Shaper, J. H. and Shaper, N. L. (1992). Enzymes associated with glycosy<strong>la</strong>tion. Current Opinion Structural Biology 2, 701-709. Shapiro-Shelef, M., Lin, K. I., McHeyzer-Williams, L. J., Liao, J., McHeyzer- Williams, M. G. and Ca<strong>la</strong>me, K. (2003). Blimp-1 is required for the formation of immunoglobulin secreting p<strong>la</strong>sma cells and pre-p<strong>la</strong>sma memory B cells. Immunity 19, 607-20. Shen, X., Bozek, G., Pinkert, C. A. and Storb, U. (1999). The C(H)1 and transmembrane domains of mu in the context of a gamma2b transgene do not suffice to promote B cell maturation. Int Immunol 11, 1663-71. Shields, R. L., Lai, J., Keck, R., O'Connell, L. Y., Hong, K., Meng, Y. G., Weikert, S. H. and Presta, L. G. (2002). Lack of fucose on human IgG1 N-linked oligosacchari<strong>de</strong> improves binding to human Fcgamma RIII and antibody-<strong>de</strong>pen<strong>de</strong>nt cellu<strong>la</strong>r toxicity. J Biol Chem 277, 26733-40. Shiloh, Y. (2003). ATM and re<strong>la</strong>ted protein kinases: safeguarding genome integrity. Nat Rev Cancer 3, 155-68. Shimizu, T., Mundt, C., Licence, S., Melchers, F. and Martensson, I. L. (2002). VpreB1/VpreB2/<strong>la</strong>mbda 5 triple-<strong>de</strong>ficient mice show impaired B cell <strong>de</strong>velopment but functional allelic exclusion of the IgH locus. J Immunol 168, 6286-93. Shinkai, Y., Rathbun, G., Lam, K. P., Oltz, E. M., Stewart, V., Men<strong>de</strong>lsohn, M., Charron, J., Datta, M., Young, F., Stall, A. M. et al. (1992). RAG-2-<strong>de</strong>ficient mice <strong>la</strong>ck mature lymphocytes owing to inability to initiate V(D)J rearrangement. Cell 68, 855-67. Shinkawa, T., Nakamura, K., Yamane, N., Shoji-Hosaka, E., Kanda, Y., Sakurada, M., Uchida, K., Anazawa, H., Satoh, M., Yamasaki, M. et al. (2003). The absence of fucose but not the presence of ga<strong>la</strong>ctose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosacchari<strong>de</strong>s shows the critical role of enhancing antibody-<strong>de</strong>pen<strong>de</strong>nt cellu<strong>la</strong>r cytotoxicity. J Biol Chem 278, 3466-73. Shinkura, R., Ito, S., Begum, N. A., Nagaoka, H., Muramatsu, M., Kinoshita, K., Sakakibara, Y., Hijikata, H. and Honjo, T. (2004). Separate domains of AID are required for somatic hypermutation and c<strong>la</strong>ss-switch recombination. Nat Immunol 5, 707-12. Shinkura, R., Tian, M., Smith, M., Chua, K., Fujiwara, Y. and Alt, F. W. (2003). The influence of transcriptional orientation on endogenous switch region function. Nat Immunol 4, 435-41. Sieckmann, D. G., Finkelman, F. D. and Scher, I. (1982). IgD as a receptor in signaling the proliferation of mouse B-lymphocytes. Ann N Y Acad Sci 399, 277-89. Silberstein, S. and Gilmore, R. (1996). Biochemistry, molecu<strong>la</strong>r biology, and genetics of the oligosaccharyltransferase. Faseb J 10, 849-58. Simons, K. and Toomre, D. (2000). Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 1, 31-9. Sirac, C., Carrion, C., Duchez, S., Comte, I. and Cogne, M. (2006). Light chain inclusion permits terminal B cell differentiation and does not necessarily result in autoreactivity. Proc Natl Acad Sci U S A 103, 7747-52. Sleckman, B. P., Gorman, J. R. and Alt, F. W. (1996). Accessibility control of antigenreceptor variable-region gene assembly: role of cis-acting elements. Annu Rev Immunol 14, 459- 81. Sonoda, E., Pewzner-Jung, Y., Schwers, S., Taki, S., Jung, S., Ei<strong>la</strong>t, D. and Rajewsky, K. (1997). B cell <strong>de</strong>velopment un<strong>de</strong>r the condition of allelic inclusion. Immunity 6, 225-33. Spanopoulou, E., Roman, C. A., Corcoran, L. M., Schlissel, M. S., Silver, D. P., Nemazee, D., Nussenzweig, M. C., Shinton, S. A., Hardy, R. R. and Baltimore, D. (1994). 174
