메뉴 건너뛰기




Volumn 160, Issue 10, 1998, Pages 4831-4840

Activated rat macrophages produce a galectin-1-like protein that induces apoptosis of T cells: Biochemical and functional characterization

Author keywords

[No Author keywords available]

Indexed keywords

GALAPTIN; GALECTIN;

EID: 0032525046     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (151)

References (51)
  • 1
    • 0002458793 scopus 로고
    • Vertebrate lectins: Properties and functions
    • Liener, N. Sharon, and I. Goldstein, eds. Academic Press, Orlando, FL
    • Barondes, S. H. 1986. Vertebrate lectins: properties and functions. In The Lectins: Properties, Functions and Applications in Biology and Medicine. 1. Liener, N. Sharon, and I. Goldstein, eds. Academic Press, Orlando, FL, p. 447.
    • (1986) The Lectins: Properties, Functions and Applications in Biology and Medicine , vol.1 , pp. 447
    • Barondes, S.H.1
  • 2
    • 0027169990 scopus 로고
    • The family of metazoan metal-independent β-galactoside-binding lectins: Structure, function and molecular evolution
    • Hirabayashi, J., and K. Kasai. 1993. The family of metazoan metal-independent β-galactoside-binding lectins: structure, function and molecular evolution. Glycobiology 3:297.
    • (1993) Glycobiology , vol.3 , pp. 297
    • Hirabayashi, J.1    Kasai, K.2
  • 3
    • 0027965708 scopus 로고
    • Galectins: Structure and function of a large family of animal lectins
    • Barondes, S. H., D. N. W. Cooper, M. A. Gitt, and H. Leffler. 1994. Galectins: structure and function of a large family of animal lectins, J. Biol. Chem. 269:20807.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20807
    • Barondes, S.H.1    Cooper, D.N.W.2    Gitt, M.A.3    Leffler, H.4
  • 5
    • 0030064027 scopus 로고    scopus 로고
    • Galectins: A family of animals lectins that decipher glycocodes
    • Kasai, K., and J. Hirabayashi. 1996. Galectins: a family of animals lectins that decipher glycocodes. J. Biochem. 119:1.
    • (1996) J. Biochem. , vol.119 , pp. 1
    • Kasai, K.1    Hirabayashi, J.2
  • 6
    • 0025203339 scopus 로고
    • Stimulation of vascular cell proliferation by β-galactoside specific lectins
    • Sandford, G. L., and S. Harris-Hooker. 1990. Stimulation of vascular cell proliferation by β-galactoside specific lectins. FASEB J. 4:2912.
    • (1990) FASEB J. , vol.4 , pp. 2912
    • Sandford, G.L.1    Harris-Hooker, S.2
  • 7
    • 0026079139 scopus 로고
    • Identification of an autocrine negative growth factor: Mouse β-galactoside-binding protein is a cytosiatic factor and cell growth regulator
    • Wells, V., and L. Mallucci. 1991. Identification of an autocrine negative growth factor: mouse β-galactoside-binding protein is a cytosiatic factor and cell growth regulator. Cell 64:91.
    • (1991) Cell , vol.64 , pp. 91
    • Wells, V.1    Mallucci, L.2
  • 8
    • 0030582135 scopus 로고    scopus 로고
    • Biphasic modulation of cell growth by recombinant human galectin-1
    • Adams, L., G. Kenneth Scott, and C. S. Weinberg. 1996. Biphasic modulation of cell growth by recombinant human galectin-1. Biochim. Biophys. Acta 1312:137.
    • (1996) Biochim. Biophys. Acta , vol.1312 , pp. 137
    • Adams, L.1    Kenneth Scott, G.2    Weinberg, C.S.3
  • 9
    • 0023488847 scopus 로고
    • Endogenous galactoside-binding lectins: A new class of functional tumor cell surface molecules related to metastasis
    • Raz, A., and R. Lotan. 1987. Endogenous galactoside-binding lectins: a new class of functional tumor cell surface molecules related to metastasis. Cancer Metast. Rev. 6:433.
