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Volumn 253, Issue 1, 2007, Pages 25-33

Galectins - Potential targets for cancer therapy

Author keywords

Cancer; Detection; Galectins; Glycoconjugates; Inhibition; Metastasis; Therapy

Indexed keywords

CISPLATIN; CYCLOPHOSPHAMIDE; GALECTIN; GLYCOCONJUGATE; PECTIN; STAUROSPORINE;

EID: 34249978481     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.canlet.2006.11.030     Document Type: Review
Times cited : (63)

References (112)
  • 1
    • 0023710284 scopus 로고
    • Two distinct classes of carbohydrate-recognition domains in animal lectins
    • Drickamer K. Two distinct classes of carbohydrate-recognition domains in animal lectins. J. Biol. Chem. 263 (1988) 9557-9560
    • (1988) J. Biol. Chem. , vol.263 , pp. 9557-9560
    • Drickamer, K.1
  • 2
    • 0024414280 scopus 로고
    • Lectins as cell recognition molecules
    • Sharon N., and Lis H. Lectins as cell recognition molecules. Science 246 (1989) 227-234
    • (1989) Science , vol.246 , pp. 227-234
    • Sharon, N.1    Lis, H.2
  • 4
    • 0041289900 scopus 로고
    • A f3-d-galactoside binding protein from electric organ tissue of electrophorus electricus
    • Teichberg V.I., Silman I., Beitsch D.D., and Resheff G. A f3-d-galactoside binding protein from electric organ tissue of electrophorus electricus. Proc. Natl. Acad. Sci. USA 72 (1975) 1383-1387
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 1383-1387
    • Teichberg, V.I.1    Silman, I.2    Beitsch, D.D.3    Resheff, G.4
  • 6
    • 0027965708 scopus 로고
    • Galectins: structure and function of a large family of animal lectins
    • Barondes S.H., Cooper D.N.W., Gitt M.A., and Leffler H. Galectins: structure and function of a large family of animal lectins. J. Biol. Chem. 269 (1994) 20807-20810
    • (1994) J. Biol. Chem. , vol.269 , pp. 20807-20810
    • Barondes, S.H.1    Cooper, D.N.W.2    Gitt, M.A.3    Leffler, H.4
  • 7
    • 0021205057 scopus 로고
    • Human placenta β-galactoside-binding lectin. Purification and some properties
    • Hirabayashi J., and Kasai K. Human placenta β-galactoside-binding lectin. Purification and some properties. Biochem. Biophys. Res. Commun. 122 (1984) 938-944
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 938-944
    • Hirabayashi, J.1    Kasai, K.2
  • 8
    • 0032875554 scopus 로고    scopus 로고
    • God must love galectins: he made so many of them
    • Cooper D.N.W., and Barondes S.H. God must love galectins: he made so many of them. Glycobiology 9 (1999) 979-984
    • (1999) Glycobiology , vol.9 , pp. 979-984
    • Cooper, D.N.W.1    Barondes, S.H.2
  • 9
    • 0027958144 scopus 로고
    • Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein
    • Liao D.I., Kapadia G., Ahmed H., Vasta G.R., and Herzberg O. Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein. Proc. Natl. Acad. Sci. USA 91 (1994) 1428-1432
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1428-1432
    • Liao, D.I.1    Kapadia, G.2    Ahmed, H.3    Vasta, G.R.4    Herzberg, O.5
  • 10
    • 0027169990 scopus 로고
    • The family of metazoan metal-independent β-galactoside binding lectins: structure, function and molecular evolution
    • Hirabayashi J., and Kasai K. The family of metazoan metal-independent β-galactoside binding lectins: structure, function and molecular evolution. Glycobiology 3 (1993) 297-304
    • (1993) Glycobiology , vol.3 , pp. 297-304
    • Hirabayashi, J.1    Kasai, K.2
  • 11
    • 17544373394 scopus 로고    scopus 로고
    • New roles for galectins in brain tumors-from prognostic markers to therapeutic targets
    • Stillman B.N., Mischel P.S., and Baum L.G. New roles for galectins in brain tumors-from prognostic markers to therapeutic targets. Brain Pathol. 15 (2005) 124-132
    • (2005) Brain Pathol. , vol.15 , pp. 124-132
    • Stillman, B.N.1    Mischel, P.S.2    Baum, L.G.3
  • 12
    • 0026089105 scopus 로고
    • Genomic sequence and organization of two members of a human lectin gene family
    • Gitt M.A., and Barondes S.H. Genomic sequence and organization of two members of a human lectin gene family. Biochemistry 30 (1991) 82-89
    • (1991) Biochemistry , vol.30 , pp. 82-89
    • Gitt, M.A.1    Barondes, S.H.2
  • 13
    • 0026768317 scopus 로고
    • Isolation and expression of a gene encoding L-14-II, a new human soluble lactose-binding lectin
    • Gitt M.A., Massa S.M., Leffler H., and Barondes S.H. Isolation and expression of a gene encoding L-14-II, a new human soluble lactose-binding lectin. J. Biol. Chem. 267 (1992) 10601-10606
    • (1992) J. Biol. Chem. , vol.267 , pp. 10601-10606
    • Gitt, M.A.1    Massa, S.M.2    Leffler, H.3    Barondes, S.H.4
  • 15
    • 0028923675 scopus 로고
    • Galectin-7, a human 14-kDa S-lectin, specifically expressed in keratinocytes and sensitive to retinoic acid
    • Magnaldo T., Bernerd F., and Darmon M. Galectin-7, a human 14-kDa S-lectin, specifically expressed in keratinocytes and sensitive to retinoic acid. Dev. Biol. 168 (1995) 259-271
