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Volumn 6, Issue 29, 2015, Pages 27359-27377

LAG3 and PD1 co-inhibitory molecules collaborate to limit CD8+ T cell signaling and dampen antitumor immunity in a murine ovarian cancer model

Author keywords

Antibody blockade; LAG3; Ovarian cancer; PD1; T cell signaling

Indexed keywords

LYMPHOCYTE RECEPTOR; PROGRAMMED DEATH 1 RECEPTOR; PROTEIN LAG3; PROTEIN TYROSINE PHOSPHATASE SHP 1; PROTEIN TYROSINE PHOSPHATASE SHP 2; UNCLASSIFIED DRUG; ANTIBODY; CD223 ANTIGEN; LEUKOCYTE ANTIGEN; PDCD1 PROTEIN, HUMAN; PDCD1 PROTEIN, MOUSE;

EID: 84944474608     PISSN: None     EISSN: 19492553     Source Type: Journal    
DOI: 10.18632/oncotarget.4751     Document Type: Article
Times cited : (263)

References (51)
  • 1
    • 84858766182 scopus 로고    scopus 로고
    • The blockade of immune checkpoints in cancer immunotherapy
    • Pardoll DM. The blockade of immune checkpoints in cancer immunotherapy. Nat Rev Cancer. 2012; 12:252-264.
    • (2012) Nat Rev Cancer. , vol.12 , pp. 252-264
    • Pardoll, D.M.1
  • 4
    • 78449243490 scopus 로고    scopus 로고
    • Anti-CTLA-4 antibody therapy: immune monitoring during clinical development of a novel immunotherapy
    • Callahan MK, Wolchok JD, Allison JP. Anti-CTLA-4 antibody therapy: immune monitoring during clinical development of a novel immunotherapy. Semin Oncol. 2010; 37:473-484.
    • (2010) Semin Oncol. , vol.37 , pp. 473-484
    • Callahan, M.K.1    Wolchok, J.D.2    Allison, J.P.3
  • 9
    • 77749279776 scopus 로고    scopus 로고
    • PD-1 and CTLA-4 combination blockade expands infiltrating T cells and reduces regulatory T and myeloid cells within B16 melanoma tumors
    • Curran MA, Montalvo W, Yagita H, Allison JP. PD-1 and CTLA-4 combination blockade expands infiltrating T cells and reduces regulatory T and myeloid cells within B16 melanoma tumors. Proc Natl Acad Sci U S A. 2010; 107:4275-4280.
    • (2010) Proc Natl Acad Sci U S A. , vol.107 , pp. 4275-4280
    • Curran, M.A.1    Montalvo, W.2    Yagita, H.3    Allison, J.P.4
  • 14
    • 0030009494 scopus 로고    scopus 로고
    • Independent modes of natural killing distinguished in mice lacking Lag3
    • Miyazaki T, Dierich A, Benoist C, Mathis D. Independent modes of natural killing distinguished in mice lacking Lag3. Science. 1996; 272:405-408.
    • (1996) Science. , vol.272 , pp. 405-408
    • Miyazaki, T.1    Dierich, A.2    Benoist, C.3    Mathis, D.4
  • 15
    • 0033180181 scopus 로고    scopus 로고
    • Development of lupus-like autoimmune diseases by disruption of the PD-1 gene encoding an ITIM motif-carrying immunoreceptor
    • Nishimura H, Nose M, Hiai H, Minato N, Honjo T. Development of lupus-like autoimmune diseases by disruption of the PD-1 gene encoding an ITIM motif-carrying immunoreceptor. Immunity. 1999; 11:141-151.
    • (1999) Immunity. , vol.11 , pp. 141-151
    • Nishimura, H.1    Nose, M.2    Hiai, H.3    Minato, N.4    Honjo, T.5
  • 17
    • 0035340798 scopus 로고    scopus 로고
    • CD150 association with either the SH2-containing inositol phosphatase or the SH2-containing protein tyrosine phosphatase is regulated by the adaptor protein SH2D1A
    • Shlapatska LM, Mikhalap SV, Berdova AG, Zelensky OM, Yun TJ, Nichols KE, Clark EA, Sidorenko SP. CD150 association with either the SH2-containing inositol phosphatase or the SH2-containing protein tyrosine phosphatase is regulated by the adaptor protein SH2D1A. J Immunol. 2001; 166:5480-5487.
    • (2001) J Immunol. , vol.166 , pp. 5480-5487
