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Volumn 15, Issue 7, 2005, Pages 709-720

Xenopus galectin-VIIa binds N-glycans of members of the cortical granule lectin family (xCGL and xCGL2)

Author keywords

Cortical granule lectin; Galectin; N acetyllac tosamine; N glycan; Xenopus

Indexed keywords

CORTICAL GRANULE LECTIN; CORTICAL GRANULE LECTIN 2; GALECTIN 3; GALECTIN 7; GALECTIN 7A; GLYCAN; GLYCOPROTEIN; LECTIN; MESSENGER RNA; OLIGOSACCHARIDE; UNCLASSIFIED DRUG;

EID: 26444556521     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwi051     Document Type: Article
Times cited : (13)

References (50)
  • 1
    • 0142135856 scopus 로고    scopus 로고
    • Determination of N-glycosylation sites and site heterogeneity in glycoproteins
    • An, H.J., Peavy, T.R., Hedrick, J.L., and Lebrilla, C.B. (2003) Determination of N-glycosylation sites and site heterogeneity in glycoproteins. Anal. Chem., 75, 5628-5637.
    • (2003) Anal. Chem. , vol.75 , pp. 5628-5637
    • An, H.J.1    Peavy, T.R.2    Hedrick, J.L.3    Lebrilla, C.B.4
  • 3
    • 0027965708 scopus 로고
    • Galectins. Structure and function of a large family of animal lectins
    • Barondes, S.H., Cooper, D.N., Gitt, M.A., and Leffler, H. (1994b) Galectins. Structure and function of a large family of animal lectins. J. Biol. Chem., 269, 20807-20810.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20807-20810
    • Barondes, S.H.1    Cooper, D.N.2    Gitt, M.A.3    Leffler, H.4
  • 4
    • 0035119957 scopus 로고    scopus 로고
    • Galectin-3 modulates ureteric bud branching in organ culture of the developing mouse kidney
    • Bullock, S.L., Johnson, T.M., Bao, Q., Hughes, R.C., Winyard, P.J., and Woolf, A.S. (2001) Galectin-3 modulates ureteric bud branching in organ culture of the developing mouse kidney. J. Am. Soc. Nephrol., 12, 515-523.
    • (2001) J. Am. Soc. Nephrol. , vol.12 , pp. 515-523
    • Bullock, S.L.1    Johnson, T.M.2    Bao, Q.3    Hughes, R.C.4    Winyard, P.J.5    Woolf, A.S.6
  • 5
    • 0023043503 scopus 로고
    • Subunit structure of a cortical granule lectin involved in the block to polyspermy in Xenopus laevis eggs
    • Chamow, S.M. and Hedrick, J.L. (1986) Subunit structure of a cortical granule lectin involved in the block to polyspermy in Xenopus laevis eggs. FEBS Lett., 206, 353-357.
    • (1986) FEBS Lett. , vol.206 , pp. 353-357
    • Chamow, S.M.1    Hedrick, J.L.2
  • 6
    • 0347285250 scopus 로고    scopus 로고
    • The Xenopus laevis cortical granule lectin: cDNA cloning, developmental expression, and identification of the eglectin family of lectins
    • Chang, B.Y., Peavy, T.R., Wardrip, N.J., and Hedrick, J.L. (2004) The Xenopus laevis cortical granule lectin: CDNA cloning, developmental expression, and identification of the eglectin family of lectins. Comp. Biochem. Physiol. A Mol. Integr. Physiol., 137, 115-129.
    • (2004) Comp. Biochem. Physiol. A Mol. Integr. Physiol. , vol.137 , pp. 115-129
    • Chang, B.Y.1    Peavy, T.R.2    Wardrip, N.J.3    Hedrick, J.L.4
  • 8
    • 0031850611 scopus 로고    scopus 로고
    • Maintenance of granulocyte numbers during acute peritonitis is defective in galectin-3-null mutant mice
    • Colnot, C., Ripoche, M.A., Milon, G., Montagutelli, X., Crocker, P.R., and Poirier, F. (1998) Maintenance of granulocyte numbers during acute peritonitis is defective in galectin-3-null mutant mice. Immunology 94, 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
  • 9
    • 0035174596 scopus 로고    scopus 로고
    • Uncoupling of chondrocyte death and vascular invasion in mouse galectin 3 null mutant bones
    • Colnot, C., Sidhu, S.S., Balmain, N., and Poirier, F. (2001) Uncoupling of chondrocyte death and vascular invasion in mouse galectin 3 null mutant bones. Dev. Biol., 229, 203-214.