    • (1987) Cancer Metast. Rev. , vol.6 , pp. 433
    • Raz, A.1    Lotan, R.2
  • 10
    • 0020606576 scopus 로고
    • Prevention and therapy with electrolectin of experimental autoimmune myasthenia gravis in rabbits
    • Levi, G., R. Tarrab-Hazdai, and V. I. Teichberg. 1983. Prevention and therapy with electrolectin of experimental autoimmune myasthenia gravis in rabbits. Eur. J. Immunol. 13:500.
    • (1983) Eur. J. Immunol. , vol.13 , pp. 500
    • Levi, G.1    Tarrab-Hazdai, R.2    Teichberg, V.I.3
  • 11
    • 0025309457 scopus 로고
    • Recombinant human β-galactoside binding lectin suppresses clinical and histological signs of experimental autoimmune encephalomyelitis
    • Offner, H., B. Celnik, T. S Bringman, D. Casentini-Borocz, G. E Nedwin, and A. Vandenbark. 1990. Recombinant human β-galactoside binding lectin suppresses clinical and histological signs of experimental autoimmune encephalomyelitis, J. Neuroimmunol. 28:177.
    • (1990) J. Neuroimmunol. , vol.28 , pp. 177
    • Offner, H.1    Celnik, B.2    Bringman, T.S.3    Casentini-Borocz, D.4    Nedwin, G.E.5    Vandenbark, A.6
  • 13
    • 0023038671 scopus 로고
    • Evidence that a human soluble β-galactoside-binding lectin is encoded by a family of genes
    • Gitt, M. A., and S. H Barondes. 1986. Evidence that a human soluble β-galactoside-binding lectin is encoded by a family of genes. Proc. Natl. Acad. Sci. USA 83:7603.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7603
    • Gitt, M.A.1    Barondes, S.H.2
  • 14
    • 0024382081 scopus 로고
    • Cloning and nucleotide sequence of a full-length cDNA for human 14-kDa β-galactoside-binding lectin
    • Hirabayashi, J., H. Akayi, G. Soma, and K. Kasai. 1989. Cloning and nucleotide sequence of a full-length cDNA for human 14-kDa β-galactoside-binding lectin. Biochim. Biophys. Acta 1008:85.
    • (1989) Biochim. Biophys. Acta , vol.1008 , pp. 85
    • Hirabayashi, J.1    Akayi, H.2    Soma, G.3    Kasai, K.4
  • 15
    • 0023678267 scopus 로고
    • Complete amino acid sequence of a β-galactoside-binding lectin from human placenta
    • Hirabayashi, J., and K. Kasai. 1988. Complete amino acid sequence of a β-galactoside-binding lectin from human placenta. J. Biochem. 104:1.
    • (1988) J. Biochem. , vol.104 , pp. 1
    • Hirabayashi, J.1    Kasai, K.2
  • 17
    • 0026077971 scopus 로고
    • β-Galactoside soluble lectin from human brain: Complete amino acid sequence
    • Bladier, D., J. P. Le Caer, R. Joubert, M. Caron, and J. Rossier. 1991. β-Galactoside soluble lectin from human brain: complete amino acid sequence. NeuroChem. Int. 18:275.
    • (1991) NeuroChem. Int. , vol.18 , pp. 275
    • Bladier, D.1    Le Caer, J.P.2    Joubert, R.3    Caron, M.4    Rossier, J.5
  • 18
    • 0024559245 scopus 로고
    • Soluble bovine galactoside-binding lectin cDNA reveals the complete amino acid sequence and an antigenic relationship with the major encephalitogenic domain of myelin basic protein
    • Abbott, W. M., A. Mellor, Y. Edwards, and T. Feizi. 1989. Soluble bovine galactoside-binding lectin cDNA reveals the complete amino acid sequence and an antigenic relationship with the major encephalitogenic domain of myelin basic protein. Biochem. J. 259:283.
    • (1989) Biochem. J. , vol.259 , pp. 283
    • Abbott, W.M.1    Mellor, A.2    Edwards, Y.3    Feizi, T.4
  • 19
    • 0023221894 scopus 로고
    • Amino acid sequence of β-galactoside-binding bovine heart lectin
    • Southan, C. A. Aitken, R. A. Childs, W. M. Abbott, and T. Feizi. 1987. Amino acid sequence of β-galactoside-binding bovine heart lectin. FEBS Lett. 214:301.
