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Volumn 127, Issue 2, 2000, Pages 193-202

Induction of rat alkaline phosphatase isozymes bearing a glycan-phosphatidylinositol anchor modified by in vivo treatment with a benzimidazole derivative linked to ethylbenzene

Author keywords

Benzimidazole derivative linked to ethylbenzene; Con A chromatography; Electrophoresis; Ficin; Glycan phosphatidylinositol anchor; Intestinal alkaline phosphatase; Phosphatidylinositol specific phospholipase C; Rat alkaline phosphatase isozymes

Indexed keywords

ALKALINE PHOSPHATASE; BENZIMIDAZOLE DERIVATIVE; ETHYLBENZENE; FICIN; GLYCAN; PHOSPHATIDYLINOSITOL; PHOSPHOLIPASE C;

EID: 0033816958     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-0491(00)00252-2     Document Type: Article
Times cited : (4)

References (33)
  • 1
    • 0020537386 scopus 로고
    • Biliary protein output by isolated perfused rat livers. Effects of bile salts
    • Barnwell, S.G., Godfrey, P.P., Lowe, P.J., Coleman, R., 1983. Biliary protein output by isolated perfused rat livers. Effects of bile salts. Biochem. J. 210, 549-557.
    • (1983) Biochem. J. , vol.210 , pp. 549-557
    • Barnwell, S.G.1    Godfrey, P.P.2    Lowe, P.J.3    Coleman, R.4
  • 2
    • 0021209650 scopus 로고
    • Partial characterization of the oligosaccharides of mouse thymocyte thy-1 glycoprotein
    • Carlsson, S.R., Stigbrand, T., 1984. Partial characterization of the oligosaccharides of mouse thymocyte thy-1 glycoprotein. Biochem. J. 221, 379-392.
    • (1984) Biochem. J. , vol.221 , pp. 379-392
    • Carlsson, S.R.1    Stigbrand, T.2
  • 3
    • 0019466089 scopus 로고
    • High-molecular-mass alkaline phosphatase in serum and bile: Physical properties and relationship with other high-molecular-mass enzymes
    • Crofton, P.M., Smith, A.F., 1981. High-molecular-mass alkaline phosphatase in serum and bile: physical properties and relationship with other high-molecular-mass enzymes. Clin. Chem. 27, 860-866.
    • (1981) Clin. Chem. , vol.27 , pp. 860-866
    • Crofton, P.M.1    Smith, A.F.2
  • 4
    • 0022465626 scopus 로고
    • Release of decay-accelerating factor (DAF) from the cell membrane by phosphatidylinositol-specific phospholipase C (PIPLC). Selective modification of a complement regulatory protein
    • Davitz, M.A., Low, M.G., Nussenzweig, V., 1986. Release of decay-accelerating factor (DAF) from the cell membrane by phosphatidylinositol-specific phospholipase C (PIPLC). Selective modification of a complement regulatory protein. J. Exp. Med. 163, 1150-1161.
    • (1986) J. Exp. Med. , vol.163 , pp. 1150-1161
    • Davitz, M.A.1    Low, M.G.2    Nussenzweig, V.3
  • 5
    • 0022342832 scopus 로고
    • Glycosyl-sn-1,2-dimyristylphosphatidylinositol is covalently linked to Trypanosoma brucei variant surface glycoprotein
    • Ferguson, M.A., Low, M.G., Cross, G.A., 1985. Glycosyl-sn-1,2-dimyristylphosphatidylinositol is covalently linked to Trypanosoma brucei variant surface glycoprotein. J. Biol. Chem. 260, 14547-14555.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14547-14555
    • Ferguson, M.A.1    Low, M.G.2    Cross, G.A.3
  • 6
    • 0016044391 scopus 로고
    • Acrylamide disc gel electrophoresis of alkaline phosphatase of human tissues, serum and ascites fluid using triton X-100 in the sample and the gel matrix
    • Fishman, L., 1974. Acrylamide disc gel electrophoresis of alkaline phosphatase of human tissues, serum and ascites fluid using triton X-100 in the sample and the gel matrix. Biochem. Med. 9, 309-315.
    • (1974) Biochem. Med. , vol.9 , pp. 309-315
    • Fishman, L.1
  • 7
    • 0022977133 scopus 로고
    • Purification and characterization of a novel glycan-phosphatidylinositol-specific phospholipase C from Trypanosoma brucei
