메뉴 건너뛰기




Volumn 47, Issue 4, 2003, Pages 265-271

Magnesium-dependent ecto-ATP diphosphohydrolase activity in Herpetomonas muscarum muscarum

Author keywords

[No Author keywords available]

Indexed keywords

4,4' DIISOTHIOCYANATOSTILBENE 2,2' DISULFONIC ACID; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE (MAGNESIUM); ADENOSINE TRIPHOSPHATE; ALKALINE PHOSPHATASE; APYRASE; BAFILOMYCIN A1; CALCIUM CHLORIDE; CATION; CYTIDINE DIPHOSPHATE; CYTIDINE TRIPHOSPHATE; ENZYME INHIBITOR; FLUORIDE SODIUM; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; LEVAMISOLE; MAGNESIUM CHLORIDE; MANGANESE CHLORIDE; OLIGOMYCIN; OUABAIN; SODIUM AZIDE; STRONTIUM CHLORIDE; SURAMIN; URIDINE DIPHOSPHATE; URIDINE TRIPHOSPHATE; VANADATE SODIUM; ZINC CHLORIDE;

EID: 0041861361     PISSN: 03438651     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00284-002-3975-3     Document Type: Article
Times cited : (4)

References (51)
  • 1
    • 0026533657 scopus 로고
    • The interaction of Leishmania species with macrophages
    • Alexander J, Russel DG (1992) The interaction of Leishmania species with macrophages. Adv Parasitol 31:175-254
    • (1992) Adv Parasitol , vol.31 , pp. 175-254
    • Alexander, J.1    Russel, D.G.2
  • 2
    • 0025134672 scopus 로고
    • Remarkable activity of nucleoside triphosphate hydrolase in tachyzoites of both virulent and avirulent strains of Toxoplasma gondii
    • Asai T, Suzuki Y (1990) Remarkable activity of nucleoside triphosphate hydrolase in tachyzoites of both virulent and avirulent strains of Toxoplasma gondii. FEMS Microbiol Lett 72:89-92
    • (1990) FEMS Microbiol Lett , vol.72 , pp. 89-92
    • Asai, T.1    Suzuki, Y.2
  • 3
    • 0029051349 scopus 로고
    • Biochemical and molecular characterization of nucleoside triphosphate hydrolase from the parasitic protozoan Toxoplasma gondii
    • Asai T, Miura S, Sibley LD, Okabayashi H, Takeushi T (1995) Biochemical and molecular characterization of nucleoside triphosphate hydrolase from the parasitic protozoan Toxoplasma gondii. J Biol Chem 270:1191-1197
    • (1995) J Biol Chem , vol.270 , pp. 1191-1197
    • Asai, T.1    Miura, S.2    Sibley, L.D.3    Okabayashi, H.4    Takeushi, T.5
  • 5
    • 0028036717 scopus 로고
    • Tandemly repeated genes encoded nucleoside triphosphate hydrolase isoforms secreted into parasitophorous vacuole of Toxoplasma gondii
    • Bermudes D, Peck KR, Afifi MA, Beckers CJM, Joiner KA (1994) TandemLy repeated genes encoded nucleoside triphosphate hydrolase isoforms secreted into parasitophorous vacuole of Toxoplasma gondii. J Biol Chem 269:2952-2960
    • (1994) J Biol Chem , vol.269 , pp. 2952-2960
    • Bermudes, D.1    Peck, K.R.2    Afifi, M.A.3    Beckers, C.J.M.4    Joiner, K.A.5
  • 8
    • 0011913143 scopus 로고
    • Bafilomycin: A class of inhibitors of membrane ATPases from microorganisms, animal cells and plant cells
    • Browman EJ, Siebers A, Altendorf K (1988) Bafilomycin: A class of inhibitors of membrane ATPases from microorganisms, animal cells and plant cells. Proc Natl Acad Sci USA 85:7972-7976
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7972-7976
    • Browman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 10
    • 0030766582 scopus 로고    scopus 로고
    • Stage specific expression of P2Y receptors, ecto-apyrase and 5′-nucleotidase in myeloid leukocytes
