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Volumn 8, Issue 3, 1996, Pages 378-382

Activation of B lymphocytes: Integrating signals from CD19, CD22 and FcγRIIb1

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN; CD19 ANTIGEN; CD22 ANTIGEN; CYTOPLASM PROTEIN; FC RECEPTOR; IMMUNOGLOBULIN; IMMUNOGLOBULIN G; LYMPHOCYTE MEMBRANE RECEPTOR; MEMBRANE PROTEIN;

EID: 0030176019     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(96)80128-2     Document Type: Article
Times cited : (52)

References (47)
  • 1
    • 0028958669 scopus 로고
    • The CD19/CR2/TAPA-1 complex of B lymphocytes: Linking natural to acquired immunity
    • Fearon DT, Carter RH. The CD19/CR2/TAPA-1 complex of B lymphocytes: linking natural to acquired immunity. Annu Rev Immunol. 13:1995;127-150.
    • (1995) Annu Rev Immunol. , vol.13 , pp. 127-150
    • Fearon, D.T.1    Carter, R.H.2
  • 2
    • 43949157081 scopus 로고
    • The CD19/CD21 signal transduction complex of B lymphocytes
    • Tedder TF, Zhou LJ, Engel P. The CD19/CD21 signal transduction complex of B lymphocytes. Immunol Today. 15:1994;437-442.
    • (1994) Immunol Today , vol.15 , pp. 437-442
    • Tedder, T.F.1    Zhou, L.J.2    Engel, P.3
  • 5
    • 0029151210 scopus 로고
    • Immunoglobulin recombinase gene activity is modulated reciprocally by interleukin 7 and CD19 in B cell progenitors
    • of special interest. This study suggests that signals generated by CD19 and the IL-7 receptor may regulate rearrangement of gene fragments. Purified human pro-B cells treated in vitro with IL-7 downregulate TdT, RAG1 and RAG2. CD19 reverses the downregulation of RAG1 and RAG2.
    • Billips LG, Nuñez CA, Bertrand FE, Stankovic AK, Gartland GL, Burrows PD, Cooper MD. Immunoglobulin recombinase gene activity is modulated reciprocally by interleukin 7 and CD19 in B cell progenitors. of special interest J Exp Med. 182:1995;973-982 This study suggests that signals generated by CD19 and the IL-7 receptor may regulate rearrangement of gene fragments. Purified human pro-B cells treated in vitro with IL-7 downregulate TdT, RAG1 and RAG2. CD19 reverses the downregulation of RAG1 and RAG2.
    • (1995) J Exp Med. , vol.182 , pp. 973-982
    • Billips, L.G.1    Nuñez, C.A.2    Bertrand, F.E.3    Stankovic, A.K.4    Gartland, G.L.5    Burrows, P.D.6    Cooper, M.D.7
  • 6
    • 0027326264 scopus 로고
    • Functional effect of IL-7-enhanced CD19 expression on human B cell precursors
    • Wolf ML, Weng W-K, Stieglbauer N, Shah N, LeBien TW. Functional effect of IL-7-enhanced CD19 expression on human B cell precursors. J Immunol. 151:1993;138-148.
    • (1993) J Immunol. , vol.151 , pp. 138-148
    • Wolf, M.L.1    Weng, W.-K.2    Stieglbauer, N.3    Shah, N.4    LeBien, T.W.5
  • 7
    • 0029064680 scopus 로고
    • Impairment of T-cell-dependent B-cell responses and B-1 cell development in CD19-deficient mice
    • of outstanding interest. This paper, along with [8], demonstrates the important biologic role for CD19 in vivo. Disruption of the CD19 gene by homologous targeted recombination results in diminished numbers of B-1a cells and impaired responses to T cell-dependent antigens.
    • Rickert RC, Rajewsky K, Roes J. Impairment of T-cell-dependent B-cell responses and B-1 cell development in CD19-deficient mice. of outstanding interest Nature. 376:1995;352-355 This paper, along with [8], demonstrates the important biologic role for CD19 in vivo. Disruption of the CD19 gene by homologous targeted recombination results in diminished numbers of B-1a cells and impaired responses to T cell-dependent antigens.
