메뉴 건너뛰기




Volumn 9, Issue 2, 2004, Pages 305-328

Galectin-3 as a multifunctional protein

Author keywords

Apoptosis; Cancer Progression; Carbohydrate Binding; Cell Adhesion; Galectin 3; Ligands; Non Classical Secretion

Indexed keywords

BETA GALACTOSIDASE; GALECTIN 3;

EID: 18244414247     PISSN: 14258153     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (205)

References (105)
  • 1
    • 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
  • 3
    • 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
  • 4
    • 0030668822 scopus 로고    scopus 로고
    • The galectin family of mammalian carbohydrate-binding molecules
    • Hughes, R.C. The galectin family of mammalian carbohydrate-binding molecules. Biochem. Soc. Transact. 25 (1997) 1194-1198.
    • (1997) Biochem. Soc. Transact. , vol.25 , pp. 1194-1198
    • Hughes, R.C.1
  • 5
    • 0032714092 scopus 로고    scopus 로고
    • Secretion of the galectin family of mammalian carbohydrate-binding proteins
    • Hughes, R.C. Secretion of the galectin family of mammalian carbohydrate-binding proteins. Biochim. Biophys. Acta 1473 (1999) 172-185.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 172-185
    • Hughes, R.C.1
  • 6
    • 0034851982 scopus 로고    scopus 로고
    • Galectins as modulators of cell adhesion
    • Hughes, R.C. Galectins as modulators of cell adhesion. Biochimie 83 (2001) 667-676.
    • (2001) Biochimie , vol.83 , pp. 667-676
    • Hughes, R.C.1
  • 10
    • 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
  • 11
    • 0035258771 scopus 로고    scopus 로고
    • Galectins galactoside-binding mammalian lectins: Clinical application of multi-functional proteins
    • Wada, J. and Makino, H. Galectins, galactoside-binding mammalian lectins: clinical application of multi-functional proteins. Acta Med. Okayama 55 (2001) 11-17.
    • (2001) Acta Med. Okayama , vol.55 , pp. 11-17
    • Wada, J.1    Makino, H.2
  • 13
    • 0023406938 scopus 로고
    • Endogenous lectins from cultured cells: Nuclear localization of carbohydrate-binding protein 35 in proliferating 3T3 fibroblasts
    • Moutsatsos, I.K., Wade, M., Schindler, M. and Wang, J.L. Endogenous lectins from cultured cells: nuclear localization of carbohydrate-binding protein 35 in proliferating 3T3 fibroblasts. Proc. Natl. Acad. Sci. USA 84 (1987) 6452-6456.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6452-6456
    • Moutsatsos, I.K.1    Wade, M.2    Schindler, M.3    Wang, J.L.4
  • 14
    • 0027169990 scopus 로고
    • The family of metazoan metal-independent beta-galactoside-binding lectins: Structure, function and molecular evolution
    • Hirabayashi, J. and Kasai, K. The family of metazoan metal-independent beta-galactoside-binding lectins: structure, function and molecular evolution. Glycobiology 4 (1993) 297-304.
    • (1993) Glycobiology , vol.4 , pp. 297-304
    • Hirabayashi, J.1    Kasai, K.2
  • 15
    • 0023952291 scopus 로고
    • Carbohydrate binding protein 35. Complementary DNA sequence reveals homology with proteins of the heterogeneous nuclear RNP
    • Jia, S. and Wang, J.L. Carbohydrate binding protein 35. Complementary DNA sequence reveals homology with proteins of the heterogeneous nuclear RNP. J. Biol. Chem. 263 (1988) 6009-6011.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6009-6011
    • Jia, S.1    Wang, J.L.2
  • 17
    • 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
  • 18
    • 0035901521 scopus 로고    scopus 로고
    • NMR solution studies of hamster galectin-3 and electron microscopic visualization of surface-adsorbed complexes: Evidence for interactions between the N- and C-terminal domains
    • Birdsall, B., Feeney, J., Burdett, I.D.J., Bawumia, S., Barboni, E.A.M. and Hughes, R.C. NMR solution studies of hamster galectin-3 and electron microscopic visualization of surface-adsorbed complexes: evidence for interactions between the N- and C-terminal domains. Biochemistry 40 (2001) 4859-4866.