    • (1987) FEBS Lett. , vol.214 , pp. 301
    • Southan1    Aitken, C.A.2    Childs, R.A.3    Abbott, W.M.4    Feizi, T.5
  • 20
    • 0024297531 scopus 로고
    • Sequence of a full-length cDNA for rat lung β-galactosidebinding protein: Primary and secondary structure of the lectin
    • Clerch, L. B., P. Whitney, M. Hass, K. Brew. T. Miller, R. Werner, and D. Massaro. 1988. Sequence of a full-length cDNA for rat lung β-galactosidebinding protein: primary and secondary structure of the lectin. Biochemistry 27:692.
    • (1988) Biochemistry , vol.27 , pp. 692
    • Clerch, L.B.1    Whitney, P.2    Hass, M.3    Brew T Miller, K.4    Werner, R.5    Massaro, D.6
  • 21
    • 0024360758 scopus 로고
    • The sequence of the mouse 14 kDa β-galactoside-binding lectin and evidence for its synthesis on free cytoplasmic ribosomes
    • Wilson, T. J. G., M. N. Firth, J. T. Powell, and F. L. Harrison. 1989. The sequence of the mouse 14 kDa β-galactoside-binding lectin and evidence for its synthesis on free cytoplasmic ribosomes. Biochem. J. 261.-847.
    • (1989) Biochem. J. , vol.261 , pp. 847
    • Wilson, T.J.G.1    Firth, M.N.2    Powell, J.T.3    Harrison, F.L.4
  • 22
    • 0023472090 scopus 로고
    • Cloning and expression of a cDNA for two endogenous uv 2237 fibrosarcoma lectin genes
    • Raz, A., A. Avivi, G. Pazerini, and P. Carmi. 1987. Cloning and expression of a cDNA for two endogenous uv 2237 fibrosarcoma lectin genes. Exp. Cell. Res. 173:109.
    • (1987) Exp. Cell. Res. , vol.173 , pp. 109
    • Raz, A.1    Avivi, A.2    Pazerini, G.3    Carmi, P.4
  • 23
    • 0025642403 scopus 로고
    • Structure of chicken 16 kDa β-gulactoside-binding lectin: Complete amino acid sequence, cloning of cDNA and production of recombinant lectin
    • Sakakura, Y., J. Hirabayashi, Y. Oda, Y. Ohyama, and K. Kasai. 1990. Structure of chicken 16 kDa β-gulactoside-binding lectin: complete amino acid sequence, cloning of cDNA and production of recombinant lectin. J. Biol. Chem. 265:21573.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21573
    • Sakakura, Y.1    Hirabayashi, J.2    Oda, Y.3    Ohyama, Y.4    Kasai, K.5
  • 26
    • 0030940913 scopus 로고    scopus 로고
    • Galectin-1, an endogenous lectin produced by thymic epithelial cells, induces apoptosis of human thymocytes
    • Perillo, N. L., C. H. Oittenbogaart, J. T. Nguyen, and L. G. Baum. 1997. Galectin-1, an endogenous lectin produced by thymic epithelial cells, induces apoptosis of human thymocytes. J. Exp. Med. 97:1851.
    • (1997) J. Exp. Med. , vol.97 , pp. 1851
    • Perillo, N.L.1    Oittenbogaart, C.H.2    Nguyen, J.T.3    Baum, L.G.4
  • 28
    • 0019152144 scopus 로고
    • Two lactose-binding lectins from chicken tissues: Purified lectin from intestine is different from those in liver and muscle
    • Beyer, E. C., S. E. Zweig, and S. H. Barondes. 1980. Two lactose-binding lectins from chicken tissues: purified lectin from intestine is different from those in liver and muscle. J. Biol. Chem. 255:4236.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4236
    • Beyer, E.C.1    Zweig, S.E.2    Barondes, S.H.3
  • 30
    • 0028326952 scopus 로고
    • An evolutionary perspective on apoptosis
    • Vaux, D. L., G. Haecker, and A. Strasser. 1994. An evolutionary perspective on apoptosis. Cell 76:777.
