메뉴 건너뛰기




Volumn 4, Issue 11, 1998, Pages 2771-2777

Elevated serum levels of Trichosanthes japonica agglutinin-I binding alkaline phosphatase in relation to high-risk groups for hepatocellular carcinomas

Author keywords

[No Author keywords available]

Indexed keywords

AGGLUTININ; ALKALINE PHOSPHATASE; ISOENZYME; TRICHOSANTHES EXTRACT;

EID: 0031756620     PISSN: 10780432     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (7)

References (41)
  • 1
    • 0023696449 scopus 로고
    • Structure of the human liver/bone/kidney alkaline phosphatase gene
    • Weiss, M. J., Ray, K., Henthorn, P. S., Lamb, B., Kadesch, T., and Harris, H. Structure of the human liver/bone/kidney alkaline phosphatase gene. J. Biol. Chem., 263: 12002-12010, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12002-12010
    • Weiss, M.J.1    Ray, K.2    Henthorn, P.S.3    Lamb, B.4    Kadesch, T.5    Harris, H.6
  • 2
    • 0023732992 scopus 로고
    • Sequence and characterization of the human intestinal alkaline phosphatase gene
    • Henthorn, P. S., Ruducha, M., Kadesch, T., Weiss, M. J., and Harris, H. Sequence and characterization of the human intestinal alkaline phosphatase gene. J. Biol. Chem., 263: 12011-12019, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12011-12019
    • Henthorn, P.S.1    Ruducha, M.2    Kadesch, T.3    Weiss, M.J.4    Harris, H.5
  • 3
    • 0023780755 scopus 로고
    • Nucleotide sequence of the human placental alkaline phosphatase gene
    • Knoll, B. J., Rothblum, K. N., and Longley, M. Nucleotide sequence of the human placental alkaline phosphatase gene. J. Biol. Chem., 263: 12020-12027, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12020-12027
    • Knoll, B.J.1    Rothblum, K.N.2    Longley, M.3
  • 4
    • 0023939569 scopus 로고
    • Seminoma-derived Nagao isozyme is encoded by a germ-cell alkaline phosphatase gene
    • Millan, J. L., and Manes, T. Seminoma-derived Nagao isozyme is encoded by a germ-cell alkaline phosphatase gene. Proc. Natl. Acad. Sci. USA. 85: 3024-3028, 1988.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3024-3028
    • Millan, J.L.1    Manes, T.2
  • 5
    • 0019132672 scopus 로고
    • Human alkaline phosphatase. Evidence of three isoenzymes (placental, intestinal and liver-bone-kidney-type) by lectin-binding affinity and immunological specificity
    • Lehmann, F. G. Human alkaline phosphatase. Evidence of three isoenzymes (placental, intestinal and liver-bone-kidney-type) by lectin-binding affinity and immunological specificity. Biochim. Biophys. Acta. 616: 41-59, 1980.
    • (1980) Biochim. Biophys. Acta , vol.616 , pp. 41-59
    • Lehmann, F.G.1
  • 6
    • 0022098460 scopus 로고
    • Incubation with neuraminidase and affinity electrophoresis with wheat-germ lectin compared for separating and quantifying alkaline phosphatase isoenzymes
    • Rosalki, S. B., and Foo, A. Y. Incubation with neuraminidase and affinity electrophoresis with wheat-germ lectin compared for separating and quantifying alkaline phosphatase isoenzymes. Clin. Chem., 31: 1198-1200, 1985.
    • (1985) Clin. Chem. , vol.31 , pp. 1198-1200
    • Rosalki, S.B.1    Foo, A.Y.2
  • 8
    • 0027955179 scopus 로고
    • Increase of fucosylated serum cholinesterase in relation to high risk groups for hepatocellular carcinomas
    • Ohkura, T., Hada, T., Higashino, K., Ohue, T., Kochibe, N., Koide, N., and Yamashita, K. Increase of fucosylated serum cholinesterase in relation to high risk groups for hepatocellular carcinomas. Cancer Res., 54: 55-61, 1994.