    • (2001) Biochemistry , vol.40 , pp. 4859-4866
    • Birdsall, B.1    Feeney, J.2    Burdett, I.D.J.3    Bawumia, S.4    Barboni, E.A.M.5    Hughes, R.C.6
  • 19
    • 0027527552 scopus 로고
    • L-29, a soluble lactose-binding lectin, is phosphorylated on serine 6 and serine 12 in vivo and by casein kinase I
    • Huflejt, M.E., Turck, C.W., Lindstedt, R., Barondes, S.H. and Leffler, H. L-29, a soluble lactose-binding lectin, is phosphorylated on serine 6 and serine 12 in vivo and by casein kinase I. J. Biol. Chem. 268 (1993) 26712-26718.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26712-26718
    • Huflejt, M.E.1    Turck, C.W.2    Lindstedt, R.3    Barondes, S.H.4    Leffler, H.5
  • 20
    • 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
  • 21
    • 0033199579 scopus 로고    scopus 로고
    • Determinants in the N-terminal domains of galectin-3 for secretion by a novel pathway circumventing the endoplasmic reticulum-Golgi complex
    • Menon, R.P. and Hughes, R.C. Determinants in the N-terminal domains of galectin-3 for secretion by a novel pathway circumventing the endoplasmic reticulum-Golgi complex. Eur. J. Biochem. 264 (1999) 569-576.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 569-576
    • Menon, R.P.1    Hughes, R.C.2
  • 22
    • 0027958144 scopus 로고
    • Structure of S-lectin, a developmentally regulated vertebrate β-galactoside-binding protein
    • Liao, D.I., Kapadia, G., Ahmed, H., Vasta, G.R. and Herzberg, O. Structure of S-lectin, a developmentally regulated vertebrate β-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
  • 23
    • 0027754166 scopus 로고
    • X-ray crystal structure of the human dimeric s-Lac lectin, L-14-II, in complex with lactose at 2.9 Å resolution
    • Lobsanov, Y.D., Gitt, M.A., Leffler, H., Barondes, S.H. and Rini, J.M. X-ray crystal structure of the human dimeric s-Lac lectin, L-14-II, in complex with lactose at 2.9 Å resolution. J. Biol. Chem. 268 (1993) 27034-27038.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27034-27038
    • Lobsanov, Y.D.1    Gitt, M.A.2    Leffler, H.3    Barondes, S.H.4    Rini, J.M.5
  • 24
    • 0032557645 scopus 로고    scopus 로고
    • X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-Å resolution
    • Seetharaman, J., Kanigsberg A., Slaaby, R., Leffler, H., Barondes, S.H. and Rini, J.M. X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-Å resolution. J. Biol. Chem. 273 (1998) 13047-13052.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13047-13052
    • Seetharaman, J.1    Kanigsberg, A.2    Slaaby, R.3    Leffler, H.4    Barondes, S.H.5    Rini, J.M.6
  • 26
    • 0027225381 scopus 로고
    • Secretion of the baby hamster kidney 30-kDa galactose-binding lectin from polarized and nonpolarized cells: A pathway independent of the endoplasmic reticulum-Golgi complex
    • Sato, S., Burdett, I. and Hughes, R.C. Secretion of the baby hamster kidney 30-kDa galactose-binding lectin from polarized and nonpolarized cells: a pathway independent of the endoplasmic reticulum-Golgi complex. Exp. Cell Res. 207 (1993) 8-18.
    • (1993) Exp. Cell Res. , vol.207 , pp. 8-18
    • Sato, S.1    Burdett, I.2    Hughes, R.C.3
  • 27
    • 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
  • 28
    • 0038701886 scopus 로고    scopus 로고
    • The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes
    • Nickel, W. The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes. Eur. J. Biochem. 270 (2003) 2109-2119.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2109-2119
    • Nickel, W.1
  • 29
    • 0030994878 scopus 로고    scopus 로고
    • Plasma membrane targeting, vesicular budding and release of galectin 3 from the cytoplasm of mammalian cells during secretion
    • Mehul, B. and Hughes, R.C. Plasma membrane targeting, vesicular budding and release of galectin 3 from the cytoplasm of mammalian cells during secretion. J. Cell Sci. 110 (1997) 1169-1178.
