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Volumn 19, Issue 3, 2006, Pages 469-474

Characterization of the interaction of galectin-1 with sodium arsenite

Author keywords

[No Author keywords available]

Indexed keywords

ARSENIC; ARSENITE SODIUM; CELL EXTRACT; GALECTIN 1; TRYPTOPHAN;

EID: 33645472232     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx0503348     Document Type: Article
Times cited : (17)

References (39)
  • 2
    • 0025171686 scopus 로고
    • Ecological correlation between arsenic level in well water and age-adjusted mortality from malignant neoplasms
    • Chen, C. J., and Wang, C. J. (1990) Ecological correlation between arsenic level in well water and age-adjusted mortality from malignant neoplasms. Cancer Res. 50, 5470-5474.
    • (1990) Cancer Res. , vol.50 , pp. 5470-5474
    • Chen, C.J.1    Wang, C.J.2
  • 3
    • 3242787337 scopus 로고    scopus 로고
    • Inhibition of insulin-dependent glucose uptake by trivalent arsenicals: Possible mechanism of arsenic-induced diabetes
    • Walton, F. S., Harmon, A. W., Paul, D. S., Drobna, Z., Patel, Y. M., and Styblo, M. (2004) Inhibition of insulin-dependent glucose uptake by trivalent arsenicals: possible mechanism of arsenic-induced diabetes. Toxicol. Appl. Pharmacol. 198, 424-433.
    • (2004) Toxicol. Appl. Pharmacol. , vol.198 , pp. 424-433
    • Walton, F.S.1    Harmon, A.W.2    Paul, D.S.3    Drobna, Z.4    Patel, Y.M.5    Styblo, M.6
  • 4
    • 2442465761 scopus 로고    scopus 로고
    • The potential biological mechanisms of arsenic-induced diabetes mellitus
    • Tseng, C. H. (2004) The potential biological mechanisms of arsenic-induced diabetes mellitus. Toxicol. Appl. Pharmacol. 197, 67-83.
    • (2004) Toxicol. Appl. Pharmacol. , vol.197 , pp. 67-83
    • Tseng, C.H.1
  • 7
    • 0021866516 scopus 로고
    • Reduction and binding of arsenate in marmoset monkeys
    • Vahter, M., and Marafante, E. (1985) Reduction and binding of arsenate in marmoset monkeys. Arch. Toxicol. 57, 119-124.
    • (1985) Arch. Toxicol. , vol.57 , pp. 119-124
    • Vahter, M.1    Marafante, E.2
  • 8
    • 0026684913 scopus 로고
    • Metal carcinogenesis: Mechanistic implications
    • Snow, E. T. (1992) Metal carcinogenesis: mechanistic implications. Pharmacol. Ther. 53, 31-65.
    • (1992) Pharmacol. Ther. , vol.53 , pp. 31-65
    • Snow, E.T.1
  • 9
    • 0034680928 scopus 로고    scopus 로고
    • Inhibition of NF-kB activation by arsenite through reaction with a critical cysteine in the activation loop of IkB kinase
    • Kapahi, P., Takahashi, T., Natoli, G., Adams, S. R., Chen, Y., Tsien, R. Y., and Karin, M. (2000) Inhibition of NF-kB activation by arsenite through reaction with a critical cysteine in the activation loop of IkB kinase. J. Biol. Chem. 275, 36062-36066.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36062-36066
    • Kapahi, P.1    Takahashi, T.2    Natoli, G.3    Adams, S.R.4    Chen, Y.5    Tsien, R.Y.6    Karin, M.7
  • 10
    • 0027965708 scopus 로고
    • Galectins, Structure and function of a large family of animal lectins
    • Barondes, S. H., Cooper, D. N., Gill, M. A., and Leffler, H. (1994) 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    Gill, M.A.3    Leffler, H.4
  • 11
    • 0027169990 scopus 로고
    • The family of metazoan metal-independent beta-galactoside-binding lectins: Structure, function and molecular evolution
    • Hirabayashi, J., and Kasai, K. (1993) The family of metazoan metal-independent beta-galactoside-binding lectins: structure, function and molecular evolution. Glycobiology 3, 297-304.
    • (1993) Glycobiology , vol.3 , pp. 297-304
    • Hirabayashi, J.1    Kasai, K.2
  • 12
    • 0018354527 scopus 로고
    • Vertebrate lectins. Comparison of properties of β-galactoside- binding lectins from tissues of calf and chicken
    • Briles, E. B., Gregory, W., Fletcher, P., and Kornfeld, S. (1979) Vertebrate lectins. Comparison of properties of β-galactoside-binding lectins from tissues of calf and chicken. J. Cell Biol. 81, 528-537.