    • (1995) Dev. Biol. , vol.168 , pp. 259-271
    • Magnaldo, T.1    Bernerd, F.2    Darmon, M.3
  • 16
    • 0030023715 scopus 로고    scopus 로고
    • Purification and molecular characterization of a novel 16-kDa galectin from the nematode Caenorhabditis elegans
    • Hirabayashi J., Ubukata T., and Kasai K. Purification and molecular characterization of a novel 16-kDa galectin from the nematode Caenorhabditis elegans. J. Biol. Chem. 271 (1996) 2497-2505
    • (1996) J. Biol. Chem. , vol.271 , pp. 2497-2505
    • Hirabayashi, J.1    Ubukata, T.2    Kasai, K.3
  • 17
    • 0031476218 scopus 로고    scopus 로고
    • Galectins from amphibian species: carbohydrate specificity, molecular structure and evolution
    • Vasta G.R., Ahmed H., Amzel L.M., and Bianchet M.A. Galectins from amphibian species: carbohydrate specificity, molecular structure and evolution. Trends Glycosci. Glycotechnol. 9 (1997) 131-144
    • (1997) Trends Glycosci. Glycotechnol. , vol.9 , pp. 131-144
    • Vasta, G.R.1    Ahmed, H.2    Amzel, L.M.3    Bianchet, M.A.4
  • 20
    • 0025642403 scopus 로고
    • Structure of chicken 16-kDa β-galactoside-binding lectin: complete amino acid sequence, cloning of cDNA and production
    • Sakakura Y., Hirabayashi J., Oda Y., Ohyama Y., and Kasai K. Structure of chicken 16-kDa β-galactoside-binding lectin: complete amino acid sequence, cloning of cDNA and production. J. Biol. Chem. 265 (1990) 21573-21579
    • (1990) J. Biol. Chem. , vol.265 , pp. 21573-21579
    • Sakakura, Y.1    Hirabayashi, J.2    Oda, Y.3    Ohyama, Y.4    Kasai, K.5
  • 23
    • 0028047113 scopus 로고
    • Mac-2: a versatile galactose-binding protein of mammalian tissues
    • Hughes R.C. Mac-2: a versatile galactose-binding protein of mammalian tissues. Glycobiology 4 (1994) 5-12
    • (1994) Glycobiology , vol.4 , pp. 5-12
    • Hughes, R.C.1
  • 24
    • 0027457991 scopus 로고
    • Soluble lactose-binding lectin from rat intestine with two different carbohydrate-binding domains in the same chain
    • Oda Y., Herrmann J., Gitt M.A., Turck C.W., Burlingame A.L., Barondes S.H., and Leffler H. Soluble lactose-binding lectin from rat intestine with two different carbohydrate-binding domains in the same chain. J. Biol. Chem. 268 (1993) 5929-5939
    • (1993) J. Biol. Chem. , vol.268 , pp. 5929-5939
    • Oda, Y.1    Herrmann, J.2    Gitt, M.A.3    Turck, C.W.4    Burlingame, A.L.5    Barondes, S.H.6    Leffler, H.7
  • 25
    • 0032579502 scopus 로고    scopus 로고
    • Galectin-4 and galectin-6 are two closely related lectins expressed in mouse gastrointestinal tract
    • Gitt M.A., Colnot C., Poirier F., Nani K.J., Barondes S.H., and Leffler H. Galectin-4 and galectin-6 are two closely related lectins expressed in mouse gastrointestinal tract. J. Biol. Chem. 273 (1998) 2954-2960
    • (1998) J. Biol. Chem. , vol.273 , pp. 2954-2960
    • Gitt, M.A.1    Colnot, C.2    Poirier, F.3    Nani, K.J.4    Barondes, S.H.5    Leffler, H.6
  • 27
    • 0042291641 scopus 로고    scopus 로고
    • Molecular definition of a novel human galectin which is immunogenic in patients with Hodgkin's disease
    • Tureci O., Schmitt H., Fadle N., Pfreundschuh M., and Sahin U. Molecular definition of a novel human galectin which is immunogenic in patients with Hodgkin's disease. J. Biol. Chem. 272 (1997) 6416-6422
    • (1997) J. Biol. Chem. , vol.272 , pp. 6416-6422
    • Tureci, O.1    Schmitt, H.2    Fadle, N.3    Pfreundschuh, M.4    Sahin, U.5
  • 28
    • 0031500199 scopus 로고    scopus 로고
    • Galectin-1: secretion and modulation of cell interactions with laminin
    • Cooper D.N.W. Galectin-1: secretion and modulation of cell interactions with laminin. Trends Glycosci. Glycotechnol. 9 (1997) 57-67
    • (1997) Trends Glycosci. Glycotechnol. , vol.9 , pp. 57-67
    • Cooper, D.N.W.1
  • 29
    • 0026079139 scopus 로고
    • Identification of an autocrine negative growth factor: mouse β-galactoside-binding protein is a cytostatic factor and cell growth regulator
    • Wells V., and Mallucci L. Identification of an autocrine negative growth factor: mouse β-galactoside-binding protein is a cytostatic factor and cell growth regulator. Cell 64 (1991) 91-97
    • (1991) Cell , vol.64 , pp. 91-97
    • Wells, V.1    Mallucci, L.2
  • 30
    • 0030582135 scopus 로고    scopus 로고
    • Biphasic modulation of cell growth by recombinant human galectin-1
    • Adams L., Kenneth S.G., and Weinberg C. Biphasic modulation of cell growth by recombinant human galectin-1. Biochem. Biophys. Acta 1312 (1996) 137-144
    • (1996) Biochem. Biophys. Acta , vol.1312 , pp. 137-144
    • Adams, L.1    Kenneth, S.G.2    Weinberg, C.3
  • 31
    • 0026724472 scopus 로고
    • Expression of the L14 lectin during mouse embryogenesis suggests multiple roles during pre and post-implantation development