    • Clifford EE, Martin KA, Dalal P, Thomas R, Dubyak GR (1997) Stage specific expression of P2Y receptors, ecto-apyrase and 5′-nucleotidase in myeloid leukocytes. Am J Physiol 42:C973-C987
    • (1997) Am J Physiol , vol.42
    • Clifford, E.E.1    Martin, K.A.2    Dalal, P.3    Thomas, R.4    Dubyak, G.R.5
  • 11
    • 0015581273 scopus 로고
    • Plasma membranes of mammalian cells: A review of methods for their characterization and isolation
    • DePierre JW, Karnovsky ML (1973) Plasma membranes of mammalian cells: A review of methods for their characterization and isolation. J Cell Biol 56:275-303
    • (1973) J Cell Biol , vol.56 , pp. 275-303
    • DePierre, J.W.1    Karnovsky, M.L.2
  • 15
    • 0031147739 scopus 로고    scopus 로고
    • Trypanosoma brucei: Ecto-phosphatase activity present on the surface of intact prociclic forms
    • Fernandes EC, Meyer-Fernandes JR, Silva-Neto MAC, Vercesi AE (1997) Trypanosoma brucei: Ecto-phosphatase activity present on the surface of intact prociclic forms. Z Naturforsch 52c:351-358
    • (1997) Z Naturforsch , vol.52 C , pp. 351-358
    • Fernandes, E.C.1    Meyer-Fernandes, J.R.2    Silva-Neto, M.A.C.3    Vercesi, A.E.4
  • 17
    • 0000352925 scopus 로고
    • 32P-labelled adenosine triphosphate of high specific activity
    • 32P-labelled adenosine triphosphate of high specific activity. Biochem J 90:147-149
    • (1964) Biochem J , vol.90 , pp. 147-149
    • Glynn, I.M.1    Chappel, J.B.2
  • 18
    • 0030034867 scopus 로고    scopus 로고
    • Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum)
    • Handa M, Guidotti G (1996) Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum). Biochem Biophys Res Commun 218:916-923
    • (1996) Biochem Biophys Res Commun , vol.218 , pp. 916-923
    • Handa, M.1    Guidotti, G.2
  • 19
    • 0024323405 scopus 로고    scopus 로고
    • The effects of some possible inhibitors of ecto-nucleotidases on the breakdown and pharmacology effects of ATP in the guinea-pig urinary bladder
    • Hourani SMO, Chown JA (1998) The effects of some possible inhibitors of ecto-nucleotidases on the breakdown and pharmacology effects of ATP in the guinea-pig urinary bladder. Gen Pharmacol 20:413-416
    • (1998) Gen Pharmacol , vol.20 , pp. 413-416
    • Hourani, S.M.O.1    Chown, J.A.2
  • 21
    • 0031012542 scopus 로고    scopus 로고
    • Complementary DNA cloning and sequencing of the chicken muscle ecto-ATPase
    • Kirley TL (1997) Complementary DNA cloning and sequencing of the chicken muscle ecto-ATPase. J Biol Chem 272:1076-1081
    • (1997) J Biol Chem , vol.272 , pp. 1076-1081
    • Kirley, T.L.1
  • 22
    • 0023821490 scopus 로고
    • 2+-ATPase activities in human hepatoma cells
    • 2+-ATPase activities in human hepatoma cells. Arch Biochem Biophys 263:264-271
    • (1988) Arch Biochem Biophys , vol.263 , pp. 264-271
    • Knowles, A.F.1
  • 23
    • 0028840189 scopus 로고
    • The rat live ecto-ATPase/C-CAM CDNA detects induction of carcinoembryonic antigen but not the mercurial-insensitive ecto-ATPase in human hepatoma Li-7A cells treated by epidermal growth factor and cholera toxin
    • Knowles AF (1995) The rat live ecto-ATPase/C-CAM CDNA detects induction of carcinoembryonic antigen but not the mercurial-insensitive ecto-ATPase in human hepatoma Li-7A cells treated by epidermal growth factor and cholera toxin. Biochem Biophys Res Commun 207:529-535
