메뉴 건너뛰기




Volumn 5, Issue 10, 2005, Pages 899-907

Characterization of an ecto-ATPase activity in Cryptococcus neoformans

Author keywords

Antifungal; Cryptococcus neoformans; Ecto ATPase

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CYTIDINE TRIPHOSPHATE; FLUCONAZOLE; GUANOSINE TRIPHOSPHATE; INOSINE TRIPHOSPHATE; PHOSPHATASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; URIDINE TRIPHOSPHATE;

EID: 21644443068     PISSN: 15671356     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsyr.2005.04.005     Document Type: Article
Times cited : (13)

References (63)
  • 1
    • 0032694180 scopus 로고    scopus 로고
    • Pathogenicity of Cryptococcus neoformans: Virulence factors and immunological mechanisms
    • M.L. Rodrigues, C.S. Alviano, and L.R. Travassos Pathogenicity of Cryptococcus neoformans: virulence factors and immunological mechanisms Microbes Infect. 1 1999 293 301
    • (1999) Microbes Infect. , vol.1 , pp. 293-301
    • Rodrigues, M.L.1    Alviano, C.S.2    Travassos, L.R.3
  • 2
    • 0028786641 scopus 로고
    • Cryptococcosis in the era of AIDS: 100 years after the discovery of Cryptococcus neoformans
    • T.G. Mitchell, and J.R. Perfect Cryptococcosis in the era of AIDS: 100 years after the discovery of Cryptococcus neoformans Clin. Microbiol. Rev. 8 1995 515 548
    • (1995) Clin. Microbiol. Rev. , vol.8 , pp. 515-548
    • Mitchell, T.G.1    Perfect, J.R.2
  • 3
    • 0033895268 scopus 로고    scopus 로고
    • Antifungals targeted to sphingolipid synthesis: Focus on inositol phosphorylceramide synthase
    • N.H. Georgopapadakou Antifungals targeted to sphingolipid synthesis: focus on inositol phosphorylceramide synthase Expert. Opin. Investig. Drugs. 9 2000 1787 1896
    • (2000) Expert. Opin. Investig. Drugs. , vol.9 , pp. 1787-1896
    • Georgopapadakou, N.H.1
  • 4
    • 0033816854 scopus 로고    scopus 로고
    • Ecto-enzymes: Physiology meets pathology
    • J.W. Goding Ecto-enzymes: physiology meets pathology J. Leukoc. Biol. 67 2000 285 311
    • (2000) J. Leukoc. Biol. , vol.67 , pp. 285-311
    • Goding, J.W.1
  • 5
    • 0036753379 scopus 로고    scopus 로고
    • An ectonucleotide ATP-diphosphohydrolase activity in Trichomonas vaginalis stimulated by galactose and its possible role in virulence
    • J.B. De Jesus, A.A. De Sa Pinheiro, A.H. Lopes, and J.R. Meyer-Fernandes An ectonucleotide ATP-diphosphohydrolase activity in Trichomonas vaginalis stimulated by galactose and its possible role in virulence Z. Naturforsch. 57 2002 890 896
    • (2002) Z. Naturforsch. , vol.57 , pp. 890-896
    • De Jesus, J.B.1    De Sa Pinheiro, A.A.2    Lopes, A.H.3    Meyer-Fernandes, J.R.4
  • 6
    • 0036757295 scopus 로고    scopus 로고
    • Ecto-ATPases in protozoa parasites: Looking for a function
    • J.R. Meyer-Fernandes Ecto-ATPases in protozoa parasites: looking for a function Parasitol. Int. 51 2002 299 303
    • (2002) Parasitol. Int. , vol.51 , pp. 299-303
    • Meyer-Fernandes, J.R.1
  • 10
    • 0028967657 scopus 로고
    • Ecto-ATPases: Identities and functions
    • L. Plesner Ecto-ATPases: identities and functions Int. Rev. Cytol 158 1995 141 214
    • (1995) Int. Rev. Cytol , vol.158 , pp. 141-214
    • Plesner, L.1
  • 11
    • 0024363567 scopus 로고
    • Cloning and expression of a cDNA coding for a rat liver plasma membrane ecto-ATPase. the primary structure of the ecto-ATPase is similar to that of the human biliary glycoprotein
    • S.H. Lin, and G. Guidotti Cloning and expression of a cDNA coding for a rat liver plasma membrane ecto-ATPase. The primary structure of the ecto-ATPase is similar to that of the human biliary glycoprotein J. Biol. Chem. 264 1989 14408 14414
