메뉴 건너뛰기




Volumn 17, Issue 2, 1997, Pages 219-230

Generation of H2O2 by human neutrophils and changes of cytosolic Ca2+ and pH of rat thymocytes in response to galactoside-binding proteins (lectins or immunoglobulins)

Author keywords

Biosignaling pathways; Endogenous lectins; Galectins; Hydrogen peroxide

Indexed keywords

CALCIUM ION; CARBOHYDRATE BINDING PROTEIN; GALAPTIN; HYDROGEN PEROXIDE; IMMUNOGLOBULIN; LECTIN; PLANT LECTIN; VISCUM ALBUM LECTIN; AMILORIDE; CALCIUM; GALECTIN; GLYCOCONJUGATE; HEMAGGLUTININ;

EID: 0030610034     PISSN: 01448463     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1027389614391     Document Type: Article
Times cited : (20)

References (37)
  • 3
    • 0026062477 scopus 로고
    • Detection and functions of mammalian lectins - With emphasis on membrane lectins
    • Gabius, H.-J. (1991) Detection and functions of mammalian lectins - with emphasis on membrane lectins. Biochim. Biophys. Acta 1071:1-18.
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 1-18
    • Gabius, H.-J.1
  • 4
    • 0029054907 scopus 로고
    • I-type lectins
    • Powell, L. D. and Varki, A. (1995) I-type lectins. J. Biol. Chem. 270:14243-14246.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14243-14246
    • Powell, L.D.1    Varki, A.2
  • 6
    • 0001810168 scopus 로고    scopus 로고
    • The information-storing potential of the sugar code
    • Gabius, H.-J. and Gabius, S., Eds. Chapman & Hall, Weinheim-London-New York
    • Laine, R. A. (1997) The information-storing potential of the sugar code. In: Glycosciences: Status and Perspectives. (Gabius, H.-J. and Gabius, S., Eds). Chapman & Hall, Weinheim-London-New York, pp. 1-14.
    • (1997) Glycosciences: Status and Perspectives , pp. 1-14
    • Laine, R.A.1
  • 7
    • 0003105605 scopus 로고    scopus 로고
    • Glycobiology of signal transduction
    • Gabius, H.-J. and Gabius, S., Eds. Chapman & Hall, Weinheim-London-New York
    • Villalobo, A., Horcajadas, J. A., André, S. and Gabius, H.-J. (1997) Glycobiology of signal transduction. In: Glycosciences: Status and Perspectives. (Gabius, H.-J. and Gabius, S., Eds). Chapman & Hall, Weinheim-London-New York, pp. 485-496.
    • (1997) Glycosciences: Status and Perspectives , pp. 485-496
    • Villalobo, A.1    Horcajadas, J.A.2    André, S.3    Gabius, H.-J.4
  • 8
    • 0000708206 scopus 로고    scopus 로고
    • Lectins and carbohydrates in animal cell adhesion and control of proliferation
    • Gabius, H.-J. and Gabius, S., Eds. Chapman & Hall, Weinheim-London-New York
    • Zanetta, J.-P. (1997) Lectins and carbohydrates in animal cell adhesion and control of proliferation. In: Glycosciences: Status and Perspectives. (Gabius, H.-J. and Gabius, S., Eds). Chapman & Hall, Weinheim-London-New York, pp. 439-458.
    • (1997) Glycosciences: Status and Perspectives , pp. 439-458
    • Zanetta, J.-P.1
  • 9
    • 0027585153 scopus 로고
    • Efficient induction of superoxide release from human neutrophils by the galactoside-specific lectin from Viscum album
    • Timoshenko, A. V. and Gabius, H.-J. (1993) Efficient induction of superoxide release from human neutrophils by the galactoside-specific lectin from Viscum album. Biol. Chem. Hoppe-Seyler 374:237-243.
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 237-243
    • Timoshenko, A.V.1    Gabius, H.-J.2
  • 10
    • 0029061878 scopus 로고
    • Viscum album agglutinin-induced aggregation of blood cells and the lectin effects on neutrophil function
    • Timoshenko, A. V., Cherenkevich, S. N. and Gabius, H.-J. (1995) Viscum album agglutinin-induced aggregation of blood cells and the lectin effects on neutrophil function. Biomed. Pharmacother. 49:153-158.
    • (1995) Biomed. Pharmacother. , vol.49 , pp. 153-158
    • Timoshenko, A.V.1    Cherenkevich, S.N.2    Gabius, H.-J.3
  • 11
    • 0028951736 scopus 로고
    • A human lectin, galectin-3 (εbp/Mac-2), stimulates superoxide production by neutrophils