    • (1994) Cell , vol.76 , pp. 777
    • Vaux, D.L.1    Haecker, G.2    Strasser, A.3
  • 31
    • 0028220078 scopus 로고
    • Isolation and characterization of a soluble lactose-binding lectin from postnatal chicken retina
    • Castagna, L. F., and C. A. Landa. 1994. Isolation and characterization of a soluble lactose-binding lectin from postnatal chicken retina. J. Neurosci. Res. 37:750.
    • (1994) J. Neurosci. Res. , vol.37 , pp. 750
    • Castagna, L.F.1    Landa, C.A.2
  • 32
    • 0017295626 scopus 로고
    • Developmentally regulated lectin in embryonic chick muscle and a myogenic cell line
    • Nowak. T. P., P. L. Haywood, and S. H. Barondes. 1976. Developmentally regulated lectin in embryonic chick muscle and a myogenic cell line. Biochem. Biophys. Res. Commun. 68:650.
    • (1976) Biochem. Biophys. Res. Commun. , vol.68 , pp. 650
    • Nowak, T.P.1    Haywood, P.L.2    Barondes, S.H.3
  • 33
    • 0027986781 scopus 로고
    • Distribution of an endogenous 16 kDa S-lac lectin in the chicken retina
    • Castagna, L. F., and C. A. Landa. 1994. Distribution of an endogenous 16 kDa S-lac lectin in the chicken retina. Invest. Ophthalmol. Vis. Sci. 35:4310.
    • (1994) Invest. Ophthalmol. Vis. Sci. , vol.35 , pp. 4310
    • Castagna, L.F.1    Landa, C.A.2
  • 34
    • 0030799196 scopus 로고    scopus 로고
    • Specific inhibition of lymphocyte proliferation and induction of apoptosis by CLL-I, a β-galactoside-binding lectin
    • Rabinovich, G. A, N. M. Modesti, L. F. Castagna, C. A. Landa, C. M. Riera, and C. E. Sotomayor. 1997. Specific inhibition of lymphocyte proliferation and induction of apoptosis by CLL-I, a β-galactoside-binding lectin. J. Biochem. 122:365.
    • (1997) J. Biochem. , vol.122 , pp. 365
    • Rabinovich, G.A.1    Modesti, N.M.2    Castagna, L.F.3    Landa, C.A.4    Riera, C.M.5    Sotomayor, C.E.6
  • 35
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248.
    • (1976) Anal. Biochem. , vol.72 , pp. 248
    • Bradford, M.M.1
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 38
    • 0027261147 scopus 로고
    • The cell cycle related differences in susceptibility of HL-60 cells to apoptosis induced by various antitumor agents
    • Gorczyca, W., J. Gong, B. Ardelt, F. Traganos, and Z. Darzynkiewicz. 1993. The cell cycle related differences in susceptibility of HL-60 cells to apoptosis induced by various antitumor agents. Cancer Res. 53:3186.
    • (1993) Cancer Res. , vol.53 , pp. 3186
    • Gorczyca, W.1    Gong, J.2    Ardelt, B.3    Traganos, F.4    Darzynkiewicz, Z.5
  • 40
    • 0029900083 scopus 로고    scopus 로고
    • Expression of galectin-3 modulates T cell growth and apoptosis
    • Yang, R. Y., D. K. Hsu, and F. T. Liu. 1996. Expression of galectin-3 modulates T cell growth and apoptosis. Proc. Natl. Acad. Sci. USA 93:6737.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6737
    • Yang, R.Y.1    Hsu, D.K.2    Liu, F.T.3
  • 41
    • 0021564388 scopus 로고
    • The cell biology of macrophage activation
    • Adams, D., and T. A. Hamilton. 1984. The cell biology of macrophage activation. Annu. Rev. Immunol. 2:283.
