메뉴 건너뛰기




Volumn 177, Issue 5, 2006, Pages 3063-3073

CD22 ligand binding regulates normal and malignant B lymphocyte survival in vivo

Author keywords

[No Author keywords available]

Indexed keywords

CD22 ANTIGEN; FC RECEPTOR; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY CD22; SIALIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

EID: 33747752856     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.177.5.3063     Document Type: Article
Times cited : (66)

References (64)
  • 1
    • 0030993376 scopus 로고    scopus 로고
    • CD22, a B lymphocyte-specific adhesion molecule that regulates antigen receptor signaling
    • Tedder, T. F., J. Tuscano, S. Sato, and J. H. Kehrt. 1997. CD22, a B lymphocyte-specific adhesion molecule that regulates antigen receptor signaling. Annu. Rev. Immunol. 15: 481-504.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 481-504
    • Tedder, T.F.1    Tuscano, J.2    Sato, S.3    Kehrt, J.H.4
  • 3
    • 0026437805 scopus 로고
    • Tyrosine phosphorylation of CD22 during B cell activation
    • Schulte, R. J., M. A. Campbell, W. H. Fischer, and B. M. Sefton. 1992. Tyrosine phosphorylation of CD22 during B cell activation. Science 258: 1001-1004.
    • (1992) Science , vol.258 , pp. 1001-1004
    • Schulte, R.J.1    Campbell, M.A.2    Fischer, W.H.3    Sefton, B.M.4
  • 4
    • 0026068592 scopus 로고
    • DNA cloning of the B cell membrane protein CD22: A mediator of B-B cell interactions
    • Wilson, G. L., C. H. Fox, A. S. Fauci, and J. H. Kehrl. 1991. cDNA cloning of the B cell membrane protein CD22: a mediator of B-B cell interactions. J. Exp. Med. 173: 137-146.
    • (1991) J. Exp. Med. , vol.173 , pp. 137-146
    • Wilson, G.L.1    Fox, C.H.2    Fauci, A.S.3    Kehrl, J.H.4
  • 5
    • 0034625416 scopus 로고    scopus 로고
    • CD22 forms a quaternary complex with SHIP, Grb2 and She: A pathway for regulation of B lymphocyte antigen receptor-induced calcium flux
    • Poe, J. C., M. Fujimoto, P. J. Jansen, A. S. Miller, and T. F. Tedder. 2000. CD22 forms a quaternary complex with SHIP, Grb2 and She: a pathway for regulation of B lymphocyte antigen receptor-induced calcium flux. J. Biol. Chem. 275: 17420-17427.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17420-17427
    • Poe, J.C.1    Fujimoto, M.2    Jansen, P.J.3    Miller, A.S.4    Tedder, T.F.5
  • 7
    • 0029103298 scopus 로고
    • Hematopoietic cell phosphatase is recruited to CD22 following B cell antigen receptor ligation
    • Lankester, A. C., G. M. van Schijndel, and R. A. van Lier. 1995. Hematopoietic cell phosphatase is recruited to CD22 following B cell antigen receptor ligation. J. Biol. Chem. 270: 20305-20308.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20305-20308
    • Lankester, A.C.1    Van Schijndel, G.M.2    Van Lier, R.A.3
  • 8
    • 0029048060 scopus 로고
    • Phosphotyrosine-dependent association between CD22 and protein tyrosine phosphatase 1C
    • Campbell, M. A., and N. R. Klinman. 1995. Phosphotyrosine-dependent association between CD22 and protein tyrosine phosphatase 1C. Eur. J. Immunol. 25: 1573-1579.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 1573-1579
    • Campbell, M.A.1    Klinman, N.R.2
  • 10
    • 0033593205 scopus 로고    scopus 로고
    • Definition of the sites of interaction between the protein tyrosine phosphatase SHP-1 and CD22
    • Blasioli, J., S. Paust, and M. L. Thomas. 1999. Definition of the sites of interaction between the protein tyrosine phosphatase SHP-1 and CD22. J. Biol. Chem. 274: 2303-2307.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2303-2307
    • Blasioli, J.1    Paust, S.2    Thomas, M.L.3
  • 11
    • 0033603054 scopus 로고    scopus 로고
    • Analysis of tyrosine phosphorylation-dependent interactions between stimulatory effector proteins and the B cell co-receptor CD22
    • Yohannan, J., J. Wienands, K. M. Coggeshall, and L. B. Justement. 1999. Analysis of tyrosine phosphorylation-dependent interactions between stimulatory effector proteins and the B cell co-receptor CD22. J. Biol. Chem. 274: 18769-18776.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18769-18776
    • Yohannan, J.1    Wienands, J.2    Coggeshall, K.M.3    Justement, L.B.4
  • 12
    • 0025366457 scopus 로고
    • The B cell antigen CD22 mediates monocyte and erythrocyte adhesion
    • Stamenkovic, I., and B. Seed. 1990. The B cell antigen CD22 mediates monocyte and erythrocyte adhesion. Nature 344: 74-77.