    • Poirier F., Timmons P.M., Chan C.-T., Guenet J.L., and Rigby P. Expression of the L14 lectin during mouse embryogenesis suggests multiple roles during pre and post-implantation development. Development 115 (1992) 143-155
    • (1992) Development , vol.115 , pp. 143-155
    • Poirier, F.1    Timmons, P.M.2    Chan, C.-T.3    Guenet, J.L.4    Rigby, P.5
  • 32
    • 0028951736 scopus 로고
    • A human lectin, galectin-3 (epsilon-BP/ Mac-2) stimulates superoxide production by neutrophils
    • Yamaoka A., Kuwabara I., Frigeri L.G., and Liu F.T. A human lectin, galectin-3 (epsilon-BP/ Mac-2) stimulates superoxide production by neutrophils. J. Immunol. 154 (1995) 3479-3487
    • (1995) J. Immunol. , vol.154 , pp. 3479-3487
    • Yamaoka, A.1    Kuwabara, I.2    Frigeri, L.G.3    Liu, F.T.4
  • 33
    • 0023488847 scopus 로고
    • Endogenous galactoside-binding lectins: a new class of functional tumor cell surface molecules related to metastasis
    • Raz A., and Lotan R. Endogenous galactoside-binding lectins: a new class of functional tumor cell surface molecules related to metastasis. Cancer Metast. Rev. 6 (1987) 433-452
    • (1987) Cancer Metast. Rev. , vol.6 , pp. 433-452
    • Raz, A.1    Lotan, R.2
  • 34
    • 0031928731 scopus 로고    scopus 로고
    • Metastasis of human colon cancer is altered by modifying expression of the β-galactoside binding protein galectin-3
    • Bresalier R.S., Mazurek N., Sternberg L.R., Byrd J.C., Yunker C.K., Makker P.N., and Raz A. Metastasis of human colon cancer is altered by modifying expression of the β-galactoside binding protein galectin-3. Gastroenterology 115 (1998) 287-296
    • (1998) Gastroenterology , vol.115 , pp. 287-296
    • Bresalier, R.S.1    Mazurek, N.2    Sternberg, L.R.3    Byrd, J.C.4    Yunker, C.K.5    Makker, P.N.6    Raz, A.7
  • 35
    • 0032525046 scopus 로고    scopus 로고
    • Activated rat macrophages produce a galectin-1-like protein that induces apoptosis of T cells: biochemical and functional characterization
    • Rabinovich G.A., Iglesias M.M., Modesti N.M., Castagna L.F., Wolfenstein-Todel C., Riera C.M., and Sotomayor C.E. Activated rat macrophages produce a galectin-1-like protein that induces apoptosis of T cells: biochemical and functional characterization. J. Immunol. 160 (1998) 4831-4840
    • (1998) J. Immunol. , vol.160 , pp. 4831-4840
    • Rabinovich, G.A.1    Iglesias, M.M.2    Modesti, N.M.3    Castagna, L.F.4    Wolfenstein-Todel, C.5    Riera, C.M.6    Sotomayor, C.E.7
  • 37
    • 0029900083 scopus 로고    scopus 로고
    • Expression of galectin-3 modulates T cell growth and apoptosis
    • Yang R.Y., Hsu D.K., and Liu F.T. Expression of galectin-3 modulates T cell growth and apoptosis. Proc. Natl. Acad. Sci. USA 93 (1996) 6737-6742
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6737-6742
    • Yang, R.Y.1    Hsu, D.K.2    Liu, F.T.3
  • 38
    • 0035445710 scopus 로고    scopus 로고
    • Association of galectin-1 and galectin-3 with Gemin4 in complexes containing the SMN protein
    • Park J.W., Voss P.G., Grabski S., Wang J.L., and Patterson R.J. Association of galectin-1 and galectin-3 with Gemin4 in complexes containing the SMN protein. Nucleic Acid Res. 29 (2001) 3595-3602
    • (2001) Nucleic Acid Res. , vol.29 , pp. 3595-3602
    • Park, J.W.1    Voss, P.G.2    Grabski, S.3    Wang, J.L.4    Patterson, R.J.5
  • 39
    • 0032567036 scopus 로고    scopus 로고
    • A novel function for SMN, the spinal muscular atrophy disease gene product, in pre-mRNA gene splicing
    • Pellizoni L., Kataoka N., Charroux B., and Dreyfuss G. A novel function for SMN, the spinal muscular atrophy disease gene product, in pre-mRNA gene splicing. Cell 95 (1998) 615-624
    • (1998) Cell , vol.95 , pp. 615-624
    • Pellizoni, L.1    Kataoka, N.2    Charroux, B.3    Dreyfuss, G.4
  • 40
    • 0030003692 scopus 로고    scopus 로고
    • Human T lymphotropic virus-I infection of human T lymphocytes induces expression of the beta-galactoside binding lectin, galectin-3
    • Hsu D.K., Hammes S.R., Kuwabara I., Greene W.C., and Liu F.T. Human T lymphotropic virus-I infection of human T lymphocytes induces expression of the beta-galactoside binding lectin, galectin-3. J. Biol. Chem. 148 (1996) 1661
    • (1996) J. Biol. Chem. , vol.148 , pp. 1661
    • Hsu, D.K.1    Hammes, S.R.2    Kuwabara, I.3    Greene, W.C.4    Liu, F.T.5
  • 41
    • 0031455986 scopus 로고    scopus 로고
    • Modulation of the expression of the rabbit galectin-3 gene by p53 and c-Ha-ras proteins and PMA
    • Gaudin J.C., Arar C., Monsigny M., and Legrand A. Modulation of the expression of the rabbit galectin-3 gene by p53 and c-Ha-ras proteins and PMA. Glycobiology 7 (1997) 1089-1098
    • (1997) Glycobiology , vol.7 , pp. 1089-1098
    • Gaudin, J.C.1    Arar, C.2    Monsigny, M.3    Legrand, A.4
  • 42
    • 0028074969 scopus 로고
    • Regulation of secretion and surface expression of Mac-2, a galactoside-binding protein of macrophages