    • Shlapatska, L.M.1    Mikhalap, S.V.2    Berdova, A.G.3    Zelensky, O.M.4    Yun, T.J.5    Nichols, K.E.6    Clark, E.A.7    Sidorenko, S.P.8
  • 18
    • 0037207518 scopus 로고    scopus 로고
    • The dual-function CD150 receptor subfamily: the viral attraction
    • Sidorenko SP, Clark EA. The dual-function CD150 receptor subfamily: the viral attraction. Nat Immunol. 2003; 4:19-24.
    • (2003) Nat Immunol. , vol.4 , pp. 19-24
    • Sidorenko, S.P.1    Clark, E.A.2
  • 21
    • 0032532284 scopus 로고    scopus 로고
    • CD3/TCR complex-associated lymphocyte activation gene-3 molecules inhibit CD3/TCR signaling
    • Hannier S, Tournier M, Bismuth G, Triebel F. CD3/TCR complex-associated lymphocyte activation gene-3 molecules inhibit CD3/TCR signaling. J Immunol. 1998; 161:4058-4065.
    • (1998) J Immunol. , vol.161 , pp. 4058-4065
    • Hannier, S.1    Tournier, M.2    Bismuth, G.3    Triebel, F.4
  • 22
    • 0037111520 scopus 로고    scopus 로고
    • Cutting edge: molecular analysis of the negative regulatory function of lymphocyte activation gene-3
    • Workman CJ, Dugger KJ, Vignali DA. Cutting edge: molecular analysis of the negative regulatory function of lymphocyte activation gene-3. J Immunol. 2002; 169:5392-5395.
    • (2002) J Immunol. , vol.169 , pp. 5392-5395
    • Workman, C.J.1    Dugger, K.J.2    Vignali, D.A.3
  • 23
    • 0038068048 scopus 로고    scopus 로고
    • The CD4-related molecule, LAG-3 (CD223), regulates the expansion of activated T cells
    • Workman CJ, Vignali DA. The CD4-related molecule, LAG-3 (CD223), regulates the expansion of activated T cells. Eur J Immunol. 2003; 33:970-979.
    • (2003) Eur J Immunol. , vol.33 , pp. 970-979
    • Workman, C.J.1    Vignali, D.A.2
  • 24
    • 0030271397 scopus 로고    scopus 로고
    • Cloning of murine LAG-3 by magnetic bead bound homologous probes and PCR (gene-capture PCR)
    • Mastrangeli R, Micangeli E, Donini S. Cloning of murine LAG-3 by magnetic bead bound homologous probes and PCR (gene-capture PCR). Anal Biochem. 1996; 241:93-102.
    • (1996) Anal Biochem. , vol.241 , pp. 93-102
    • Mastrangeli, R.1    Micangeli, E.2    Donini, S.3
  • 25
    • 9144255487 scopus 로고    scopus 로고
    • Biochemical analysis of the regulatory T cell protein lymphocyte activation gene-3 (LAG-3, CD223)
    • Li N, Workman CJ, Martin SM, Vignali DA. Biochemical analysis of the regulatory T cell protein lymphocyte activation gene-3 (LAG-3, CD223). J Immunol. 2004; 173:6806-6812.
    • (2004) J Immunol. , vol.173 , pp. 6806-6812
    • Li, N.1    Workman, C.J.2    Martin, S.M.3    Vignali, D.A.4
  • 26
    • 84907068049 scopus 로고    scopus 로고
    • Trafficking of LAG-3 to the surface on activated T cells via its cytoplasmic domain and protein kinase C signaling
    • Bae J, Lee SJ, Park CG, Lee YS, Chun T. Trafficking of LAG-3 to the surface on activated T cells via its cytoplasmic domain and protein kinase C signaling. J Immunol. 2014; 193:3101-3112.
    • (2014) J Immunol. , vol.193 , pp. 3101-3112
    • Bae, J.1    Lee, S.J.2    Park, C.G.3    Lee, Y.S.4    Chun, T.5
  • 28
    • 36749010774 scopus 로고    scopus 로고
    • Programmed death-1 concentration at the immunological synapse is determined by ligand affinity and availability
    • Pentcheva-Hoang T, Chen L, Pardoll DM, Allison JP. Programmed death-1 concentration at the immunological synapse is determined by ligand affinity and availability. Proc Natl Acad Sci U S A. 2007; 104:17765-17770.
    • (2007) Proc Natl Acad Sci U S A. , vol.104 , pp. 17765-17770
    • Pentcheva-Hoang, T.1    Chen, L.2    Pardoll, D.M.3    Allison, J.P.4
