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Volumn 119, Issue 5, 1996, Pages 878-886

Structural and functional characterization of a novel tumor-derived rat galectin-1 having transforming growth factor (TGF) activity: The relationship between intramolecular disulfide bridges and TGF activity

Author keywords

BALB3T3; Disulfide bond; Galectin; MALDI TOF; Transforming growth factor

Indexed keywords

CARBON 14; GALECTIN; MERCAPTOETHANOL; TRANSFORMING GROWTH FACTOR; TUMOR PROTEIN;

EID: 0029954457     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021325     Document Type: Article
Times cited : (43)

References (50)
  • 1
    • 0000201238 scopus 로고
    • Growth factors from murine sarcoma virus-transformed cells
    • DeLarco, J.E. and Todaro, G.J. (1978) Growth factors from murine sarcoma virus-transformed cells. Proc. Natl. Acad. Sci. USA 75, 4001-4005
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4001-4005
    • DeLarco, J.E.1    Todaro, G.J.2
  • 2
    • 0019297767 scopus 로고
    • Kirsten murine sarcoma virus transformed cell lines and a spontaneously transformed rat cell line produce transforming growth factor
    • Ozanne, B., Fulton, R.J., and Kaplan, P.L. (1980) Kirsten murine sarcoma virus transformed cell lines and a spontaneously transformed rat cell line produce transforming growth factor. J. Cell. Physiol. 105, 163-180
    • (1980) J. Cell. Physiol. , vol.105 , pp. 163-180
    • Ozanne, B.1    Fulton, R.J.2    Kaplan, P.L.3
  • 3
    • 0019465899 scopus 로고
    • Transforming growth factor production by chemically transformed cells
    • Moses, H.L., Branum, E.L., Proper, J.A., and Robinson, R.A. (1981) Transforming growth factor production by chemically transformed cells. Cancer Res. 41, 2842-2848
    • (1981) Cancer Res. , vol.41 , pp. 2842-2848
    • Moses, H.L.1    Branum, E.L.2    Proper, J.A.3    Robinson, R.A.4
  • 5
    • 0020086335 scopus 로고
    • Mouse embryos contain polypeptide growth factor(s) capable of inducing a reversible neoplastic phenotype in nontransformed cells in culture
    • Proper, J.A., Bjornson, C.L., and Moses, H.L. (1982) Mouse embryos contain polypeptide growth factor(s) capable of inducing a reversible neoplastic phenotype in nontransformed cells in culture. J. Cell. Physiol. 110, 169-174
    • (1982) J. Cell. Physiol. , vol.110 , pp. 169-174
    • Proper, J.A.1    Bjornson, C.L.2    Moses, H.L.3
  • 6
    • 0346254671 scopus 로고
    • New class of transforming growth factors potentiated by epidermal growth factor: Isolation from nonneoplastic tissues
    • Roberts, A.B., Anzano, M.A., Lamb, L.C., Smith, J.M., and Sporn, M.B. (1981) New class of transforming growth factors potentiated by epidermal growth factor: Isolation from nonneoplastic tissues. Proc. Natl. Acad. Sci. USA 78, 5339-5343
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 5339-5343
    • Roberts, A.B.1    Anzano, M.A.2    Lamb, L.C.3    Smith, J.M.4    Sporn, M.B.5
  • 8
    • 0020533055 scopus 로고
    • Simian sarcoma virus oncogene v-sis, is derived from the gene (or genes) encoding a platelet-derived growth factor
    • Doolittle, R.F., Hunkappilar, M.W., Hood, L.E., Devare, S.G., Robbins, K.C., Aaronson, S.A., and Antoniades, H.N. (1983) Simian sarcoma virus oncogene v-sis, is derived from the gene (or genes) encoding a platelet-derived growth factor. Science 221, 775-277
    • (1983) Science , vol.221 , pp. 775-277
    • Doolittle, R.F.1    Hunkappilar, M.W.2    Hood, L.E.3    Devare, S.G.4    Robbins, K.C.5    Aaronson, S.A.6    Antoniades, H.N.7
  • 10
    • 0021089336 scopus 로고
    • Isolation and partial purification of a new class of transforming growth factor from an avian sarcoma virus-transformed rat cell line
    • Hirai, R., Yamaoka, K., and Mitsui, H. (1983) Isolation and partial purification of a new class of transforming growth factor from an avian sarcoma virus-transformed rat cell line. Cancer Res. 43, 5742-5746