    • (1994) Cancer Res. , vol.54 , pp. 55-61
    • Ohkura, T.1    Hada, T.2    Higashino, K.3    Ohue, T.4    Kochibe, N.5    Koide, N.6    Yamashita, K.7
  • 9
    • 77957014557 scopus 로고
    • Affinity chromatography
    • W. B. Jakoby (ed.), New York: Academic Press
    • Cuatrecasas, P., and Anfinsen, CB. Affinity chromatography. In: W. B. Jakoby (ed.), Methods in Enzymology, Vol. 22, pp. 345-378, New York: Academic Press, 1971.
    • (1971) Methods in Enzymology , vol.22 , pp. 345-378
    • Cuatrecasas, P.1    Anfinsen, C.B.2
  • 10
    • 0017715417 scopus 로고
    • Systematic purification of five glycosidases from Streptococcus (Diplococcus) pneumoniae
    • Glasgow, L. R., Paulson, J. C., and Hill, R. L. Systematic purification of five glycosidases from Streptococcus (Diplococcus) pneumoniae. J. Biol. Chem., 252: 8615-8623, 1977.
    • (1977) J. Biol. Chem. , vol.252 , pp. 8615-8623
    • Glasgow, L.R.1    Paulson, J.C.2    Hill, R.L.3
  • 11
    • 0020490930 scopus 로고
    • Purification of an almond emulsin fucosidase on Cibacron Blue-Sepharose and demonstration of its activity toward fucose-containing glycoproteins
    • Imber, M. J., Glasgow, L. R., and Pizzo, S. V. Purification of an almond emulsin fucosidase on Cibacron Blue-Sepharose and demonstration of its activity toward fucose-containing glycoproteins. J. Biol. Chem., 257: 8205-8210, 1982.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8205-8210
    • Imber, M.J.1    Glasgow, L.R.2    Pizzo, S.V.3
  • 12
    • 0019877155 scopus 로고
    • The carbohydrate-binding specificity of pea and lentil lectins: Fucose is an important determinant
    • Kornfeld, K., Reitman, M. L., and Kornfeld, R. The carbohydrate-binding specificity of pea and lentil lectins: fucose is an important determinant. J. Biol. Chem., 256: 6633-6640, 1981.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6633-6640
    • Kornfeld, K.1    Reitman, M.L.2    Kornfeld, R.3
  • 13
    • 0019572737 scopus 로고
    • Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins
    • Debray, H., Decout, D., Strecker, G., Spik, G., and Montreuil, J. Specificity of twelve lectins towards oligosaccharides and glycopeptides related to N-glycosylproteins. Eur. J. Biochem., 117: 41-55, 1981.
    • (1981) Eur. J. Biochem. , vol.117 , pp. 41-55
    • Debray, H.1    Decout, D.2    Strecker, G.3    Spik, G.4    Montreuil, J.5
  • 14
    • 0016772320 scopus 로고
    • Fractionation of glycopeptides by affinity column chromatography on concanavalin A-Sepharose
    • Tokyo
    • Ogata, S., Muramatsu, T., and Kobata, A. Fractionation of glycopeptides by affinity column chromatography on concanavalin A-Sepharose. J. Biochem. (Tokyo), 78: 687-696, 1975.
    • (1975) J. Biochem. , vol.78 , pp. 687-696
    • Ogata, S.1    Muramatsu, T.2    Kobata, A.3
  • 15
    • 0018786476 scopus 로고
    • Structural determinants of concanavalin A specificity for oligosaccharides
    • Baenziger, J. U., and Fiete, D. Structural determinants of concanavalin A specificity for oligosaccharides. J. Biol. Chem., 254: 2400-2407, 1979.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2400-2407
    • Baenziger, J.U.1    Fiete, D.2
  • 16
    • 0021449415 scopus 로고
    • Carbohydrate binding studies on the lectin from Datura stramonium seeds
    • Crowley, J. F., Goldstein, I. J., Arnarp, J., and Lönngren, J. Carbohydrate binding studies on the lectin from Datura stramonium seeds. Arch. Biochem. Biophys., 231: 524-533, 1984.
