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Volumn 28, Issue 5, 1996, Pages 591-599

ATP-diphosphohydrolase activity in rat renal microvillar membranes and vascular tissue

Author keywords

Apyrase; ATP diphosphohydrolase; Ca2+ Mg2+ ATPase; Ecto nucleotidase

Indexed keywords

APYRASE;

EID: 0029887452     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/1357-2725(95)00153-0     Document Type: Article
Times cited : (11)

References (42)
  • 1
    • 0026321837 scopus 로고
    • Characterization of an ATP diphosphohydrolase (EC 3.6.1.5) in synaptosomes from cerebral cortex in adult rats
    • Battastini A. M. O., de Rocha J. B. T., Barcellos C. K., Dias R. D. and Sarkis J. J. F. (1991) Characterization of an ATP diphosphohydrolase (EC 3.6.1.5) in synaptosomes from cerebral cortex in adult rats. Neurochem. Res. 16, 1303-1310.
    • (1991) Neurochem. Res. , vol.16 , pp. 1303-1310
    • Battastini, A.M.O.1    De Rocha, J.B.T.2    Barcellos, C.K.3    Dias, R.D.4    Sarkis, J.J.F.5
  • 3
    • 0014898933 scopus 로고
    • Isolation and biochemical characterization of brush borders from rabbit kidney
    • Berger S. J. and Sacktor B. (1970) Isolation and biochemical characterization of brush borders from rabbit kidney. J. Cell Biol. 47, 637-645.
    • (1970) J. Cell Biol. , vol.47 , pp. 637-645
    • Berger, S.J.1    Sacktor, B.2
  • 4
    • 0019225853 scopus 로고
    • 2+ -dependent adenosine triphosphatase activity in the brush border of rabbit kidney cortex
    • 2+ -dependent adenosine triphosphatase activity in the brush border of rabbit kidney cortex. Arch. Biochem. Biophys. 201, 147-159.
    • (1980) Arch. Biochem. Biophys. , vol.201 , pp. 147-159
    • Busse, D.1    Pohl, B.2    Bartel, H.3    Buschmann, F.4
  • 5
    • 0025221076 scopus 로고
    • The stepwise hydrolysis of adenosine nucleotides by ecto-enzymes of renal brush-border membranes
    • Čulić O., Sabolić I. and Zanić-Grubisic T. (1990) The stepwise hydrolysis of adenosine nucleotides by ecto-enzymes of renal brush-border membranes. Biochim. Biophys. Acta 1030, 143-151.
    • (1990) Biochim. Biophys. Acta , vol.1030 , pp. 143-151
    • Čulić, O.1    Sabolić, I.2    Zanić-Grubisic, T.3
  • 8
    • 0008916475 scopus 로고
    • Method for the determination of tracer phosphate in biological material
    • Ernster L., Zetterström R. C. and Lindberg O. (1950) Method for the determination of tracer phosphate in biological material. Acta Chem. Scand. 4, 942-947.
    • (1950) Acta Chem. Scand. , vol.4 , pp. 942-947
    • Ernster, L.1    Zetterström, R.C.2    Lindberg, O.3
  • 9
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • Fiske C. H. and SubbaRow Y. (1925) The colorimetric determination of phosphorus. J. Biol. Chem. 66, 375-400.
    • (1925) J. Biol. Chem. , vol.66 , pp. 375-400
    • Fiske, C.H.1    SubbaRow, Y.2
  • 10
    • 0020473546 scopus 로고
    • 2+ )-ATPase in isolated kidney cortex plasma membranes
    • 2+ )-ATPase in isolated kidney cortex plasma membranes. FEBS Lett. 144, 226-230.
    • (1982) FEBS Lett. , vol.144 , pp. 226-230
    • Gmaj, P.1    Murer, H.2    Carafoli, E.3
  • 11
    • 0022629214 scopus 로고
    • Extracellular ATP: Effects, sources and fate
    • Gordon J. L. (1986) Extracellular ATP: effects, sources and fate. Biochem. J. 233, 309-319.
    • (1986) Biochem. J. , vol.233 , pp. 309-319
    • Gordon, J.L.1
  • 12
    • 0026591648 scopus 로고
    • Nucleoside transport in brush border membranes vesicles from human kidney
    • Gutiérrez M., Brett C., Ott R., Hui A. and Giacomini K. (1992) Nucleoside transport in brush border membranes vesicles from human kidney. Biochem. Biophys. Acta 1105, 1-9.
    • (1992) Biochem. Biophys. Acta , vol.1105 , pp. 1-9
    • Gutiérrez, M.1    Brett, C.2    Ott, R.3    Hui, A.4    Giacomini, K.5