    • (2001) Dev. Biol. , vol.229 , pp. 203-214
    • Colnot, C.1    Sidhu, S.S.2    Balmain, N.3    Poirier, F.4
  • 10
    • 0032875554 scopus 로고    scopus 로고
    • God must love galectins; he made so many of them
    • Cooper, D.N. and Barondes, S.H. (1999) God must love galectins; he made so many of them. Glycobiology, 9, 979-984.
    • (1999) Glycobiology , vol.9 , pp. 979-984
    • Cooper, D.N.1    Barondes, S.H.2
  • 13
    • 0037177843 scopus 로고    scopus 로고
    • Isolation and characterization of a novel eosinophil-specific galectin released into the lungs in response to allergen challenge
    • Epub. February 11
    • Dunphy, J.L., Barcham, G.J., Bischof, R.J., Young, A.R., Nash, A., and Meeusen, E.N. (2002) Isolation and characterization of a novel eosinophil-specific galectin released into the lungs in response to allergen challenge. J. Biol. Chem., 277, 14916-14924. Epub. February 11, 2002.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14916-14924
    • Dunphy, J.L.1    Barcham, G.J.2    Bischof, R.J.3    Young, A.R.4    Nash, A.5    Meeusen, E.N.6
  • 14
    • 0037136405 scopus 로고    scopus 로고
    • The mannose receptor family
    • East, L. and Isacke, C.M. (2002) The mannose receptor family. Biochim. Biophys. Acta, 1572, 364-386.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 364-386
    • East, L.1    Isacke, C.M.2
  • 15
    • 0029991817 scopus 로고    scopus 로고
    • A monoclonal antibody against neural crest-stage Xenopus laevis lectin perturbs craniofacial development of Xenopus
    • Evanson, J.E. and Milos, N.C. (1996) A monoclonal antibody against neural crest-stage Xenopus laevis lectin perturbs craniofacial development of Xenopus. J. Craniofac. Genet. Dev. Biol., 16, 74-93.
    • (1996) J. Craniofac. Genet. Dev. Biol. , vol.16 , pp. 74-93
    • Evanson, J.E.1    Milos, N.C.2
  • 16
    • 0028998657 scopus 로고
    • Galectin-3 is expressed in the notochord, developing bones, and skin of the postimplantation mouse embryo
    • Fowlis, D., Colnot, C., Ripoche, M.A., and Poirier, F. (1995) Galectin-3 is expressed in the notochord, developing bones, and skin of the postimplantation mouse embryo. Dev. Dyn., 203, 241-251.
    • (1995) Dev. Dyn. , vol.203 , pp. 241-251
    • Fowlis, D.1    Colnot, C.2    Ripoche, M.A.3    Poirier, F.4
  • 17
    • 0027159256 scopus 로고
    • Alterations of heart development in Xenopus laevis by galactoside-binding lectin or its sugar hapten inhibitor
    • Frunchak, Y.N., Martha, G.N., McFadden, K.D., and Milos, N.C. (1993) Alterations of heart development in Xenopus laevis by galactoside-binding lectin or its sugar hapten inhibitor. Anat. Embryol. (Berl), 187, 299-316.
    • (1993) Anat. Embryol. (Berl.) , vol.187 , pp. 299-316
    • Frunchak, Y.N.1    Martha, G.N.2    McFadden, K.D.3    Milos, N.C.4
  • 19
    • 0031467569 scopus 로고    scopus 로고
    • Detection and distribution of the carbohydrate binding protein galectin-3 in human notochord, intervertebral disc and chordoma
    • Gotz, W., Kasper, M., Miosge, N., and Hughes, R.C. (1997) Detection and distribution of the carbohydrate binding protein galectin-3 in human notochord, intervertebral disc and chordoma. Differentiation, 62, 149-157.
    • (1997) Differentiation , vol.62 , pp. 149-157
    • Gotz, W.1    Kasper, M.2    Miosge, N.3    Hughes, R.C.4
  • 20
    • 0028207949 scopus 로고
    • High-performance liquid chromatography of pyridylaminated saccharides
    • Hase, S. (1994) High-performance liquid chromatography of pyridylaminated saccharides. Methods Enzymol., 230, 225-237.
    • (1994) Methods Enzymol. , vol.230 , pp. 225-237
    • Hase, S.1
  • 21
    • 0021308647 scopus 로고
    • Reexamination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins
    • Hase, S., Ibuki, T., and Ikenaka, T. (1984) Reexamination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins. J. Biochem. (Tokyo), 95, 197-203.
