메뉴 건너뛰기




Volumn 162, Issue 9, 1999, Pages 5278-5286

CD45 regulates tyrosine phosphorylation of CD22 and its association with the protein tyrosine phosphatase SHP-1

Author keywords

[No Author keywords available]

Indexed keywords

CD22 ANTIGEN; CD45 ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE SHP 1; UNCLASSIFIED DRUG;

EID: 0033136946     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (31)

References (48)
  • 1
    • 0030885363 scopus 로고    scopus 로고
    • The role of CD45 in signal transduction
    • Justement, L. B. 1997. The role of CD45 in signal transduction. Adv. Immunol. 66:1.
    • (1997) Adv. Immunol. , vol.66 , pp. 1
    • Justement, L.B.1
  • 3
    • 0030023652 scopus 로고    scopus 로고
    • Regulation of B-lymphocyte negative and positive selection by tyrosine phosphatase CD45
    • Cyster, J. G., J. I. Healy, K. Kishihara, T. W. Mak, M. L. Thomas, and C. C. Goodnow. 1996. Regulation of B-lymphocyte negative and positive selection by tyrosine phosphatase CD45. Nature 381:325.
    • (1996) Nature , vol.381 , pp. 325
    • Cyster, J.G.1    Healy, J.I.2    Kishihara, K.3    Mak, T.W.4    Thomas, M.L.5    Goodnow, C.C.6
  • 6
    • 0032496240 scopus 로고    scopus 로고
    • Major histocompatability class II-mediated signal transduction is regulated by the protein tyrosine phosphatase CD45
    • Greer, S. F., J. Lin, C. H. Clarke, and L. B. Justement. 1998. Major histocompatability class II-mediated signal transduction is regulated by the protein tyrosine phosphatase CD45. J. Biol. Chem. 273:11970.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11970
    • Greer, S.F.1    Lin, J.2    Clarke, C.H.3    Justement, L.B.4
  • 7
    • 0030070349 scopus 로고    scopus 로고
    • Immunoglobulin-mediated signal transduction in B cells from CD45-deficient mice
    • Benatar, T., R. Carsetti, C. Furlonger, N. Kamalia, T. Mak, and C. J. Paige, 1996. Immunoglobulin-mediated signal transduction in B cells from CD45-deficient mice. J. Exp. Med. 183:329.
    • (1996) J. Exp. Med. , vol.183 , pp. 329
    • Benatar, T.1    Carsetti, R.2    Furlonger, C.3    Kamalia, N.4    Mak, T.5    Paige, C.J.6
  • 9
    • 0031066598 scopus 로고    scopus 로고
    • Molecular targets of CD45 in B cell antigen receptor signal transduction
    • Pao, L. I., W. D. Bedzyk, C. Persin, and J. C. Cambier. 1997. Molecular targets of CD45 in B cell antigen receptor signal transduction. J. Immunol. 158:1116.
    • (1997) J. Immunol. , vol.158 , pp. 1116
    • Pao, L.I.1    Bedzyk, W.D.2    Persin, C.3    Cambier, J.C.4
  • 10
    • 0029846429 scopus 로고    scopus 로고
    • CD45 modulates phosphorylation of both autophosphorylation and negative regulatory tyrosines of Lyn in B cells
    • Yanagi, S., H. Sugawara, M. Kurosaki, H. Sabe, H. Yamamura, and T. Kurosaki. 1996. CD45 modulates phosphorylation of both autophosphorylation and negative regulatory tyrosines of Lyn in B cells. J. Biol. Chem. 271:30487.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30487
    • Yanagi, S.1    Sugawara, H.2    Kurosaki, M.3    Sabe, H.4    Yamamura, H.5    Kurosaki, T.6
  • 13
    • 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.
    • (1996) Immunity , vol.5 , pp. 551
    • 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
  • 18
    • 0032550365 scopus 로고    scopus 로고