    • Fox, J.A., Duszenko, M., Ferguson, M.A., Low, M.G., Cross, G.A., 1986. Purification and characterization of a novel glycan-phosphatidylinositol-specific phospholipase C from Trypanosoma brucei. J. Biol. Chem. 261, 15767-15771.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15767-15771
    • Fox, J.A.1    Duszenko, M.2    Ferguson, M.A.3    Low, M.G.4    Cross, G.A.5
  • 8
    • 2642651316 scopus 로고
    • Expression of alkaline phosphatase loci in mammalian tissues
    • Goldstein, D.J., Rogers, C.E., Harris, H., 1980. Expression of alkaline phosphatase loci in mammalian tissues. Proc. Natl. Acad. Sci. USA 77, 2857-2860.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2857-2860
    • Goldstein, D.J.1    Rogers, C.E.2    Harris, H.3
  • 9
    • 0025139287 scopus 로고
    • Purified tetrameric alkaline phosphatase: The effect of treatments with phosphatidylinositol phospholipase C and sodium dodecyl sulfate
    • Hawrylak, K., Stinson, R.A., 1990. Purified tetrameric alkaline phosphatase: the effect of treatments with phosphatidylinositol phospholipase C and sodium dodecyl sulfate. Clin. Chim. Acta 186, 197-201.
    • (1990) Clin. Chim. Acta , vol.186 , pp. 197-201
    • Hawrylak, K.1    Stinson, R.A.2
  • 10
    • 0023018792 scopus 로고
    • A phospholipase C from Trypanosoma brucei which selectively cleaves the glycolipid on the variant surface glycoprotein
    • Hereld, D., Krakow, J.L., Bang, J.D., Hart, G.W., Englund, P.T., 1986. A phospholipase C from Trypanosoma brucei which selectively cleaves the glycolipid on the variant surface glycoprotein. J. Biol. Chem. 261, 13813-13819.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13813-13819
    • Hereld, D.1    Krakow, J.L.2    Bang, J.D.3    Hart, G.W.4    Englund, P.T.5
  • 11
    • 0022335244 scopus 로고
    • Cloning, sequencing, and chromosomal ocalization of human term placental alkaline phosphatase cDNA
    • Kam, W., Clauser, E., Kim, Y.S., Kan, Y.W., Rutter, W.J., 1985. Cloning, sequencing, and chromosomal ocalization of human term placental alkaline phosphatase cDNA. Proc. Natl. Acad. Sci. USA 82, 8715-8719.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8715-8719
    • Kam, W.1    Clauser, E.2    Kim, Y.S.3    Kan, Y.W.4    Rutter, W.J.5
  • 12
    • 0021809748 scopus 로고
    • Electrophoretic characterization of hepatic alkaline phosphatase released by phosphatidylinositol-specific phospholipase C. A comparison with liver membrane and serum-soluble forms
    • Kominami, T., Miki, A., Ikehara, Y., 1985. Electrophoretic characterization of hepatic alkaline phosphatase released by phosphatidylinositol-specific phospholipase C. A comparison with liver membrane and serum-soluble forms. Biochem. J. 227, 183-189.
    • (1985) Biochem. J. , vol.227 , pp. 183-189
    • Kominami, T.1    Miki, A.2    Ikehara, Y.3
  • 13
    • 0019867390 scopus 로고
    • Multiple forms of human intestinal alkaline phosphatase: Chemical and enzymatic properties, and circulating clearances of the fast- and slow-moving enzymes
    • Komoda, T., Sakagishi, Y., Sekine, T., 1981. Multiple forms of human intestinal alkaline phosphatase: chemical and enzymatic properties, and circulating clearances of the fast- and slow-moving enzymes. Clin. Chim. Acta 117, 167-187.
    • (1981) Clin. Chim. Acta , vol.117 , pp. 167-187
    • Komoda, T.1    Sakagishi, Y.2    Sekine, T.3
  • 14
    • 0023007772 scopus 로고
    • A possible mechanism of induction and translocation into blood stream of rat alkaline phosphatase activity by bile duct ligation
    • Komoda, T., Koyama, I., Nagata, A., Sakagishi, Y., Kurata, M., Kumegawa, M., 1986. A possible mechanism of induction and translocation into blood stream of rat alkaline phosphatase activity by bile duct ligation. Arch. Biochem. Biophys. 251, 323-335.
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 323-335
    • Komoda, T.1    Koyama, I.2    Nagata, A.3    Sakagishi, Y.4    Kurata, M.5    Kumegawa, M.6
