메뉴 건너뛰기




Volumn 11, Issue 9, 1999, Pages 1411-1422

Defective TCR signaling events in glycosylphosphatidylinositol-deficient T cells derived from paroxysmal nocturnal hemoglobinuria patients

Author keywords

Glycosylphosphatidylinositol; Paroxysmal nocturnal hemoalobinuria; TCR signaling

Indexed keywords

CD4 ANTIGEN; CD8 ANTIGEN; GLYCOSYLPHOSPHATIDYLINOSITOL; MONOCLONAL ANTIBODY CD3; PROTEIN TYROSINE KINASE; T LYMPHOCYTE RECEPTOR;

EID: 0032836138     PISSN: 09538178     EISSN: None     Source Type: Journal    
DOI: 10.1093/intimm/11.9.1411     Document Type: Article
Times cited : (17)

References (45)
  • 1
    • 0028288927 scopus 로고
    • The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction
    • Chan, A. C., Desai, D. M. and Weiss, A. 1994. The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction. Annu. Rev. Immunol. 12:555.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 555
    • Chan, A.C.1    Desai, D.M.2    Weiss, A.3
  • 2
    • 0029874657 scopus 로고    scopus 로고
    • T cell antigen receptor signal transduction pathways
    • Cantrell, D. 1996. T cell antigen receptor signal transduction pathways. Annu. Rev. Immunol. 14:259.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 259
    • Cantrell, D.1
  • 3
    • 0030250114 scopus 로고    scopus 로고
    • Complex complexes: Signaling at the TCR
    • Wange, R. L. and Samelson, L. E. 1996. Complex complexes: signaling at the TCR. Immunity 5:197.
    • (1996) Immunity , vol.5 , pp. 197
    • Wange, R.L.1    Samelson, L.E.2
  • 4
    • 0030250003 scopus 로고    scopus 로고
    • Regulation of cellular signaling by fatty acid acylation and prenylation of signal transduction proteins
    • Resh, M. D. 1996. Regulation of cellular signaling by fatty acid acylation and prenylation of signal transduction proteins. Cell Signal. 8:403.
    • (1996) Cell Signal. , vol.8 , pp. 403
    • Resh, M.D.1
  • 5
    • 0030746106 scopus 로고    scopus 로고
    • S-acylation of Lck protein tyrosine kinase is essential for its signaling function in T lymphocytes
    • Kabouridis, P. S., Magee, A. I. and Ley, S. C. 1997. S-acylation of Lck protein tyrosine kinase is essential for its signaling function in T lymphocytes. EMBO J. 16:4983.
    • (1997) EMBO J. , vol.16 , pp. 4983
    • Kabouridis, P.S.1    Magee, A.I.2    Ley, S.C.3
  • 6
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K. and Ikonen, E. 1997. Functional rafts in cell membranes. Nature 387:569.
    • (1997) Nature , vol.387 , pp. 569
    • Simons, K.1    Ikonen, E.2
  • 7
    • 0031558768 scopus 로고    scopus 로고
    • Structure of detergent-resistant membrane domains: Does phase separation occur in biological membranes?
    • Brown, D. A. and London, E. 1997. Structure of detergent-resistant membrane domains: does phase separation occur in biological membranes? Biochem. Biophys. Res. Commun. 240:1.
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , pp. 1
    • Brown, D.A.1    London, E.2
  • 8
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation
    • Zhang, W., Trible, R. P. and Samelson, L. E. 1998. LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity 9:239.
    • (1998) Immunity , vol.9 , pp. 239
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3
  • 10
    • 0023091209 scopus 로고
    • Pleiotropic loss of activation pathways in a T-cell receptor α-chain deletion variant of a cytolytic T-cell clone
    • Schmitt-Verhulst, A. M., Guimezanes, A., Boyer, C., Poenie, M., Tsien, R., Buferne, M., Hua, C. and Leserman, L 1987. Pleiotropic loss of activation pathways in a T-cell receptor α-chain deletion variant of a cytolytic T-cell clone. Nature 325:628.
    • (1987) Nature , vol.325 , pp. 628
    • Schmitt-Verhulst, A.M.1    Guimezanes, A.2    Boyer, C.3    Poenie, M.4    Tsien, R.5    Buferne, M.6    Hua, C.7    Leserman, L.8
  • 11
    • 0026612411 scopus 로고
    • fyn mutant mice display differential signaling in thymocytes and peripheral T cells