    • (1979) J. Cell Biol. , vol.81 , pp. 528-537
    • Briles, E.B.1    Gregory, W.2    Fletcher, P.3    Kornfeld, S.4
  • 13
    • 0027162467 scopus 로고
    • L-14 lectin recognition of laminin and its promotion of in vitro cell adhesion
    • Zhou, Q., and Cummings, R. D. (1993) L-14 lectin recognition of laminin and its promotion of in vitro cell adhesion. Arch. Biochem. Biophys. 300, 6-17.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 6-17
    • Zhou, Q.1    Cummings, R.D.2
  • 14
    • 0025786162 scopus 로고
    • Endogenous muscle lectin inhibits myoblast adhesion to laminin
    • Cooper, D. N., Massa, S. M., and Barondes, S. H. (1991) Endogenous muscle lectin inhibits myoblast adhesion to laminin. J. Cell Biol. 115, 1437-1448.
    • (1991) J. Cell Biol. , vol.115 , pp. 1437-1448
    • Cooper, D.N.1    Massa, S.M.2    Barondes, S.H.3
  • 15
    • 0021246322 scopus 로고
    • Endogenous mammalian lectin localized extracellularly in lung elastic fibers
    • Cerra, R. F., Haywood-Reid, P. L., and Barondes, S. H. (1984) Endogenous mammalian lectin localized extracellularly in lung elastic fibers. J. Cell Biol. 98, 1580-1589.
    • (1984) J. Cell Biol. , vol.98 , pp. 1580-1589
    • Cerra, R.F.1    Haywood-Reid, P.L.2    Barondes, S.H.3
  • 16
    • 0025335432 scopus 로고
    • Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism
    • Cooper, D. N., and Barondes, S. H. (1990) Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism. J. Cell Biol. 110, 1681-1691.
    • (1990) J. Cell Biol. , vol.110 , pp. 1681-1691
    • Cooper, D.N.1    Barondes, S.H.2
  • 17
    • 0030000860 scopus 로고    scopus 로고
    • A new pathway for protein export in Saccharomyces cerevisiae
    • Cleves, A. E., Cooper, D. N., Barondes, S. H., and Kelly, R. B. (1996) A new pathway for protein export in Saccharomyces cerevisiae. J. Cell Biol. 133, 1017-1026.
    • (1996) J. Cell Biol. , vol.133 , pp. 1017-1026
    • Cleves, A.E.1    Cooper, D.N.2    Barondes, S.H.3    Kelly, R.B.4
  • 18
    • 0029858594 scopus 로고    scopus 로고
    • The tumor promotor arsenite stimulates AP-1 activity by inhibiting a JNK phosphatase
    • Cavigelli, M., Li, W. W., Lin, A., Su, B., Yoshioka, K., and Karin, M. (1996) The tumor promotor arsenite stimulates AP-1 activity by inhibiting a JNK phosphatase. EMBO J. 15, 6269-6279.
    • (1996) EMBO J. , vol.15 , pp. 6269-6279
    • Cavigelli, M.1    Li, W.W.2    Lin, A.3    Su, B.4    Yoshioka, K.5    Karin, M.6
  • 19
    • 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. (1994) Structure of S-lectin, a developmentally regulated vertebrate β-galactoside-binding protein. Proc. Natl. Acad. Sci. U.S.A. 91, 1428-1432.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1428-1432
    • Liao, D.I.1    Kapadia, G.2    Ahmed, H.3    Vasta, G.R.4    Herzberg, O.5
  • 20
    • 0026344814 scopus 로고
    • Effect of amino acid substitution by sited-directed mutagenesis on the carbohydrate recognition and stability of human 14-kDa β-galactoside- binding lectin
    • Hirabayashi, J., and Kasai, K. (1991) Effect of amino acid substitution by sited-directed mutagenesis on the carbohydrate recognition and stability of human 14-kDa β-galactoside-binding lectin. J. Biol. Chem. 266, 23648-23653.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23648-23653
    • Hirabayashi, J.1    Kasai, K.2
  • 21
    • 0021360008 scopus 로고
    • Soluble lectins: A new class of extracellular proteins
    • Barondes, S. H. (1984) Soluble lectins: a new class of extracellular proteins. Science 223, 1259-1264.
    • (1984) Science , vol.223 , pp. 1259-1264
    • Barondes, S.H.1
  • 22
    • 0038641643 scopus 로고    scopus 로고
    • Identification of galectin I and thioredoxin peroxidase II as two arsenic binding proteins in Chinese hamster ovary cells