    • (1990) Nature , vol.344 , pp. 74-77
    • Stamenkovic, I.1    Seed, B.2
  • 13
    • 0029084603 scopus 로고
    • Ig domains 1 and 2 of murine CD22 constitute the ligand-binding domain and bind multiple sialylated ligands expressed on B and T cells
    • Law, C.-L., A. Aruffo, K. A. Chandran, R. T. Doty, and E. A. Clark. 1995. Ig domains 1 and 2 of murine CD22 constitute the ligand-binding domain and bind multiple sialylated ligands expressed on B and T cells. J. Immunol. 155: 3368-3376.
    • (1995) J. Immunol. , vol.155 , pp. 3368-3376
    • Law, C.-L.1    Aruffo, A.2    Chandran, K.A.3    Doty, R.T.4    Clark, E.A.5
  • 14
    • 0027159813 scopus 로고
    • The same epitope on CD22 of B lymphocytes mediates the adhesion of erythrocytes, T and B lymphocytes, neutrophils and monocytes
    • Engel, P., Y. Nojima, D. Rothstein, L.-J. Zhou, G. L. Wilson, J. H. Kehrl, and T. F. Tedder. 1993. The same epitope on CD22 of B lymphocytes mediates the adhesion of erythrocytes, T and B lymphocytes, neutrophils and monocytes. J. Immunol. 150: 4719-4732.
    • (1993) J. Immunol. , vol.150 , pp. 4719-4732
    • Engel, P.1    Nojima, Y.2    Rothstein, D.3    Zhou, L.-J.4    Wilson, G.L.5    Kehrl, J.H.6    Tedder, T.F.7
  • 16
    • 0028079344 scopus 로고
    • A B-cell superfamily receptor with sialic acid-binding lectin activity
    • Sgroi, D., and I. Stamenkovic. 1994. A B-cell superfamily receptor with sialic acid-binding lectin activity. The Immunologist 2: 161.
    • (1994) The Immunologist , vol.2 , pp. 161
    • Sgroi, D.1    Stamenkovic, I.2
  • 17
    • 0028595625 scopus 로고
    • Modifications of cell surface sialic acids modulate cell adhesion mediated by Sialoadhesin and CD22
    • Keim, S., R. Schaur, J. C. Manuguerra, H. J. Gross, and P. R. Crocker. 1994. Modifications of cell surface sialic acids modulate cell adhesion mediated by Sialoadhesin and CD22. Glycoconjugate J. 11: 576-585.
    • (1994) Glycoconjugate J. , vol.11 , pp. 576-585
    • Keim, S.1    Schaur, R.2    Manuguerra, J.C.3    Gross, H.J.4    Crocker, P.R.5
  • 18
    • 0028929567 scopus 로고
    • Identification of the ligand binding domains of CD22, a member of the immunoglobulin superfamily that uniquely binds a sialic acid-dependent ligand
    • Engel, P., N. Wagner, A. Miller, and T. F. Tedder. 1995. 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: 1581-1586.