  • 15
    • 0022633178 scopus 로고
    • Different lectin affinities in rat alkaline phosphatase isozymes: Multiple forms of the isozyme isolated by heterogeneities of sugar moieties
    • Koyama, I., Sakagishi, Y., Komoda, T., 1986. Different lectin affinities in rat alkaline phosphatase isozymes: multiple forms of the isozyme isolated by heterogeneities of sugar moieties. J. Chromatogr. 374, 51-59.
    • (1986) J. Chromatogr. , vol.374 , pp. 51-59
    • Koyama, I.1    Sakagishi, Y.2    Komoda, T.3
  • 16
    • 0023662701 scopus 로고
    • Sugar-chain heterogeneity of human alkaline phosphatases: Differences between normal and tumour-associated isozymes
    • Koyama, I., Miura, M., Matsuzaki, H., Sakagishi, Y., Komoda, T., 1987. Sugar-chain heterogeneity of human alkaline phosphatases: differences between normal and tumour-associated isozymes. J. Chromatogr. 413, 65-78.
    • (1987) J. Chromatogr. , vol.413 , pp. 65-78
    • Koyama, I.1    Miura, M.2    Matsuzaki, H.3    Sakagishi, Y.4    Komoda, T.5
  • 17
    • 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, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0024316809 scopus 로고
    • The glycosyl-phosphatidylinositol anchor of membrane proteins
    • Low, M.G., 1989. The glycosyl-phosphatidylinositol anchor of membrane proteins. Biochim. Biophy. Acta 988, 427-454.
    • (1989) Biochim. Biophy. Acta , vol.988 , pp. 427-454
    • Low, M.G.1
  • 19
    • 0017743279 scopus 로고
    • Release of alkaline phosphatase from membranes by a phosphatidylinositol-specific phospholipase C
    • Low, M.G., Finean, J.B., 1977. Release of alkaline phosphatase from membranes by a phosphatidylinositol-specific phospholipase C. Biochem. J. 167, 281-284.
    • (1977) Biochem. J. , vol.167 , pp. 281-284
    • Low, M.G.1    Finean, J.B.2
  • 20
    • 0023103933 scopus 로고
    • Removal of covalently bound inositol from Torpedo acetylcholinesterase and mammalian alkaline phosphatases by deamination with nitrous acid. Evidence for a common membrane-anchoring structure
    • Low, M.G., Futerman, A.H., Ackermann, K.E., Sherman, W.R., Silman, I., 1987. Removal of covalently bound inositol from Torpedo acetylcholinesterase and mammalian alkaline phosphatases by deamination with nitrous acid. Evidence for a common membrane-anchoring structure. Biochem. J. 241, 615-619.
    • (1987) Biochem. J. , vol.241 , pp. 615-619
    • Low, M.G.1    Futerman, A.H.2    Ackermann, K.E.3    Sherman, W.R.4    Silman, I.5
  • 22
    • 0022970889 scopus 로고
    • Molecular cloning and sequence analysis of human placental alkaline phosphatase
    • Millán, J.L., 1986. Molecular cloning and sequence analysis of human placental alkaline phosphatase. J. Biol. Chem. 261, 3112-3115.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3112-3115
    • Millán, J.L.1
  • 23
    • 0019989821 scopus 로고
    • Alkaline phosphatase isoenzymes
    • Moss, D.W., 1982. Alkaline phosphatase isoenzymes. Clin. Chem. 28, 2007-2016.
    • (1982) Clin. Chem. , vol.28 , pp. 2007-2016
    • Moss, D.W.1
  • 24
    • 0023713647 scopus 로고
    • Chemical characterization of the membrane-anchoring domain of human placental alkaline phosphatase
    • Ogata, S., Hayashi, Y., Takami, N., Ikehara, Y., 1988. Chemical characterization of the membrane-anchoring domain of human placental alkaline phosphatase. J. Biol. Chem. 263, 10489-10494.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10489-10494
    • Ogata, S.1    Hayashi, Y.2    Takami, N.3    Ikehara, Y.4
  • 25
    • 0022510544 scopus 로고
    • Selective radio-labeling and isolation of the hydrophobic membrane-binding domain of human erythrocyte acetylcholinesterase
    • Roberts, W.L., Rosenberry, T.L., 1986. Selective radio-labeling and isolation of the hydrophobic membrane-binding domain of human erythrocyte acetylcholinesterase. Biochemistry 25, 3091-3098.