    • (1995) Nature , vol.376 , pp. 352-355
    • Rickert, R.C.1    Rajewsky, K.2    Roes, J.3
  • 8
    • 0029094609 scopus 로고
    • Abnormal B lymphocyte development, activation, and differentiation in mice that lack or overexpress the CD19 signal transduction molecule
    • of outstanding interest. See annotation [7].
    • Engel P, Zhou L-J, Ord DC, Sato S, Koller B, Tedder TF. Abnormal B lymphocyte development, activation, and differentiation in mice that lack or overexpress the CD19 signal transduction molecule. of outstanding interest Immunity. 3:1995;39-50 See annotation [7].
    • (1995) Immunity , vol.3 , pp. 39-50
    • Engel, P.1    Zhou, L.-J.2    Ord, D.C.3    Sato, S.4    Koller, B.5    Tedder, T.F.6
  • 9
    • 0028355752 scopus 로고
    • Tissue-specific expression of human CD19 gene in transgenic mice inhibits antigen-independent B-lymphocyte development
    • Zhou LJ, Smith HM, Waldschmidt TJ, Schwarting R, Daley J, Tedder TF. Tissue-specific expression of human CD19 gene in transgenic mice inhibits antigen-independent B-lymphocyte development. Mol Cell Biol. 14:1994;3884-3894.
    • (1994) Mol Cell Biol. , vol.14 , pp. 3884-3894
    • Zhou, L.J.1    Smith, H.M.2    Waldschmidt, T.J.3    Schwarting, R.4    Daley, J.5    Tedder, T.F.6
  • 11
    • 0028915948 scopus 로고
    • Defective signalling through the T- and B-cell antigen receptors in lymphoid cells lacking the vav proto-oncogene
    • null gene into mice deficient in RAG resulted in an absence of B-1 cells. The similarity of this effect to that of a deficiency in CD19 supports the demonstration of a functional interaction between Vav and CD19 and a role for CD19-mediated signaling in B-1 cells.
    • null gene into mice deficient in RAG resulted in an absence of B-1 cells. The similarity of this effect to that of a deficiency in CD19 supports the demonstration of a functional interaction between Vav and CD19 and a role for CD19-mediated signaling in B-1 cells.
    • (1995) Nature , vol.374 , pp. 470-473
    • Zhang, R.1    Alt, F.W.2    Davidson, L.3    Orkin, S.H.4    Swat, W.5
  • 12
    • 0028956337 scopus 로고
    • Defective antigen receptor-mediated proliferation of B and T cells in the absence of Vav
    • of outstanding interest. See annotation [11].
    • Tarakhovsky A, Turner M, Schaal S, Mee PJ, Duddy LP, Rajewsky K, Tybulewicz VLJ. Defective antigen receptor-mediated proliferation of B and T cells in the absence of Vav. of outstanding interest Nature. 374:1995;467-470 See annotation [11].
    • (1995) Nature , vol.374 , pp. 467-470
    • Tarakhovsky, A.1    Turner, M.2    Schaal, S.3    Mee, P.J.4    Duddy, L.P.5    Rajewsky, K.6    Tybulewicz, V.L.J.7
  • 13
    • 0028597993 scopus 로고
    • Signalling through CD19 activates a Vas/mitogen-activated protein kinase pathway and induces formation of a CD19/phosphatidylinositol 3-kinase complex in human B cell precursors
    • Weng WK, Jarvis L, LeBien TW. Signalling through CD19 activates a Vas/mitogen-activated protein kinase pathway and induces formation of a CD19/phosphatidylinositol 3-kinase complex in human B cell precursors. J Biol Chem. 263:1994;32514-32521.