    • Sato S., and Hughes R.C. Regulation of secretion and surface expression of Mac-2, a galactoside-binding protein of macrophages. J. Biol. Chem. 269 (1994) 4424-4430
    • (1994) J. Biol. Chem. , vol.269 , pp. 4424-4430
    • Sato, S.1    Hughes, R.C.2
  • 43
    • 0032545640 scopus 로고    scopus 로고
    • Modulation of galectin-1 content in human head and neck squamous carcinoma cells by sodium butyrate
    • Gillenwater A., Xu X.C., Estrov Y., Sacks P.G., Lotan D., and Lotan R. Modulation of galectin-1 content in human head and neck squamous carcinoma cells by sodium butyrate. Int. J. Cancer 75 (1998) 217-224
    • (1998) Int. J. Cancer , vol.75 , pp. 217-224
    • Gillenwater, A.1    Xu, X.C.2    Estrov, Y.3    Sacks, P.G.4    Lotan, D.5    Lotan, R.6
  • 44
    • 0030064027 scopus 로고    scopus 로고
    • Galectins: a family of animal lectins that decipher glycocodes
    • Kasai K., and Hirabayashi J. Galectins: a family of animal lectins that decipher glycocodes. J. Biochem. 119 (1996) 1-8
    • (1996) J. Biochem. , vol.119 , pp. 1-8
    • Kasai, K.1    Hirabayashi, J.2
  • 45
    • 0030000860 scopus 로고    scopus 로고
    • A new pathway for protein export in Saccharomyces cerevisiae
    • Cleves A.E., Cooper D.N., Barondes H.S., and Kelly R.B. A new pathway for protein export in Saccharomyces cerevisiae. J. Cell Biol. 133 (1996) 1017-1026
    • (1996) J. Cell Biol. , vol.133 , pp. 1017-1026
    • Cleves, A.E.1    Cooper, D.N.2    Barondes, H.S.3    Kelly, R.B.4
  • 46
    • 0036798862 scopus 로고    scopus 로고
    • Ah, sweet mystery of death! Galectins and control of cell fate
    • Hernandez J.D., and Baum L.G. Ah, sweet mystery of death! Galectins and control of cell fate. Glycobiology 12 (2002) 127-136
    • (2002) Glycobiology , vol.12 , pp. 127-136
    • Hernandez, J.D.1    Baum, L.G.2
  • 47
    • 0032521627 scopus 로고    scopus 로고
    • Galectin-1 from ovine placenta: amino-acid sequence, physicochemical properties and implications in T-cell death
    • Iglesias M.M., Rabinovich G.A., Ivanovic V., Sotomayor C.E., and Wolfenstein-Todel C. Galectin-1 from ovine placenta: amino-acid sequence, physicochemical properties and implications in T-cell death. Eur. J. Biochem. 252 (1998) 400-407
    • (1998) Eur. J. Biochem. , vol.252 , pp. 400-407
    • Iglesias, M.M.1    Rabinovich, G.A.2    Ivanovic, V.3    Sotomayor, C.E.4    Wolfenstein-Todel, C.5
  • 48
    • 0032852619 scopus 로고    scopus 로고
    • Galectins: an evolutionarily conserved family of animal lectins with multifunctional properties; a trip from the gene to clinical therapy
    • Rabinovich G.A. Galectins: an evolutionarily conserved family of animal lectins with multifunctional properties; a trip from the gene to clinical therapy. Cell Death Differ. 6 (1999) 711-721
    • (1999) Cell Death Differ. , vol.6 , pp. 711-721
    • Rabinovich, G.A.1
  • 49
    • 0010646727 scopus 로고    scopus 로고
    • Lectin-induced immunoregulation in ovine placenta
    • Lectins. van Driessche E., Beeckmans S., and Bog-Hansen T.C. (Eds), Lextop, Hellerup Denmark
    • Iglesias M.M., Rabinovich G.A., Ambrosio A.L., Sotomayor C.E., and Todel C.W. Lectin-induced immunoregulation in ovine placenta. In: van Driessche E., Beeckmans S., and Bog-Hansen T.C. (Eds). Lectins. Biol. Biochem. Clin. Biochem. vol. 12 (1998), Lextop, Hellerup Denmark
    • (1998) Biol. Biochem. Clin. Biochem. , vol.12
    • Iglesias, M.M.1    Rabinovich, G.A.2    Ambrosio, A.L.3    Sotomayor, C.E.4    Todel, C.W.5
  • 51
    • 1542373593 scopus 로고    scopus 로고
    • Expression of galectins in cancer: a critical review
    • van den Brule F., Califice S., and Castronovo V. Expression of galectins in cancer: a critical review. Glycoconj. J. 19 (2004) 537-542
    • (2004) Glycoconj. J. , vol.19 , pp. 537-542
    • van den Brule, F.1    Califice, S.2    Castronovo, V.3
  • 52
    • 0035829731 scopus 로고    scopus 로고
    • Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anchorage and cell transformation
    • Paz A., Haklai R., Elad-Sfadai G., Ballan E., and Kloog Y. Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anchorage and cell transformation. Oncogene 20 (2001) 7486-7493
    • (2001) Oncogene , vol.20 , pp. 7486-7493
    • Paz, A.1    Haklai, R.2    Elad-Sfadai, G.3    Ballan, E.4    Kloog, Y.5
  • 54
    • 0344653662 scopus 로고    scopus 로고
    • Adhesion of human breast carcinoma to extracellular matrix proteins is modulated by galectin-3
    • Warfield P.R., Makker P.N., Raz A., and Ochieng J. Adhesion of human breast carcinoma to extracellular matrix proteins is modulated by galectin-3. Inv. Metastas. 17 (1997) 101-112
    • (1997) Inv. Metastas. , vol.17 , pp. 101-112
    • Warfield, P.R.1    Makker, P.N.2    Raz, A.3    Ochieng, J.4
  • 55
    • 0027414461 scopus 로고
    • Decreased expression of Mac-2 (carbohydrate binding protein 35) and loss of its nuclear localization are associated with the neoplastic progression of colon carcinoma