    • Chang, K. N., Lee, T. C., Tam, M. F., Chen, Y. C., Lee, L. W., Lee, S. Y., Lin, P. J., and Huang, R. N. (2003) Identification of galectin I and thioredoxin peroxidase II as two arsenic binding proteins in Chinese hamster ovary cells. Biochem. J. 371, 495-503.
    • (2003) Biochem. J. , vol.371 , pp. 495-503
    • Chang, K.N.1    Lee, T.C.2    Tam, M.F.3    Chen, Y.C.4    Lee, L.W.5    Lee, S.Y.6    Lin, P.J.7    Huang, R.N.8
  • 23
    • 0030043154 scopus 로고    scopus 로고
    • Cellular uptake of trivalent arsenite and pentavalent arsenate in KB cells cultured in phosphate-free medium
    • Huang, R. N., and Lee, T. C. (1996) Cellular uptake of trivalent arsenite and pentavalent arsenate in KB cells cultured in phosphate-free medium. Toxicol. Appl. Pharmacol. 136, 243-249.
    • (1996) Toxicol. Appl. Pharmacol. , vol.136 , pp. 243-249
    • Huang, R.N.1    Lee, T.C.2
  • 24
    • 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. (2000) Phosphorylation of the β-galactoside-binding protein galectin-3 modulates binding to its ligands. J. Biol. Chem. 275, 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
  • 25
    • 0034074288 scopus 로고    scopus 로고
    • Oxidized galectin-1 promotes axonal regeneration in peripheral nerves but does not possess lectin properties
    • Inagaki, Y., Sohma, Y., Horie, H., Nozawa, R., and Kadoya, T. (2000) Oxidized galectin-1 promotes axonal regeneration in peripheral nerves but does not possess lectin properties. Eur. J. Biochem. 267, 2955-2964.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2955-2964
    • Inagaki, Y.1    Sohma, Y.2    Horie, H.3    Nozawa, R.4    Kadoya, T.5
  • 26
    • 0035815522 scopus 로고    scopus 로고
    • Microcalorimetric studies of the interaction mechanisms between proteins and Q-sepharose at pH near the isoelectric point (pI): Effects of NaCl concentratrion, pH value, and temperature
    • Lin, F. Y., Chen, C. S., Chen, W. Y., and Yamamoto, S. (2001) Microcalorimetric studies of the interaction mechanisms between proteins and Q-sepharose at pH near the isoelectric point (pI): effects of NaCl concentratrion, pH value, and temperature. J. Chromatogr., A 912, 281-289.
    • (2001) J. Chromatogr., a , vol.912 , pp. 281-289
    • Lin, F.Y.1    Chen, C.S.2    Chen, W.Y.3    Yamamoto, S.4
  • 27
    • 0038305511 scopus 로고    scopus 로고
    • Identification of an equilibrium intermediate in the unfolding process of galectin-1, which retains its carbohydrate-binding specificity
    • Iglesias, M. M., Elola, M. T., Martinez, V., Fink, N., and Wolfenstein-Todel, C. (2003) Identification of an equilibrium intermediate in the unfolding process of galectin-1, which retains its carbohydrate-binding specificity. Biochim. Biophys. Acta 1648, 164-173.
    • (2003) Biochim. Biophys. Acta , vol.1648 , pp. 164-173
    • Iglesias, M.M.1    Elola, M.T.2    Martinez, V.3    Fink, N.4    Wolfenstein-Todel, C.5
  • 28
    • 0037251051 scopus 로고    scopus 로고
    • Intrinsic tryptophan fluorescence as a probe of metal and alpha-ketoglutarate binding to TfdA, a mononuclear non-heme iron dioxygenase
    • Dunning Hotopp, J. C., Auchtung, T. A., Hogan, D. A., and Hausinger, R. P. (2003) Intrinsic tryptophan fluorescence as a probe of metal and alpha-ketoglutarate binding to TfdA, a mononuclear non-heme iron dioxygenase. J. Inorg. Biochem. 93, 66-70.
    • (2003) J. Inorg. Biochem. , vol.93 , pp. 66-70
    • Dunning Hotopp, J.C.1    Auchtung, T.A.2    Hogan, D.A.3    Hausinger, R.P.4
  • 29
    • 0030030710 scopus 로고    scopus 로고
    • Examination of the origin, variation, and proper use of expressions for the estimation of association constants by capillary electrophoresis
    • Rundlett, K. L., and Armstrong, D. W. (1996) Examination of the origin, variation, and proper use of expressions for the estimation of association constants by capillary electrophoresis. J. Chromatogr., A 721, 173-186.
    • (1996) J. Chromatogr., A , vol.721 , pp. 173-186