    • (1994) J Biol Chem. , vol.263 , pp. 32514-32521
    • Weng, W.K.1    Jarvis, L.2    LeBien, T.W.3
  • 14
    • 0029558617 scopus 로고
    • The Cd19 signal transduction molecule is a response regulator of B-lymphocyte differentiation
    • Sato S, Steeba DA, Tedder TF. The Cd19 signal transduction molecule is a response regulator of B-lymphocyte differentiation. Proc Natl Acad Sci USA. 92:1995;11558-11562.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11558-11562
    • Sato, S.1    Steeba, D.A.2    Tedder, T.F.3
  • 15
    • 0028786573 scopus 로고
    • Engaging CD19 or the target of an antiproliferative antibody 1 on human B lymphocytes induces binding of B cells to the interfollicular stroma of human tonsils via integrin α4β1 and fibronectin
    • Behr S, Schriever F. Engaging CD19 or the target of an antiproliferative antibody 1 on human B lymphocytes induces binding of B cells to the interfollicular stroma of human tonsils via integrin α4β1 and fibronectin. J Exp Med. 182:1995;1191-1199.
    • (1995) J Exp Med. , vol.182 , pp. 1191-1199
    • Behr, S.1    Schriever, F.2
  • 16
    • 0028358087 scopus 로고
    • CD19 has a potential CD77 (Globotriasoyl ceramide)-binding site with sequence similarity to verotoxin B-subunits: Implications of molecular mimicry for B cell adhesion and enterohemorrhagic Escherichia coli pathogenesis
    • Maloney MD, Lingwood CA. CD19 has a potential CD77 (Globotriasoyl ceramide)-binding site with sequence similarity to verotoxin B-subunits: implications of molecular mimicry for B cell adhesion and enterohemorrhagic Escherichia coli pathogenesis. J Exp Med. 180:1994;191-201.
    • (1994) J Exp Med. , vol.180 , pp. 191-201
    • Maloney, M.D.1    Lingwood, C.A.2
  • 17
    • 0029916530 scopus 로고    scopus 로고
    • Antibody response to a T-dependent antigen requires B cell expression of complement receptors
    • Croix DA, Aheam JM, Rosengard AM, Han S, Kelsoe G, Ma M, Carroll MC. Antibody response to a T-dependent antigen requires B cell expression of complement receptors. J Exp Med. 183:1996;1857-1864.
    • (1996) J Exp Med. , vol.183 , pp. 1857-1864
    • Croix, D.A.1    Aheam, J.M.2    Rosengard, A.M.3    Han, S.4    Kelsoe, G.5    Ma, M.6    Carroll, M.C.7
  • 18
    • 0028036854 scopus 로고
    • Modulation of signalling via the B cell antigen receptor by CD21, the receptor for C3dg and EBV
    • Luxembourg AT, Cooper NR. Modulation of signalling via the B cell antigen receptor by CD21, the receptor for C3dg and EBV. J Immunol. 153:1994;4448-4457.
    • (1994) J Immunol. , vol.153 , pp. 4448-4457
    • Luxembourg, A.T.1    Cooper, N.R.2
  • 19
    • 0028905909 scopus 로고
    • Co-ligation of mouse complement receptors 1 and 2 with surface IgM rescues splenic B cells and WEHI-231 cells from anti-surface IgM-induced apoptosis
    • Kozono Y, Duke RC, Schleicher MS, Holers VM. Co-ligation of mouse complement receptors 1 and 2 with surface IgM rescues splenic B cells and WEHI-231 cells from anti-surface IgM-induced apoptosis. Eur J Immunol. 25:1995;1013-1017.
    • (1995) Eur J Immunol. , vol.25 , pp. 1013-1017
    • Kozono, Y.1    Duke, R.C.2    Schleicher, M.S.3    Holers, V.M.4
  • 20
    • 0030593030 scopus 로고    scopus 로고
    • C3d of complement as a molecular adjuvant: Bridging innate and acquired immunity
    • of outstanding interest. A physiologic ligand for the CD19-CD21 complex relies on the intersection between innate and acquired immunity. Targeting the antigen HEL to this complex with the CD21 ligand C3d enhances the potency of the antigen by two to three orders of magnitude both in vitro and in vivo.
    • Dempsey PW, Allison MED, Akkaraju S, Goodnow CC, Fearon DT. C3d of complement as a molecular adjuvant: bridging innate and acquired immunity. of outstanding interest Science. 271:1996;348-350 A physiologic ligand for the CD19-CD21 complex relies on the intersection between innate and acquired immunity. Targeting the antigen HEL to this complex with the CD21 ligand C3d enhances the potency of the antigen by two to three orders of magnitude both in vitro and in vivo.