    • Lotz M.M., Andrews Jr. C.W., Korzelius C.A., Lee E.C., Steele Jr. G.D., Clarke A., and Mercurio A.M. Decreased expression of Mac-2 (carbohydrate binding protein 35) and loss of its nuclear localization are associated with the neoplastic progression of colon carcinoma. Proc. Natl. Acad. Sci. USA 90 (1993) 3466-3470
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3466-3470
    • Lotz, M.M.1    Andrews Jr., C.W.2    Korzelius, C.A.3    Lee, E.C.4    Steele Jr., G.D.5    Clarke, A.6    Mercurio, A.M.7
  • 58
    • 0343962593 scopus 로고    scopus 로고
    • Alteration of the cytoplasmic/nuclear expression pattern of galectin-3 correlates with prostate carcinoma progression
    • van den Brule F.A., Waltregny D., Liu F.-T., and Castronovo V. Alteration of the cytoplasmic/nuclear expression pattern of galectin-3 correlates with prostate carcinoma progression. Int. J. Cancer 89 (2000) 361-367
    • (2000) Int. J. Cancer , vol.89 , pp. 361-367
    • van den Brule, F.A.1    Waltregny, D.2    Liu, F.-T.3    Castronovo, V.4
  • 60
    • 6344261571 scopus 로고    scopus 로고
    • Dual activities of galectin-3 in human prostate cancer: tumor suppression of nuclear galectin-3 vs tumor promotion of cytoplasmic galectin-3
    • Califice S., Castronovo V., Bracke M., and van den Brule F. Dual activities of galectin-3 in human prostate cancer: tumor suppression of nuclear galectin-3 vs tumor promotion of cytoplasmic galectin-3. Oncogene 23 (2004) 7527-7536
    • (2004) Oncogene , vol.23 , pp. 7527-7536
    • Califice, S.1    Castronovo, V.2    Bracke, M.3    van den Brule, F.4
  • 61
    • 0029091352 scopus 로고
    • Function of the homeo and paired domain proteins TTF-1 and Pax-8 in thyroid cell proliferation
    • Rossi D.L., Acebran A., and Santisteban P. Function of the homeo and paired domain proteins TTF-1 and Pax-8 in thyroid cell proliferation. J. Biol. Chem. 270 (1995) 23139-23142
    • (1995) J. Biol. Chem. , vol.270 , pp. 23139-23142
    • Rossi, D.L.1    Acebran, A.2    Santisteban, P.3
  • 62
    • 18244414247 scopus 로고    scopus 로고
    • Galectin-3 as a multifunctional protein
    • Krzeslak A., and Lipinska A. Galectin-3 as a multifunctional protein. Cell. Mol. Biol. Lett. 9 (2004) 305-328
    • (2004) Cell. Mol. Biol. Lett. , vol.9 , pp. 305-328
    • Krzeslak, A.1    Lipinska, A.2
  • 63
    • 0029157473 scopus 로고
    • Differential expression of galectin-1 and galectin-3 in thyroid tumors. Potential diagnostic implications
    • Xu X.C., el-Naggar A.K., and Lotan R. Differential expression of galectin-1 and galectin-3 in thyroid tumors. Potential diagnostic implications. Am. J. Pathol. 147 (1995) 815-822
    • (1995) Am. J. Pathol. , vol.147 , pp. 815-822
    • Xu, X.C.1    el-Naggar, A.K.2    Lotan, R.3
  • 65
    • 0035170375 scopus 로고    scopus 로고
    • Increased expression of galectin-1 in carcinoma-associated stroma predicts poor outcome in prostrate carcinoma patients
    • van Den Brule F.A., Waltregny D., and Castronovo V. Increased expression of galectin-1 in carcinoma-associated stroma predicts poor outcome in prostrate carcinoma patients. J. Pathol. 193 (2001) 80-87
    • (2001) J. Pathol. , vol.193 , pp. 80-87
    • van Den Brule, F.A.1    Waltregny, D.2    Castronovo, V.3
  • 66
    • 0033070974 scopus 로고    scopus 로고
    • Differential expression of endogenous galectin-1 and galectin-3 in human prostate cancer cell lines and effects of overexpressing galectin-1 on cell phenotype
    • Ellehorst J., Nguven T., Cooper D.N.W., Lotan D., and Lotan R. Differential expression of endogenous galectin-1 and galectin-3 in human prostate cancer cell lines and effects of overexpressing galectin-1 on cell phenotype. Int. J. Oncol. 14 (1999) 217-224
    • (1999) Int. J. Oncol. , vol.14 , pp. 217-224
    • Ellehorst, J.1    Nguven, T.2    Cooper, D.N.W.3    Lotan, D.4    Lotan, R.5
  • 68
    • 0034653127 scopus 로고    scopus 로고
    • Expression of galectin-1 mRNA correlates with the malignant potential of human gliomas and expression of antisense galectin-1 inhibits the growth of 9 glioma cells
    • Yamaoka K., Mishima K., Nagashima Y., Asai A., Sanai Y., and Kirino T. Expression of galectin-1 mRNA correlates with the malignant potential of human gliomas and expression of antisense galectin-1 inhibits the growth of 9 glioma cells. J. Neurosci. Res. 59 (2000) 722-730
    • (2000) J. Neurosci. Res. , vol.59 , pp. 722-730
    • Yamaoka, K.1    Mishima, K.2    Nagashima, Y.3    Asai, A.4    Sanai, Y.5    Kirino, T.6
  • 70
    • 0033613211 scopus 로고    scopus 로고
    • Galectin-7 overexpression is associated with the apoptotic process in UVB-induced sunburn keratinocytes
    • Bernard F., Sarasin A., and Magnaldo T. Galectin-7 overexpression is associated with the apoptotic process in UVB-induced sunburn keratinocytes. Proc. Natl. Acad. Sci. USA 96 (1999) 11329-11334
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11329-11334
    • Bernard, F.1    Sarasin, A.2    Magnaldo, T.3