    • (1997) J. Cell Sci. , vol.110 , pp. 1169-1178
    • Mehul, B.1    Hughes, R.C.2
  • 31
    • 0030948362 scopus 로고    scopus 로고
    • Retargeting of cytosolic proteins to the plasma membrane by the Lck protein tyrosine kinase dual acylation motif
    • Zlatkine, P., Mehul, B. and Magee, A.I. Retargeting of cytosolic proteins to the plasma membrane by the Lck protein tyrosine kinase dual acylation motif. J. Cell Sci. 110 (1997) 673-679.
    • (1997) J. Cell Sci. , vol.110 , pp. 673-679
    • Zlatkine, P.1    Mehul, B.2    Magee, A.I.3
  • 32
    • 0025317697 scopus 로고
    • The major non-integrin laminin binding protein of macrophages is identical to carbohydrate binding pro-tein 35 (Mac-2)
    • Woo, H.-J., Shaw, L.M., Messier, J.M. and Mercurio, A.M. The major non-integrin laminin binding protein of macrophages is identical to carbohydrate binding pro-tein 35 (Mac-2). J. Biol. Chem. 265 (1990) 7097-7099.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7097-7099
    • Woo, H.-J.1    Shaw, L.M.2    Messier, J.M.3    Mercurio, A.M.4
  • 33
    • 0026047293 scopus 로고
    • Mac-2-binding glycoproteins. Putative ligands for a cytosolic β-galactoside lectin
    • Rosenberg, I., Cherayil, B.J., Isselbacher, K.J. and Pillai, S. Mac-2-binding glycoproteins. Putative ligands for a cytosolic β-galactoside lectin. J. Biol. Chem. 266 (1991) 18731-18736.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18731-18736
    • Rosenberg, I.1    Cherayil, B.J.2    Isselbacher, K.J.3    Pillai, S.4
  • 34
    • 0027229657 scopus 로고
    • Cloning and characterization of a human Mac-2-binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain
    • Koths, K., Taylor, E., Halenbeck, R., Casipit, C. and Wang, A. Cloning and characterization of a human Mac-2-binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain. J. Biol. Chem. 268 (1993) 14245-14249.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14245-14249
    • Koths, K.1    Taylor, E.2    Halenbeck, R.3    Casipit, C.4    Wang, A.5
  • 35
    • 0026673762 scopus 로고
    • Binding specificity of a baby hamster kidney lectin for H type I and II chains, polylactosamine glycans, and appropriately glycosylated forms of laminin and fibronectin
    • Sato, S. and Hughes, R.C. Binding specificity of a baby hamster kidney lectin for H type I and II chains, polylactosamine glycans, and appropriately glycosylated forms of laminin and fibronectin. J. Biol. Chem. 267 (1992) 6983-6990.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6983-6990
    • Sato, S.1    Hughes, R.C.2
  • 36
    • 0028988528 scopus 로고
    • Galectin-3 a β-galactoside-binding animal lectin, binds to neural recognition molecules
    • Probstmeier, R., Montag, D. and Schachner, M. Galectin-3, a β-galactoside-binding animal lectin, binds to neural recognition molecules. J. Neurochem. 64 (1995) 2465-2472.
    • (1995) J. Neurochem. , vol.64 , pp. 2465-2472
    • Probstmeier, R.1    Montag, D.2    Schachner, M.3
  • 37
    • 0029566272 scopus 로고
    • Galectin-3 binding potentials of mouse tumor RHS and human placental laminins
    • Ochieng, J. and Warfield, P. Galectin-3 binding potentials of mouse tumor RHS and human placental laminins. Biochem. Biophys. Res. Commun. 217 (1995) 402-406.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 402-406
    • Ochieng, J.1    Warfield, P.2
  • 38
    • 0030941612 scopus 로고    scopus 로고
    • Macrophage surface glycoproteins binding to galectin-3 (Mac-2-antigen)
    • Dong, S. and Hughes, R.C. Macrophage surface glycoproteins binding to galectin-3 (Mac-2-antigen). Glycoconj. J. 14 (1997) 267-274.