    • A double-edged kinase Lyn: A positive and negative regulator for antigen receptor-mediated signals
    • Nishizumi, H., K. Horikawa, I. Mlinaric-Rascan, and T. Yamamoto. 1998. A double-edged kinase Lyn: a positive and negative regulator for antigen receptor-mediated signals. J. Exp. Med. 187:1343.
    • (1998) J. Exp. Med. , vol.187 , pp. 1343
    • Nishizumi, H.1    Horikawa, K.2    Mlinaric-Rascan, I.3    Yamamoto, T.4
  • 19
    • 0032492994 scopus 로고    scopus 로고
    • Defective negative regulation of antigen receptor signaling in Lyn-deficient B lymphocytes
    • Chan, V. W. F., C. A. Lowell, and A. L. DeFranco. 1998. Defective negative regulation of antigen receptor signaling in Lyn-deficient B lymphocytes. Curr. Biol. 8:545.
    • (1998) Curr. Biol. , vol.8 , pp. 545
    • Chan, V.W.F.1    Lowell, C.A.2    DeFranco, A.L.3
  • 20
    • 0032055828 scopus 로고    scopus 로고
    • Polygenic autoimmune traits: Lyn, CD22 and SHP-1 are limiting elements of a biochemical pathway regulating BCR signaling and selection
    • Cornall, R. J., J. G. Cyster, M. L. Hibbs, A. R. Dunn, K. L. Otipoby, E. A. Clark, and C. C. Goodnow. 1998. Polygenic autoimmune traits: Lyn, CD22 and SHP-1 are limiting elements of a biochemical pathway regulating BCR signaling and selection. Immunity 8:497.
    • (1998) Immunity , vol.8 , pp. 497
    • Cornall, R.J.1    Cyster, J.G.2    Hibbs, M.L.3    Dunn, A.R.4    Otipoby, K.L.5    Clark, E.A.6    Goodnow, C.C.7
  • 21
    • 0031278336 scopus 로고    scopus 로고
    • B cell antigen receptor-evoked calcium influx is enhanced in CD22-deficient B cell lines
    • Nadler, M. J. S., P. A. McLean, B. G. Neel, and H. H. Wortis. 1997. B cell antigen receptor-evoked calcium influx is enhanced in CD22-deficient B cell lines. J. Immunol. 159:4233.
    • (1997) J. Immunol. , vol.159 , pp. 4233
    • Nadler, M.J.S.1    McLean, P.A.2    Neel, B.G.3    Wortis, H.H.4
  • 23
    • 0024366793 scopus 로고
    • Production of multiple lymphokines by the A20.1 B cell lymphoma after cross-linking of membrane Ig by immobilized anti-Ig
    • Justement, L. B., J. Kreiger, and J. C. Cambier. 1989. Production of multiple lymphokines by the A20.1 B cell lymphoma after cross-linking of membrane Ig by immobilized anti-Ig. J. Immunol. 143:881.
    • (1989) J. Immunol. , vol.143 , pp. 881
    • Justement, L.B.1    Kreiger, J.2    Cambier, J.C.3
  • 24
    • 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.
    • (1991) Cell , vol.66 , pp. 1133
    • Stamenkovic, I.1    Sgroi, D.2    Aruffo, A.3    Sy, M.S.4    Anderson, T.5
  • 25
    • 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. 155:336.
    • (1995) J. Immunol. , vol.155 , pp. 336
    • Law, C.-L.1    Aruffo, A.2    Chandran, K.A.3    Doty, R.T.4    Clark, E.A.5
  • 26
    • 0028337449 scopus 로고
    • Multiple components of the B cell antigen receptor complex associate with the protein tyrosine phosphatase, CD45
    • Brown, V. K., E. W. Ogle, A. L. Burkhardt, R. B. Rowley, J. B. Bolen, and L. B. Justement. 1994. Multiple components of the B cell antigen receptor complex associate with the protein tyrosine phosphatase, CD45. J. Biol. Chem. 269: 17238.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17238
    • Brown, V.K.1    Ogle, E.W.2    Burkhardt, A.L.3    Rowley, R.B.4    Bolen, J.B.5    Justement, L.B.6
  • 28
