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Volumn 434, Issue 1, 2011, Pages 153-160

Galectin-8 tandem-repeat structure is essential for T-cell proliferation but not for co-stimulation

Author keywords

Galectin alternative inhibitor; Glycan binding; Lattice formation; T cell activation

Indexed keywords

3 O BETA DEXTRO GALACTOPYRANOSYL DEXTRO ARABINOSE; GALECTIN 8; LACTOSE; PHYTOHEMAGGLUTININ; PROTEIN INHIBITOR; THIODIGALACTOSIDE; UNCLASSIFIED DRUG;

EID: 79251546715     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20101691     Document Type: Article
Times cited : (40)

References (37)
  • 1
  • 2
    • 75749101401 scopus 로고    scopus 로고
    • Galectins: Regulators of acute and chronic inflammation
    • Liu, F. T. and Rabinovich, G. A. (2010) Galectins: regulators of acute and chronic inflammation. Ann. N.Y. Acad. Sci. 1183, 158-182
    • (2010) Ann. N.Y. Acad. Sci. , vol.1183 , pp. 158-182
    • Liu, F.T.1    Rabinovich, G.A.2
  • 4
    • 67650708852 scopus 로고    scopus 로고
    • Endogenous galectins and the control of the host inflammatory response
    • Norling, L. V., Perretti, M. and Cooper, D. (2009) Endogenous galectins and the control of the host inflammatory response. J. Endocrinol. 201, 169-184
    • (2009) J. Endocrinol. , vol.201 , pp. 169-184
    • Norling, L.V.1    Perretti, M.2    Cooper, D.3
  • 5
    • 67349258025 scopus 로고    scopus 로고
    • Turning 'sweet' on immunity: Galectin-glycan interactions in immune tolerance and inflammation
    • Rabinovich, G. A. and Toscano, M. A. (2009) Turning 'sweet' on immunity: galectin-glycan interactions in immune tolerance and inflammation. Nat. Rev. Immunol. 9, 338-352
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 338-352
    • Rabinovich, G.A.1    Toscano, M.A.2
  • 7
    • 0029900759 scopus 로고    scopus 로고
    • Surface-epitope masking and expression cloning identifies the human prostate carcinoma tumor antigen gene PCTA-1 a member of the galectin gene family
    • Su, Z. Z., Lin, J., Shen, R., Fisher, P. E., Goldstein, N. I. and Fisher, P. B. (1996) Surface-epitope masking and expression cloning identifies the human prostate carcinoma tumor antigen gene PCTA-1 a member of the galectin gene family. Proc. Natl. Acad. Sci. U.S.A. 93, 7252-7257
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 7252-7257
    • Su, Z.Z.1    Lin, J.2    Shen, R.3    Fisher, P.E.4    Goldstein, N.I.5    Fisher, P.B.6
  • 9
    • 0035934234 scopus 로고    scopus 로고
    • Two messenger RNAs and five isoforms for Po66-CBP, a galectin-8 homolog in a human lung carcinoma cell line
    • DOI 10.1016/S0378-1119(01)00598-4, PII S0378111901005984
    • Bidon, N., Brichory, F., Hanash, S., Bourguet, P., Dazord, L. and Le Pennec, J. P. (2001) Two messenger RNAs and five isoforms for Po66-CBP, a galectin-8 homolog in a human lung carcinoma cell line. Gene 274, 253-262 (Pubitemid 32817143)
    • (2001) Gene , vol.274 , Issue.1-2 , pp. 253-262
    • Bidon, N.1    Brichory, F.2    Hanash, S.3    Bourguet, P.4    Dazord, L.5    Le, P.J.-P.6
  • 10
    • 0035194504 scopus 로고    scopus 로고
    • Galectins are differentially expressed in supratentorial pilocytic astrocytomas, astrocytomas, anaplastic astrocytomas and glioblastomas, and significantly modulate tumor astrocyte migration