    • (1997) Glycoconj. J. , vol.14 , pp. 267-274
    • Dong, S.1    Hughes, R.C.2
  • 39
    • 0032577178 scopus 로고    scopus 로고
    • Regulation of cellular adhesion to extracellular matrix proteins by galectin-3
    • Ochieng, J., Leite-Browning, M.L. and Warfield, P. Regulation of cellular adhesion to extracellular matrix proteins by galectin-3. Biochem. Biophys. Res. Commun. 246 (1998) 788-791.
    • (1998) Biochem. Biophys. Res. Commun. , vol.246 , pp. 788-791
    • Ochieng, J.1    Leite-Browning, M.L.2    Warfield, P.3
  • 40
    • 0029942555 scopus 로고    scopus 로고
    • Galectin-3 promotes adhesion of human neutrophils to laminin
    • Kuwabara, I. and Liu, F.T. Galectin-3 promotes adhesion of human neutrophils to laminin. J. Immunol. 156 (1996) 3939-3944.
    • (1996) J. Immunol. , vol.156 , pp. 3939-3944
    • Kuwabara, I.1    Liu, F.T.2
  • 42
    • 0001913054 scopus 로고    scopus 로고
    • MP20 the second most abundant lens membrane protein and member of the tetraspanin superfamily, joins the list of ligands of galectin-3
    • Gonen, T., Grey, A.C., Jacobs, M.D., Donaldson, P.J. and Kistler, J. MP20, the second most abundant lens membrane protein and member of the tetraspanin superfamily, joins the list of ligands of galectin-3. BMC Cell Biol. 2 (2001) 17.
    • (2001) BMC Cell Biol. , vol.2 , pp. 17
    • Gonen, T.1    Grey, A.C.2    Jacobs, M.D.3    Donaldson, P.J.4    Kistler, J.5
  • 43
    • 0030750226 scopus 로고    scopus 로고
    • Novel αGalNAc containing glycans on cytokeratins are recognized in vitro by galectins with type II carbohydrate recognition domains
    • Goletz, S., Hanisch, F.-G. and Karsten, U. Novel αGalNAc containing glycans on cytokeratins are recognized in vitro by galectins with type II carbohydrate recognition domains. J. Cell Sci. 110 (1997) 1585-1596.
    • (1997) J. Cell Sci. , vol.110 , pp. 1585-1596
    • Goletz, S.1    Hanisch, F.-G.2    Karsten, U.3
  • 44
  • 45
    • 0034737710 scopus 로고    scopus 로고
    • Interaction of a novel cysteine and histidine-rich cytoplasmic protein with galectin-3 in a carbohydrate-independent manner
    • Menon, R.P., Strom, M. and Hughes, R.C. Interaction of a novel cysteine and histidine-rich cytoplasmic protein with galectin-3 in a carbohydrate- independent manner. FEBS Lett. 470 (2000) 227-231.
    • (2000) FEBS Lett. , vol.470 , pp. 227-231
    • Menon, R.P.1    Strom, M.2    Hughes, R.C.3
  • 46
    • 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. Nucl. Acids Res. 27 (2001) 3595-3602.
    • (2001) Nucl. Acids Res. , vol.27 , pp. 3595-3602
    • Park, J.W.1    Voss, P.G.2    Grabski, S.3    Wang, J.L.4    Patterson, R.J.5
  • 47
    • 0030707480 scopus 로고    scopus 로고
    • Galectin-3 a novel antiapoptotic molecule with a functional BH1 (NWGR) domain of Bcl-2 family
    • Akahani, S., Nangia-Makker, P., Inohara, H., Kim, H.-R.C. and Raz, A. Galectin-3: a novel antiapoptotic molecule with a functional BH1 (NWGR) domain of Bcl-2 family. Cancer Res. 57 (1997) 5272-5276.
    • (1997) Cancer Res. , vol.57 , pp. 5272-5276
    • Akahani, S.1    Nangia-Makker, P.2    Inohara, H.3    Kim, H.-R.C.4    Raz, A.5
  • 48
    • 0033862317 scopus 로고    scopus 로고
    • Glycosylated nuclear lectin CBP70 also associated with endoplasmic reticulum and the Golgi apparatus: Does the "classic pathway" of glycosylation also apply to nuclear glycoproteins?