    • 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.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 1358
    • Peaker, C.J.G.1    Neuberger, M.S.2
  • 29
    • 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. Kehrl. 1997. CD22, a B lymphocyte-specific adhesion molecule that regulates antigen receptor signaling. Annu. Rev. Immunol. 15:481.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 481
    • Tedder, T.F.1    Tuscano, J.2    Sato, S.3    Kehrl, J.H.4
  • 30
    • 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.
    • (1992) Science , vol.258 , pp. 1001
    • Schulte, R.J.1    Campbell, M.A.2    Fischer, W.H.3    Sefton, B.M.4
  • 31
    • 0026447125 scopus 로고
    • Regulation of basal tyrosine phosphorylation of the B cell antigen receptor complex by the protein tyrosine phosphatase, CD45
    • Lin, J., V. K. Brown, and L. B. Justement. 1992. Regulation of basal tyrosine phosphorylation of the B cell antigen receptor complex by the protein tyrosine phosphatase, CD45. J. Immunol. 149:3182.
    • (1992) J. Immunol. , vol.149 , pp. 3182
    • Lin, J.1    Brown, V.K.2    Justement, L.B.3
  • 32
    • 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.
    • (1996) Blood , vol.87 , pp. 4723
    • Tuscano, J.1    Engel, P.2    Tedder, T.F.3    Kehrl, J.H.4
  • 33
    • 0030053270 scopus 로고    scopus 로고
    • lyn kinase and phosphatidyl inositol-3 kinase in signal transduction via the human B lymphocyte antigen CD22
    • lyn kinase and phosphatidyl inositol-3 kinase in signal transduction via the human B lymphocyte antigen CD22. Eur. J. Immunol. 226:1246.
    • (1996) Eur. J. Immunol. , vol.226 , pp. 1246
    • Tuscano, J.M.1    Engel, P.2    Tedder, T.F.3    Agarwal, A.4    Kehrl, J.H.5
  • 34
    • 0025898888 scopus 로고
    • Regulation of B cell antigen receptor signal transduction and phosphorylation by CD45
    • Justement, L. B., K. S. Campbell, N. C. Chien, and J. C. Cambier. 1991. Regulation of B cell antigen receptor signal transduction and phosphorylation by CD45. Science 252:1839.
    • (1991) Science , vol.252 , pp. 1839
    • Justement, L.B.1    Campbell, K.S.2    Chien, N.C.3    Cambier, J.C.4
  • 35
    • 0030297552 scopus 로고    scopus 로고
    • From form to function: Signaling by protein tyrosine phosphatases
    • Tonks, N. K., and B. G. Neel. 1996. From form to function: signaling by protein tyrosine phosphatases. Cell 87:365.
    • (1996) Cell , vol.87 , pp. 365
    • Tonks, N.K.1    Neel, B.G.2
  • 37
    • 0027266773 scopus 로고
    • Ligand-mediated negative regulation of a chimeric transmembrane receptor tyrosine phosphatase
    • Desai, D. M., J. Sap, J. Schlessinger, and A. Weiss. 1993. Ligand-mediated negative regulation of a chimeric transmembrane receptor tyrosine phosphatase. Cell 73:541.
    • (1993) Cell , vol.73 , pp. 541
    • Desai, D.M.1    Sap, J.2    Schlessinger, J.3    Weiss, A.4
  • 38
    • 0032472226 scopus 로고    scopus 로고
    • Dimerization-induced inhibition of receptor protein tyrosine phosphatase function through an inhibitory wedge
    • Majeti, R., A. M. Bilwes, J. P. Noel, T. Hunter, and A. Weiss. 1998. Dimerization-induced inhibition of receptor protein tyrosine phosphatase function through an inhibitory wedge. Science 279:88.
    • (1998) Science , vol.279 , pp. 88
    • Majeti, R.1    Bilwes, A.M.2    Noel, J.P.3    Hunter, T.4    Weiss, A.5