    • (1995) Biochem Biophys Res Commun , vol.207 , pp. 529-535
    • Knowles, A.F.1
  • 26
    • 0000807711 scopus 로고
    • The determination of inorganic phosphate in the presence of labile phosphate esters
    • Lowry HO, Lopez M (1946) The determination of inorganic phosphate in the presence of labile phosphate esters. J Biol Chem 162:421-428
    • (1946) J Biol Chem , vol.162 , pp. 421-428
    • Lowry, H.O.1    Lopez, M.2
  • 28
    • 0025138734 scopus 로고
    • Hepatocytes plasma membrane ecto-ATPase (pp120/HA4) is a substrate for tyrosine kinase activity of the insulin receptor
    • Margolis RN, Schell MJ, Taylor SL, Hubbard AL (1990) Hepatocytes plasma membrane ecto-ATPase (pp120/HA4) is a substrate for tyrosine kinase activity of the insulin receptor. Biochem Biophys Res Commun 166:562-566
    • (1990) Biochem Biophys Res Commun , vol.166 , pp. 562-566
    • Margolis, R.N.1    Schell, M.J.2    Taylor, S.L.3    Hubbard, A.L.4
  • 30
    • 0032782792 scopus 로고    scopus 로고
    • Altered tyrosine phosphrilation of ERK1 MAP kinase and other macrophage molecules by Leishmania amastigotes
    • Martiny A, Meyer-Fernandes JR, De Souza W, Vannier-Santos MA (1999) Altered tyrosine phosphrilation of ERK1 MAP kinase and other macrophage molecules by Leishmania amastigotes. Mol Biochem Parasitol 102:1-12
    • (1999) Mol Biochem Parasitol , vol.102 , pp. 1-12
    • Martiny, A.1    Meyer-Fernandes, J.R.2    De Souza, W.3    Vannier-Santos, M.A.4
  • 31
    • 0023679991 scopus 로고
    • Pyrophosphatase formation from acetyl phosphate and ortophosphate: Evidence of heterogenous catalysis
    • Meyer-Fernandes JR, Vieyra A (1988) Pyrophosphatase formation from acetyl phosphate and ortophosphate: Evidence of heterogenous catalysis. Arch Biochem Biophys 266:132-141
    • (1988) Arch Biochem Biophys , vol.266 , pp. 132-141
    • Meyer-Fernandes, J.R.1    Vieyra, A.2
  • 36
    • 0027458375 scopus 로고
    • pp120/Ecto-ATPase, an endogenous substrate of the insulin receptor tyrosine kinase, is expressed as two variably spliced isofirms
    • Najjar SM, Accili D, Philippe N, Jemberg J, Margolis R, Taylor SI (1993) pp120/Ecto-ATPase, an endogenous substrate of the insulin receptor tyrosine kinase, is expressed as two variably spliced isofirms. J Biol Chem 268:1201-1206
    • (1993) J Biol Chem , vol.268 , pp. 1201-1206
    • Najjar, S.M.1    Accili, D.2    Philippe, N.3    Jemberg, J.4    Margolis, R.5    Taylor, S.I.6
  • 37
    • 0032583188 scopus 로고    scopus 로고
    • Basis for substrate specificity of the Toxoplasma gondii nucleotide triphosphate hydrolase
    • Nakaar V, Beckers CJM, Polotsky V, Joiner KA (1998) Basis for substrate specificity of the Toxoplasma gondii nucleotide triphosphate hydrolase. Mol Biochem Parasitol 97:209-220
    • (1998) Mol Biochem Parasitol , vol.97 , pp. 209-220
    • Nakaar, V.1    Beckers, C.J.M.2    Polotsky, V.3    Joiner, K.A.4
  • 38
    • 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
  • 41
    • 0025721115 scopus 로고
    • Comparative studies of the cytotoxic T lymphocyte-mediated cytotoxicity and of extracellular ATP-induced cell lysis
    • Redegeld F, Filippini A, Sitkovsky M (1991) Comparative studies of the cytotoxic T lymphocyte-mediated cytotoxicity and of extracellular ATP-induced cell lysis. J Immunol 147:3638-3645