    • Rousseau, C., Muriel, M.-P., Musset, M., Botti, J. and Sève, A.-P. Glycosylated nuclear lectin CBP70 also associated with endoplasmic reticulum and the Golgi apparatus: does the "classic pathway" of glycosylation also apply to nuclear glycoproteins? J. Cell. Biochem. 78 (2000) 638-649.
    • (2000) J. Cell. Biochem. , vol.78 , pp. 638-649
    • Rousseau, C.1    Muriel, M.-P.2    Musset, M.3    Botti, J.4    Sève, A.-P.5
  • 49
    • 0038513916 scopus 로고    scopus 로고
    • Specificity of interactions of galectin-3 with Chrp, a cysteine- and histidine-rich cytoplasmic protein
    • Bawumia S., Barboni, E.A.M., Menon, R.P. and Hughes, R.C. Specificity of interactions of galectin-3 with Chrp, a cysteine- and histidine-rich cytoplasmic protein. Biochimie 85 (2003) 189-194.
    • (2003) Biochimie , vol.85 , pp. 189-194
    • Bawumia, S.1    Barboni, E.A.M.2    Menon, R.P.3    Hughes, R.C.4
  • 51
    • 0029027525 scopus 로고
    • Carcinoembryonic antigen and other glycoconjugates act as ligands for galectin-3 in human colon carcinoma cells
    • Ohannesian, D.W., Lotan, D., Thoman, P., Jessup, J.M., Fukuda, M., Gabius, H.J. and Lotan, R. Carcinoembryonic antigen and other glycoconjugates act as ligands for galectin-3 in human colon carcinoma cells. Cancer Res. 55 (1995) 2191-2199.
    • (1995) Cancer Res. , vol.55 , pp. 2191-2199
    • Ohannesian, D.W.1    Lotan, D.2    Thoman, P.3    Jessup, J.M.4    Fukuda, M.5    Gabius, H.J.6    Lotan, R.7
  • 52
    • 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
  • 53
    • 0029366113 scopus 로고
    • Identification of galectin 3 as a high affinity binding protein for advanced glycation end products (AGE): A new member of the AGE-receptor complex
    • Vlassara, H., Li, Y.M., Imani, F., Wojciechowicz, D., Yang, Z., Liu, F.T., and Cerami, A. Identification of galectin 3 as a high affinity binding protein for advanced glycation end products (AGE): a new member of the AGE-receptor complex. Mol. Med. 1 (1995) 634-646.
    • (1995) Mol. Med. , vol.1 , pp. 634-646
    • Vlassara, H.1    Li, Y.M.2    Imani, F.3    Wojciechowicz, D.4    Yang, Z.5    Liu, F.T.6    Cerami, A.7
  • 55
    • 0034813639 scopus 로고    scopus 로고
    • The role of galectin-3 in endocytosis of advanced glycation end products and modified low density lipoproteins
    • Zhu, W., Sano, H., Nagai, R., Fukuhara, K., Miyazaki, A., and Horiuchi, S. The role of galectin-3 in endocytosis of advanced glycation end products and modified low density lipoproteins. Biochem. Biophys. Res. Commun. 280 (2001) 1183-1188.
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 1183-1188
    • Zhu, W.1    Sano, H.2    Nagai, R.3    Fukuhara, K.4    Miyazaki, A.5    Horiuchi, S.6
  • 56
    • 0034685681 scopus 로고    scopus 로고
    • Galectin-3 overexpression protects from cell damage and death by influencing mitochondrial homeostasis
    • Matarrese, P., Tinari, N., Semeraro, M.L., Natoli, C., Iacobelli, S. and Malomi, W. Galectin-3 overexpression protects from cell damage and death by influencing mitochondrial homeostasis. FEBS Lett. 473 (2000) 311-315.
    • (2000) FEBS Lett. , vol.473 , pp. 311-315
    • Matarrese, P.1    Tinari, N.2    Semeraro, M.L.3    Natoli, C.4    Iacobelli, S.5    Malomi, W.6
  • 58
    • 0034855758 scopus 로고    scopus 로고
    • Galectin-3 protects human breast carcinoma cells against nitric oxide-induced apoptosis. Implication of galectin-3 function during metastasis
    • Moon, B.-K., Lee, Y.J., Battle, P., Jessup, J.M., Raz, A. and Kim, H.-R.C. Galectin-3 protects human breast carcinoma cells against nitric oxide-induced apoptosis. Implication of galectin-3 function during metastasis. Am. J. Pathol. 159 (2001) 1055-1060.