    • (1996) Science , vol.271 , pp. 348-350
    • Dempsey, P.W.1    Allison, M.E.D.2    Akkaraju, S.3    Goodnow, C.C.4    Fearon, D.T.5
  • 24
    • 0028807888 scopus 로고
    • Tyrosine-phosphorylated forms of Igβ, CD22, TCRζ and HOSS are major ligands for tandem SH2 domains of Syk
    • Wienands J, Freuler F, Baumann G. Tyrosine-phosphorylated forms of Igβ, CD22, TCRζ and HOSS are major ligands for tandem SH2 domains of Syk. Int Immunol. 7:1995;1701-1708.
    • (1995) Int Immunol. , vol.7 , pp. 1701-1708
    • Wienands, J.1    Freuler, F.2    Baumann, G.3
  • 25
    • 0027175115 scopus 로고
    • Association of CD22 with the B-cell antigen receptor
    • Peaker CJG, Neuberger MS. Association of CD22 with the B-cell antigen receptor. Eur J Immunol. 23:1993;1359-1364.
    • (1993) Eur J Immunol. , vol.23 , pp. 1359-1364
    • Peaker, C.J.G.1    Neuberger, M.S.2
  • 26
    • 0029012969 scopus 로고
    • A role in B cell activation for CD22 and the protein tyrosine phosphatase SHP
    • of special interest. This paper describes the functional association of CD22 with the tyrosine phosphatase SHP and the augmentation of antigen receptor signaling following ligation of CD22. See also [27].
    • Doody GD, Justement LB, Delibrias CC, Matthews RJ, Lin J, Thomas ML, Fearon DT. A role in B cell activation for CD22 and the protein tyrosine phosphatase SHP. of special interest Science. 269:1995;242-244 This paper describes the functional association of CD22 with the tyrosine phosphatase SHP and the augmentation of antigen receptor signaling following ligation of CD22. See also [27].
    • (1995) Science , vol.269 , pp. 242-244
    • Doody, G.D.1    Justement, L.B.2    Delibrias, C.C.3    Matthews, R.J.4    Lin, J.5    Thomas, M.L.6    Fearon, D.T.7
  • 27
    • 0029048060 scopus 로고
    • Phosphotyrosine-dependent association between CD22 and protein tyrosine phosphatase
    • of outstanding interest. of outstanding interest. See annotation [26].
    • of outstanding interest Campbell MA, Kinman NR. Phosphotyrosine-dependent association between CD22 and protein tyrosine phosphatase. of outstanding interest Eur J Immunol. 25:1995;1573-1579 See annotation [26].
    • (1995) Eur J Immunol. , vol.25 , pp. 1573-1579
    • Campbell, M.A.1    Kinman, N.R.2
  • 28
    • 0029001872 scopus 로고
    • Regulation of immune function by protein tyrosine phosphatases
    • of special interest
    • of special interest Okumura M, Thomas ML. Regulation of immune function by protein tyrosine phosphatases. Curr Opin Immunol. 7:1995;312-319.
    • (1995) Curr Opin Immunol. , vol.7 , pp. 312-319
    • Okumura, M.1    Thomas, M.L.2
  • 29
    • 0028961264 scopus 로고
    • Protein tyrosine phosphatase 1C negatively regulates antigen receptor signaling in B lymphocytes and determines thresholds for negative selection
    • of outstanding interest. These authors show that the deficiency of SHP in motheaten viable mice resulted in hyperresponsive signaling through membrane immunoglobulin, indicating the negative regulatory role of this phosphatase.
    • Cyster JG, Goodnow CC. Protein tyrosine phosphatase 1C negatively regulates antigen receptor signaling in B lymphocytes and determines thresholds for negative selection. of outstanding interest Immunity. 2:1995;13-24 These authors show that the deficiency of SHP in motheaten viable mice resulted in hyperresponsive signaling through membrane immunoglobulin, indicating the negative regulatory role of this phosphatase.