    • (1989) J. Biol. Chem. , vol.264 , pp. 14408-14414
    • Lin, S.H.1    Guidotti, G.2
  • 12
    • 0027197470 scopus 로고
    • Identification and partial characterization of an ectoATPase expressed by human natural killer cells
    • K.E. Dombrowski, J.M. Trevillyan, J.C. Cone, Y. Lu, and C.A. Phillips Identification and partial characterization of an ectoATPase expressed by human natural killer cells Biochemistry 32 1993 6515 6522
    • (1993) Biochemistry , vol.32 , pp. 6515-6522
    • Dombrowski, K.E.1    Trevillyan, J.M.2    Cone, J.C.3    Lu, Y.4    Phillips, C.A.5
  • 13
    • 0028109187 scopus 로고
    • Purification and characterization of the ecto-Mg-ATPase of chicken gizzard smooth muscle
    • J.G. Stout, and T.L. Kirley Purification and characterization of the ecto-Mg-ATPase of chicken gizzard smooth muscle J. Biochem. Biophys. Methods 29 1994 61 75
    • (1994) J. Biochem. Biophys. Methods , vol.29 , pp. 61-75
    • Stout, J.G.1    Kirley, T.L.2
  • 14
    • 0025177280 scopus 로고
    • Ecto ATPase activity in cytolytic T-lymphocytes - Protection from cytolytic effects of extracellular ATP
    • A. Filippini, R.E. Taffs, T. Agui, and M.V. Sitkovsky Ecto ATPase activity in cytolytic T-lymphocytes - protection from cytolytic effects of extracellular ATP J. Biol. Chem. 265 1990 334 340
    • (1990) J. Biol. Chem. , vol.265 , pp. 334-340
    • Filippini, A.1    Taffs, R.E.2    Agui, T.3    Sitkovsky, M.V.4
  • 15
    • 0024988964 scopus 로고
    • Responses of mouse lymphocytes to extracellular ATP. II. Extracellular ATP causes cell type-dependent lysis and DNA fragmentation
    • P. Zanovello, V. Bronte, A. Rosato, P. Pizzo, and F. Di Virgilio Responses of mouse lymphocytes to extracellular ATP. II. Extracellular ATP causes cell type-dependent lysis and DNA fragmentation J. Immunol. 145 1990 1545 1550
    • (1990) J. Immunol. , vol.145 , pp. 1545-1550
    • Zanovello, P.1    Bronte, V.2    Rosato, A.3    Pizzo, P.4    Di Virgilio, F.5
  • 16
    • 0026061115 scopus 로고
    • Cell-mediated cytotoxicity: ATP as an effector and the role of target cells
    • T.H. Steinberg, and F. Di Virgilio Cell-mediated cytotoxicity: ATP as an effector and the role of target cells Curr. Opin. Immunol. 3 1991 71 75
    • (1991) Curr. Opin. Immunol. , vol.3 , pp. 71-75
    • Steinberg, T.H.1    Di Virgilio, F.2
  • 18
    • 0042386007 scopus 로고    scopus 로고
    • Coordinated adenine nucleotide phosphohydrolysis and nucleoside signaling in posthypoxic endothelium: Role of ectonucleotidases and adenosine A2B receptors
    • H.K. Eltzschig, J.C. Ibla, G.T. Furuta, M.O. Leonard, K.A. Jacobson, K. Enjyoji, S.C. Robson, and S.P. Colgan Coordinated adenine nucleotide phosphohydrolysis and nucleoside signaling in posthypoxic endothelium: role of ectonucleotidases and adenosine A2B receptors J. Exp. Med. 198 2003 783 796
    • (2003) J. Exp. Med. , vol.198 , pp. 783-796
    • Eltzschig, H.K.1    Ibla, J.C.2    Furuta, G.T.3    Leonard, M.O.4    Jacobson, K.A.5    Enjyoji, K.6    Robson, S.C.7    Colgan, S.P.8
  • 19
    • 0025138734 scopus 로고
    • Hepatocyte plasma membrane ecto-ATPase (pp120/HA4) is a substrate for tyrosine kinase activity of the insulin receptor
    • R.N. Margolis, M.J. Schell, P. Taylor, and A.L. Hubbard Hepatocyte plasma membrane ecto-ATPase (pp120/HA4) is a substrate for tyrosine kinase activity of the insulin receptor Biochem. Biophys. Res. Commun. 166 1990 562 566