    • (2001) Am. J. Pathol. , vol.159 , pp. 1055-1060
    • Moon, B.-K.1    Lee, Y.J.2    Battle, P.3    Jessup, J.M.4    Raz, A.5    Kim, H.-R.C.6
  • 62
    • 0037013214 scopus 로고    scopus 로고
    • Galectin-3 translocates to the perinuclear membranes and inhibits cytochrome c release from the mitochondria. A role for synexin in galectin-3 translocation
    • Yu, F., Finley, R.L., Jr., Raz, A. and Kim, H.-R.C. Galectin-3 translocates to the perinuclear membranes and inhibits cytochrome c release from the mitochondria. A role for synexin in galectin-3 translocation. J. Biol. Chem. 277 (2002) 15819-15827.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15819-15827
    • Yu, F.1    Finley Jr., R.L.2    Raz, A.3    Kim, H.-R.C.4
  • 63
    • 0033566695 scopus 로고    scopus 로고
    • Cell cycle arrest and inhibition of anoikis by galectin-3 in human breast epithelial cells
    • Kim, H.-R.C., Lin, H.-M., Biliran, H. and Raz, A. Cell cycle arrest and inhibition of anoikis by galectin-3 in human breast epithelial cells. Cancer Res. 59 (1999) 4148-4154.
    • (1999) Cancer Res. , vol.59 , pp. 4148-4154
    • Kim, H.-R.C.1    Lin, H.-M.2    Biliran, H.3    Raz, A.4
  • 64
    • 0033736730 scopus 로고    scopus 로고
    • Galectin-3 mediates genistein-induced G2/M arrest and inhibits apoptosis
    • Lin, H.-M., Moon, B.-K., Yu, F. and Kim, H.-R.C. Galectin-3 mediates genistein-induced G2/M arrest and inhibits apoptosis. Carcinogenesis 21 (2000) 1941-1945.
    • (2000) Carcinogenesis , vol.21 , pp. 1941-1945
    • Lin, H.-M.1    Moon, B.-K.2    Yu, F.3    Kim, H.-R.C.4
  • 66
    • 0028855759 scopus 로고
    • Identification of galectin-3 as a factor in pre-mRNA splicing
    • Dagher, S.F., Wang, J.L. and Patterson, R.J. Identification of galectin-3 as a factor in pre-mRNA splicing. Proc. Natl. Acad. Sci. USA 92 (1995) 1213-1217.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1213-1217
    • Dagher, S.F.1    Wang, J.L.2    Patterson, R.J.3
  • 67
    • 18744394603 scopus 로고    scopus 로고
    • 1 promoter activity through SP1 and a cAMP-responsive element in human breast epithelial cells
    • 1 promoter activity through SP1 and a cAMP-responsive element in human breast epithelial cells. Oncogene 21 (2002) 8001-8010.
    • (2002) Oncogene , vol.21 , pp. 8001-8010
    • Lin, H.-M.1    Pestell, R.G.2    Raz, A.3    Kim, H.-R.C.4
  • 68
    • 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
  • 69
    • 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
  • 72
    • 0033151803 scopus 로고    scopus 로고
    • Expression of galectin-3 in fine-needle aspirates as a diagnostic marker differentiating benign from malignant thyroid neoplasms
    • Inohara, H., Honjo, Y., Yoshii, T., Akahani, S., Yoshida, J., Hattori, K., Okamoto, S., Sawada, T., Raz, A. and Kubo, T. Expression of galectin-3 in fine-needle aspirates as a diagnostic marker differentiating benign from malignant thyroid neoplasms. Cancer 85 (1999) 2475-2484.
    • (1999) Cancer , vol.85 , pp. 2475-2484
    • Inohara, H.1    Honjo, Y.2    Yoshii, T.3    Akahani, S.4    Yoshida, J.5    Hattori, K.6    Okamoto, S.7    Sawada, T.8    Raz, A.9    Kubo, T.10
  • 73
    • 0034495038 scopus 로고    scopus 로고
    • Galectin-3 and carcinoembryonic antigen expression in medullary thyroid carcinoma: Possible relation to tumour progression
    • Cvejic, D., Savin, S., Golubovic, S., Paunovic, I., Tatic, S. and Havelka, M. Galectin-3 and carcinoembryonic antigen expression in medullary thyroid carcinoma: possible relation to tumour progression. Histopathology 37 (2000) 530-535.
