16:2898–2905.
  • Zhuang, Y., P. Soriano, and J. Weintraub 1994. The helix-loop-helix gene E2A is required for B cell formation. Cell 79:875–884.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.