    • (1983) Cancer Res. , vol.43 , pp. 5742-5746
    • Hirai, R.1    Yamaoka, K.2    Mitsui, H.3
  • 11
    • 0021238054 scopus 로고
    • Purification of an acid- and heat-labile transforming growth factor from an avian sarcoma virus transformed rat cell line
    • Yamaoka, K., Hirai, R., Tsugita, A., and Mitsui, H. (1984) Purification of an acid- and heat-labile transforming growth factor from an avian sarcoma virus transformed rat cell line. J. Cell. Physiol. 119, 307-314
    • (1984) J. Cell. Physiol. , vol.119 , pp. 307-314
    • Yamaoka, K.1    Hirai, R.2    Tsugita, A.3    Mitsui, H.4
  • 12
    • 0013543749 scopus 로고
    • Transforming growth factors produced by certain human tumor cells: Polypeptides that interact with epidermal growth factor receptors
    • Todaro, G.J., Fryling, C., and DeLarco, J.E. (1980) Transforming growth factors produced by certain human tumor cells: Polypeptides that interact with epidermal growth factor receptors. Proc. Natl. Acad. Sci. USA 77, 5258-5262
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5258-5262
    • Todaro, G.J.1    Fryling, C.2    DeLarco, J.E.3
  • 13
    • 0020806079 scopus 로고
    • Transforming growth factor produced by retrovirus-transformed rodent fibroblasts and human melanoma cells: Amino acid sequence homology with epidermal growth factor
    • Marquardt, H., Hunkappiler, M.W., Hood, L.E., Twardzik, J.E., DeLarco, J.E., Stephenson, J.R., and Todaro, G.J. (1983) Transforming growth factor produced by retrovirus-transformed rodent fibroblasts and human melanoma cells: Amino acid sequence homology with epidermal growth factor. Proc. Natl. Acad. Sci. USA 80, 4684-4688
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 4684-4688
    • Marquardt, H.1    Hunkappiler, M.W.2    Hood, L.E.3    Twardzik, J.E.4    DeLarco, J.E.5    Stephenson, J.R.6    Todaro, G.J.7
  • 14
    • 0020324123 scopus 로고
    • Transformation induced by Abelson murine sarcoma leukemia virus involves production of a polypeptide growth factor
    • Twardzik, D.R., Todaro, G.J., Marquardt, H., Reynold, F.H., and Stephanson, J.R. (1982) Transformation induced by Abelson murine sarcoma leukemia virus involves production of a polypeptide growth factor. Science 216, 894-897
    • (1982) Science , vol.216 , pp. 894-897
    • Twardzik, D.R.1    Todaro, G.J.2    Marquardt, H.3    Reynold, F.H.4    Stephanson, J.R.5
  • 16
    • 0008469177 scopus 로고
    • Mammalian lectin as transforming growth factor
    • Gabious, H.-J., ed. Springer-Verlag, Heidelberg
    • Yamaoka, K., Ohn, S., Kawasaki, H., and Suzuki, S. (1993) Mammalian lectin as transforming growth factor in Lectins and Glycobiology (Gabious, H.-J., ed.) pp. 492-499, Springer-Verlag, Heidelberg
    • (1993) Lectins and Glycobiology , pp. 492-499
    • Yamaoka, K.1    Ohn, S.2    Kawasaki, H.3    Suzuki, S.4
  • 17
    • 0024297531 scopus 로고
    • Sequence of full-length cDNA for rat lung β-galactoside-binding protein primary and secondary structure of the lectin
    • Clerch, L.B., Whitney, P., Hass, M., Brew, K., Miller, T., Werner, R., and Massaro, D. (1988) Sequence of full-length cDNA for rat lung β-galactoside-binding protein primary and secondary structure of the lectin. Biochemistry 27, 692-699
    • (1988) Biochemistry , vol.27 , pp. 692-699
    • Clerch, L.B.1    Whitney, P.2    Hass, M.3    Brew, K.4    Miller, T.5    Werner, R.6    Massaro, D.7
  • 18
    • 0026001374 scopus 로고
    • Overexpression of a β-galactoside binding protein causes transformation of BALB3T3 fibroblast cells
    • Yamaoka, K., Ohno, S., Kawasaki, H., and Suzuki, K. (1991) Overexpression of a β-galactoside binding protein causes transformation of BALB3T3 fibroblast cells. Biochem. Biophys. Res. Commun. 179, 272-279