    • (1986) Biochemistry , vol.25 , pp. 3091-3098
    • Roberts, W.L.1    Rosenberry, T.L.2
  • 26
    • 0024267353 scopus 로고
    • Lipid analysis of the glycoinositol phospholipid membrane anchor of human erythrocyte acetylcholinesterase. Palmitoylation of inositol results in resistance to phosphatidylinositol-specific phospholipase C
    • Roberts, W.L., Myher, J.J., Kuksis, A., Low, M.G., Rosenberry, T.L., 1988. Lipid analysis of the glycoinositol phospholipid membrane anchor of human erythrocyte acetylcholinesterase. Palmitoylation of inositol results in resistance to phosphatidylinositol-specific phospholipase C. J. Biol. Chem. 263, 18766-18775.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18766-18775
    • Roberts, W.L.1    Myher, J.J.2    Kuksis, A.3    Low, M.G.4    Rosenberry, T.L.5
  • 27
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • Stahl, N., Borchelt, D.R., Hsiao, K., Prusiner, S.B., 1987. Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 51, 229-240.
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 28
    • 0022506768 scopus 로고
    • Mapping of the gene coding for the human liver/bone/ kidney isozyme of alkaline phosphatase to chromosome 1
    • Swallow, D.M., Povey, S., Parkar, M., Andrews, P.W., Harris, H., Pym, V.B., Goodfellow, P., 1986. Mapping of the gene coding for the human liver/bone/ kidney isozyme of alkaline phosphatase to chromosome 1. Ann. Hum. Genet. 50, 229-235.
    • (1986) Ann. Hum. Genet. , vol.50 , pp. 229-235
    • Swallow, D.M.1    Povey, S.2    Parkar, M.3    Andrews, P.W.4    Harris, H.5    Pym, V.B.6    Goodfellow, P.7
  • 29
    • 0028085226 scopus 로고
    • Microheterogeneity in glycosylphosphatidylinositol anchor structures of bovine liver 5′-nucleotidase
    • Taguchi, R., Hamakawa, N., Harada-Nishida, M., Fukui, T., Nojima, K., Ikezawa, H., 1994. Microheterogeneity in glycosylphosphatidylinositol anchor structures of bovine liver 5′-nucleotidase. Biochemistry 33, 1017-1022.
    • (1994) Biochemistry , vol.33 , pp. 1017-1022
    • Taguchi, R.1    Hamakawa, N.2    Harada-Nishida, M.3    Fukui, T.4    Nojima, K.5    Ikezawa, H.6
  • 30
    • 0022346423 scopus 로고
    • A glycophospholipid tail at the carboxyl terminus of the thy-1 glycoprotein of neurons and thymocytes
    • Tse, A.G., Barclay, A.N., Watts, A., Williams, A.F., 1985. A glycophospholipid tail at the carboxyl terminus of the thy-1 glycoprotein of neurons and thymocytes. Science 230, 1003-1008.
    • (1985) Science , vol.230 , pp. 1003-1008
    • Tse, A.G.1    Barclay, A.N.2    Watts, A.3    Williams, A.F.4
  • 31
    • 0028099997 scopus 로고
    • Interpretation and clinical significance of alkaline phosphatase isoenzyme patterns
    • Van Hoof, V.O., De Broe, M.E., 1994. Interpretation and clinical significance of alkaline phosphatase isoenzyme patterns. Crit. Rev. Clin. Lab. Sci. 31, 197-293.
    • (1994) Crit. Rev. Clin. Lab. Sci. , vol.31 , pp. 197-293
    • Van Hoof, V.O.1    De Broe, M.E.2
  • 32
    • 0027065032 scopus 로고
    • Phospholipase resis-tance of the glycosyl-phosphatidylinositol membrane anchor on human alkaline phosphatase
    • Wong, Y.W., Low, M.G., 1992. Phospholipase resis-tance of the glycosyl-phosphatidylinositol membrane anchor on human alkaline phosphatase. Clin. Chem. 38, 2517-2525.
    • (1992) Clin. Chem. , vol.38 , pp. 2517-2525
    • Wong, Y.W.1    Low, M.G.2
  • 33
    • 0028276769 scopus 로고
    • Secretion and distribution of rat intestinal surfactant-like particles after fat feeding
    • Yamagishi, F., Komoda, T., Alpers, D.H., 1994. Secretion and distribution of rat intestinal surfactant-like particles after fat feeding. Am. J. Physiol. 266, G944-G952.
    • (1994) Am. J. Physiol. , vol.266
    • Yamagishi, F.1    Komoda, T.2    Alpers, D.H.3


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