    • (1990) Biochem. Biophys. Res. Commun. , vol.166 , pp. 562-566
    • Margolis, R.N.1    Schell, M.J.2    Taylor, P.3    Hubbard, A.L.4
  • 20
    • 0027661421 scopus 로고
    • Signal transduction via P2-purinergic receptors for extracellular ATP and other nucleotides
    • G.R. Dubyak, and C. El-Moatassim Signal transduction via P2-purinergic receptors for extracellular ATP and other nucleotides Am. J. Physiol. 34 1993 C577 C606
    • (1993) Am. J. Physiol. , vol.34
    • Dubyak, G.R.1    El-Moatassim, C.2
  • 21
    • 0028040456 scopus 로고
    • Involvement of ecto-ATPase as an ATP receptor in the stimulatory effect of extracellular ATP on NO release in bovine aorta endothelial cells
    • K. Yagi, I. Nishino, M. Eguchi, M. Kitagawa, Y. Miura, and T. Mizoguchi Involvement of ecto-ATPase as an ATP receptor in the stimulatory effect of extracellular ATP on NO release in bovine aorta endothelial cells Biochem. Biophys. Res. Commun. 203 1994 1237 1243
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 1237-1243
    • Yagi, K.1    Nishino, I.2    Eguchi, M.3    Kitagawa, M.4    Miura, Y.5    Mizoguchi, T.6
  • 22
    • 0242266131 scopus 로고    scopus 로고
    • Ecto-ATPase activity on the surface of Trypanosoma cruzi and its possible role in the parasite-host cell interaction
    • D.F. Bisaggio, C.E. Peres-Sampaio, J.R. Meyer-Fernandes, and T. Souto-Padrón Ecto-ATPase activity on the surface of Trypanosoma cruzi and its possible role in the parasite-host cell interaction Parasitol. Res. 91 2003 273 282
    • (2003) Parasitol. Res. , vol.91 , pp. 273-282
    • Bisaggio, D.F.1    Peres-Sampaio, C.E.2    Meyer-Fernandes, J.R.3    Souto-Padrón, T.4
  • 23
    • 0027496721 scopus 로고
    • Structure and function of C-CAM1. the first immunoglobulin domain is required for intercellular adhesion
    • P.H. Cheung, W. Luo, Y. Qiu, X. Zhang, K. Earley, P. Millirons, and S.-H. Lin Structure and function of C-CAM1. The first immunoglobulin domain is required for intercellular adhesion J. Biol. Chem. 268 1993 24303 24310
    • (1993) J. Biol. Chem. , vol.268 , pp. 24303-24310
    • Cheung, P.H.1    Luo, W.2    Qiu, Y.3    Zhang, X.4    Earley, K.5    Millirons, P.6    Lin, S.-H.7
  • 24
    • 0027331304 scopus 로고
    • 2+)-ATPase activity of the neural cell adhesion molecule
    • 2+)-ATPase activity of the neural cell adhesion molecule FEBS Lett. 336 1993 279 283
    • (1993) FEBS Lett. , vol.336 , pp. 279-283
    • Dzhandzhugazyan, K.1    Bock, E.2
  • 25
    • 0029010182 scopus 로고
    • Properties of and proteins associated with the extracellular ATPase of chicken gizzard smooth muscle. a monoclonal antibody study
    • J.G. Stout, R.S. Strobel, and T.L. Kirley Properties of and proteins associated with the extracellular ATPase of chicken gizzard smooth muscle. A monoclonal antibody study J. Biol. Chem. 270 1995 11845 11850
    • (1995) J. Biol. Chem. , vol.270 , pp. 11845-11850
    • Stout, J.G.1    Strobel, R.S.2    Kirley, T.L.3
  • 26
    • 0031012542 scopus 로고    scopus 로고
    • Complementary DNA cloning and sequencing of the chicken muscle ecto-ATPase. Homology with the lymphoid cell activation antigen CD39
    • T.L. Kirley Complementary DNA cloning and sequencing of the chicken muscle ecto-ATPase. Homology with the lymphoid cell activation antigen CD39 J. Biol. Chem. 272 1997 1076 1081
    • (1997) J. Biol. Chem. , vol.272 , pp. 1076-1081
    • Kirley, T.L.1
  • 31
    • 0030840333 scopus 로고    scopus 로고
    • Identification of N-acetylneuraminic acid and its 9-O-acetylated derivative on the cell surface of Cryptococcus neoformans: Influence on fungal phagocytosis