    • (1995) Immunity , vol.2 , pp. 13-24
    • Cyster, J.G.1    Goodnow, C.C.2
  • 30
    • 0026587743 scopus 로고
    • CD19: Lowering the threshold for antigen receptor stimulation of B lymphocytes
    • Carter RH, Fearon DT. CD19: lowering the threshold for antigen receptor stimulation of B lymphocytes. Science. 256:1992;105-107.
    • (1992) Science , vol.256 , pp. 105-107
    • Carter, R.H.1    Fearon, D.T.2
  • 31
    • 0023907422 scopus 로고
    • Role of the CD22 human B cell antigen in B cell triggering by anti-immunoglobulin
    • Pezzutto A, Rabinovitch PS, Dörken B, Moldenhauer G, Clark EA. Role of the CD22 human B cell antigen in B cell triggering by anti-immunoglobulin. J Immunol. 140:1988;1791-1795.
    • (1988) J Immunol. , vol.140 , pp. 1791-1795
    • Pezzutto, A.1    Rabinovitch, P.S.2    Dörken, B.3    Moldenhauer, G.4    Clark, E.A.5
  • 32
    • 0028206055 scopus 로고
    • The oligosaccharide binding specificities of CD22, β, a sialic-acid-specific lectin of B cells
    • Powell L, Varki A. The oligosaccharide binding specificities of CD22, β, a sialic-acid-specific lectin of B cells. J Biol Chem. 269:1994;10628-10636.
    • (1994) J Biol Chem. , vol.269 , pp. 10628-10636
    • Powell, L.1    Varki, A.2
  • 33
    • 0028962757 scopus 로고
    • Characterization of sialyloligossacharide binding by recombinant soluble and native cell-associated CD22
    • Powell LD, Jain RK, Matta KL, Sabesan S, Varki A. Characterization of sialyloligossacharide binding by recombinant soluble and native cell-associated CD22. J Biol Chem. 270:1995;7523-7532.
    • (1995) J Biol Chem. , vol.270 , pp. 7523-7532
    • Powell, L.D.1    Jain, R.K.2    Matta, K.L.3    Sabesan, S.4    Varki, A.5
  • 34
    • 0028987134 scopus 로고
    • CD22-mediated cell adhesion to cytokine-activated human endothelial cells
    • Hanasaki K, Varki A, Powell LD. CD22-mediated cell adhesion to cytokine-activated human endothelial cells. J Biol Chem. 270:1995;7533-7542.
    • (1995) J Biol Chem. , vol.270 , pp. 7533-7542
    • Hanasaki, K.1    Varki, A.2    Powell, L.D.3
  • 35
    • 0028177588 scopus 로고
    • Cytokine-induced β-galactoside α-2,6-sialyltransferase in human endothelial cells mediates α2,6-sialylation of adhesion molecules and CD22 molecules
    • Hanasaki K, Varki A, Stamenkovic I, Bevilacqua MP. Cytokine-induced β-galactoside α-2,6-sialyltransferase in human endothelial cells mediates α2,6-sialylation of adhesion molecules and CD22 molecules. J Biol Chem. 269:1994;10637-10643.
    • (1994) J Biol Chem. , vol.269 , pp. 10637-10643
    • Hanasaki, K.1    Varki, A.2    Stamenkovic, I.3    Bevilacqua, M.P.4
  • 36
    • 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, Wagner N, Miller AS, Tedder TF. 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. 181:1995;1581-1586.
    • (1995) J Exp Med. , vol.181 , pp. 1581-1586
    • Engel, P.1    Wagner, N.2    Miller, A.S.3    Tedder, T.F.4
  • 37
    • 0028928442 scopus 로고
    • Binding of human plasma sialoglycoproteins by the B cell-specific lectin CD22
    • Hanasaki K, Powell LD, Varki A. Binding of human plasma sialoglycoproteins by the B cell-specific lectin CD22. J Biol Chem. 270:1995;7543-7550.
    • (1995) J Biol Chem. , vol.270 , pp. 7543-7550
    • Hanasaki, K.1    Powell, L.D.2    Varki, A.3
  • 38
    • 0028276413 scopus 로고
    • Natural ligands of the B cell adhesion molecule CD22βcan be masked by 9-O-acetylation of sialic acids
    • Sjoberg ER, Powell LD, Klein A, Varki A. Natural ligands of the B cell adhesion molecule CD22βcan be masked by 9-O-acetylation of sialic acids. J Cell Biol. 126:1994;549-562.