    • (1995) J. Exp. Med. , vol.181 , pp. 1581-1586
    • Engel, P.1    Wagner, N.2    Miller, A.3    Tedder, T.F.4
  • 19
    • 0027175115 scopus 로고
    • Association of CD22 with the B cell antigen receptor
    • Peaker, C. J. G., and M. S. Neuberger. 1993. Association of CD22 with the B cell antigen receptor. Eur. J. Immunol. 23: 1358-1363.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 1358-1363
    • Peaker, C.J.G.1    Neuberger, M.S.2
  • 21
    • 0036838611 scopus 로고    scopus 로고
    • Ly-6 superfamily members Ly-6A/E, Ly-6C, and Ly-6I recognize two potential ligands expressed by B lymphocytes
    • Pflugh, D. L., S. E. Maher, and A. L. M. Bothwell. 2002. Ly-6 superfamily members Ly-6A/E, Ly-6C, and Ly-6I recognize two potential ligands expressed by B lymphocytes. J. Immunol. 169: 5130-5136.
    • (2002) J. Immunol. , vol.169 , pp. 5130-5136
    • Pflugh, D.L.1    Maher, S.E.2    Bothwell, A.L.M.3
  • 22
    • 0025913892 scopus 로고
    • The B lymphocyte adhesion molecule CD22 interacts with leukocyte common antigen CD45RO on T cells and α2,6 sialyltransferase, CD75, on B cells
    • Stamenkovic, I., D. Sgroi, A. Aruffo, M. S. Sy, and T. Anderson. 1991. The B lymphocyte adhesion molecule CD22 interacts with leukocyte common antigen CD45RO on T cells and α2,6 sialyltransferase, CD75, on B cells. Cell 66: 1133-1144.
    • (1991) Cell , vol.66 , pp. 1133-1144
    • Stamenkovic, I.1    Sgroi, D.2    Aruffo, A.3    Sy, M.S.4    Anderson, T.5
  • 23
    • 28444493924 scopus 로고    scopus 로고
    • Homomultimeric complexes of CD22 in B cells revealed by protein-glycan cross-linking
    • Han, S., B. E. Collins, P. Bengtson, and J. C. Paulson. 2005. Homomultimeric complexes of CD22 in B cells revealed by protein-glycan cross-linking. Nat. Chem. Biol. 1: 93-97.
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 93-97
    • Han, S.1    Collins, B.E.2    Bengtson, P.3    Paulson, J.C.4
  • 25
    • 0030499431 scopus 로고    scopus 로고
    • CD22 is both a positive and negative regulator of B lymphocyte antigen receptor signal transduction: Altered signaling in CD22-deficient mice
    • Sato, S., A. S. Miller, M. Inaoki, C. B. Bock, P. J. Jansen, M. L. K. Tang, and T. F. Tedder. 1996. CD22 is both a positive and negative regulator of B lymphocyte antigen receptor signal transduction: altered signaling in CD22-deficient mice. Immunity 5: 551-562.
    • (1996) Immunity , vol.5 , pp. 551-562
    • Sato, S.1    Miller, A.S.2    Inaoki, M.3    Bock, C.B.4    Jansen, P.J.5    Tang, M.L.K.6    Tedder, T.F.7
  • 29
    • 0036008486 scopus 로고    scopus 로고
    • Interaction of CD22 with α2,6-linked sialoglycoconjugates: Innate recognition of self to dampen B cell autoreactivity?
    • Lanoue, A., F. D. Batista, M. Stewart, and M. S. Neuberger. 2002. Interaction of CD22 with α2,6-linked sialoglycoconjugates: innate recognition of self to dampen B cell autoreactivity? Eur. J. Immunol. 32: 348-355.
    • (2002) Eur. J. Immunol. , vol.32 , pp. 348-355
    • Lanoue, A.1    Batista, F.D.2    Stewart, M.3    Neuberger, M.S.4
  • 30
    • 0037029637 scopus 로고    scopus 로고
    • Sialic acid binding domains of CD22 are required for negative regulation of B cell receptor signaling
    • Jin, L., P. A. McLean, B. G. Neel, and H. H. Wortis. 2002. Sialic acid binding domains of CD22 are required for negative regulation of B cell receptor signaling. J. Exp. Med. 195: 1199-1205.
    • (2002) J. Exp. Med. , vol.195 , pp. 1199-1205
    • Jin, L.1    McLean, P.A.2    Neel, B.G.3    Wortis, H.H.4
  • 31
    • 0037029667 scopus 로고    scopus 로고
    • The ligand-binding domain of CD22 is needed for inhibition of the B cell receptor signal, as demonstrated by a novel human CD22-specific inhibitor compound
    • Kelm, S., J. Gerlach, R. Brossmer, C.-P. Danzer, and L. Nitschke. 2002. The ligand-binding domain of CD22 is needed for inhibition of the B cell receptor signal, as demonstrated by a novel human CD22-specific inhibitor compound. J. Exp. Med. 195, 1207-1213.