    • Camby, I., Belot, N., Rorive, S., Lefranc, F., Maurage, C. A., Lahm, H., Kaltner, H., Hadari, Y., Ruchoux, M. M., Brotchi, J. et al. (2001) Galectins are differentially expressed in supratentorial pilocytic astrocytomas, astrocytomas, anaplastic astrocytomas and glioblastomas, and significantly modulate tumor astrocyte migration. Brain Pathol. 11, 12-26
    • (2001) Brain Pathol. , vol.11 , pp. 12-26
    • Camby, I.1    Belot, N.2    Rorive, S.3    Lefranc, F.4    Maurage, C.A.5    Lahm, H.6    Kaltner, H.7    Hadari, Y.8    Ruchoux, M.M.9    Brotchi, J.10
  • 14
    • 0242287981 scopus 로고    scopus 로고
    • The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity
    • DOI 10.1093/glycob/cwg094
    • Ideo, H., Seko, A., Ishizuka, I. and Yamashita, K. (2003) The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity. Glycobiology 13, 713-723 (Pubitemid 37337052)
    • (2003) Glycobiology , vol.13 , Issue.10 , pp. 713-723
    • Ideo, H.1    Seko, A.2    Ishizuka, I.3    Yamashita, K.4
  • 15
    • 33645102970 scopus 로고    scopus 로고
    • Complex N-glycans are the major ligands for galectin-1, -3, and -8 on Chinese hamster ovary cells
    • Patnaik, S. K., Potvin, B., Carlsson, S., Sturm, D., Leffler, H. and Stanley, P. (2006) Complex N-glycans are the major ligands for galectin-1, -3, and -8 on Chinese hamster ovary cells. Glycobiology 16, 305-317
    • (2006) Glycobiology , vol.16 , pp. 305-317
    • Patnaik, S.K.1    Potvin, B.2    Carlsson, S.3    Sturm, D.4    Leffler, H.5    Stanley, P.6
  • 17
    • 50649125265 scopus 로고    scopus 로고
    • Dimeric galectin-8 induces phosphatidylserine exposure in leukocytes through polylactosamine recognition by the carboxyl terminal domain
    • Stowell, S. R., Arthur, C. M., Slanina, K. A., Horton, J. R., Smith, D. F. and Cummings, R. D. (2008) Dimeric galectin-8 induces phosphatidylserine exposure in leukocytes through polylactosamine recognition by the carboxyl terminal domain. J. Biol. Chem. 283, 20547-20559
    • (2008) J. Biol. Chem. , vol.283 , pp. 20547-20559
    • Stowell, S.R.1    Arthur, C.M.2    Slanina, K.A.3    Horton, J.R.4    Smith, D.F.5    Cummings, R.D.6
  • 19
    • 33646882385 scopus 로고    scopus 로고
    • It depends on the hinge: A structure-functional analysis of galectin-8, a tandem-repeat type lectin
    • Levy, Y., Auslender, S., Eisenstein, M., Vidavski, R. R., Ronen, D., Bershadsky, A. D. and Zick, Y. (2006) It depends on the hinge: a structure-functional analysis of galectin-8, a tandem-repeat type lectin. Glycobiology 16, 463-476
    • (2006) Glycobiology , vol.16 , pp. 463-476
    • Levy, Y.1    Auslender, S.2    Eisenstein, M.3    Vidavski, R.R.4    Ronen, D.5    Bershadsky, A.D.6    Zick, Y.7
  • 25
    • 0033215424 scopus 로고    scopus 로고
    • Restricted receptor segregation into membrane microdomains occurs on human T cells during apoptosis induced by galectin-1
    • Pace, K. E., Lee, C., Stewart, P. L. and Baum, L. G. (1999) Restricted receptor segregation into membrane microdomains occurs on human T cells during apoptosis induced by galectin-1. J. Immunol. 163, 3801-3811
    • (1999) J. Immunol. , vol.163 , pp. 3801-3811
    • Pace, K.E.1    Lee, C.2    Stewart, P.L.3    Baum, L.G.4
  • 26