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 272-279
    • Yamaoka, K.1    Ohno, S.2    Kawasaki, H.3    Suzuki, K.4
  • 19
    • 0026694658 scopus 로고
    • Evidence that Caenorhabditis elegans 32-kDa β-galactoside-binding protein is homologous to vertebrate β-galactoside-binding lectins
    • Hirabayashi, J., Satoh, J., and Kasai, K. (1992) Evidence that Caenorhabditis elegans 32-kDa β-galactoside-binding protein is homologous to vertebrate β-galactoside-binding lectins. J. Biol. Chem. 267, 15485-15490
    • (1992) J. Biol. Chem. , vol.267 , pp. 15485-15490
    • Hirabayashi, J.1    Satoh, J.2    Kasai, K.3
  • 20
    • 0027457991 scopus 로고
    • Soluble lactose-binding lectin from rat intestine with two different carbohydrate-binding domains in the same peptide chain
    • Oda, Y., Herrmann, J., Gitt, M., Turck, C.W., Burlingame, A.L., Barondes, B.N., and Leffler, H. (1993) Soluble lactose-binding lectin from rat intestine with two different carbohydrate-binding domains in the same peptide chain, J. Biol. Chem. 268, 5929-5930
    • (1993) J. Biol. Chem. , vol.268 , pp. 5929-5930
    • Oda, Y.1    Herrmann, J.2    Gitt, M.3    Turck, C.W.4    Burlingame, A.L.5    Barondes, B.N.6    Leffler, H.7
  • 21
    • 0024461974 scopus 로고
    • Soluble lactose-binding vertebrate lectins: A growing family
    • Leffler, H., Masiarz, F.R., and Barondes, S.H. (1989) Soluble lactose-binding vertebrate lectins: A growing family. Biochemistry 28, 9222-9229
    • (1989) Biochemistry , vol.28 , pp. 9222-9229
    • Leffler, H.1    Masiarz, F.R.2    Barondes, S.H.3
  • 22
    • 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. (1991) Identification of an autocrine negative growth factor: Mouse β-galactoside-binding protein is a cytostatic factor and cell growth regulator. Cell 64, 91-97
    • (1991) Cell , vol.64 , pp. 91-97
    • Wells, V.1    Mallucci, L.2
  • 23
    • 0022456705 scopus 로고
    • Release of cytotoxin by macrophages treated with human placenta lectin
    • Kajikawa, T., Nakajima, Y., Hirabayashi, J., Kasai, K., and Yamazaki, M. (1986) Release of cytotoxin by macrophages treated with human placenta lectin. Life Sci. 39, 1177-1181
    • (1986) Life Sci. , vol.39 , pp. 1177-1181
    • Kajikawa, T.1    Nakajima, Y.2    Hirabayashi, J.3    Kasai, K.4    Yamazaki, M.5
  • 24
    • 0025309457 scopus 로고
    • Recombinant human beta-galactoside binding lectin supresses clinical and histological signs of experimental autoimmune encephalomyelitis
    • Offinerrr, H., Celnik, B., Bringman, T.S., Casentini-B, D., Nedwin, G.E., and Vandenbark, A.A. (1990) Recombinant human beta-galactoside binding lectin supresses clinical and histological signs of experimental autoimmune encephalomyelitis. J. Neuro-immunol. 28, 177-184
    • (1990) J. Neuro-immunol. , vol.28 , pp. 177-184
    • Offinerrr, H.1    Celnik, B.2    Bringman, T.S.3    Casentini-B, D.4    Nedwin, G.E.5    Vandenbark, A.A.6
  • 25
    • 0024414280 scopus 로고
    • Lectins as recognition molecules
    • Sharon, N. and Lis, H. (1989) Lectins as recognition molecules. Science 246, 227-234
    • (1989) Science , vol.246 , pp. 227-234
    • Sharon, N.1    Lis, H.2
  • 26
    • 0019829470 scopus 로고
    • Mitogenicity and binding properties of beta-galactoside-binding lectin from chick-embryo kidney
    • Pitts, M.J. and Yang, D.C.H. (1981) Mitogenicity and binding properties of beta-galactoside-binding lectin from chick-embryo kidney. Biochem. J. 195, 435-439
    • (1981) Biochem. J. , vol.195 , pp. 435-439
    • Pitts, M.J.1    Yang, D.C.H.2
  • 28
    • 0022624749 scopus 로고
    • Differential expression of endogenous lectins on the surface of non-tumorigenic, tumorigenic, and metastatic cells