    • (2002) J. Exp. Med. , vol.195 , pp. 1207-1213
    • Kelm, S.1    Gerlach, J.2    Brossmer, R.3    Danzer, C.-P.4    Nitschke, L.5
  • 32
    • 0020367270 scopus 로고
    • Lyb-8.2: A new B cell antigen defined and characterized with a monoclonal antibody
    • Symington, F. W., B. Subbarao, D. E. Mosier, and J. Sprent. 1982. Lyb-8.2: a new B cell antigen defined and characterized with a monoclonal antibody. Immunogenetics 16: 381-391.
    • (1982) Immunogenetics , vol.16 , pp. 381-391
    • Symington, F.W.1    Subbarao, B.2    Mosier, D.E.3    Sprent, J.4
  • 34
    • 27144474948 scopus 로고    scopus 로고
    • B-cell depletion inhibits arthritis in a collagen-induced arthritis (CIA) model, but does not adversely affect humoral responses in a respiratory syncytial virus (RSV) vaccination model
    • Dunussi-Joannopoulos, K., G. E. Hancock, A. Kunz, M. Hegen, X. X. Zhou, B. J. Sheppard, J. Lamothe, E. Li, H. L. Ma, P. R. Hamann, et al. 2005. B-cell depletion inhibits arthritis in a collagen-induced arthritis (CIA) model, but does not adversely affect humoral responses in a respiratory syncytial virus (RSV) vaccination model. Blood 106: 2235-2243.
    • (2005) Blood , vol.106 , pp. 2235-2243
    • Dunussi-Joannopoulos, K.1    Hancock, G.E.2    Kunz, A.3    Hegen, M.4    Zhou, X.X.5    Sheppard, B.J.6    Lamothe, J.7    Li, E.8    Ma, H.L.9    Hamann, P.R.10
  • 35
    • 0033519233 scopus 로고    scopus 로고
    • Identification of CD22 ligands on bone marrow sinusoidal endothelium implicated in CD22-dependent homing of recirculating B cells
    • Nitschke, L., H. Floyd, D. J. P. Ferguson, and P. R. Crocker. 1999. Identification of CD22 ligands on bone marrow sinusoidal endothelium implicated in CD22-dependent homing of recirculating B cells. J. Exp. Med. 189: 1513-1518.
    • (1999) J. Exp. Med. , vol.189 , pp. 1513-1518
    • Nitschke, L.1    Floyd, H.2    Ferguson, D.J.P.3    Crocker, P.R.4
  • 36
    • 0029944192 scopus 로고    scopus 로고
    • Engagement of the adhesion receptor CD22 triggers a potent stimulatory signal for B cells and blocking CD22/CD22L interactions impairs T-cell proliferation
    • Tuscano, J., P. Engel, T. F. Tedder, and J. H. Kehrl. 1996. Engagement of the adhesion receptor CD22 triggers a potent stimulatory signal for B cells and blocking CD22/CD22L interactions impairs T-cell proliferation. Blood 87: 4723-4730.
    • (1996) Blood , vol.87 , pp. 4723-4730
    • Tuscano, J.1    Engel, P.2    Tedder, T.F.3    Kehrl, J.H.4
  • 37
    • 0033566993 scopus 로고    scopus 로고
    • CD22 cross-linking generates B-cell antigen receptor-independent signals that activate the JNK/SAPK signaling cascade
    • Tuscano, J. M., A. Riva, S. N. Toscano, T. F. Tedder, and J. H. Kehrl. 1999. CD22 cross-linking generates B-cell antigen receptor-independent signals that activate the JNK/SAPK signaling cascade. Blood 94: 1382-1392.