    • Yamaoka, A., Kuwabara, I., Frigeri, L. G. and Liu, F.-T. (1995) A human lectin, galectin-3 (εbp/Mac-2), stimulates superoxide production by neutrophils. J. Immunol. 154:3479-3487.
    • (1995) J. Immunol. , vol.154 , pp. 3479-3487
    • Yamaoka, A.1    Kuwabara, I.2    Frigeri, L.G.3    Liu, F.-T.4
  • 12
    • 0026700180 scopus 로고
    • Rat surfactant protein D enhances the production of oxygen radicals by rat alveolar macrophages
    • Van Iwaarden, J. F., Shimizu, H., Van Colde, P. H. M., Voelker, D. R. and Van Golde, L. M. G. (1992) Rat surfactant protein D enhances the production of oxygen radicals by rat alveolar macrophages. Biochem. J. 286:5-8.
    • (1992) Biochem. J. , vol.286 , pp. 5-8
    • Van Iwaarden, J.F.1    Shimizu, H.2    Van Colde, P.H.M.3    Voelker, D.R.4    Van Golde, L.M.G.5
  • 13
    • 0025076613 scopus 로고
    • Influence of type of linkage and spacer on the interaction of β-galactoside-binding proteins with immobilized affinity ligands
    • Gabius, H.-J. (1990) Influence of type of linkage and spacer on the interaction of β-galactoside-binding proteins with immobilized affinity ligands. Anal. Biochem. 189:91-94.
    • (1990) Anal. Biochem. , vol.189 , pp. 91-94
    • Gabius, H.-J.1
  • 14
    • 0028786452 scopus 로고
    • Differential binding of two chicken β-galactoside-specific lectins to homologous lymphocyte subpopulations and evidence for inhibitory activity of the dimeric lectin on stimulated T cells
    • Schneller, M., et al. (1995) Differential binding of two chicken β-galactoside-specific lectins to homologous lymphocyte subpopulations and evidence for inhibitory activity of the dimeric lectin on stimulated T cells. Cell. Immunol. 166:35-43.
    • (1995) Cell. Immunol. , vol.166 , pp. 35-43
    • Schneller, M.1
  • 15
    • 17544377102 scopus 로고    scopus 로고
    • Different architecture of the combining site of the two chicken galectins revealed by chemical mapping studies with synthetic ligand derivates
    • Solís, D., Romero, A., Kaltner, H., Gabius, H.-J. and Díaz-Mauriño, T. (1996) Different architecture of the combining site of the two chicken galectins revealed by chemical mapping studies with synthetic ligand derivates. J. Biol. Chem. 271:12744-12748.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12744-12748
    • Solís, D.1    Romero, A.2    Kaltner, H.3    Gabius, H.-J.4    Díaz-Mauriño, T.5
  • 16
    • 0028903781 scopus 로고
    • Expression of lectin, interleukin-2 and histopathologic blood group binding sites in prostate cancer and its correlation with integrated optical density and syntactic structure analysis
    • Kayser, K., et al. (1995) Expression of lectin, interleukin-2 and histopathologic blood group binding sites in prostate cancer and its correlation with integrated optical density and syntactic structure analysis. Analyt. Quant. Cytol. Histol. 17:135-142.
    • (1995) Analyt. Quant. Cytol. Histol. , vol.17 , pp. 135-142
    • Kayser, K.1
  • 17
    • 0028075763 scopus 로고
    • Phenotype-associated lectin-binding profiles of normal and transformed blood cells: A comparative analysis of mannose- and galactose-binding lectins from plants and human serum/placenta
    • Mann, K. K., André, S., Gabius, H.-J. and Sharp, J. G. (1994) Phenotype-associated lectin-binding profiles of normal and transformed blood cells: a comparative analysis of mannose- and galactose-binding lectins from plants and human serum/placenta. Eur. J. Cell Biol. 65:145-151.
    • (1994) Eur. J. Cell Biol. , vol.65 , pp. 145-151
    • Mann, K.K.1    André, S.2    Gabius, H.-J.3    Sharp, J.G.4
  • 18
    • 0029001278 scopus 로고
    • Carbohydrate-binding proteins (plant/human lectins and autoantibodies from human serum) as mediators of release of lysozyme, elastase, and myeloperoxidase from human neutrophils