    • fyn mutant mice display differential signaling in thymocytes and peripheral T cells. Cell 70:741.
    • (1992) Cell , vol.70 , pp. 741
    • Stein, P.L.1    Lee, H.M.2    Rich, S.3    Soriano, P.4
  • 12
    • 0029007251 scopus 로고
    • Differential requirement for protein tyrosine kinase Fyn in the functional activation of antigen-specific T lymphocyte clones through the TCR or Thy-1
    • Lancki, D. W., Qian, D., Fields, P., Gajewski, T. and Fitch, F. W. 1995. Differential requirement for protein tyrosine kinase Fyn in the functional activation of antigen-specific T lymphocyte clones through the TCR or Thy-1. J. Immunol. 154:4363.
    • (1995) J. Immunol. , vol.154 , pp. 4363
    • Lancki, D.W.1    Qian, D.2    Fields, P.3    Gajewski, T.4    Fitch, F.W.5
  • 14
    • 0026352248 scopus 로고
    • GPI-anchored cell-surface molecules complexed to protein tyrosine kinases
    • Stefanova, I., Horejsi, V., Ansotegui, I. J., Knapp, W. and Stockinger, H. 1991. GPI-anchored cell-surface molecules complexed to protein tyrosine kinases. Science 254:1016.
    • (1991) Science , vol.254 , pp. 1016
    • Stefanova, I.1    Horejsi, V.2    Ansotegui, I.J.3    Knapp, W.4    Stockinger, H.5
  • 15
    • 0026771308 scopus 로고
    • Differences in activation of normal and glycosylphosphatidylinositol-negative lymphocytes derived from patients with paroxysmal nocturnal hemogiobinuria
    • Schubert, J., Uciechowski, P., Zielinska-Skowronek, M., Tietjen, C., Leo, R. and Schmidt, R. E. 1992. Differences in activation of normal and glycosylphosphatidylinositol-negative lymphocytes derived from patients with paroxysmal nocturnal hemogiobinuria. J. Immunol. 148:3814.
    • (1992) J. Immunol. , vol.148 , pp. 3814
    • Schubert, J.1    Uciechowski, P.2    Zielinska-Skowronek, M.3    Tietjen, C.4    Leo, R.5    Schmidt, R.E.6
  • 16
    • 0028835072 scopus 로고
    • Glycosylphosphatidylinositol (GPI)-anchored surface antigens in the allogeneic activation of T cells
    • Schubert, J., Stroehmann, A., Scholz, C. and Schmidt, R. E. 1995. Glycosylphosphatidylinositol (GPI)-anchored surface antigens in the allogeneic activation of T cells. Clin. Exp. Immunol 102:199.
    • (1995) Clin. Exp. Immunol , vol.102 , pp. 199
    • Schubert, J.1    Stroehmann, A.2    Scholz, C.3    Schmidt, R.E.4
  • 17
    • 0024284098 scopus 로고
    • TAP transcription and phosphatidylinositol linkage mutants are defective in activation through the T cell receptor
    • Yeh, E. T. H., Reiser, H., Bamezai, A. and Rock, K. L. 1988. TAP transcription and phosphatidylinositol linkage mutants are defective in activation through the T cell receptor. Cell 52:665.
    • (1988) Cell , vol.52 , pp. 665
    • Yeh, E.T.H.1    Reiser, H.2    Bamezai, A.3    Rock, K.L.4
  • 18
    • 0031570462 scopus 로고    scopus 로고
    • Phosphatidylinositol-based glycolipid-anchored proteins enhance proximal TCR signaling events
    • Romagnoli, P. and Bron, C. 1997. Phosphatidylinositol-based glycolipid-anchored proteins enhance proximal TCR signaling events. J. Immunol. 158:5757.
    • (1997) J. Immunol. , vol.158 , pp. 5757
    • Romagnoli, P.1    Bron, C.2
  • 19
    • 0027310539 scopus 로고
    • Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria
    • Takeda, J., Miyata, T., Kawagoe, K., Iida, Y., Endo, Y., Fujita, T., Takahashi, M., Kitani, T., and Kinoshita, T. 1993. Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria. Cell 73:703.
    • (1993) Cell , vol.73 , pp. 703
    • Takeda, J.1    Miyata, T.2    Kawagoe, K.3    Iida, Y.4    Endo, Y.5    Fujita, T.6    Takahashi, M.7    Kitani, T.8    Kinoshita, T.9
  • 20
    • 0027963158 scopus 로고
    • Developmental regulation of the TCR-zeta chain. Differential expression and tyrosine phosphorylation of the TCR-zeta chain in resting immature and mature T lymphocytes
    • Rozdial, M. M., Kubo, R. T., Turner, S. L. and Finkel, T. H. 1994. Developmental regulation of the TCR-zeta chain. Differential expression and tyrosine phosphorylation of the TCR-zeta chain in resting immature and mature T lymphocytes. J. Immunol. 153:1563.