    • (1984) Annu. Rev. Immunol. , vol.2 , pp. 283
    • Adams, D.1    Hamilton, T.A.2
  • 42
    • 0024398164 scopus 로고
    • Activation-driven T cell death. 1. Requirements for the novo transcription and translation and association with genome fragmentation
    • Ucker, D. S., J. D. Ashwell, and G. Nickas. 1989. Activation-driven T cell death. 1. Requirements for the novo transcription and translation and association with genome fragmentation. J. Immunol. 143:3461.
    • (1989) J. Immunol. , vol.143 , pp. 3461
    • Ucker, D.S.1    Ashwell, J.D.2    Nickas, G.3
  • 43
    • 0028047113 scopus 로고
    • Mac-2: A versatile galactoside-binding protein of mammalian tissues
    • Hughes, R. C. 1994. Mac-2: a versatile galactoside-binding protein of mammalian tissues. Glycobiology 4:5.
    • (1994) Glycobiology , vol.4 , pp. 5
    • Hughes, R.C.1
  • 44
    • 0028074969 scopus 로고
    • Regulation of secretion and surface expression of Mac-2, a galactoside-binding protein of macrophages
    • Sato, S., and R. C. Hughes. 1994. Regulation of secretion and surface expression of Mac-2, a galactoside-binding protein of macrophages. J. Biol. Chem. 269:4424.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4424
    • Sato, S.1    Hughes, R.C.2
  • 45
    • 0027482681 scopus 로고
    • Regulation of the expression of galactoside-binding lectin during human monocylic differentiation
    • Nangia-Makker, P., J. Ochieng, J. K. Christman, and A. Raz. 1993. Regulation of the expression of galactoside-binding lectin during human monocylic differentiation. Cancer Res. 53:5033.
    • (1993) Cancer Res. , vol.53 , pp. 5033
    • Nangia-Makker, P.1    Ochieng, J.2    Christman, J.K.3    Raz, A.4
  • 46
    • 0029993331 scopus 로고    scopus 로고
    • Apoptosis and the maintenance of homeostasis in the immune system
    • Osborne, B. A. 1996. Apoptosis and the maintenance of homeostasis in the immune system. Curr. Opin. Immunol. 8:245.
    • (1996) Curr. Opin. Immunol. , vol.8 , pp. 245
    • Osborne, B.A.1
  • 47
    • 0030023715 scopus 로고    scopus 로고
    • Purification and molecular characterization of a novel 16-kDa galectin from the nematode Caenorhabditis elegans
    • Hirabayashi, J., M. Ubukata, and K. Kasai. 1996. Purification and molecular characterization of a novel 16-kDa galectin from the nematode Caenorhabditis elegans. J. Biol. Chem. 271:2497.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2497
    • Hirabayashi, J.1    Ubukata, M.2    Kasai, K.3
  • 48
    • 0026336384 scopus 로고
    • Isolation of a cDNA clone, encoding a human β-galactoside-binding protein overexpressed during glucocorticoid-induced cell death
    • Goldstone, S. D., and M. F. Lavin. 1991. Isolation of a cDNA clone, encoding a human β-galactoside-binding protein overexpressed during glucocorticoid-induced cell death. Biochem. Biophys. Res. Commun. 178:746.
    • (1991) Biochem. Biophys. Res. Commun. , vol.178 , pp. 746
    • Goldstone, S.D.1    Lavin, M.F.2
  • 49
    • 0027485050 scopus 로고
    • Normal development of mice carrying a null mutation in the gene encoding the L14 S-type lectin
    • Poirrier, F., and E. J. Robertson. 1993. Normal development of mice carrying a null mutation in the gene encoding the L14 S-type lectin. Development 119:1229.
    • (1993) Development , vol.119 , pp. 1229
    • Poirrier, F.1    Robertson, E.J.2
  • 50
    • 0022497852 scopus 로고
    • Genetic control of programmed cell death in the nematode C. elegans
    • Ellis, H. M., and H. R. Horvitz. 1986. Genetic control of programmed cell death in the nematode C. elegans. Cell 44:817.
    • (1986) Cell , vol.44 , pp. 817
    • Ellis, H.M.1    Horvitz, H.R.2
  • 51
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltvai, Z. N., C. L. Milliman, and S. J. Korsmeyer. 1993. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 74:609.
    • (1993) Cell , vol.74 , pp. 609
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.