  • 71
    • 0035017215 scopus 로고    scopus 로고
    • comprehensive galectin fingerprinting in a panel of 61 human tumor cell lines by RT-PCR and its implications for diagnostic and therapeutic procedures
    • Lahm H., Andre S., Hoeflich A., fischer J.R., Sordat B., Kaltner h., Wolf E., and Gabius H.J. comprehensive galectin fingerprinting in a panel of 61 human tumor cell lines by RT-PCR and its implications for diagnostic and therapeutic procedures. J. Cancer Res. Clin. Oncol. 127 (2001) 375-386
    • (2001) J. Cancer Res. Clin. Oncol. , vol.127 , pp. 375-386
    • Lahm, H.1    Andre, S.2    Hoeflich, A.3    fischer, J.R.4    Sordat, B.5    Kaltner, h.6    Wolf, E.7    Gabius, H.J.8
  • 72
    • 0034618401 scopus 로고    scopus 로고
    • Molecular characterization of prostate carcinoma tumor antigen-I, a human galectin-8 related gene
    • Gopalkrishnan R.V., Roberts T., Tuli S., Kang D., Christiansen K.A., and Fisher P.B. Molecular characterization of prostate carcinoma tumor antigen-I, a human galectin-8 related gene. Oncogene 19 (2000) 4405-4416
    • (2000) Oncogene , vol.19 , pp. 4405-4416
    • Gopalkrishnan, R.V.1    Roberts, T.2    Tuli, S.3    Kang, D.4    Christiansen, K.A.5    Fisher, P.B.6
  • 73
    • 0034267935 scopus 로고    scopus 로고
    • Gene expression of galectin-9/ecalectin, a potent eosinophil chemoattractant, and/ or the insertional isoform in human colorectal carcinoma cell lines and detection of frameshift mutations for protein sequence truncations in the second functional lectin domain
    • Lahm H., Hoeflich A., Andre S., Sordat B., Kaltner H., Wolf E., and Gabius H. Gene expression of galectin-9/ecalectin, a potent eosinophil chemoattractant, and/ or the insertional isoform in human colorectal carcinoma cell lines and detection of frameshift mutations for protein sequence truncations in the second functional lectin domain. Int. J. Oncol. 17 (2000) 519-524
    • (2000) Int. J. Oncol. , vol.17 , pp. 519-524
    • Lahm, H.1    Hoeflich, A.2    Andre, S.3    Sordat, B.4    Kaltner, H.5    Wolf, E.6    Gabius, H.7
  • 74
    • 0027485050 scopus 로고
    • Normal development of mice carrying a null mutation in the gene encoding the L-14S-type lectin
    • Poirier F., and Robertson E.J. Normal development of mice carrying a null mutation in the gene encoding the L-14S-type lectin. Development 119 (1993) 1229-1236
    • (1993) Development , vol.119 , pp. 1229-1236
    • Poirier, F.1    Robertson, E.J.2
  • 75
    • 0031949975 scopus 로고    scopus 로고
    • Embryonic implantation in galectin-1/galectin-3 double mutant mice
    • Colnot C., Fowlis D., Ripoche M.A., Bouchaert I., and Poirier F. Embryonic implantation in galectin-1/galectin-3 double mutant mice. Dev. Dyn. 211 (1998) 306-313
    • (1998) Dev. Dyn. , vol.211 , pp. 306-313
    • Colnot, C.1    Fowlis, D.2    Ripoche, M.A.3    Bouchaert, I.4    Poirier, F.5
  • 76
    • 0036677372 scopus 로고    scopus 로고
    • Glycosylation defining cancer malignancy: new wine in an old bottle
    • Hakomori S. Glycosylation defining cancer malignancy: new wine in an old bottle. Proc. Natl. Acad. Sci. USA 99 (2002) 10231-10233
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10231-10233
    • Hakomori, S.1
  • 77
    • 0025945830 scopus 로고
    • Spreading, and motility of GM3-expressing cells based on glycolipid-glycolipid interaction
    • Kojima N., Hakomori S., and Adhesion C. Spreading, and motility of GM3-expressing cells based on glycolipid-glycolipid interaction. J. Biol. Chem. 266 (1991) 17552-17558
    • (1991) J. Biol. Chem. , vol.266 , pp. 17552-17558
    • Kojima, N.1    Hakomori, S.2    Adhesion, C.3
  • 78
    • 9244234958 scopus 로고    scopus 로고
    • Reversion of the Jun-induced oncogenic phenotype by enhanced synthesis of sialosyllactosylceramide (GM3 ganglioside)
    • Miura Y., Kainuma M., Jiang H., Velasco H., Vogt P.K., and Hakomori S. Reversion of the Jun-induced oncogenic phenotype by enhanced synthesis of sialosyllactosylceramide (GM3 ganglioside). Proc. Natl. Acad. Sci. USA 101 (2004) 16204-16209
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16204-16209
    • Miura, Y.1    Kainuma, M.2    Jiang, H.3    Velasco, H.4    Vogt, P.K.5    Hakomori, S.6
  • 79
    • 0035967503 scopus 로고    scopus 로고
    • GM3 ganglioside inhibits CD9-facilitated haptotactic cell motility: coexpression of GM3 and CD9 is essential in the downregulation of tumor cell motility and malignancy
    • Ono M., Handa K., Sonnino S., Withers D.A., Nagai H., and Hakomori S. GM3 ganglioside inhibits CD9-facilitated haptotactic cell motility: coexpression of GM3 and CD9 is essential in the downregulation of tumor cell motility and malignancy. Biochemistry 4 (2001) 6414-6421
    • (2001) Biochemistry , vol.4 , pp. 6414-6421
    • Ono, M.1    Handa, K.2    Sonnino, S.3    Withers, D.A.4    Nagai, H.5    Hakomori, S.6
  • 80
    • 0035486703 scopus 로고    scopus 로고