    • (1999) Blood , vol.94 , pp. 1382-1392
    • Tuscano, J.M.1    Riva, A.2    Toscano, S.N.3    Tedder, T.F.4    Kehrl, J.H.5
  • 39
    • 0036182540 scopus 로고    scopus 로고
    • Immunotherapy of non-Hodgkin's lymphoma with hLL2 (epratuzumab, an anti-CD22 monoclonal antibody) and Hu1D10 (apolizumab)
    • Leonard, J. P., and B. K. Link. 2002. Immunotherapy of non-Hodgkin's lymphoma with hLL2 (epratuzumab, an anti-CD22 monoclonal antibody) and Hu1D10 (apolizumab). Semin. Oncol. 29: 81-86.
    • (2002) Semin. Oncol. , vol.29 , pp. 81-86
    • Leonard, J.P.1    Link, B.K.2
  • 41
    • 31044433511 scopus 로고    scopus 로고
    • New prospects for autoimmune disease therapy: B cells on deathwatch
    • St. Clair, W. E., and T. F. Tedder. 2006. New prospects for autoimmune disease therapy: B cells on deathwatch. Arthritis Rheum. 54: 1-9.
    • (2006) Arthritis Rheum. , vol.54 , pp. 1-9
    • St. Clair, W.E.1    Tedder, T.F.2
  • 43
    • 0029558338 scopus 로고
    • Studies of group B streptococcal infection in mice deficient in complement C3 or C4 demonstrate an essential role for complement in both innate and acquired immunity
    • Wessels, M. R., P. Butko, M. Ma, H. B. Warren, A. Lage, and M. C. Carroll. 1995. Studies of group B streptococcal infection in mice deficient in complement C3 or C4 demonstrate an essential role for complement in both innate and acquired immunity. Proc. Natl. Acad. Sci. USA 92: 11490-11494.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11490-11494
    • Wessels, M.R.1    Butko, P.2    Ma, M.3    Warren, H.B.4    Lage, A.5    Carroll, M.C.6
  • 44
    • 0032520727 scopus 로고    scopus 로고
    • The need for IgG2c specific antiserum when isotyping antibodies from C57BL/6 and NOD mice
    • Martin, R. M., J. L. Brady, and A. M. Lew. 1998. The need for IgG2c specific antiserum when isotyping antibodies from C57BL/6 and NOD mice. J. Immunol. Methods 212: 187-192.
    • (1998) J. Immunol. Methods , vol.212 , pp. 187-192
    • Martin, R.M.1    Brady, J.L.2    Lew, A.M.3
  • 45
    • 0842278644 scopus 로고    scopus 로고
    • Severely-impaired B lymphocyte proliferation, survival and induction of the c-Myc:Cullin 1 ubiquitin ligase pathway resulting from CD22 deficiency on the C57BL/6 genetic background
    • Poe, J. C., K. M. Haas, J. Uchida, Y. Lee, M. Fujimoto, and T. F. Tedder. 2004. Severely-impaired B lymphocyte proliferation, survival and induction of the c-Myc:Cullin 1 ubiquitin ligase pathway resulting from CD22 deficiency on the C57BL/6 genetic background. J. Immunol. 172: 2100-2110.
    • (2004) J. Immunol. , vol.172 , pp. 2100-2110
    • Poe, J.C.1    Haas, K.M.2    Uchida, J.3    Lee, Y.4    Fujimoto, M.5    Tedder, T.F.6
  • 46
    • 0028042424 scopus 로고
    • FcRγ chain depletion results in pleiotrophic effector cell defects
    • Takai, T., M. Li, D. Sylvestre, R. Clynes, and J. V. Ravetch. 1994. FcRγ chain depletion results in pleiotrophic effector cell defects. Cell 76: 519-529.
    • (1994) Cell , vol.76 , pp. 519-529
    • Takai, T.1    Li, M.2    Sylvestre, D.3    Clynes, R.4    Ravetch, J.V.5
  • 47
    • 17344368340 scopus 로고    scopus 로고
    • Divergent roles for Fc receptors and complement in vivo
    • Ravetch, J. V., and R. A. Clynes. 1998. Divergent roles for Fc receptors and complement in vivo. Annu. Rev. Immunol. 16: 421-432.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 421-432
    • Ravetch, J.V.1    Clynes, R.A.2
  • 48
    • 22544487815 scopus 로고    scopus 로고
    • FcγRIV: A novel FcR with distinct IgG subclass specificity
    • Nimmerjahn, F., P. Bruhns, K. Horiuchi, and J. V. Ravetch. 2005. FcγRIV: a novel FcR with distinct IgG subclass specificity. Immunity 23: 41-51.