  • 13
    • 0028355116 scopus 로고
    • Extracellular ATP in the regulation of renal microvascular function
    • Inscho E. W., Mitchell K. D. and Navar L. G. (1994) Extracellular ATP in the regulation of renal microvascular function. FASEB J. 8, 319-328.
    • (1994) FASEB J. , vol.8 , pp. 319-328
    • Inscho, E.W.1    Mitchell, K.D.2    Navar, L.G.3
  • 14
    • 0018400554 scopus 로고
    • Size determination of enzymes by radiation inactivation
    • Kempner E. S. and Schlegel W. (1979) Size determination of enzymes by radiation inactivation. Analyt. Biochem. 92, 2-10.
    • (1979) Analyt. Biochem. , vol.92 , pp. 2-10
    • Kempner, E.S.1    Schlegel, W.2
  • 17
    • 0016228201 scopus 로고
    • Localization of a calcium-stimulated ATPase in the basal-lateral plasma membranes of the proximal tubule of rat kidney cortex
    • Kinne-Saffran E. and Kinne R. (1974) Localization of a calcium-stimulated ATPase in the basal-lateral plasma membranes of the proximal tubule of rat kidney cortex. J. Membrane Biol. 17, 263-274.
    • (1974) J. Membrane Biol. , vol.17 , pp. 263-274
    • Kinne-Saffran, E.1    Kinne, R.2
  • 18
    • 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
  • 19
    • 0021101432 scopus 로고
    • Sequential hydrolysis of γ- and β-phosphate groups of ATP by the ATP-diphosphohydrolase from pig pancreas
    • Laliberté J. F. and Beaudoin A. R. (1983) Sequential hydrolysis of γ- and β-phosphate groups of ATP by the ATP-diphosphohydrolase from pig pancreas. Biochim. Biophys. Acta 742, 9-15.
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 9-15
    • Laliberté, J.F.1    Beaudoin, A.R.2
  • 20
    • 0019320639 scopus 로고
    • Characterization and purification of a calcium-sensitive ATP diphosphohydrolase from pig pancreas
    • LeBel D., Poirier G. G., Phaneuf S., St-jean P., Laliberté J. F. and Beaudoin A. R. (1980) Characterization and purification of a calcium-sensitive ATP diphosphohydrolase from pig pancreas. J. Biol. Chem. 255, 1227-1233.
    • (1980) J. Biol. Chem. , vol.255 , pp. 1227-1233
    • LeBel, D.1    Poirier, G.G.2    Phaneuf, S.3    St-Jean, P.4    Laliberté, J.F.5    Beaudoin, A.R.6
  • 21
    • 0014288490 scopus 로고
    • The large scale separation of peroxisomes, mitochondria and lysosomes from the livers of rats injected with Triton WR-1339
    • Leighton F., Poda B., Beaufay H., Baudhiun P., Coffey J. W., Fowler S. and De Duve C. (1968) The large scale separation of peroxisomes, mitochondria and lysosomes from the livers of rats injected with Triton WR-1339. J. Cell Biol. 37, 482-513.
    • (1968) J. Cell Biol. , vol.37 , pp. 482-513
    • Leighton, F.1    Poda, B.2    Beaufay, H.3    Baudhiun, P.4    Coffey, J.W.5    Fowler, S.6    De Duve, C.7
  • 24
    • 0027538618 scopus 로고
    • Modulation of tubuloglomerular feedback responsiveness by extracelular ATP
    • Mitchell K. D. and Navar G. (1993) Modulation of tubuloglomerular feedback responsiveness by extracelular ATP. Am. J. Physiol. 264, F458-F466.
    • (1993) Am. J. Physiol. , vol.264
    • Mitchell, K.D.1    Navar, G.2
  • 26
    • 0027412463 scopus 로고
    • Demonstration of a novel type of ATP-diphosphohydrolase (EC 3.6.1.5) in bovine lung
    • Picher M., Coté Y. P., Béliveau Potier M., Beaudoin A. R. (1993) Demonstration of a novel type of ATP-diphosphohydrolase (EC 3.6.1.5) in bovine lung. J. Biol. Chem. 268, 4699-4703.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4699-4703
    • Picher, M.1    Coté, Y.P.2    Béliveau Potier, M.3    Beaudoin, A.R.4
  • 28
    • 0028967657 scopus 로고
    • Ecto-ATPases: Identities and functions
    • Plesner L. (1995) Ecto-ATPases: identities and functions. Int. Rev. Cytol. 158, 141-214.
    • (1995) Int. Rev. Cytol. , vol.158 , pp. 141-214
    • Plesner, L.1
  • 29
    • 0025743045 scopus 로고