  • 39
    • 0030800121 scopus 로고    scopus 로고
    • The motheaten mutation rescues B cell signaling and development in CD45-deficient mice
    • Pani, G., K. A. Siminovitch, and C. J. Paige. 1997. The motheaten mutation rescues B cell signaling and development in CD45-deficient mice. J. Exp. Med. 186:581.
    • (1997) J. Exp. Med. , vol.186 , pp. 581
    • Pani, G.1    Siminovitch, K.A.2    Paige, C.J.3
  • 40
    • 0027418367 scopus 로고
    • Cross-linking of IgG receptors inhibits membrane immunoglobulin-stimulated calcium influx in B lymphocytes
    • Choquet, D., M. Partiseti, S. Amigorena, C. Bonnerot, W. H. Fridman, and H. Korn. 1993. Cross-linking of IgG receptors inhibits membrane immunoglobulin-stimulated calcium influx in B lymphocytes. J. Cell. Biol. 121:355.
    • (1993) J. Cell. Biol. , vol.121 , pp. 355
    • Choquet, D.1    Partiseti, M.2    Amigorena, S.3    Bonnerot, C.4    Fridman, W.H.5    Korn, H.6
  • 41
    • 0028179403 scopus 로고
    • Cross-linking of Fcγ receptor to surface immunoglobulin on B cells provides an inhibitory signal that closes the plasma membrane calcium channel
    • Diegel, M. L., B. M. Rankin, J. B. Bolen, P. M. Dubois, and P. A. Kiener. 1994. Cross-linking of Fcγ receptor to surface immunoglobulin on B cells provides an inhibitory signal that closes the plasma membrane calcium channel. J. Biol. Chem. 269:11409.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11409
    • Diegel, M.L.1    Rankin, B.M.2    Bolen, J.B.3    Dubois, P.M.4    Kiener, P.A.5
  • 42
    • 0032503687 scopus 로고    scopus 로고
    • PtdIns-3,4,5-P3: A regulatory nexus between tyrosine kinases and sustained calcium signals
    • Scharenberg, A. M., and J.-P. Kinet. 1998. PtdIns-3,4,5-P3: a regulatory nexus between tyrosine kinases and sustained calcium signals. Cell 94:5.
    • (1998) Cell , vol.94 , pp. 5
    • Scharenberg, A.M.1    Kinet, J.-P.2
  • 43
    • 0343307005 scopus 로고    scopus 로고
    • Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling
    • Ono, M., H. Okada, S. Boland, S. Yanagi, T. Kurosaki, and J. V. Ravetch. 1997. Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling. Cell 90:293.
    • (1997) Cell , vol.90 , pp. 293
    • Ono, M.1    Okada, H.2    Boland, S.3    Yanagi, S.4    Kurosaki, T.5    Ravetch, J.V.6
  • 44
    • 0032055485 scopus 로고    scopus 로고
    • SHIP modulates immune receptor responses by regulating membrane association of BTK
    • Bolland, S., R. Pearse, T. Kurosaki, and J. V. Ravetch. 1998. SHIP modulates immune receptor responses by regulating membrane association of BTK. Immunity 8:509.
    • (1998) Immunity , vol.8 , pp. 509
    • Bolland, S.1    Pearse, R.2    Kurosaki, T.3    Ravetch, J.V.4
  • 45
    • 0030840550 scopus 로고    scopus 로고
    • Role of Btk in B cell development and signaling
    • Desiderio, S. 1997. Role of Btk in B cell development and signaling. Curr. Opin. Immunol. 9:534.
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 534
    • Desiderio, S.1
  • 47
    • 0028965645 scopus 로고
    • Potassium and calcium channels in lymphocytes
    • Lewis, R. S., and M. D. Cahalan. 1995. Potassium and calcium channels in lymphocytes. Annu. Rev. Immunol. 13:623.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 623
    • Lewis, R.S.1    Cahalan, M.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.