    • 67649794824 scopus 로고    scopus 로고
    • Galectin-8 induces apoptosis in Jurkat T cells by phosphatidic acid-mediated ERK1/2 activation supported by protein kinase A down-regulation
    • Norambuena, A., Metz, C., Vicuna, L., Silva, A., Pardo, E., Oyanadel, C., Massardo, L., Gonzalez, A. and Soza, A. (2009) Galectin-8 induces apoptosis in Jurkat T cells by phosphatidic acid-mediated ERK1/2 activation supported by protein kinase A down-regulation. J. Biol. Chem. 284, 12670-12679
    • (2009) J. Biol. Chem. , vol.284 , pp. 12670-12679
    • Norambuena, A.1    Metz, C.2    Vicuna, L.3    Silva, A.4    Pardo, E.5    Oyanadel, C.6    Massardo, L.7    Gonzalez, A.8    Soza, A.9
  • 28
    • 40549093937 scopus 로고    scopus 로고
    • Induction of cell adhesion by galectin-8 and its target molecules in Jurkat T-cells
    • Yamamoto, H., Nishi, N., Shoji, H., Itoh, A., Lu, L. H., Hirashima, M. and Nakamura, T. (2008) Induction of cell adhesion by galectin-8 and its target molecules in Jurkat T-cells. J. Biochem. 143, 311-324
    • (2008) J. Biochem. , vol.143 , pp. 311-324
    • Yamamoto, H.1    Nishi, N.2    Shoji, H.3    Itoh, A.4    Lu, L.H.5    Hirashima, M.6    Nakamura, T.7
  • 30
    • 79251589403 scopus 로고    scopus 로고
    • Galectin multimerization and lattice formation is regulated by linker region structure
    • Earl, L. A., Bi, S. and Baum, L. G. (2011) Galectin multimerization and lattice formation is regulated by linker region structure. Glycobiology 21, 6-12
    • (2011) Glycobiology , vol.21 , pp. 6-12
    • Earl, L.A.1    Bi, S.2    Baum, L.G.3
  • 31
    • 0036816147 scopus 로고    scopus 로고
    • Clusters, bundles, arrays and lattices: Novel mechanisms for lectin-saccharide-mediated cellular interactions
    • Brewer, C. F., Miceli, M. C. and Baum, L. G. (2002) Clusters, bundles, arrays and lattices: novel mechanisms for lectin-saccharide-mediated cellular interactions. Curr. Opin. Struct. Biol. 12, 616-623
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 616-623
    • Brewer, C.F.1    Miceli, M.C.2    Baum, L.G.3
  • 32
    • 36849040950 scopus 로고    scopus 로고
    • Lateral compartmentalization of T cell receptor versus CD45 by galectin-N-glycan binding and microfilaments coordinate basal and activation signaling
    • Chen, I. J., Chen, H. L. and Demetriou, M. (2007) Lateral compartmentalization of T cell receptor versus CD45 by galectin-N-glycan binding and microfilaments coordinate basal and activation signaling. J. Biol. Chem. 282, 35361-35372
    • (2007) J. Biol. Chem. , vol.282 , pp. 35361-35372
    • Chen, I.J.1    Chen, H.L.2    Demetriou, M.3
  • 34
    • 11144293485 scopus 로고    scopus 로고
    • The trans-sialidase from Trypanosoma cruzi induces thrombocytopenia during acute Chagas' disease by reducing the platelet sialic acid contents
    • Tribulatti, M. V., Mucci, J., Van Rooijen, N., Leguizamón, M. S. and Campetella, O. (2005) The trans-sialidase from Trypanosoma cruzi induces thrombocytopenia during acute Chagas' disease by reducing the platelet sialic acid contents. Infect. Immun. 73, 201-207
    • (2005) Infect. Immun. , vol.73 , pp. 201-207
    • Tribulatti, M.V.1    Mucci, J.2    Van Rooijen, N.3    Leguizamón, M.S.4    Campetella, O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.