  • 29
    • 4444369694 scopus 로고    scopus 로고
    • B7-1 and B7-2 selectively recruit CTLA-4 and CD28 to the immunological synapse
    • Pentcheva-Hoang T, Egen JG, Wojnoonski K, Allison JP. B7-1 and B7-2 selectively recruit CTLA-4 and CD28 to the immunological synapse. Immunity. 2004; 21:401-413.
    • (2004) Immunity. , vol.21 , pp. 401-413
    • Pentcheva-Hoang, T.1    Egen, J.G.2    Wojnoonski, K.3    Allison, J.P.4
  • 30
    • 19544374904 scopus 로고    scopus 로고
    • The negative regulatory function of the lymphocyte-activation gene-3 co-receptor (CD223) on human T cells
    • Macon-Lemaitre L, Triebel F. The negative regulatory function of the lymphocyte-activation gene-3 co-receptor (CD223) on human T cells. Immunology. 2005; 115:170-178.
    • (2005) Immunology. , vol.115 , pp. 170-178
    • Macon-Lemaitre, L.1    Triebel, F.2
  • 31
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • Monks CR, Freiberg BA, Kupfer H, Sciaky N, Kupfer A. Three-dimensional segregation of supramolecular activation clusters in T cells. Nature. 1998; 395:82-86.
    • (1998) Nature. , vol.395 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 32
    • 0036166541 scopus 로고    scopus 로고
    • Dynamic polarization of the microtubule cytoskeleton during CTL-mediated killing
    • Kuhn JR, Poenie M. Dynamic polarization of the microtubule cytoskeleton during CTL-mediated killing. Immunity. 2002; 16:111-121.
    • (2002) Immunity. , vol.16 , pp. 111-121
    • Kuhn, J.R.1    Poenie, M.2
  • 33
    • 33749185296 scopus 로고    scopus 로고
    • Centrosome polarization delivers secretory granules to the immunological synapse
    • Stinchcombe JC, Majorovits E, Bossi G, Fuller S, Griffiths GM. Centrosome polarization delivers secretory granules to the immunological synapse. Nature. 2006; 443:462-465.
    • (2006) Nature. , vol.443 , pp. 462-465
    • Stinchcombe, J.C.1    Majorovits, E.2    Bossi, G.3    Fuller, S.4    Griffiths, G.M.5
  • 35
    • 0035923535 scopus 로고    scopus 로고
    • PD-1 immunoreceptor inhibits B cell receptor-mediated signaling by recruiting src homology 2-domain-containing tyrosine phosphatase 2 to phosphotyrosine
    • Okazaki T, Maeda A, Nishimura H, Kurosaki T, Honjo T. PD-1 immunoreceptor inhibits B cell receptor-mediated signaling by recruiting src homology 2-domain-containing tyrosine phosphatase 2 to phosphotyrosine. Proc Natl Acad Sci U S A. 2001; 98:13866-13871.
    • (2001) Proc Natl Acad Sci U S A. , vol.98 , pp. 13866-13871
    • Okazaki, T.1    Maeda, A.2    Nishimura, H.3    Kurosaki, T.4    Honjo, T.5
  • 36
    • 3142688997 scopus 로고    scopus 로고
    • SHP-1 and SHP-2 associate with immunoreceptor tyrosine-based switch motif of programmed death 1 upon primary human T cell stimulation, but only receptor ligation prevents T cell activation
    • Chemnitz JM, Parry RV, Nichols KE, June CH, Riley JL. SHP-1 and SHP-2 associate with immunoreceptor tyrosine-based switch motif of programmed death 1 upon primary human T cell stimulation, but only receptor ligation prevents T cell activation. J Immunol. 2004; 173:945-954.
    • (2004) J Immunol. , vol.173 , pp. 945-954
    • Chemnitz, J.M.1    Parry, R.V.2    Nichols, K.E.3    June, C.H.4    Riley, J.L.5
  • 38
    • 0032736718 scopus 로고    scopus 로고
    • The MHC class II ligand lymphocyte activation gene-3 is co-distributed with CD8 and CD3-TCR molecules after their engagement by mAb or peptide-MHC class I complexes