    • (1984) J. Biochem. (Tokyo) , vol.95 , pp. 197-203
    • Hase, S.1    Ibuki, T.2    Ikenaka, T.3
  • 22
    • 0018163581 scopus 로고
    • Structure analyses of oligosaccharides by tagging of the reducing end sugars with a fluorescent compound
    • Hase, S., Ikenaka, T., and Matsushima, Y. (1978) Structure analyses of oligosaccharides by tagging of the reducing end sugars with a fluorescent compound. Biochem. Biophys. Res. Commun., 85, 257-263.
    • (1978) Biochem. Biophys. Res. Commun. , vol.85 , pp. 257-263
    • Hase, S.1    Ikenaka, T.2    Matsushima, Y.3
  • 24
    • 0036651817 scopus 로고    scopus 로고
    • Affinity capturing and gene assignment of soluble glycoproteins produced by the nematode Caenorhabditis elegans
    • Hirabayashi, J., Hayama, K., Kaji, H., Isobe, T., and Kasai, K. (2002b) Affinity capturing and gene assignment of soluble glycoproteins produced by the nematode Caenorhabditis elegans. J. Biochem. (Tokyo), 132, 103-114.
    • (2002) J. Biochem. (Tokyo) , vol.132 , pp. 103-114
    • Hirabayashi, J.1    Hayama, K.2    Kaji, H.3    Isobe, T.4    Kasai, K.5
  • 25
    • 0033870111 scopus 로고    scopus 로고
    • Targeted disruption of the galectin-3 gene results in attenuated peritoneal inflammatory responses
    • Hsu, D.K., Yang, R.Y., Pan, Z., Yu, L., Salomon, D.R., Fung-Leung, W.P., and Liu, F.T. (2000) Targeted disruption of the galectin-3 gene results in attenuated peritoneal inflammatory responses. Am. J. Pathol., 156, 1073-1083.
    • (2000) Am. J. Pathol. , vol.156 , pp. 1073-1083
    • Hsu, D.K.1    Yang, R.Y.2    Pan, Z.3    Yu, L.4    Salomon, D.R.5    Fung-Leung, W.P.6    Liu, F.T.7
  • 26
    • 0034851982 scopus 로고    scopus 로고
    • Galectins as modulators of cell adhesion
    • Hughes, R.C. (2001) Galectins as modulators of cell adhesion. Biochimie, 83, 667-676.
    • (2001) Biochimie , vol.83 , pp. 667-676
    • Hughes, R.C.1
  • 27
    • 1542343884 scopus 로고    scopus 로고
    • Galectins in kidney development
    • Hughes, R.C. (2004) Galectins in kidney development. Glycoconj. J. 19, 621-629.
    • (2004) Glycoconj. J. , vol.19 , pp. 621-629
    • Hughes, R.C.1
  • 28
    • 0030064027 scopus 로고    scopus 로고
    • Galectins: A family of animal lectins that decipher glycocodes
    • Kasai, K. and Hirabayashi, J. (1996) Galectins: A family of animal lectins that decipher glycocodes. J. Biochem. (Tokyo), 119, 1-8.
    • (1996) J. Biochem. (Tokyo) , vol.119 , pp. 1-8
    • Kasai, K.1    Hirabayashi, J.2
  • 29
    • 0037136419 scopus 로고    scopus 로고
    • Animal lectins: A historical introduction and overview
    • Kilpatrick, D.C. (2002) Animal lectins: A historical introduction and overview. Biochim. Biophys. Acta, 1572, 187-197.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 187-197
    • Kilpatrick, D.C.1
  • 30
    • 0030895387 scopus 로고    scopus 로고
    • Cloning and expression of a Xenopus laevis oocyte lectin and characterization of its mRNA levels during early development
    • Lee, J.K., Buckhaults, P., Wilkes, C., Teilhet, M., King, M.L., Moremen, K.W., and Pierce, M. (1997) Cloning and expression of a Xenopus laevis oocyte lectin and characterization of its mRNA levels during early development. Glycobiology, 7, 367-372.