    • (1994) J. Immunol. , vol.153 , pp. 1563
    • Rozdial, M.M.1    Kubo, R.T.2    Turner, S.L.3    Finkel, T.H.4
  • 22
    • 0024448771 scopus 로고
    • The role of CD2/LFA-3 interaction in antigen- and mitogen-induced activation of human T cells
    • Tiefenthaler, G. and Hunig, T. 1989. The role of CD2/LFA-3 interaction in antigen- and mitogen-induced activation of human T cells. Int. Immunol. 1:169.
    • (1989) Int. Immunol. , vol.1 , pp. 169
    • Tiefenthaler, G.1    Hunig, T.2
  • 24
    • 0028979704 scopus 로고
    • Rapid turnover of the CD3 zeta chain independent of the TCR-D3 complex in normal T cells
    • Ono, S., Ohno, H. and Saito, T. 1995. Rapid turnover of the CD3 zeta chain independent of the TCR-D3 complex in normal T cells. Immunity 2:639.
    • (1995) Immunity , vol.2 , pp. 639
    • Ono, S.1    Ohno, H.2    Saito, T.3
  • 27
    • 0028797801 scopus 로고
    • CD8 modulation of T-cell antigen receptor-ligand interactions on living cytotoxic T lymphocytes
    • Luescher, I. F., Vivier, E., Layer, A., Mahiou, J., Godeau, F., Malissen, B. and Romero, P. 1995. CD8 modulation of T-cell antigen receptor-ligand interactions on living cytotoxic T lymphocytes. Nature 373:353.
    • (1995) Nature , vol.373 , pp. 353
    • Luescher, I.F.1    Vivier, E.2    Layer, A.3    Mahiou, J.4    Godeau, F.5    Malissen, B.6    Romero, P.7
  • 28
    • 0031048822 scopus 로고    scopus 로고
    • The efficiency of CD4 recruitment to ligand-engaged TCR controls the agonist/partial agonist properties of peptide-MHC molecule ligands
    • Madrenas, J., Chau, L. A., Smith, J., Bluestone, J. A. and Germain, R. N. 1997. The efficiency of CD4 recruitment to ligand-engaged TCR controls the agonist/partial agonist properties of peptide-MHC molecule ligands. J. Exp. Med. 185:219.
    • (1997) J. Exp. Med. , vol.185 , pp. 219
    • Madrenas, J.1    Chau, L.A.2    Smith, J.3    Bluestone, J.A.4    Germain, R.N.5
  • 29
    • 0027389272 scopus 로고
    • CD45 specifically modulates binding of Lck to a phosphopeptide encompassing the negative regulatory tyrosine of Lck
    • Sieh, M., Bolen, J. B. and Weiss, A. 1993. CD45 specifically modulates binding of Lck to a phosphopeptide encompassing the negative regulatory tyrosine of Lck. EMBO J. 12:315.
    • (1993) EMBO J. , vol.12 , pp. 315
    • Sieh, M.1    Bolen, J.B.2    Weiss, A.3
  • 30
    • 0028279060 scopus 로고
    • Distinct intracellular localization of Lck and Fyn protein tyrosine kinases in human T lymphocytes
    • Ley, S. C., Marsh, M., Bebbington, C. R., Proudfoot, K. and Jordan, P. 1994, Distinct intracellular localization of Lck and Fyn protein tyrosine kinases in human T lymphocytes. J. Cell Biol. 125:639.
    • (1994) J. Cell Biol. , vol.125 , pp. 639
    • Ley, S.C.1    Marsh, M.2    Bebbington, C.R.3    Proudfoot, K.4    Jordan, P.5
  • 31
    • 0029866039 scopus 로고    scopus 로고
    • Lck regulates the tyrosine phosphorylation of the T cell receptor subunits and ZAP-70 in murine thymocytes
    • van Oers, N. S. C., Killeen, N. and Weiss, A. 1996. Lck regulates the tyrosine phosphorylation of the T cell receptor subunits and ZAP-70 in murine thymocytes. J. Exp. Med. 183:1053.
    • (1996) J. Exp. Med. , vol.183 , pp. 1053
    • Van Oers, N.S.C.1    Killeen, N.2    Weiss, A.3
  • 32
    • 0024802918 scopus 로고
    • lck is hyperphosphorylated on serine and tyrosine residues within minutes after activation via T cell receptor or CD2
    • lck is hyperphosphorylated on serine and tyrosine residues within minutes after activation via T cell receptor or CD2. Eur. J. Immunol. 19:2183.
    • (1989) Eur. J. Immunol. , vol.19 , pp. 2183
    • Danielian, S.1    Fagard, R.2    Alcover, A.3    Acuto, O.4    Fisher, S.5
  • 33
    • 0030812812 scopus 로고    scopus 로고
    • Maintenance of human T cell anergy: Blocking of IL-2 gene transcription by activated Rap-1