    • (1984) Arch. Biochem. Biophys. , vol.231 , pp. 524-533
    • Crowley, J.F.1    Goldstein, I.J.2    Arnarp, J.3    Lönngren, J.4
  • 17
    • 0023644519 scopus 로고
    • Carbohydrate binding properties of complex-type oligosaccharides on immobilized Datura stramonium lectin
    • Yamashita, K., Totani, K., Ohkura, T., Takasaki, S., Goldstein, I. J., and Kobata, A. Carbohydrate binding properties of complex-type oligosaccharides on immobilized Datura stramonium lectin. J. Biol. Chem., 262: 1602-1607, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1602-1607
    • Yamashita, K.1    Totani, K.2    Ohkura, T.3    Takasaki, S.4    Goldstein, I.J.5    Kobata, A.6
  • 18
    • 0024278423 scopus 로고
    • The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complex-type Asn-linked oligosaccharides containing terminal sialic acid-linked α2→3 to penultimate galactose residues
    • Wang, W. C., and Cummings, R. D. The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complex-type Asn-linked oligosaccharides containing terminal sialic acid-linked α2→3 to penultimate galactose residues. J. Biol. Chem., 263: 4576-4585, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4576-4585
    • Wang, W.C.1    Cummings, R.D.2
  • 19
    • 0026439093 scopus 로고
    • -→6 Galβ1→4GlcNAc specific lectin in tuberous roots of Trichosanthes japonica
    • -→6 Galβ1→4GlcNAc specific lectin in tuberous roots of Trichosanthes japonica. Biochemistry, 31: 11647-11650, 1992.
    • (1992) Biochemistry , vol.31 , pp. 11647-11650
    • Yamashita, K.1    Umetsu, K.2    Suzuki, T.3    Ohkura, T.4
  • 20
    • 0026461130 scopus 로고
    • Purification and characterization of a Fucα1→2Galβ1→ and GalNAcβ1→-specific lectin in root tubers of Trichosanthes japonica
    • Yamashita, K., Ohkura, T. Umetsu, K., and Suzuki, T. Purification and characterization of a Fucα1→2Galβ1→ and GalNAcβ1→-specific lectin in root tubers of Trichosanthes japonica. J. Biol. Chem., 267: 25414-25422, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25414-25422
    • Yamashita, K.1    Ohkura, T.2    Umetsu, K.3    Suzuki, T.4
  • 21
    • 0021893594 scopus 로고
    • Fractionation of L-fucose-containing oligosaccharides on immobilized Aleuria aurantia lectin
    • Yamashita, K., Kochibe, N., Ohkura, T., Ueda, I., and Kobata, A. Fractionation of L-fucose-containing oligosaccharides on immobilized Aleuria aurantia lectin. J. Biol. Chem., 260: 4688-4693, 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 4688-4693
    • Yamashita, K.1    Kochibe, N.2    Ohkura, T.3    Ueda, I.4    Kobata, A.5
  • 22
    • 0024969427 scopus 로고
    • Aleuria aurantia agglutinin. A new isolation procedure and further study of its specificity towards various glycopeptides and oligosaccharides
    • Debray, H., and Montreuil, J. Aleuria aurantia agglutinin. A new isolation procedure and further study of its specificity towards various glycopeptides and oligosaccharides. Carbohydr. Res., 185: 15-26, 1989.
    • (1989) Carbohydr. Res. , vol.185 , pp. 15-26
    • Debray, H.1    Montreuil, J.2
  • 23
    • 0018787411 scopus 로고
    • Structural determinants of Ricinus communis agglutinin and toxin specificity for oligosaccharides
    • Baenziger, J. U., and Fiete, D. Structural determinants of Ricinus communis agglutinin and toxin specificity for oligosaccharides. J. Biol. Chem., 254: 9795-9799, 1979.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9795-9799
    • Baenziger, J.U.1    Fiete, D.2
  • 24
    • 0009594419 scopus 로고
    • Lectins. Properties and applications to the study of complex carbohydrates in solution and on cell surfaces
    • V. Ginsburg and P. W. Robbins (eds.), New York: John Wiley & Sons
    • Lis, H., and Sharon, N. Lectins. Properties and applications to the study of complex carbohydrates in solution and on cell surfaces. In: V. Ginsburg and P. W. Robbins (eds.), Biology of carbohydrates. Vol 2, pp. 1-85. New York: John Wiley & Sons, 1984.