    • Timoshenko, A. V., et al. (1995) Carbohydrate-binding proteins (plant/human lectins and autoantibodies from human serum) as mediators of release of lysozyme, elastase, and myeloperoxidase from human neutrophils. Res. Exp. Med. 195:153-162.
    • (1995) Res. Exp. Med. , vol.195 , pp. 153-162
    • Timoshenko, A.V.1
  • 19
    • 0029026209 scopus 로고
    • Are matrix-immobilized neoglycoproteins, plant and human lectins and carbohydrate-binding antibodies from human serum mediators of adhesion in vitro for carcinoma and lymphosarcoma cells?
    • Wawotzny, R., André, S., Dong, X., Joshi, S. S. and Gabius, H.-J. (1995) Are matrix-immobilized neoglycoproteins, plant and human lectins and carbohydrate-binding antibodies from human serum mediators of adhesion in vitro for carcinoma and lymphosarcoma cells? Anticancer Res. 15:169-174.
    • (1995) Anticancer Res. , vol.15 , pp. 169-174
    • Wawotzny, R.1    André, S.2    Dong, X.3    Joshi, S.S.4    Gabius, H.-J.5
  • 20
    • 0029111925 scopus 로고
    • Affinity-purified antibodies against α-galactosyl residues from human serum: Comparison of their binding in bovine testicular tissue with that of the Griffonia simplicifolia lectin (GSL-B-4) and impact of labelling on epitope localization
    • Dong, X., Amselgruber, W. M., Kaltner, H., Gabius, H.-J. and Sinowatz, F. (1995) Affinity-purified antibodies against α-galactosyl residues from human serum: comparison of their binding in bovine testicular tissue with that of the Griffonia simplicifolia lectin (GSL-B-4) and impact of labelling on epitope localization. Eur. J. Cell. Biol. 68:96-101.
    • (1995) Eur. J. Cell. Biol. , vol.68 , pp. 96-101
    • Dong, X.1    Amselgruber, W.M.2    Kaltner, H.3    Gabius, H.-J.4    Sinowatz, F.5
  • 22
    • 0028913784 scopus 로고
    • Influence of the galactoside-specific lectin from Viscum album and its subunits on cell aggregation and selected intracellular parameters of rat thymocytes
    • Tomoshenko, A. V. and Gabius, H.-J. (1995) Influence of the galactoside-specific lectin from Viscum album and its subunits on cell aggregation and selected intracellular parameters of rat thymocytes. Planta Med. 61:130-133.
    • (1995) Planta Med. , vol.61 , pp. 130-133
    • Tomoshenko, A.V.1    Gabius, H.-J.2
  • 23
    • 0023876336 scopus 로고
    • Calcium-dependent intracellular acidification dominates the pH response to mitogen in human T cells
    • Gelfand, E. W., Cheung, R. K. and Grinstein, S. (1988) Calcium-dependent intracellular acidification dominates the pH response to mitogen in human T cells. J. Immunol. 140:246-252.
    • (1988) J. Immunol. , vol.140 , pp. 246-252
    • Gelfand, E.W.1    Cheung, R.K.2    Grinstein, S.3
  • 25
    • 0342923115 scopus 로고
    • Glycobiological aspects of the activation of phagocytes' respiratory chain
    • Timoshenko, A. V. and Cherenkevich, S. N. (1994) Glycobiological aspects of the activation of phagocytes' respiratory chain. Biopolimery i kletka 10:58-65 [in Russian].
    • (1994) Biopolimery i Kletka , vol.10 , pp. 58-65
    • Timoshenko, A.V.1    Cherenkevich, S.N.2
  • 27
    • 0024529464 scopus 로고
    • + exchange and growth factor-induced cytosolic pH changes. Role in cellular proliferation
    • + exchange and growth factor-induced cytosolic pH changes. Role in cellular proliferation. Biochim. Biophys. Acta 988:73-97.
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 73-97
    • Grinstein, S.1    Rotin, D.2    Mason, M.J.3
  • 28
    • 0002003782 scopus 로고    scopus 로고
    • Lectins in tumors - With focus on galectins
    • Gabius, H.-J. and Gabius, S., Eds. Chapman & Hall, Weinheim-London-New York
    • Ohannesian, D. W. and Lotan, R. (1997) Lectins in tumors - with focus on galectins. In: Glycosiences: Status and Perspectives. (Gabius, H.-J. and Gabius, S., Eds). Chapman & Hall, Weinheim-London-New York, pp. 459-469.
    • (1997) Glycosiences: Status and Perspectives , pp. 459-469