    • Enhanced GM3 expression, associated with decreased invasiveness, is induced by brefeldin A in bladder cancer cells
    • Satoh M., Ito A., Nojiri H., Handa K., Numahata K., Ohyama C., Saito S., Hoshi S., and Hakomori S.I. Enhanced GM3 expression, associated with decreased invasiveness, is induced by brefeldin A in bladder cancer cells. Int. J. Oncol. 19 (2001) 723-731
    • (2001) Int. J. Oncol. , vol.19 , pp. 723-731
    • Satoh, M.1    Ito, A.2    Nojiri, H.3    Handa, K.4    Numahata, K.5    Ohyama, C.6    Saito, S.7    Hoshi, S.8    Hakomori, S.I.9
  • 81
    • 0242287981 scopus 로고    scopus 로고
    • The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity
    • Ideo H., Seko A., Ishizuka I., and Yamashita K. The N-terminal carbohydrate recognition domain of galectin-8 recognizes specific glycosphingolipids with high affinity. Glycobiology 13 (2003) 713-723
    • (2003) Glycobiology , vol.13 , pp. 713-723
    • Ideo, H.1    Seko, A.2    Ishizuka, I.3    Yamashita, K.4
  • 82
    • 0031528585 scopus 로고    scopus 로고
    • Cross-linking activities of galectins and other multivalent lectins
    • Brewer C.F. Cross-linking activities of galectins and other multivalent lectins. Trends Glycosci. Glycotechnol. 9 (1997) 155-165
    • (1997) Trends Glycosci. Glycotechnol. , vol.9 , pp. 155-165
    • Brewer, C.F.1
  • 83
    • 0027169990 scopus 로고
    • The family of metazoan metal-independent β-galactoside-binding lectins: structure, function and molecular evolution
    • Hirabayashi J., and Kasai K. The family of metazoan metal-independent β-galactoside-binding lectins: structure, function and molecular evolution. Glycobiology 3 (1993) 297-304
    • (1993) Glycobiology , vol.3 , pp. 297-304
    • Hirabayashi, J.1    Kasai, K.2
  • 84
    • 0017689514 scopus 로고
    • Developmentally regulated lectin from embryonic chick pectoral muscle. Purification by affinity chromatography
    • Nowak T.P., Kobiler D., Roel L.E., and Barondes S.H. Developmentally regulated lectin from embryonic chick pectoral muscle. Purification by affinity chromatography. J. Biol. Chem. 252 (1977) 6026-6030
    • (1977) J. Biol. Chem. , vol.252 , pp. 6026-6030
    • Nowak, T.P.1    Kobiler, D.2    Roel, L.E.3    Barondes, S.H.4
  • 85
    • 0016564484 scopus 로고
    • The use of glutaraldehyde-treated erythrocytes for assaying the agglutinating activity of lectins
    • Turner R.H., and Liener I.E. The use of glutaraldehyde-treated erythrocytes for assaying the agglutinating activity of lectins. Anal. Biochem. 68 (1975) 651-653
    • (1975) Anal. Biochem. , vol.68 , pp. 651-653
    • Turner, R.H.1    Liener, I.E.2
  • 86
    • 18644370571 scopus 로고    scopus 로고
    • Galectin fingerprinting in human endometrium and decidua during the menstrual cycle and in early gestation
    • von Wolff M., Wang X., Gabius H.-J., and Strowitzki T. Galectin fingerprinting in human endometrium and decidua during the menstrual cycle and in early gestation. Mol. Hum. Reprod. 11 (2005) 189-194
    • (2005) Mol. Hum. Reprod. , vol.11 , pp. 189-194
    • von Wolff, M.1    Wang, X.2    Gabius, H.-J.3    Strowitzki, T.4
  • 88
    • 0031959770 scopus 로고    scopus 로고
    • Galectins: versatile modulators of cell adhesion, cell proliferation and cell death
    • Perillo N.L., Marcus M.E., and Baum L.G. Galectins: versatile modulators of cell adhesion, cell proliferation and cell death. J. Mol. Med. 76 (1998) 402-412
    • (1998) J. Mol. Med. , vol.76 , pp. 402-412
    • Perillo, N.L.1    Marcus, M.E.2    Baum, L.G.3
  • 89
    • 33646782605 scopus 로고    scopus 로고
    • Inhibition and detection of galectins
    • Pieters R.J. Inhibition and detection of galectins. ChemBioChem 7 (2006) 721-728
    • (2006) ChemBioChem , vol.7 , pp. 721-728
    • Pieters, R.J.1
  • 91
    • 10844252383 scopus 로고    scopus 로고
    • Protein expression profiles in pancreatic adenocarcinoma compared with normal pancreatic tissue and tissue affected by pancreatitis as detected by two-dimensional gel electrophoresis and mass spectrometry
    • Shen J., Person M.D., Zhu J., Abbruzzese J.L., and Li D. Protein expression profiles in pancreatic adenocarcinoma compared with normal pancreatic tissue and tissue affected by pancreatitis as detected by two-dimensional gel electrophoresis and mass spectrometry. Cancer Res. 64 (2004) 9018-9026
    • (2004) Cancer Res. , vol.64 , pp. 9018-9026
    • Shen, J.1    Person, M.D.2    Zhu, J.3    Abbruzzese, J.L.4    Li, D.5
  • 93
    • 0032079480 scopus 로고    scopus 로고
    • Detection of lectins using ligand blotting and polyacrylamide-type glycoconjugate probes
    • Kamemura K., and Kato S. Detection of lectins using ligand blotting and polyacrylamide-type glycoconjugate probes. Anal. Biochem. 258 (1998) 305-310
    • (1998) Anal. Biochem. , vol.258 , pp. 305-310
    • Kamemura, K.1    Kato, S.2
  • 94
    • 34250006448 scopus 로고    scopus 로고
    • Human Galectin-3 ELISA, BMS279, Bender MedSystems GmbH, Vienna (Austria).