Functional immunoglobulin transgenes gui<strong>de</strong> or<strong>de</strong>red B-cell differentiation in Rag-1-<strong>de</strong>ficient mice. Genes Dev 8, 1030-42. Spillmann, D., Witt, D. and Lindahl, U. (1998). Defining the interleukin-8-binding domain of heparan sulfate. J Biol Chem 273, 15487-93. Spiro, R. G. (2002). Protein glycosy<strong>la</strong>tion: nature, distribution, enzymatic formation, and disease implications of glycopepti<strong>de</strong> bonds. Glycobiology 12, 43R-56R. Staal, F. J. and Clevers, H. C. (2003). Wnt signaling in the thymus. Curr Opin Immunol 15, 204-8. Stall, A. M., Wells, S. M. and Lam, K. P. (1996). B-1 cells: unique origins and functions. Semin Immunol 8, 45-59. Stavnezer-Nordgren, J. and Sirlin, S. (1986). Specificity of immunoglobulin heavy chain switch corre<strong>la</strong>tes with activity of germline heavy chain genes prior to switching. Embo J 5, 95-102. Stavnezer, J. (2000). Immunology. A touch of antibody c<strong>la</strong>ss. Science 288, 984-5. Stevens, F. J. (2000). Four structural risk factors i<strong>de</strong>ntify most fibril-forming kappa light chains. Amyloid 7, 200-11. Stillman, B. N., Hsu, D. K., Pang, M., Brewer, C. F., Johnson, P., Liu, F. T. and Baum, L. G. (2006). Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell <strong>de</strong>ath. J Immunol 176, 778-89. Storb, U. and Arp, B. (1983). Methy<strong>la</strong>tion patterns of immunoglobulin genes in lymphoid cells: corre<strong>la</strong>tion of expression and differentiation with un<strong>de</strong>rmethy<strong>la</strong>tion. Proc Natl Acad Sci U S A 80, 6642-6. Stringer, S. E. and Gal<strong>la</strong>gher, J. T. (1997). Specific binding of the chemokine p<strong>la</strong>telet factor 4 to heparan sulfate. J Biol Chem 272, 20508-14. Sturm, A., Lensch, M., Andre, S., Kaltner, H., Wie<strong>de</strong>nmann, B., Rosewicz, S., Dignass, A. U. and Gabius, H. J. (2004). Human galectin-2: novel inducer of T cell apoptosis with distinct profile of caspase activation. J Immunol 173, 3825-37. Su, T. T. and Rawlings, D. J. (2002). Transitional B lymphocyte subsets operate as distinct checkpoints in murine splenic B cell <strong>de</strong>velopment. J Immunol 168, 2101-10. Sugahara, K. and Kitagawa, H. (2002). Heparin and heparan sulfate biosynthesis. IUBMB Life 54, 163-75. Suzuki, H., Matsuda, S., Terauchi, Y., Fujiwara, M., Ohteki, T., Asano, T., Behrens, T. W., Kouro, T., Takatsu, K., Kadowaki, T. et al. (2003). PI3K and Btk differentially regu<strong>la</strong>te B cell antigen receptor-mediated signal transduction. Nat Immunol 4, 280-6. Tanaka, Y., Fujii, K., Hubscher, S., Aso, M., Takazawa, A., Saito, K., Ota, T. and Eto, S. (1998). Heparan sulfate proteoglycan on endothelium efficiently induces integrinmediated T cell adhesion by immobilizing chemokines in patients with rheumatoid synovitis. Arthritis Rheum 41, 1365-77. Tanigaki, K., Han, H., Yamamoto, N., Tashiro, K., Ikegawa, M., Kuroda, K., Suzuki, A., Nakano, T. and Honjo, T. (2002). Notch-RBP-J signaling is involved in cell fate <strong>de</strong>termination of marginal zone B cells. Nat Immunol 3, 443-50. Tanigaki, K. and Honjo, T. (2007). Regu<strong>la</strong>tion of lymphocyte <strong>de</strong>velopment by Notch signaling. Nat Immunol 8, 451-6. Tashiro, J., Kinoshita, K. and Honjo, T. (2001). Palindromic but not G-rich sequences are targets of c<strong>la</strong>ss switch recombination. Int Immunol 13, 495-505. Tedford, K., Nitschke, L., Girkontaite, I., Charlesworth, A., Chan, G., Sakk, V., Barbacid, M. and Fischer, K. D. (2001). Compensation between Vav-1 and Vav-2 in B cell <strong>de</strong>velopment and antigen receptor signaling. Nat Immunol 2, 548-55. 175
- Page 1:
UNIVERSITE DE LIMOGES Ecole doctora
- Page 4 and 5:
de m’avoir donnée le goût pour
- Page 6 and 7:
KO : « knock-out » : délétion d
- Page 8 and 9:
Figure 27 : Les trois types de N-gl
- Page 10 and 11:
5.2.2. Les galectines, les voies No
- Page 13 and 14:
Afin d’assurer la défense de l
- Page 15:
conduire les cellules B au long de
- Page 19 and 20:
Les immunoglobulines sont des hét
- Page 21 and 22:
antigènes et dans la transduction
- Page 23 and 24:
1.2.2 Le Locus Igλ Les gènes de c
- Page 25 and 26:
empêcher des recombinaisons illég
- Page 27 and 28:
de l’ADN est réalisée par les p
- Page 29 and 30:
Figure 8 : Les nucléotides N et P.