    • Ohannesian, D.W.1    Lotan, R.2
  • 29
    • 0029586586 scopus 로고
    • Protein-Zucker-Erkennung: Grundlagen und medizinische Anwendung am Beispiel der Tumorlektinologie
    • Gabius, H.-J., Kayser, K. and Gabius, S. (1995) Protein-Zucker-Erkennung: Grundlagen und medizinische Anwendung am Beispiel der Tumorlektinologie. Naturwissenschaften 82:533-543.
    • (1995) Naturwissenschaften , vol.82 , pp. 533-543
    • Gabius, H.-J.1    Kayser, K.2    Gabius, S.3
  • 30
    • 0030766193 scopus 로고    scopus 로고
    • Concepts of tumor lectinology
    • in press
    • Gabius, H.-J. (1997) Concepts of tumor lectinology. Cancer Investig. (in press).
    • (1997) Cancer Investig.
    • Gabius, H.-J.1
  • 31
    • 0030445222 scopus 로고    scopus 로고
    • Comparative cross-linking activities of lactose-specific plant and animal lectins and a natural lactose-binding immunoglobulin G fraction from human serum with asialofetuin
    • in press
    • Gupta, D., Kaltner, H., Dong, X., Gabius, H.-J. and Brewer, C. F. (1996) Comparative cross-linking activities of lactose-specific plant and animal lectins and a natural lactose-binding immunoglobulin G fraction from human serum with asialofetuin. Glycobiology (in press).
    • (1996) Glycobiology
    • Gupta, D.1    Kaltner, H.2    Dong, X.3    Gabius, H.-J.4    Brewer, C.F.5
  • 32
    • 0024553735 scopus 로고
    • The human mannose-binding protein functions as an opsonin
    • Kuhlman, M., Joiner, K. and Ezekowitz, R. A. B. (1989). The human mannose-binding protein functions as an opsonin. J. Exp. Med. 169:1733-1745.
    • (1989) J. Exp. Med. , vol.169 , pp. 1733-1745
    • Kuhlman, M.1    Joiner, K.2    Ezekowitz, R.A.B.3
  • 33
    • 0027191914 scopus 로고
    • Lectin-like inhibition of immune complex receptor-mediated stimulation of neutrophils. Effects of cytosolic calcium release and Superoxide production
    • Sehgal, G., Zhang, K., Todd III, R. F., Boxer, L. A. and Petty, H. R. (1993) Lectin-like inhibition of immune complex receptor-mediated stimulation of neutrophils. Effects of cytosolic calcium release and Superoxide production. J. Immunol. 150:4571-4580.
    • (1993) J. Immunol. , vol.150 , pp. 4571-4580
    • Sehgal, G.1    Zhang, K.2    Todd III, R.F.3    Boxer, L.A.4    Petty, H.R.5
  • 34
    • 0023908198 scopus 로고
    • Cytosolic calcium, oxygen consumption and the intracellular pH of stimulated neutrophils
    • Nasmith, P. E. and Grinstein, S. (1988) Cytosolic calcium, oxygen consumption and the intracellular pH of stimulated neutrophils. Biosci. Rep. 8:65-76.
    • (1988) Biosci. Rep. , vol.8 , pp. 65-76
    • Nasmith, P.E.1    Grinstein, S.2
  • 35
    • 0020537718 scopus 로고
    • Intracellular pH of stimulated thymocytes measured with a new fluorescent indicator
    • Rogers, J., Hesketh, T. R., Smith, G. A. and Metcalfe, J. C. (1983) Intracellular pH of stimulated thymocytes measured with a new fluorescent indicator. J. Biol. Chem. 258:5994-5997.
    • (1983) J. Biol. Chem. , vol.258 , pp. 5994-5997
    • Rogers, J.1    Hesketh, T.R.2    Smith, G.A.3    Metcalfe, J.C.4
  • 36
    • 0025361833 scopus 로고
    • + exchanger in AR42J cells by increasing its affinity for intracellular pH
    • + exchanger in AR42J cells by increasing its affinity for intracellular pH. Am. J. Physiol. 258:G958-G966.
    • (1990) Am. J. Physiol. , vol.258
    • Bastie, M.1    Williams, J.A.2
  • 37
    • 0018764575 scopus 로고
    • Intracellular pH measurements in Ehrlich ascites tumor cells utilizing spectroscopic probes generated in situ
    • Thomas, J. A., Buchsbaum, R. N., Zimniak, A. and Racker, E. (1979) Intracellular pH measurements in Ehrlich ascites tumor cells utilizing spectroscopic probes generated in situ. Biochemistry 18:2210-2218.
    • (1979) Biochemistry , vol.18 , pp. 2210-2218
    • Thomas, J.A.1    Buchsbaum, R.N.2    Zimniak, A.3    Racker, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.