    • Raz, A., Meromsky, L., and Lotan, R. (1986) Differential expression of endogenous lectins on the surface of non-tumorigenic, tumorigenic, and metastatic cells. Cancer Res. 46, 3667-3672
    • (1986) Cancer Res. , vol.46 , pp. 3667-3672
    • Raz, A.1    Meromsky, L.2    Lotan, R.3
  • 29
    • 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. J., Guenet, J.-L., and Rigby, P.W. J. (1992) Expression of the L14 lectin during mouse embryogenesis suggests multiple roles during pre- and post-implantation development. Development 115, 143-155
    • (1992) Development , vol.115 , pp. 143-155
    • Poirier, F.1    Timmons, P.M.2    Chan, C.-T.J.3    Guenet, J.-L.4    Rigby, P.W.J.5
  • 30
    • 0026344814 scopus 로고
    • Effect of amino acid substitution by site-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 site-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
  • 31
    • 0022514861 scopus 로고
    • Oxidation and chemical modification of lung β-galactoside-binding-specific lectin
    • Whitney, P.L., Powell, J.T., and Sanford, G.L. (1986) Oxidation and chemical modification of lung β-galactoside-binding-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
  • 32
    • 0023678267 scopus 로고
    • Complete amino acid sequence of a β-galactoside-binding lectin from human placenta
    • Hirabayashi, J. and Kasai, K. (1988) Complete amino acid sequence of a β-galactoside-binding lectin from human placenta. J. Biochem. 104, 1-4
    • (1988) J. Biochem. , vol.104 , pp. 1-4
    • Hirabayashi, J.1    Kasai, K.2
  • 33
    • 0024356783 scopus 로고
    • Production and purification of recombinant 14 kDa beta-galactoside-binding lectin
    • Hirabayashi, J., Ayaki, H., Soma, G., and Kasai, K. (1989) Production and purification of recombinant 14 kDa beta-galactoside-binding lectin. FEBS Lett. 250, 161-165
    • (1989) FEBS Lett. , vol.250 , pp. 161-165
    • Hirabayashi, J.1    Ayaki, H.2    Soma, G.3    Kasai, K.4
  • 34
    • 0022481299 scopus 로고
    • Expression in rat fibroblasts of a human transforming growth factor-α cDNA resulted in transformation
    • Rosental, A., Lindquist, P.B., Bringman, T.S., Goeddel, D.V., and Derynck, R. (1986) Expression in rat fibroblasts of a human transforming growth factor-α cDNA resulted in transformation. Cell 46, 301-309
    • (1986) Cell , vol.46 , pp. 301-309
    • Rosental, A.1    Lindquist, P.B.2    Bringman, T.S.3    Goeddel, D.V.4    Derynck, R.5
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of the bacteriophage T4
    • Laemmli, U.K. (1979) Cleavage of structural proteins during assembly of the head of the bacteriophage T4. Nature 227, 680-685
    • (1979) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0019152144 scopus 로고
    • Two lactose binding lectins from chicken tissues
    • Beyer, E.C., Zweig, S.E., and Barondes, S.H. (1980) Two lactose binding lectins from chicken tissues. J. Biol. Chem. 255, 4236-4239
    • (1980) J. Biol. Chem. , vol.255 , pp. 4236-4239
    • Beyer, E.C.1    Zweig, S.E.2    Barondes, S.H.3
  • 37
    • 0023710284 scopus 로고
    • Two distinct classes of carbohydrate-recognition domains in animal lectins
    • Drickamer, K. (1988) Two distinct classes of carbohydrate-recognition domains in animal lectins. J. Biol. Chem. 263, 9557-9560
    • (1988) J. Biol. Chem. , vol.263 , pp. 9557-9560
    • Drickamer, K.1
  • 38
    • 0020640234 scopus 로고
    • Low colony formation in vivo and in culture as exhibited by metastatic melanoma cells selected for reduced homotypic aggregation
    • Lotan, R. and Raz, A. (1983) Low colony formation in vivo and in culture as exhibited by metastatic melanoma cells selected for reduced homotypic aggregation. Cancer Res. 43, 2088-2093
    • (1983) Cancer Res. , vol.43 , pp. 2088-2093
    • Lotan, R.1    Raz, A.2
  • 39
    • 0022394368 scopus 로고
    • Inhibition of tumor cell colony formation in culture by monoclonal antibody to endogenous lectins