    • (1997) Glycobiology , vol.7 , pp. 367-372
    • Lee, J.K.1    Buckhaults, P.2    Wilkes, C.3    Teilhet, M.4    King, M.L.5    Moremen, K.W.6    Pierce, M.7
  • 31
    • 0025321165 scopus 로고
    • Binding characteristics of galactoside-binding lectin (galaptin) from human spleen
    • Lee, R.T., Ichikawa, Y., Allen, H.J., and Lee, Y.C. (1990) Binding characteristics of galactoside-binding lectin (galaptin) from human spleen. J. Biol. Chem., 265, 7864-7871.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7864-7871
    • Lee, R.T.1    Ichikawa, Y.2    Allen, H.J.3    Lee, Y.C.4
  • 32
    • 0025906415 scopus 로고
    • Ligand-binding characteristics of rat serum-type mannose-binding protein (MBP-A). Homology of binding site architecture with mammalian and chicken hepatic lectins
    • Lee, R.T., Ichikawa, Y., Fay, M., Drickamer, K., Shao, M.C., and Lee, Y.C. (1991) Ligand-binding characteristics of rat serum-type mannose-binding protein (MBP-A). Homology of binding site architecture with mammalian and chicken hepatic lectins. J. Biol. Chem., 266 4810-4815.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4810-4815
    • Lee, R.T.1    Ichikawa, Y.2    Fay, M.3    Drickamer, K.4    Shao, M.C.5    Lee, Y.C.6
  • 33
    • 0021772463 scopus 로고
    • New synthetic cluster ligands for galactose/N-acetylgalactosamine-specific lectin of mammalian liver
    • Lee, R.T., Lin, P., and Lee, Y.C. (1984) New synthetic cluster ligands for galactose/N-acetylgalactosamine-specific lectin of mammalian liver. Biochemistry, 23, 4255-4261.
    • (1984) Biochemistry , vol.23 , pp. 4255-4261
    • Lee, R.T.1    Lin, P.2    Lee, Y.C.3
  • 34
    • 0024418546 scopus 로고
    • Binding characteristics of N-acetylglucosamine-specific lectin of the isolated chicken hepatocytes: Similarities to mammalian hepatic galactose/N-acetylgalactosamine-specific lectin
    • Lee, R.T., Rice, K.G., Rao, N.B., Ichikawa, Y., Barthel, T., Piskarev, V., and Lee, Y.C. (1989) Binding characteristics of N-acetylglucosamine-specific lectin of the isolated chicken hepatocytes: similarities to mammalian hepatic galactose/ N-acetylgalactosamine-specific lectin. Biochemistry, 28, 8351-8358.
    • (1989) Biochemistry , vol.28 , pp. 8351-8358
    • Lee, R.T.1    Rice, K.G.2    Rao, N.B.3    Ichikawa, Y.4    Barthel, T.5    Piskarev, V.6    Lee, Y.C.7
  • 37
    • 0043135100 scopus 로고    scopus 로고
    • Developmental expression of XEEL, a novel molecule of the Xenopus oocyte cortical granule lectin family
    • Epub. June 07
    • Nagata, S., Nakanishi, M., Nanba, R., and Fujita, N. (2003) Developmental expression of XEEL, a novel molecule of the Xenopus oocyte cortical granule lectin family. Dev. Genes Evol., 213 368-370. Epub. June 07, 2003.
    • (2003) Dev. Genes Evol. , vol.213 , pp. 368-370
    • Nagata, S.1    Nakanishi, M.2    Nanba, R.3    Fujita, N.4
  • 38
    • 0023044272 scopus 로고
    • Isolation and characterization of a lectin from the cortical granules of Xenopus laevis eggs
    • Nishihara, T., Wyrick, R.E., Working, P.K., Chen, Y.H., and Hedrick, J.L. (1986) Isolation and characterization of a lectin from the cortical granules of Xenopus laevis eggs. Biochemistry, 25, 6013-6020.
    • (1986) Biochemistry , vol.25 , pp. 6013-6020
    • Nishihara, T.1    Wyrick, R.E.2    Working, P.K.3    Chen, Y.H.4    Hedrick, J.L.5
  • 40
    • 0023907086 scopus 로고
    • Endogenous lectin secretion into the extracellular matrix of early embryos of Xenopus laevis
    • Outenreath, R.L., Roberson, M.M., and Barondes, S.H. (1988) Endogenous lectin secretion into the extracellular matrix of early embryos of Xenopus laevis. Dev. Biol., 125, 187-194.
    • (1988) Dev. Biol. , vol.125 , pp. 187-194
    • Outenreath, R.L.1    Roberson, M.M.2    Barondes, S.H.3
  • 41
    • 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. (1998) Galectins: Versatile modulators of cell adhesion, cell proliferation, and cell death. J. Mol. Med., 76, 402-412.
    • (1998) J. Mol. Med. , vol.76 , pp. 402-412
    • Perillo, N.L.1    Marcus, M.E.2    Baum, L.G.3
  • 42
    • 0030587536 scopus 로고    scopus 로고
    • The fertilization layer mediated block to polyspermy in Xenopus laevis: Isolation of the cortical granule lectin ligand
    • Quill, T.A. and Hedrick, J.L. (1996) The fertilization layer mediated block to polyspermy in Xenopus laevis: Isolation of the cortical granule lectin ligand. Arch. Biochem. Biophys., 333, 326-332.