    • Boussiotis, V. A., Freeman, G. J., Berezovskaya, A., Barber, D. L. and Nadler, L. M. 1997. Maintenance of human T cell anergy: blocking of IL-2 gene transcription by activated Rap-1. Science 278:124.
    • (1997) Science , vol.278 , pp. 124
    • Boussiotis, V.A.1    Freeman, G.J.2    Berezovskaya, A.3    Barber, D.L.4    Nadler, L.M.5
  • 34
    • 0029037210 scopus 로고
    • Serial triggering of many T-cell receptors by a few peptide-MHC complexes
    • Valitutti, S., Muller, S., Cella, M., Radovan, E. and Lanzavecchia, A. 1995. Serial triggering of many T-cell receptors by a few peptide-MHC complexes. Nature 375:148.
    • (1995) Nature , vol.375 , pp. 148
    • Valitutti, S.1    Muller, S.2    Cella, M.3    Radovan, E.4    Lanzavecchia, A.5
  • 36
    • 0027970448 scopus 로고
    • Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae
    • Fra, A. M., Williamson, E., Simons, K. and Parton, R. G. 1994. Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae. J. Biol. Chem. 269:30745.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30745
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 37
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • Xavier, R., Brennan, T., Li, Q., McCormack, C. and Seed, B. 1998. Membrane compartmentation is required for efficient T cell activation. Immunity 8:723.
    • (1998) Immunity , vol.8 , pp. 723
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 39
    • 0028175989 scopus 로고
    • Cysteine3 of Src family protein tyrosine kinases determines palmitoylation and localization in caveolae
    • Shenoy-Scaria, A. M., Dietzen, D. J., Kwong, J., Link, D. C. and Lublin, D. M. 1994. Cysteine3 of Src family protein tyrosine kinases determines palmitoylation and localization in caveolae. J. Cell Biol. 126:353.
    • (1994) J. Cell Biol. , vol.126 , pp. 353
    • Shenoy-Scaria, A.M.1    Dietzen, D.J.2    Kwong, J.3    Link, D.C.4    Lublin, D.M.5
  • 40
    • 0029956855 scopus 로고    scopus 로고
    • Novel determinants of H-Ras plasma membrane localization and transformation
    • Willumsen, B. M., Cox, A. D., Solski, P. A., Der, C. J. and Buss, J. E. 1996. Novel determinants of H-Ras plasma membrane localization and transformation. Oncogene 13:1901.
    • (1996) Oncogene , vol.13 , pp. 1901
    • Willumsen, B.M.1    Cox, A.D.2    Solski, P.A.3    Der, C.J.4    Buss, J.E.5
  • 41
    • 0026637568 scopus 로고
    • Glycosyl-phosphatidylinositol anchoring of membrane proteins
    • Lublin, D. M. 1992. Glycosyl-phosphatidylinositol anchoring of membrane proteins. Curr. Top. Microbiol. Immunol. 178:141.
    • (1992) Curr. Top. Microbiol. Immunol. , vol.178 , pp. 141
    • Lublin, D.M.1
  • 42
    • 0030453582 scopus 로고    scopus 로고
    • Exclusion of CD45 inhibits activity of p56lck associated with the glycolipid-enriched membrane domains
    • Rodgers, W. and Rose, J. K. 1996. Exclusion of CD45 inhibits activity of p56lck associated with the glycolipid-enriched membrane domains. J. Cell Biol. 135:1515.
    • (1996) J. Cell Biol. , vol.135 , pp. 1515
    • Rodgers, W.1    Rose, J.K.2
  • 43
    • 0026662674 scopus 로고
    • The nature of large noncovalent complexes containing glycosylphosphatidylinositol-anchored membrane glycoproteins and protein tyrosine kinases
    • Cinek, T. and Horejsi, V. 1992. The nature of large noncovalent complexes containing glycosylphosphatidylinositol-anchored membrane glycoproteins and protein tyrosine kinases. J. Immunol. 149:2262.
    • (1992) J. Immunol. , vol.149 , pp. 2262
    • Cinek, T.1    Horejsi, V.2
  • 45
    • 0029082412 scopus 로고
    • Separation of caveolae from associated microdomains of GPI-anchored proteins
    • Schnitzer, J. E., McIntosh, D. P., Dvorak, A. M., Liu, J. and Oh, P. 1995. Separation of caveolae from associated microdomains of GPI-anchored proteins. Science 269:1435.
    • (1995) Science , vol.269 , pp. 1435
    • Schnitzer, J.E.1    McIntosh, D.P.2    Dvorak, A.M.3    Liu, J.4    Oh, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.