    • (1991) J Immunol , vol.147 , pp. 3638-3645
    • Redegeld, F.1    Filippini, A.2    Sitkovsky, M.3
  • 43
    • 0015333046 scopus 로고
    • Growth of an insect trypanosomatid at 37°C in a defined medium
    • Roitman C, Roitman I, De Azevedo HP (1972) Growth of an insect trypanosomatid at 37°C in a defined medium. J Protozool 19346-19349
    • (1972) J Protozool , pp. 19346-19349
    • Roitman, C.1    Roitman, I.2    De Azevedo, H.P.3
  • 44
    • 0031194746 scopus 로고    scopus 로고
    • A contribution of the mitochondrial adenosinetriphosphatase inhibitor protein to the thermal stability of the FOF1-ATPase complex
    • Saad-Nehme J, Bezerra AL, Fornells LAM, Silva JL, Meyer-Fernandes JR (1997) A contribution of the mitochondrial adenosinetriphosphatase inhibitor protein to the thermal stability of the FOF1-ATPase complex. Z Naturforsch 52c:459-465
    • (1997) Z Naturforsch , vol.52 C , pp. 459-465
    • Saad-Nehme, J.1    Bezerra, A.L.2    Fornells, L.A.M.3    Silva, J.L.4    Meyer-Fernandes, J.R.5
  • 45
    • 0026061115 scopus 로고
    • Cell-mediated cytotoxicity: ATP as an effector and the role of target cells
    • Steinberg TH, Di Virgilio F (1991) Cell-mediated cytotoxicity: ATP as an effector and the role of target cells. Curr Opin Immunol 3:71-75
    • (1991) Curr Opin Immunol , vol.3 , pp. 71-75
    • Steinberg, T.H.1    Di Virgilio, F.2
  • 46
    • 0019443730 scopus 로고
    • Herpetomonas samuelpessoai: Changes in cell shape and induction of cell differentiation induced by local anesthesiscs
    • Thomas EM, De Souza ET, Esteves MJG, Angluster J, De Souza W (1981) Herpetomonas samuelpessoai: Changes in cell shape and induction of cell differentiation induced by local anesthesiscs. Exp Parasitol 51:366-372
    • (1981) Exp Parasitol , vol.51 , pp. 366-372
    • Thomas, E.M.1    De Souza, E.T.2    Esteves, M.J.G.3    Angluster, J.4    De Souza, W.5
  • 47
    • 0029050597 scopus 로고
    • Leishmanial protein kinase C may regulate parasite infection via secreted acid phosphatase
    • Vannier-Santos MA, Martiny A, Meyer-Fernandes JR, De Souza W (1995) Leishmanial protein kinase C may regulate parasite infection via secreted acid phosphatase. Eur J Cell Biol 67:112-119
    • (1995) Eur J Cell Biol , vol.67 , pp. 112-119
    • Vannier-Santos, M.A.1    Martiny, A.2    Meyer-Fernandes, J.R.3    De Souza, W.4
  • 48
    • 0017170293 scopus 로고
    • Alkaline phosphatase. I. Kinetics and inhibition by levamisole of purified isoenzymes from humans
    • Van Belle H (1976) Alkaline phosphatase. I. Kinetics and inhibition by levamisole of purified isoenzymes from humans. Clin Chem 22:972-976
    • (1976) Clin Chem , vol.22 , pp. 972-976
    • Van Belle, H.1
  • 49
    • 0013881848 scopus 로고
    • The trypanosomatid parasites of insects and arachnids
    • Wallace FG (1966) The trypanosomatid parasites of insects and arachnids. Exp Parasitol 18:124-193
    • (1966) Exp Parasitol , vol.18 , pp. 124-193
    • Wallace, F.G.1
  • 51
    • 0028061958 scopus 로고
    • The role of pH and temperature in the development of Leishmania parasites
    • Zilberstein D, Shapira M (1994) The role of pH and temperature in the development of Leishmania parasites. Annu Rev Microbiol 48:449-470
    • (1994) Annu Rev Microbiol , vol.48 , pp. 449-470
    • Zilberstein, D.1    Shapira, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.