    • Demonstration of antithrombotic activity of glomerular adenosine diphosphatase
    • Poelstra K., Baller J. F. W., Hardonk M. J. and Bakker W. W. (1991) Demonstration of antithrombotic activity of glomerular adenosine diphosphatase. Blood 78, 141-148.
    • (1991) Blood , vol.78 , pp. 141-148
    • Poelstra, K.1    Baller, J.F.W.2    Hardonk, M.J.3    Bakker, W.W.4
  • 30
    • 0026628261 scopus 로고
    • Modulation by anti-thy 1 nephritis in the rat by nucleotides: Evidence for an anti-inflammatory role for nucleotidases
    • Poelstra K., Heynen E. R., Baller J. F. W., Hardonk M. J. and Bakker W. W. (1992) Modulation by anti-thy 1 nephritis in the rat by nucleotides: evidence for an anti-inflammatory role for nucleotidases. Lab. Inv. 66, 555-563.
    • (1992) Lab. Inv. , vol.66 , pp. 555-563
    • Poelstra, K.1    Heynen, E.R.2    Baller, J.F.W.3    Hardonk, M.J.4    Bakker, W.W.5
  • 31
    • 0001247308 scopus 로고
    • Thin-layer separation methods for nucleic acid derivatives
    • Academic Press. London
    • Randerath K. and Randerath E. (1967) Thin-layer separation methods for nucleic acid derivatives. In Methods in Enzymology, Vol. XII, pp. 323-339. Academic Press. London.
    • (1967) Methods in Enzymology , vol.12 , pp. 323-339
    • Randerath, K.1    Randerath, E.2
  • 32
    • 0345760130 scopus 로고
    • Kallikrein-like activity in perfusates and urine of isolated rat kidneys
    • Roblero J., Croxatto H., García R., Corthon J. and De Vito E. (1976) Kallikrein-like activity in perfusates and urine of isolated rat kidneys. Am. J. Physiol. 231, 1383-1386.
    • (1976) Am. J. Physiol. , vol.231 , pp. 1383-1386
    • Roblero, J.1    Croxatto, H.2    García, R.3    Corthon, J.4    De Vito, E.5
  • 33
    • 0026576151 scopus 로고
    • Localization of ecto-ATPase in rat kidney and isolated renal cortical membranes vesicles
    • Sabolić I., Čulić O., Lin, S. H. and Brown D. (1992) Localization of ecto-ATPase in rat kidney and isolated renal cortical membranes vesicles. Am. J. Physiol. 262, F217-F228.
    • (1992) Am. J. Physiol. , vol.262
    • Sabolić, I.1    Čulić, O.2    Lin, S.H.3    Brown, D.4
  • 34
    • 0019226251 scopus 로고
    • IgM-like natural hemagglutinin from rat fish serum: Isolation and physicochemical characterization (Callorhynchus callorhynchus)
    • Sánchez G., Gajardo M. and De Ioannes A. (1980) IgM-like natural hemagglutinin from rat fish serum: isolation and physicochemical characterization (Callorhynchus callorhynchus). Devl. Comp. Immun. 4, 667-678.
    • (1980) Devl. Comp. Immun. , vol.4 , pp. 667-678
    • Sánchez, G.1    Gajardo, M.2    De Ioannes, A.3
  • 36
    • 0019888435 scopus 로고
    • γ-Glutamyl transpeptidase: Catalytic, structural and functional aspects
    • Tate S. S. and Meister A. (1981) γ-Glutamyl transpeptidase: catalytic, structural and functional aspects. Molec. Cell. Biochem. 39, 357-368.
    • (1981) Molec. Cell. Biochem. , vol.39 , pp. 357-368
    • Tate, S.S.1    Meister, A.2
  • 37
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T. and Gordon J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 42
    • 0025718488 scopus 로고
    • ATP diphosphohydrolase is responsible for ecto-ATPase and ecto-ADPase activities in bovine aorta endothelial and smooth muscle cells
    • Yagi K., Shinbo M., Hashizume M., Shimba L. S., Kurimura S. and Miura Y. (1991) ATP diphosphohydrolase is responsible for ecto-ATPase and ecto-ADPase activities in bovine aorta endothelial and smooth muscle cells. Biochem. Biophys. Res. Commun. 180, 1200-1206.
    • (1991) Biochem. Biophys. Res. Commun. , vol.180 , pp. 1200-1206
    • Yagi, K.1    Shinbo, M.2    Hashizume, M.3    Shimba, L.S.4    Kurimura, S.5    Miura, Y.6


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