    • (2005) Immunity , vol.23 , pp. 41-51
    • Nimmerjahn, F.1    Bruhns, P.2    Horiuchi, K.3    Ravetch, J.V.4
  • 49
  • 50
    • 31344445556 scopus 로고    scopus 로고
    • Ablation of CD22 in ligand-deficient mice restores B cell receptor signaling
    • Collins, B. E., B. A. Smith, P. Bengtson, and J. C. Paulson. 2006. Ablation of CD22 in ligand-deficient mice restores B cell receptor signaling. Nat. Immunol. 7: 199-206.
    • (2006) Nat. Immunol. , vol.7 , pp. 199-206
    • Collins, B.E.1    Smith, B.A.2    Bengtson, P.3    Paulson, J.C.4
  • 51
    • 0029025026 scopus 로고
    • Constitutive endocytosis and degradation of CD22 by human B cells
    • Shan, D., and O. W. Press. 1995. Constitutive endocytosis and degradation of CD22 by human B cells. J. Immunol. 154: 4466-4475.
    • (1995) J. Immunol. , vol.154 , pp. 4466-4475
    • Shan, D.1    Press, O.W.2
  • 52
    • 0346034779 scopus 로고    scopus 로고
    • The B cell coreceptor CD22 associates with AP50, a clathrin-coated pit adapter protein, via tyrosine-dependent interaction
    • John, B., B. R. Herrin, C. Raman, Y. Wang, K. R. Bobbin, B. A. Brody, and L. B. Justement. 2003. The B cell coreceptor CD22 associates with AP50, a clathrin-coated pit adapter protein, via tyrosine-dependent interaction. J. Immunol. 170: 3534-3543.
    • (2003) J. Immunol. , vol.170 , pp. 3534-3543
    • John, B.1    Herrin, B.R.2    Raman, C.3    Wang, Y.4    Bobbin, K.R.5    Brody, B.A.6    Justement, L.B.7
  • 53
    • 0023886893 scopus 로고
    • Evaluation of ricin a chain-containing immunotoxins directed against CD19 and CD22 antigens on normal and malignant human B-cells as potential reagents for in vivo therapy
    • Ghetie, M.-A., R. D. May, M. Till, J. W. Uhr, V. Ghetie, P. P. Knowles, M. Relf, A. Brown, P. M. Wallace, G. Janossy, et al. 1988. Evaluation of ricin A chain-containing immunotoxins directed against CD19 and CD22 antigens on normal and malignant human B-cells as potential reagents for in vivo therapy. Cancer Res. 48: 2610-2617.
    • (1988) Cancer Res. , vol.48 , pp. 2610-2617
    • Ghetie, M.-A.1    May, R.D.2    Till, M.3    Uhr, J.W.4    Ghetie, V.5    Knowles, P.P.6    Relf, M.7    Brown, A.8    Wallace, P.M.9    Janossy, G.10
  • 55
    • 0141617534 scopus 로고    scopus 로고
    • Transitional and marginal zone B cells have a high proportion of unmasked CD22: Implications for BCR signaling
    • Danzer, C. P., B. E. Collins, O. Blixt, J. C. Paulson, and L. Nitschke. 2003. Transitional and marginal zone B cells have a high proportion of unmasked CD22: implications for BCR signaling. Int. Immunol. 15: 1137-1147.
    • (2003) Int. Immunol. , vol.15 , pp. 1137-1147
    • Danzer, C.P.1    Collins, B.E.2    Blixt, O.3    Paulson, J.C.4    Nitschke, L.5
  • 56
    • 3042592452 scopus 로고    scopus 로고
    • The innate mononuclear phagocyte network depletes B lymphocytes through Fc receptor-dependent mechanisms during anti-CD20 antibody immunotherapy
    • Uchida, J., Y. Hamaguchi, J. A. Oliver, J. V. Ravetch, J. C. Poe, K. M. Haas, and T. F. Tedder. 2004. The innate mononuclear phagocyte network depletes B lymphocytes through Fc receptor-dependent mechanisms during anti-CD20 antibody immunotherapy. J. Exp. Med. 199: 1659-1669.