    • Hannier S, Triebel F. The MHC class II ligand lymphocyte activation gene-3 is co-distributed with CD8 and CD3-TCR molecules after their engagement by mAb or peptide-MHC class I complexes. Int Immunol. 1999; 11:1745-1752.
    • (1999) Int Immunol. , vol.11 , pp. 1745-1752
    • Hannier, S.1    Triebel, F.2
  • 39
    • 84893199565 scopus 로고    scopus 로고
    • Combinatorial PD-1 blockade and CD137 activation has therapeutic efficacy in murine cancer models and synergizes with cisplatin
    • Wei H, Zhao L, Li W, Fan K, Qian W, Hou S, Wang H, Dai M, Hellstrom I, Hellstrom KE, Guo Y. Combinatorial PD-1 blockade and CD137 activation has therapeutic efficacy in murine cancer models and synergizes with cisplatin. PLoS One. 2013; 8:e84927.
    • (2013) PLoS One. , vol.8
    • Wei, H.1    Zhao, L.2    Li, W.3    Fan, K.4    Qian, W.5    Hou, S.6    Wang, H.7    Dai, M.8    Hellstrom, I.9    Hellstrom, K.E.10    Guo, Y.11
  • 40
    • 0029844431 scopus 로고    scopus 로고
    • Multiple in vivo phosphorylated tyrosine phosphatase SHP-2 engages binding to Grb2 via tyrosine 584
    • Vogel W, Ullrich A. Multiple in vivo phosphorylated tyrosine phosphatase SHP-2 engages binding to Grb2 via tyrosine 584. Cell Growth Differ. 1996; 7:1589-1597.
    • (1996) Cell Growth Differ. , vol.7 , pp. 1589-1597
    • Vogel, W.1    Ullrich, A.2
  • 41
    • 0027965513 scopus 로고
    • Binding of the Grb2 SH2 domain to phosphotyrosine motifs does not change the affinity of its SH3 domains for Sos proline-rich motifs
    • Cussac D, Frech M, Chardin P. Binding of the Grb2 SH2 domain to phosphotyrosine motifs does not change the affinity of its SH3 domains for Sos proline-rich motifs. Embo J. 1994; 13:4011-4021.
    • (1994) Embo J. , vol.13 , pp. 4011-4021
    • Cussac, D.1    Frech, M.2    Chardin, P.3
  • 42
    • 2142815854 scopus 로고    scopus 로고
    • Lymphocyte activation gene-3 (CD223) regulates the size of the expanding T cell population following antigen activation in vivo
    • Workman CJ, Cauley LS, Kim IJ, Blackman MA, Woodland DL, Vignali DA. Lymphocyte activation gene-3 (CD223) regulates the size of the expanding T cell population following antigen activation in vivo. J Immunol. 2004; 172:5450-5455.
    • (2004) J Immunol. , vol.172 , pp. 5450-5455
    • Workman, C.J.1    Cauley, L.S.2    Kim, I.J.3    Blackman, M.A.4    Woodland, D.L.5    Vignali, D.A.6
  • 43
    • 0141790894 scopus 로고    scopus 로고
    • MHC class II signal transduction in human dendritic cells induced by a natural ligand, the LAG-3 protein (CD223)
    • Andreae S, Buisson S, Triebel F. MHC class II signal transduction in human dendritic cells induced by a natural ligand, the LAG-3 protein (CD223). Blood. 2003; 102:2130-2137.
    • (2003) Blood. , vol.102 , pp. 2130-2137
    • Andreae, S.1    Buisson, S.2    Triebel, F.3
  • 47
    • 0029873311 scopus 로고    scopus 로고
    • LAG-3 is not responsible for selecting T helper cells in CD4-deficient mice
    • Miyazaki T, Dierich A, Benoist C, Mathis D. LAG-3 is not responsible for selecting T helper cells in CD4-deficient mice. Int Immunol. 1996; 8:725-729.
    • (1996) Int Immunol. , vol.8 , pp. 725-729
    • Miyazaki, T.1    Dierich, A.2    Benoist, C.3    Mathis, D.4
  • 50
    • 0023821578 scopus 로고
    • Introduction of soluble protein into the class I pathway of antigen processing and presentation
    • Moore MW, Carbone FR, Bevan MJ. Introduction of soluble protein into the class I pathway of antigen processing and presentation. Cell. 1988; 54:777-785.
    • (1988) Cell. , vol.54 , pp. 777-785
    • Moore, M.W.1    Carbone, F.R.2    Bevan, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.