  • 96
    • 0030579163 scopus 로고    scopus 로고
    • Role of galectin-1 in the developing mouse olfactory system
    • Puche A.C., Poirier F., Hair M., Barlett P.F., and Key B. Role of galectin-1 in the developing mouse olfactory system. Dev. Biol. 179 (1996) 274-287
    • (1996) Dev. Biol. , vol.179 , pp. 274-287
    • Puche, A.C.1    Poirier, F.2    Hair, M.3    Barlett, P.F.4    Key, B.5
  • 97
    • 0031850611 scopus 로고    scopus 로고
    • Maintenance of granulocyte numbers during acute peritonitis is defective in galectin-3-null mutanat mice
    • Colnot C., Ripoche M.A., Milon G., Montagutelli X., Crocker P.R., and Poirier F. Maintenance of granulocyte numbers during acute peritonitis is defective in galectin-3-null mutanat mice. Immunology 94 (1998) 290-296
    • (1998) Immunology , vol.94 , pp. 290-296
    • Colnot, C.1    Ripoche, M.A.2    Milon, G.3    Montagutelli, X.4    Crocker, P.R.5    Poirier, F.6
  • 98
  • 103
    • 0031058735 scopus 로고    scopus 로고
    • Topological analysis of the functional mimicry between a peptide and a carbohydrate moiety
    • Kaur K.J., Khurana S., and Salunke D.M. Topological analysis of the functional mimicry between a peptide and a carbohydrate moiety. J. Biol. Chem. 272 (1997) 5539-5543
    • (1997) J. Biol. Chem. , vol.272 , pp. 5539-5543
    • Kaur, K.J.1    Khurana, S.2    Salunke, D.M.3
  • 105
    • 37049067264 scopus 로고
    • A PEGA resin for use in the solid phase chemical/enzymatic synthesis of glycopeptides
    • Meldal M., Auzanneau F.I., Hindsgaul O., and Palcic M.M. A PEGA resin for use in the solid phase chemical/enzymatic synthesis of glycopeptides. J. Chem Soc. Chem. Commun. (1994) 1849-1850
    • (1994) J. Chem Soc. Chem. Commun. , pp. 1849-1850
    • Meldal, M.1    Auzanneau, F.I.2    Hindsgaul, O.3    Palcic, M.M.4
  • 108
    • 13844256109 scopus 로고    scopus 로고
    • Peptides specific to the galectin-3 carbohydrate recognition domain inhibit metastasis-associated cancer cell adhesion
    • Zou J., Glinsky V.V., Landon L.A., Matthews L., and Deutscher S.L. Peptides specific to the galectin-3 carbohydrate recognition domain inhibit metastasis-associated cancer cell adhesion. Carcinogenesis 26 (2005) 309-318
    • (2005) Carcinogenesis , vol.26 , pp. 309-318
    • Zou, J.1    Glinsky, V.V.2    Landon, L.A.3    Matthews, L.4    Deutscher, S.L.5
  • 109
    • 0036510564 scopus 로고    scopus 로고
    • Galectin-3 phosphorylation is required for its anti-apoptotic function and cell cycle arrest
    • Yoshii T., Fukumori T., Honjo Y., Inohara H., Kim H.-R.C., and Raz A. Galectin-3 phosphorylation is required for its anti-apoptotic function and cell cycle arrest. J. Biol. Chem. 277 (2002) 6852-6857
    • (2002) J. Biol. Chem. , vol.277 , pp. 6852-6857
    • Yoshii, T.1    Fukumori, T.2    Honjo, Y.3    Inohara, H.4    Kim, H.-R.C.5    Raz, A.6
  • 110
    • 0034680933 scopus 로고    scopus 로고
    • Phosphorylation of the β-galactoside- binding protein galectin-3 modulates binding to its ligands
    • Mazurek N., Conklin J., Byrd J.C., Raz A., and Bresalier R.S. Phosphorylation of the β-galactoside- binding protein galectin-3 modulates binding to its ligands. J. Biol. Chem. 275 (2000) 36311-36315
    • (2000) J. Biol. Chem. , vol.275 , pp. 36311-36315
    • Mazurek, N.1    Conklin, J.2    Byrd, J.C.3    Raz, A.4    Bresalier, R.S.5
  • 112


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