    • (1984) Biology of Carbohydrates , vol.2 , pp. 1-85
    • Lis, H.1    Sharon, N.2
  • 25
    • 0024800215 scopus 로고
    • Lectin affinity chromatography of alycolipids and glycolipid-derived oligosaccharides
    • V. Ginsburg (ed.), New York: Academic Press
    • Smith, D. F., and Torres, B. V. Lectin affinity chromatography of alycolipids and glycolipid-derived oligosaccharides. In: V. Ginsburg (ed.), Methods in Enzymology, Vol. 179, pp. 30-45. New York: Academic Press, 1989.
    • (1989) Methods in Enzymology , vol.179 , pp. 30-45
    • Smith, D.F.1    Torres, B.V.2
  • 26
    • 0017413222 scopus 로고
    • Five α-D-galactopyranosyl-binding isolectins from Bandeiraea simplicifolia seeds
    • Murphy, L. A., and Goldstein, I. J. Five α-D-galactopyranosyl-binding isolectins from Bandeiraea simplicifolia seeds. J. Biol. Chem., 252: 4739-4742, 1977.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4739-4742
    • Murphy, L.A.1    Goldstein, I.J.2
  • 27
    • 0023879374 scopus 로고
    • Structural study on the carbohydrate moiety of human placental alkaline phosphatase
    • Tokyo
    • Endo, T., Ohbayashi, H., Hayashi, Y., Ikehara, Y., Kochibe, N., and Kobata, A. Structural study on the carbohydrate moiety of human placental alkaline phosphatase. J. Biochem. (Tokyo), 103: 182-187, 1988.
    • (1988) J. Biochem. , vol.103 , pp. 182-187
    • Endo, T.1    Ohbayashi, H.2    Hayashi, Y.3    Ikehara, Y.4    Kochibe, N.5    Kobata, A.6
  • 28
    • 0024358246 scopus 로고
    • Comparative study of sugar chains of γ-glutamyltranspeptidases purified from human hepatocellular carcinoma and from human liver
    • Tokyo
    • Yamashita, K., Totani, K., Iwaki, Y., Takamizawa, I., Tateishi, N., Higashi, T., Sakamoto, Y., and Kobata, A. Comparative study of sugar chains of γ-glutamyltranspeptidases purified from human hepatocellular carcinoma and from human liver. J. Biochem. (Tokyo), 105: 728-735, 1989.
    • (1989) J. Biochem. , vol.105 , pp. 728-735
    • Yamashita, K.1    Totani, K.2    Iwaki, Y.3    Takamizawa, I.4    Tateishi, N.5    Higashi, T.6    Sakamoto, Y.7    Kobata, A.8
  • 29
    • 0026785327 scopus 로고
    • Structures of the asparagine-linked oligosaccharide chains of human von Willebrand factor. Occurrence of blood group A, B, and H(O) structures
    • Matsui, T., Titani, K., and Mizuochi, T. Structures of the asparagine-linked oligosaccharide chains of human von Willebrand factor. Occurrence of blood group A, B, and H(O) structures. J. Biol. Chem., 267: 8723-8731, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8723-8731
    • Matsui, T.1    Titani, K.2    Mizuochi, T.3
  • 30
    • 0025835071 scopus 로고
    • Hepatocellular carcinoma: A worldwide problems and the major risk factors
    • Simonetti, R. G., Gamma, C., Fiolello, F., et al. Hepatocellular carcinoma: a worldwide problems and the major risk factors. Dig. Dis. Sci., 36: 962-972, 1995.
    • (1995) Dig. Dis. Sci. , vol.36 , pp. 962-972
    • Simonetti, R.G.1    Gamma, C.2    Fiolello, F.3
  • 31
    • 0024562457 scopus 로고
    • Altered glycosylation of serum transferrin of patients with hepatocellular carcinoma
    • Yamashita, K., Koide, N., Endo, T., Iwaki, Y., and Kobata, A. Altered glycosylation of serum transferrin of patients with hepatocellular carcinoma. J. Biol. Chem., 264: 2415-2423, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2415-2423
    • Yamashita, K.1    Koide, N.2    Endo, T.3    Iwaki, Y.4    Kobata, A.5
  • 34
    • 0029006085 scopus 로고
    • Analysing connective tissue metabolites in human serum. Biochemical, physiological and methodological aspects
    • Risteli, J., and Risteli, L. Analysing connective tissue metabolites in human serum. Biochemical, physiological and methodological aspects. J. Hepatol., 22 (Suppl. 2): 77-81, 1995.