    • (2004) J. Exp. Med. , vol.199 , pp. 1659-1669
    • Uchida, J.1    Hamaguchi, Y.2    Oliver, J.A.3    Ravetch, J.V.4    Poe, J.C.5    Haas, K.M.6    Tedder, T.F.7
  • 57
    • 15444368773 scopus 로고    scopus 로고
    • The peritoneal cavity provides a protective niche for B1 and conventional B lymphocytes during anti-CD20 immunotherapy in mice
    • Hamaguchi, Y., J. Uchida, D. W. Cain, G. M. Venturi, J. C. Poe, K. M. Haas, and T. F. Tedder. 2005. The peritoneal cavity provides a protective niche for B1 and conventional B lymphocytes during anti-CD20 immunotherapy in mice. J. Immunol. 7: 4389-4399.
    • (2005) J. Immunol. , vol.7 , pp. 4389-4399
    • Hamaguchi, Y.1    Uchida, J.2    Cain, D.W.3    Venturi, G.M.4    Poe, J.C.5    Haas, K.M.6    Tedder, T.F.7
  • 58
    • 33645053518 scopus 로고    scopus 로고
    • Antibody isotype-specific engagement of Fcγ receptors regulates B lymphocyte depletion during CD20 immunotherapy
    • Hamaguchi, Y., Y. Xiu, K. Komura, F. Nimmerjahn, and T. F. Tedder. 2006. Antibody isotype-specific engagement of Fcγ receptors regulates B lymphocyte depletion during CD20 immunotherapy. J. Exp. Med. 203: 743-753.
    • (2006) J. Exp. Med. , vol.203 , pp. 743-753
    • Hamaguchi, Y.1    Xiu, Y.2    Komura, K.3    Nimmerjahn, F.4    Tedder, T.F.5
  • 59
    • 27244432745 scopus 로고    scopus 로고
    • Immunotherapy using unconjugated CD19 monoclonal antibodies in animal models for B lymphocyte malignancies and autoimmune disease
    • Yazawa, N., Y. Hamaguchi, J. C. Poe, and T. F. Tedder. 2005. Immunotherapy using unconjugated CD19 monoclonal antibodies in animal models for B lymphocyte malignancies and autoimmune disease. Proc. Natl. Acad. Sci. USA 102: 15178-15183.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15178-15183
    • Yazawa, N.1    Hamaguchi, Y.2    Poe, J.C.3    Tedder, T.F.4
  • 61
    • 0031114872 scopus 로고    scopus 로고
    • Membrane IgM-induced tyrosine phosphorylation of CD19 requires a CD19 domain that mediates association with components of the B cell antigen receptor complex
    • Carter, R. H., G. M. Doody, J. B. Bolen, and D. T. Fearon. 1997. Membrane IgM-induced tyrosine phosphorylation of CD19 requires a CD19 domain that mediates association with components of the B cell antigen receptor complex. J. Immunol. 158: 3062-3069.
    • (1997) J. Immunol. , vol.158 , pp. 3062-3069
    • Carter, R.H.1    Doody, G.M.2    Bolen, J.B.3    Fearon, D.T.4
  • 62
    • 7244254363 scopus 로고    scopus 로고
    • Cell surface sialic acids do not affect primary CD22 interactions with CD45 and surface IgM nor the rate of constitutive CD22 endocytosis
    • Zhang, M., and A. Varki. 2004. Cell surface sialic acids do not affect primary CD22 interactions with CD45 and surface IgM nor the rate of constitutive CD22 endocytosis. Glycobiology 14: 939-949.
    • (2004) Glycobiology , vol.14 , pp. 939-949
    • Zhang, M.1    Varki, A.2
  • 63
    • 0030053270 scopus 로고    scopus 로고
    • syk kinase, p53/56lyn kinase and phosphatidyl inositol-3 kinase in signal transduction via the human B lymphocyte antigen CD22
    • syk kinase, p53/56lyn kinase and phosphatidyl inositol-3 kinase in signal transduction via the human B lymphocyte antigen CD22. Eur. J. Immunol. 26: 1246-1252.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 1246-1252
    • Tuscano, J.M.1    Engel, P.2    Tedder, T.F.3    Agarwal, A.4    Kehrl, J.H.5
  • 64


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.