    • (1996) Arch. Biochem. Biophys. , vol.333 , pp. 326-332
    • Quill, T.A.1    Hedrick, J.L.2
  • 43
    • 0036265373 scopus 로고    scopus 로고
    • Purification and cDNA cloning of Xenopus liver galectins and their expression
    • Shoji, H., Nishi, N., Hirashima, M., and Nakamura, T. (2002) Purification and cDNA cloning of Xenopus liver galectins and their expression. Glycobiology, 12, 163-172.
    • (2002) Glycobiology , vol.12 , pp. 163-172
    • Shoji, H.1    Nishi, N.2    Hirashima, M.3    Nakamura, T.4
  • 44
    • 0038146931 scopus 로고    scopus 로고
    • Characterization of the Xenopus galectin family. Three structurally different types as in mammals and regulated expression during embryogenesis
    • Epub. January 21
    • Shoji, H., Nishi, N., Hirashima, M., and Nakamura, T. (2003) Characterization of the Xenopus galectin family. Three structurally different types as in mammals and regulated expression during embryogenesis. J. Biol. Chem., 278, 12285-12293. Epub. January 21, 2003.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12285-12293
    • Shoji, H.1    Nishi, N.2    Hirashima, M.3    Nakamura, T.4
  • 45
    • 0035660192 scopus 로고    scopus 로고
    • Homology modelling and molecular dynamics studies of human placental tissue protein 13 (galectin-13)
    • Visegrady, B., Than, N.G., Kilar, F., Sumegi, B., Than, G.N., and Bohn, H. (2001) Homology modelling and molecular dynamics studies of human placental tissue protein 13 (galectin-13). Protein Eng, 14, 875-880.
    • (2001) Protein Eng. , vol.14 , pp. 875-880
    • Visegrady, B.1    Than, N.G.2    Kilar, F.3    Sumegi, B.4    Than, G.N.5    Bohn, H.6
  • 46
    • 0037136420 scopus 로고    scopus 로고
    • Glycans as endocytosis signals: The cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors
    • Weigel, P.H., and Yik, J.H. (2002) Glycans as endocytosis signals: The cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors. Biochim. Biophys. Acta, 1572, 341-363.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 341-363
    • Weigel, P.H.1    Yik, J.H.2
  • 47
    • 0030695974 scopus 로고    scopus 로고
    • Epithelial galectin-3 during human nephrogenesis and childhood cystic diseases
    • Winyard, P.J., Bao, Q., Hughes, R.C., and Woolf, A.S. (1997) Epithelial galectin-3 during human nephrogenesis and childhood cystic diseases. J. Am. Soc. Nephrol., 8, 1647-1657.
    • (1997) J. Am. Soc. Nephrol. , vol.8 , pp. 1647-1657
    • Winyard, P.J.1    Bao, Q.2    Hughes, R.C.3    Woolf, A.S.4
  • 48
    • 0033570084 scopus 로고    scopus 로고
    • The early expression control of Xepsin by nonaxial and planar posteriorizing signals in Xenopus epidermis
    • Yamada, K., Takabatake, Y., Takabatake, T., and Takeshima, K. (1999) The early expression control of Xepsin by nonaxial and planar posteriorizing signals in Xenopus epidermis. Dev. Biol., 214, 318-330.
    • (1999) Dev. Biol. , vol.214 , pp. 318-330
    • Yamada, K.1    Takabatake, Y.2    Takabatake, T.3    Takeshima, K.4
  • 49
    • 0032571438 scopus 로고    scopus 로고
    • Introduction of a new scale into reversed-phase high-performance liquid chromatography of pyridylamino sugar chains for structural assignment
    • Yanagida, K., Ogawa, H., Omichi, K., and Hase, S. (1998) Introduction of a new scale into reversed-phase high-performance liquid chromatography of pyridylamino sugar chains for structural assignment. J. Chromatogr. A, 800, 187-198.
    • (1998) J. Chromatogr. A , vol.800 , pp. 187-198
    • Yanagida, K.1    Ogawa, H.2    Omichi, K.3    Hase, S.4
  • 50
    • 0035827555 scopus 로고    scopus 로고
    • Cell cycle regulation by galectin-12, a new member of the galectin superfamily
    • Yang, R.Y., Hsu, D.K., Yu, L., Ni, J., and Liu, F.T. (2001) Cell cycle regulation by galectin-12, a new member of the galectin superfamily. J. Biol. Chem., 276, 20252-20260.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20252-20260
    • Yang, R.Y.1    Hsu, D.K.2    Yu, L.3    Ni, J.4    Liu, F.T.5


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