- Page 31 and 32:
séquences Ig (Goodhardt et al., 19
- Page 33 and 34:
B, le nombre de cellules exprimant
- Page 35 and 36:
Des promoteurs ont également été
- Page 37 and 38:
maturation : aux stades précoces,
- Page 39 and 40:
jusqu’à Cδ, ne supprime pas pou
- Page 41 and 42:
3.1 La phase indépendante des anti
- Page 43 and 44:
Novobrantseva et al., 1999) et que
- Page 45 and 46:
Figure 14 : Bilan des blocages part
- Page 47 and 48:
Dendritic Cells »). Elles devienne
- Page 49 and 50:
sécrétrices est controversée. De
- Page 51 and 52:
et al., 2000; Chumley et al., 2000;
- Page 53 and 54:
La commutation isotypique, permetta
- Page 55 and 56:
L’action des cytokines semble s
- Page 57 and 58:
l’hypermutation (Muramatsu et al.
- Page 59 and 60:
IV. L’activation des lymphocytes
- Page 61 and 62:
La translocation du BCR après pont
- Page 63 and 64:
protéines. La protéine ZAP-70 ét
- Page 65 and 66:
comme NF-κB (Krappmann et al., 200
- Page 67 and 68:
démontré que CD22 était continue
- Page 69 and 70:
Figure 24 : Comparaison des région
- Page 71 and 72:
Au cours du développement B, le pr
- Page 73 and 74:
membranaire s’avère possible exp
- Page 75 and 76:
IgM/IgD (Brink et al., 1992; Spanop
- Page 77 and 78:
V. « Glycannes et glycoconjugués
- Page 79 and 80:
Groupe d'enzymes Sialyltransférase
- Page 81 and 82:
L’édification d’une structure
- Page 83 and 84:
5.1.2. La O-glycosylation des prot
- Page 85 and 86:
• la O-glucosylation qui a lieu s
- Page 87 and 88:
Les protéoglycannes peuvent varier
- Page 89 and 90:
o L’Héparane Sulfate (HS) et l
- Page 91 and 92:
C’est le premier hexosamine greff
- Page 93 and 94:
égion constante. L’analyse des d
- Page 95 and 96:
pathologies pour lesquelles l’ars
- Page 97 and 98:
intégrines VLA-4, VLA-5 et α4β7,
- Page 99 and 100:
thymocytes double négatifs CD4- CD
- Page 101 and 102:
délétion conditionnelle des gène
- Page 103 and 104:
Dans la MEC, les protéoglycannes f
- Page 105 and 106:
endothéliale, de façon à permett
- Page 107 and 108:
Résultats - Discussion 107
- Page 109 and 110:
Première partie : les BCR modifié
- Page 111 and 112:
Article 1 “Premature expression o
- Page 113 and 114:
Article 2 “B cells carying an IgE
- Page 115 and 116:
Demande de dépôt de brevet Etabli
- Page 117 and 118:
mécanismes relèvent les différen
- Page 119 and 120:
Etablissement et caractérisation d
- Page 121 and 122:
AUSUBEL, 2000, Wiley and son Inc, L
- Page 123 and 124: 4) Dosage du taux des IgG1 sérique
- Page 125 and 126: - distribution d’un antisérum an
- Page 127 and 128: périphériques expriment pour envi
- Page 129 and 130: C. CONCLUSION Ce travail a reposé
- Page 131 and 132: Deuxième partie : les glycosaminog
- Page 133 and 134: Article 3 “Modulation of glycotra
- Page 135 and 136: Perspectives 135
- Page 137 and 138: L’état des réflexions sur les i
- Page 139 and 140: équipes de Tsubata et Goodnow avai
- Page 141 and 142: L’ouverture d’un nouveau champ
- Page 143 and 144: « Lymphomagenèse » dirigé par l
- Page 145 and 146: Annexes 145
- Page 147 and 148: Article 4 “RNA surveillance down-
- Page 149 and 150: Article 5 “Light chain inclusion
- Page 151 and 152: Références Bibliographiques 151
- Page 153 and 154: Abney, E. R., Cooper, M. D., Kearne
- Page 155 and 156: Brink, R., Goodnow, C. C., Crosbie,
- Page 157 and 158: Cogne, M., Lansford, R., Bottaro, A
- Page 159 and 160: Franke, T. F., Kaplan, D. R., Cantl
- Page 161 and 162: Hauke, G., Epplen, J. T., Chluba, J
- Page 163 and 164: Kao, Y. H., Lee, G. F., Wang, Y., S
- Page 165 and 166: Lieberson, R., Giannini, S. L., Bir
- Page 167 and 168: Meek, K. D., Hasemann, C. A. and Ca
- Page 169 and 170: Oberdoerffer, P., Novobrantseva, T.
- Page 171 and 172: Poellinger, L., Yoza, B. K. and Roe
- Page 173: Sato, M., Adachi, T. and Tsubata, T
- Page 177 and 178: Vilen, B. J., Famiglietti, S. J., C
- Page 179 and 180: Zarrin, A. A., Tian, M., Wang, J.,