    • Rundlett, K.L.1    Armstrong, D.W.2
  • 30
    • 0036160022 scopus 로고    scopus 로고
    • Determination of the affinity constant of recombinant human galectin-1 and -3 for simple saccharides by capillary affinophoresis
    • Shimura, K., Arata, Y., Uchiyama, N., Hirabayashi, J., and Kasai, K. (2002) Determination of the affinity constant of recombinant human galectin-1 and -3 for simple saccharides by capillary affinophoresis. J. Chromatogr., B 768, 199-210.
    • (2002) J. Chromatogr., B , vol.768 , pp. 199-210
    • Shimura, K.1    Arata, Y.2    Uchiyama, N.3    Hirabayashi, J.4    Kasai, K.5
  • 31
    • 0025269205 scopus 로고
    • Carbohydrates and carbohydrate-binding proteins in the nervous system
    • Jessell, T. M., Hynes, M. A., and Dodd, J. (1990) Carbohydrates and carbohydrate-binding proteins in the nervous system. Annu. Rev. Neurosci. 13, 227-255.
    • (1990) Annu. Rev. Neurosci. , vol.13 , pp. 227-255
    • Jessell, T.M.1    Hynes, M.A.2    Dodd, J.3
  • 32
    • 0018754744 scopus 로고
    • Mechanism of metal carcinogens
    • Sunderman, F. W. (1979) Mechanism of metal carcinogens. Biol. Trace Elem. Res. 1, 53-58.
    • (1979) Biol. Trace Elem. Res. , vol.1 , pp. 53-58
    • Sunderman, F.W.1
  • 35
    • 0026007210 scopus 로고
    • Soluble 14-kDa beta-galactoside-specific bovine lectin. Evidence from mutagenesis and proteolysis that almost the complete polypeptide chain is necessary for integrity of the carbohydrate recognition domain
    • Abbott, W. M., and Feizi, T. (1991) Soluble 14-kDa beta-galactoside- specific bovine lectin. Evidence from mutagenesis and proteolysis that almost the complete polypeptide chain is necessary for integrity of the carbohydrate recognition domain. J. Biol. Chem. 266, 5552-5557.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5552-5557
    • Abbott, W.M.1    Feizi, T.2
  • 36
    • 0029661442 scopus 로고    scopus 로고
    • Spatial proximity of Cys113, Cys172, and Cys422 in the metalloactivation domain of the ArsA ATPase
    • Bhattacharjee, H., and Rosen, B. P. (1996) Spatial proximity of Cys113, Cys172, and Cys422 in the metalloactivation domain of the ArsA ATPase. J. Biol. Chem. 271, 24465-24470.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24465-24470
    • Bhattacharjee, H.1    Rosen, B.P.2
  • 37
    • 0026739782 scopus 로고
    • Subunit molecular mass assignment of 14,654 Da to the soluble β-galactoside-binding lectin from bovine heart muscle and demonstration of intramolecular disulfide bonding associated with oxidative inactivation
    • Tracy, B. M., Feizi, T., Abbott, W. M., Carruthers, R. A., Green, B. N., and Lawson, A. M. (1992) Subunit molecular mass assignment of 14,654 Da to the soluble β-galactoside-binding lectin from bovine heart muscle and demonstration of intramolecular disulfide bonding associated with oxidative inactivation. J. Biol. Chem. 267, 10342-10347.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10342-10347
    • Tracy, B.M.1    Feizi, T.2    Abbott, W.M.3    Carruthers, R.A.4    Green, B.N.5    Lawson, A.M.6
  • 38
    • 0022514861 scopus 로고
    • Oxidation and chemical modification of lung β-galactoside-specific lectin
    • Whitney, P. L., Powell, J. T., and Sanford, G. L. (1986) Oxidation and chemical modification of lung β-galactoside-specific lectin. Biochem. J. 238, 683-689.
    • (1986) Biochem. J. , vol.238 , pp. 683-689
    • Whitney, P.L.1    Powell, J.T.2    Sanford, G.L.3
  • 39
    • 0037566874 scopus 로고    scopus 로고
    • Oxidation of goat hepatic galectin-1 induces change in secondary structure
    • Pande, A. H., Gupta, R. K., Sumati, and Hajela, K. (2003) Oxidation of goat hepatic galectin-1 induces change in secondary structure. Protein Pept. Lett. 10, 265-275.
    • (2003) Protein Pept. Lett. , vol.10 , pp. 265-275
    • Pande, A.H.1    Gupta, R.K.2    Sumati3    Hajela, K.4


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