    • (2000) Histopathology , vol.37 , pp. 530-535
    • Cvejic, D.1    Savin, S.2    Golubovic, S.3    Paunovic, I.4    Tatic, S.5    Havelka, M.6
  • 77
    • 0036156211 scopus 로고    scopus 로고
    • Galectin-3 a marker of well-differentiated thyroid carcinoma, is expressed in thyroid nodules with cytological atypia
    • Coli, A., Bigotti, G., Zuchetti, F., Negro, F. and Massi, G. Galectin-3, a marker of well-differentiated thyroid carcinoma, is expressed in thyroid nodules with cytological atypia. Histopathology 40 (2002) 80-87.
    • (2002) Histopathology , vol.40 , pp. 80-87
    • Coli, A.1    Bigotti, G.2    Zuchetti, F.3    Negro, F.4    Massi, G.5
  • 82
    • 0032963712 scopus 로고    scopus 로고
    • Galectin-3 expression is induced in cirrhotic liver and hepatocellular carcinoma
    • Hsu, D.K., Dowling, C.A., Jeng, K.-C.G., Chen, J.-T., Yang, R.-Y. and Liu, F.-T. Galectin-3 expression is induced in cirrhotic liver and hepatocellular carcinoma. Int. J. Cancer 81 (1999) 519-526.
    • (1999) Int. J. Cancer , vol.81 , pp. 519-526
    • Hsu, D.K.1    Dowling, C.A.2    Jeng, K.-C.G.3    Chen, J.-T.4    Yang, R.-Y.5    Liu, F.-T.6
  • 84
    • 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, C.W. Jr., Korzelius, C.A., Lee, E.C., Steele, G.D. Jr., 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
  • 86
    • 0029073986 scopus 로고
    • Expression of an endogenous galactose-binding lectin correlates with neoplastic progression in the colon
    • Schoeppner, H.L., Raz, A., Ho, S.B. and Bresalier, R.S. Expression of an endogenous galactose-binding lectin correlates with neoplastic progression in the colon. Cancer 75 (1995) 2818-2826.
    • (1995) Cancer , vol.75 , pp. 2818-2826
    • Schoeppner, H.L.1    Raz, A.2    Ho, S.B.3    Bresalier, R.S.4
  • 89
    • 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., Nangia-Makker, P. 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    Nangia-Makker, P.6    Raz, A.7
  • 90
    • 0036727315 scopus 로고    scopus 로고
    • Expression of human intestinal mucin is modulated by the β-galactoside binding protein galectin-3 in colon cancer
    • Dudas, S.P., Yunker, C.K., Sternberg, L.R., Byrd, J.C. and Bresalier, R.S. Expression of human intestinal mucin is modulated by the β-galactoside binding protein galectin-3 in colon cancer. Gastroenterology 123 (2002) 817-826.
    • (2002) Gastroenterology , vol.123 , pp. 817-826
    • Dudas, S.P.1    Yunker, C.K.2    Sternberg, L.R.3    Byrd, J.C.4    Bresalier, R.S.5
  • 92
    • 0031866263 scopus 로고    scopus 로고
    • Galectin-3 expression in human breast carcinoma: Correlation with cancer histologic grade
    • Idikio, H. Galectin-3 expression in human breast carcinoma: correlation with cancer histologic grade. Int. J. Oncol. 12 (1998) 1287-1290.
    • (1998) Int. J. Oncol. , vol.12 , pp. 1287-1290
    • Idikio, H.1
  • 93
    • 0034904150 scopus 로고    scopus 로고
    • Down-regulation of galectin-3 suppresses tumorigenecity of human breast carcinoma cells
    • Honjo, Y., Nangia-Makker, P., Inohara, H. and Raz, A. Down-regulation of galectin-3 suppresses tumorigenecity of human breast carcinoma cells. Clin. Cancer Res. 7 (2001) 661-668.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 661-668
    • Honjo, Y.1    Nangia-Makker, P.2    Inohara, H.3    Raz, A.4
  • 94
    • 0036118467 scopus 로고    scopus 로고
    • Role of galectin-3 in breast cancer metastasis. Involvement of nitric oxide
    • Song, Y.K., Billiar, T.R. and Lee, Y.J. Role of galectin-3 in breast cancer metastasis. Involvement of nitric oxide. Am. J. Pathol. 160 (2002) 1069-1075.