    • (1995) J. Hepatol. , vol.22 , Issue.2 SUPPL. , pp. 77-81
    • Risteli, J.1    Risteli, L.2
  • 35
    • 0024587195 scopus 로고
    • Liver fibrosis and extracellular matrix
    • Biagini, G., and Ballardini, G. Liver fibrosis and extracellular matrix. J. Hepatol., 8: 115-124, 1989.
    • (1989) J. Hepatol. , vol.8 , pp. 115-124
    • Biagini, G.1    Ballardini, G.2
  • 36
    • 0021847331 scopus 로고
    • Increased serum levels of hyaluronate in liver disease
    • Engstrom-Laurent, A., Loof, L., Nyberg, A., and Schroder, T. Increased serum levels of hyaluronate in liver disease. Hepatology, 5: 638-642, 1985.
    • (1985) Hepatology , vol.5 , pp. 638-642
    • Engstrom-Laurent, A.1    Loof, L.2    Nyberg, A.3    Schroder, T.4
  • 37
    • 0030011961 scopus 로고    scopus 로고
    • Clinical significance of serum hyaluronan in patients with chronic viral liver disease
    • Murawaki, Y., Ikuta, Y., Koda, M., Nishimura, Y., and Kawasaki, H. Clinical significance of serum hyaluronan in patients with chronic viral liver disease. J. Gastroenterol. Hepatol., 11: 459-465, 1996.
    • (1996) J. Gastroenterol. Hepatol. , vol.11 , pp. 459-465
    • Murawaki, Y.1    Ikuta, Y.2    Koda, M.3    Nishimura, Y.4    Kawasaki, H.5
  • 39
    • 0024847844 scopus 로고
    • N-Acetylglucosaminyltransferase III in human serum and liver and hepatoma tissues: Increased activity in liver cirrhosis and hepatoma patients
    • Ishibashi, K., Nishikawa, A., Hayashi, N., Kasahara, A., Sato, N., Fujii, S., Kamada, T., and Taniguchi, N. N-Acetylglucosaminyltransferase III in human serum and liver and hepatoma tissues: increased activity in liver cirrhosis and hepatoma patients. Clin. Chim. Acta, 185: 325-332, 1989.
    • (1989) Clin. Chim. Acta , vol.185 , pp. 325-332
    • Ishibashi, K.1    Nishikawa, A.2    Hayashi, N.3    Kasahara, A.4    Sato, N.5    Fujii, S.6    Kamada, T.7    Taniguchi, N.8
  • 40
    • 0031550510 scopus 로고    scopus 로고
    • Human T-cell leukemia virus-1 encoded Tax protein transactivated α1-3fucosyltransferase Fuc-T VII, which synthesizes sialyl Lexis X, a selectin ligand expressed on adult T-cell leukemia cells
    • Hiraiwa, N., Hiraiwa, M., and Kannagi, R. Human T-cell leukemia virus-1 encoded Tax protein transactivated α1-3fucosyltransferase Fuc-T VII, which synthesizes sialyl Lexis X, a selectin ligand expressed on adult T-cell leukemia cells. Biochem. Biophys. Res. Commun., 231: 183-186, 1997.
    • (1997) Biochem. Biophys. Res. Commun. , vol.231 , pp. 183-186
    • Hiraiwa, N.1    Hiraiwa, M.2    Kannagi, R.3
  • 41
    • 0029911075 scopus 로고    scopus 로고
    • Transcriptional regulation of the N-acetylglucosaminyltransferase V gene in human bile duct carcinoma (HuCC-T1) is mediated by Ets-1
    • Kang, R., Saito, H., Ihara, Y., Miyoshi, E., Koyama, N., Sheng, Y., and Taniguchi, N. Transcriptional regulation of the N-acetylglucosaminyltransferase V gene in human bile duct carcinoma (HuCC-T1) is mediated by Ets-1. J. Biol. Chem., 271: 26706-26712, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26706-26712
    • Kang, R.1    Saito, H.2    Ihara, Y.3    Miyoshi, E.4    Koyama, N.5    Sheng, Y.6    Taniguchi, N.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.