    • Lotan, R., Lotan, D., and Raz, A. (1985) Inhibition of tumor cell colony formation in culture by monoclonal antibody to endogenous lectins. Cancer Res. 45, 4349-4353
    • (1985) Cancer Res. , vol.45 , pp. 4349-4353
    • Lotan, R.1    Lotan, D.2    Raz, A.3
  • 40
    • 0021246322 scopus 로고
    • Endogenous mammalian lectin is localized extracellularly in lung elastic fibers
    • Cerra, R.F., Haywood-Reid, P.L., and Barondes, S.H. (1984) Endogenous mammalian lectin is 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
  • 41
    • 0019822646 scopus 로고
    • Externalization of an endogenous chicken muscle lectin with in vivo development
    • Barondes, S.H. and Haywood-Reid, P.L. (1981) Externalization of an endogenous chicken muscle lectin with in vivo development. J. Cell Biol. 91, 568-572
    • (1981) J. Cell Biol. , vol.91 , pp. 568-572
    • Barondes, S.H.1    Haywood-Reid, P.L.2
  • 42
    • 0020032661 scopus 로고
    • Quantitation of two endogenous lactose-inhibitable lectins in embryonic and adult chicken tissues
    • Beyer, E.C. and Barondes, S.H. (1982) Quantitation of two endogenous lactose-inhibitable lectins in embryonic and adult chicken tissues. J. Cell Biol. 92, 23-27
    • (1982) J. Cell Biol. , vol.92 , pp. 23-27
    • Beyer, E.C.1    Barondes, S.H.2
  • 44
    • 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
  • 45
    • 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
    • Tracey, 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
    • Tracey, B.M.1    Feizi, T.2    Abbott, W.M.3    Carruthers, R.A.4    Green, B.N.5    Lawson, A.M.6
  • 46
    • 0028235289 scopus 로고
    • Formation of a disulfide bond in the immmuoglobulin domain of the myelin P0 protein is essential for its adhesion
    • Zhang, K. and Filbin, M.T. (1994) Formation of a disulfide bond in the immmuoglobulin domain of the myelin P0 protein is essential for its adhesion. J. Neurochem. 63, 367-370
    • (1994) J. Neurochem. , vol.63 , pp. 367-370
    • Zhang, K.1    Filbin, M.T.2
  • 47
    • 0023488847 scopus 로고
    • Endogenous galactoside-binding lectin: A new class of functional tumor cell surface molecules related to metastasis
    • Raz, A. and Lotan, R. (1987) Endogenous galactoside-binding lectin: A new class of functional tumor cell surface molecules related to metastasis. Cancer Res. 6, 433-452
    • (1987) Cancer Res. , vol.6 , pp. 433-452
    • Raz, A.1    Lotan, R.2
  • 48
    • 0026768317 scopus 로고
    • Isolation and expresion of a gene coding L14-II, a new human soluble lactose binding lectin
    • Gitt, M.A., Massa, S.M., Leffler, H., and Barondes, S.H. (1992) Isolation and expresion of a gene coding L14-II, a new human soluble lactose binding lectin. J. Biol. Chem. 267, 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
  • 49
    • 0025689136 scopus 로고
    • Isolation and characterization of a 60-70-kD plasma membrane glycoprotein involved in the contact-dependent inhibition of growth
    • Wieser, R.J., Schutz, S., Tschank, G., Thomas, H., Dienes, H.-P., and Oesch, F. (1990) Isolation and characterization of a 60-70-kD plasma membrane glycoprotein involved in the contact-dependent inhibition of growth. J. Cell Biol. 111, 2681-2692
    • (1990) J. Cell Biol. , vol.111 , pp. 2681-2692
    • Wieser, R.J.1    Schutz, S.2    Tschank, G.3    Thomas, H.4    Dienes, H.-P.5    Oesch, F.6
  • 50
    • 0022515077 scopus 로고
    • Contact inhibition of growth of human diploid fibroblasts by immobilized plasma membrane glycoproteins
    • Wieser, R.J. and Oesch, F. (1986) Contact inhibition of growth of human diploid fibroblasts by immobilized plasma membrane glycoproteins. J. Cell Biol. 103, 361-367
    • (1986) J. Cell Biol. , vol.103 , pp. 361-367
    • Wieser, R.J.1    Oesch, F.2


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