    • (2002) Am. J. Pathol. , vol.160 , pp. 1069-1075
    • Song, Y.K.1    Billiar, T.R.2    Lee, Y.J.3
  • 95
    • 0032719687 scopus 로고    scopus 로고
    • Galectin-1 and galectin-3 expression in human prostate tissue and prostate cancer
    • Ellerhorst, J., Troncoso, P., Xu, X.C., Lee, J. and Lotan, R. Galectin-1 and galectin-3 expression in human prostate tissue and prostate cancer. Urol. Res. 27 (1999) 362-367.
    • (1999) Urol. Res. , vol.27 , pp. 362-367
    • Ellerhorst, J.1    Troncoso, P.2    Xu, X.C.3    Lee, J.4    Lotan, R.5
  • 97
    • 0343962593 scopus 로고    scopus 로고
    • Alteration of the cytoplasmic/nuclear expression pattern of galectin-3 correlates with prostate carcinoma progression
    • Van den Brûle, 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 Brûle, F.A.1    Waltregny, D.2    Liu, F.-T.3    Castronovo, V.4
  • 98
    • 0033404665 scopus 로고    scopus 로고
    • The levels of expression of galectin-1, galectin-3, and the Thomsen-Friedenreich antigen and their binding sites decrease as clinical aggressiveness increases in head and neck cancers
    • Choufani, G., Nagy, N., Saussez, S., Marchant, H., Bisschop, P., Burchert, M., Danguy, A., Louryan, S., Salmon, I., Gabius, H.-J., Kiss, R. and Hassid, S. The levels of expression of galectin-1, galectin-3, and the Thomsen-Friedenreich antigen and their binding sites decrease as clinical aggressiveness increases in head and neck cancers. Cancer 86 (1999) 2353-2363.
    • (1999) Cancer , vol.86 , pp. 2353-2363
    • Choufani, G.1    Nagy, N.2    Saussez, S.3    Marchant, H.4    Bisschop, P.5    Burchert, M.6    Danguy, A.7    Louryan, S.8    Salmon, I.9    Gabius, H.-J.10    Kiss, R.11    Hassid, S.12
  • 100
    • 0037223020 scopus 로고    scopus 로고
    • Characterization of the levels of expression of retinoic acid receptors, galectin-3, macrophage migration inhibiting factor, and p53 in 51 adamantinomatous craniopharyngiomas
    • Lefranc, F., Chevalier, C., Vinchon, M., Dhellemmes, P., Schüring, M.-P., Kaltner, H., Brotchi, J., Ruchoux, M.-M., Gabius, H.-J., Salmon, I. and Kiss, R. Characterization of the levels of expression of retinoic acid receptors, galectin-3, macrophage migration inhibiting factor, and p53 in 51 adamantinomatous craniopharyngiomas. J. Neurosurg. 98 (2003) 145-153.
    • (2003) J. Neurosurg. , vol.98 , pp. 145-153
    • Lefranc, F.1    Chevalier, C.2    Vinchon, M.3    Dhellemmes, P.4    Schüring, M.-P.5    Kaltner, H.6    Brotchi, J.7    Ruchoux, M.-M.8    Gabius, H.-J.9    Salmon, I.10    Kiss, R.11
  • 103
    • 0030872450 scopus 로고    scopus 로고
    • Expression of the endogenous galactose-binding protein galectin-3 correlates with the malignant potential of tumors in the central nervous system
    • Bresalier, R.S., Yan, P.-S., Byrd, J.C., Lotan, R. and Raz, A. Expression of the endogenous galactose-binding protein galectin-3 correlates with the malignant potential of tumors in the central nervous system. Cancer 80 (1997) 776-787.
    • (1997) Cancer , vol.80 , pp. 776-787
    • Bresalier, R.S.1    Yan, P.-S.2    Byrd, J.C.3    Lotan, R.4    Raz, A.5
  • 105


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.