    • (1994) J Cell Biol. , vol.126 , pp. 549-562
    • Sjoberg, E.R.1    Powell, L.D.2    Klein, A.3    Varki, A.4
  • 39
    • 0028365277 scopus 로고
    • Sialylation of the B lymphocyte molecule CD22 by α2,6-sialyltransferase is implicated in the regulation of CD22-mediated adhesion
    • Braesch-Andersen S, Stamenkovic I. Sialylation of the B lymphocyte molecule CD22 by α2,6-sialyltransferase is implicated in the regulation of CD22-mediated adhesion. J Biol Chem. 269:1994;11783-11786.
    • (1994) J Biol Chem. , vol.269 , pp. 11783-11786
    • Braesch-Andersen, S.1    Stamenkovic, I.2
  • 41
    • 0030031886 scopus 로고    scopus 로고
    • Augmented humoral and anaphylactic responses in FcγRII-deficient mice
    • of special interest. Analysis of FcγRII-deficient mice confirmed the negative regulatory role of this receptor in immune complex initiated signaling.
    • Takai T, Ono M, Hikida M, Ohmori H, Ravetch JV. Augmented humoral and anaphylactic responses in FcγRII-deficient mice. of special interest Nature. 379:1996;346-349 Analysis of FcγRII-deficient mice confirmed the negative regulatory role of this receptor in immune complex initiated signaling.
    • (1996) Nature , vol.379 , pp. 346-349
    • Takai, T.1    Ono, M.2    Hikida, M.3    Ohmori, H.4    Ravetch, J.V.5
  • 42
    • 0027418367 scopus 로고
    • Cross-linking of IgG receptors inhibits membrane immunoglobulin-stimulated calcium influx in B lymphocytes
    • Choquet D, Partiseti M, Amigorena S, Bonnerot C, Fridman WH, Kom H. Cross-linking of IgG receptors inhibits membrane immunoglobulin-stimulated calcium influx in B lymphocytes. J Cell Biol. 121:1993;355-363.
    • (1993) J Cell Biol. , vol.121 , pp. 355-363
    • Choquet, D.1    Partiseti, M.2    Amigorena, S.3    Bonnerot, C.4    Fridman, W.H.5    Kom, H.6
  • 43
    • 0028347321 scopus 로고
    • A 13-amino-acid motif in the cytoplasmic domain of FcγRIIb modulates B-cell receptor signaling
    • of outstanding interest. Dissection of FcγRIIb revealed that a single tyrosine residue mediates the negative modulation of membrane immunoglobulin signaling by FcγRIIb.
    • Muta T, Kurosaki T, Misulovin Z, Sanchez M, Nussenzweig MC, Ravetch JV. A 13-amino-acid motif in the cytoplasmic domain of FcγRIIb modulates B-cell receptor signaling. of outstanding interest Nature. 368:1994;70-73 Dissection of FcγRIIb revealed that a single tyrosine residue mediates the negative modulation of membrane immunoglobulin signaling by FcγRIIb.
    • (1994) Nature , vol.368 , pp. 70-73
    • Muta, T.1    Kurosaki, T.2    Misulovin, Z.3    Sanchez, M.4    Nussenzweig, M.C.5    Ravetch, J.V.6
  • 45
    • 0028032257 scopus 로고
    • Tyrosine-containing sequence motifs of the human immunoglobulin G receptors FcRIIb1 and FcRIIb2 essential for endocytosis and regulation of calcium in B cells
    • Budde P, Bewarder N, Weinrich V, Schulzeck O, Frey J. Tyrosine-containing sequence motifs of the human immunoglobulin G receptors FcRIIb1 and FcRIIb2 essential for endocytosis and regulation of calcium in B cells. J Biol Chem. 269:1994;30636-30644.
    • (1994) J Biol Chem. , vol.269 , pp. 30636-30644
    • Budde, P.1    Bewarder, N.2    Weinrich, V.3    Schulzeck, O.4    Frey, J.5


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