    • M.L. Rodrigues, S. Rozental, J.N.N. Couceiro, J. Angluster, C.S. Alviano, and L.R. Travassos Identification of N-acetylneuraminic acid and its 9-O-acetylated derivative on the cell surface of Cryptococcus neoformans: influence on fungal phagocytosis Infect. Immun. 65 1997 4937 4942
    • (1997) Infect. Immun. , vol.65 , pp. 4937-4942
    • Rodrigues, M.L.1    Rozental, S.2    Couceiro, J.N.N.3    Angluster, J.4    Alviano, C.S.5    Travassos, L.R.6
  • 34
    • 0023679991 scopus 로고
    • Pyrophosphate formation from acetyl phosphate and orthophosphate: Evidence for heterogeneous catalysis
    • J.R. Meyer-Fernandes, and A. Vieyra Pyrophosphate formation from acetyl phosphate and orthophosphate: evidence for heterogeneous catalysis Arch. Biochem. Biophys. 266 1988 132 141
    • (1988) Arch. Biochem. Biophys. , vol.266 , pp. 132-141
    • Meyer-Fernandes, J.R.1    Vieyra, A.2
  • 37
    • 0000352925 scopus 로고
    • A simple method for the preparation of 32-P-labelled adenosine triphosphate of high specific activity
    • I.M. Glynn, and J.B. Chappell A simple method for the preparation of 32-P-labelled adenosine triphosphate of high specific activity Biochem. J. 90 1964 147 149
    • (1964) Biochem. J. , vol.90 , pp. 147-149
    • Glynn, I.M.1    Chappell, J.B.2
  • 38
    • 0022517661 scopus 로고
    • Caffeine inhibition of calcium accumulation by the sarcoplasmic reticulum in mammalian skinned fibers
    • M.M. Sorenson, H.S.L. Coelho, and J.P. Reuben Caffeine inhibition of calcium accumulation by the sarcoplasmic reticulum in mammalian skinned fibers J. Membr. Biol. 90 1986 219 230
    • (1986) J. Membr. Biol. , vol.90 , pp. 219-230
    • Sorenson, M.M.1    Coelho, H.S.L.2    Reuben, J.P.3
  • 39
    • 0018733531 scopus 로고
    • Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells
    • A. Fabiato, and F. Fabiato Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells J. Physiol. (Paris) 75 1979 463 505
    • (1979) J. Physiol. (Paris) , vol.75 , pp. 463-505
    • Fabiato, A.1    Fabiato, F.2
  • 40
    • 0023821490 scopus 로고
    • 2+-ATPase activities in human hepatoma cells
    • 2+-ATPase activities in human hepatoma cells Arch. Biochem. Biophys. 263 1988 264 271
    • (1988) Arch. Biochem. Biophys. , vol.263 , pp. 264-271
    • Knowles, A.F.1
  • 41
  • 44
    • 0024323405 scopus 로고
    • The effects of some possible inhibitors of ectonucleotidases on the breakdown and pharmacological effects of ATP in the guinea-pig urinary bladder
    • S.M. Hourani, and J.A. Chown The effects of some possible inhibitors of ectonucleotidases on the breakdown and pharmacological effects of ATP in the guinea-pig urinary bladder Gen. Pharmacol. 20 1989 413 416
    • (1989) Gen. Pharmacol. , vol.20 , pp. 413-416
    • Hourani, S.M.1    Chown, J.A.2
  • 45
    • 0028895360 scopus 로고
    • Characteristics of ecto-ATPase of Xenopus oocytes and the inhibitory actions of suramin on ATP breakdown
    • A.U. Ziganshin, L.E. Ziganshina, B.F. King, and G. Burnstock Characteristics of ecto-ATPase of Xenopus oocytes and the inhibitory actions of suramin on ATP breakdown Pflügers Arch. 429 1995 412 418
    • (1995) Pflügers Arch. , vol.429 , pp. 412-418
    • Ziganshin, A.U.1    Ziganshina, L.E.2    King, B.F.3    Burnstock, G.4
  • 46
    • 0016229898 scopus 로고
    • Cytochemistry of acid mucosubstance and acid phosphatase in Cryptococcus neoformans
    • T.A. Mahvi, S.S. Spicer, and N.J. Wright Cytochemistry of acid mucosubstance and acid phosphatase in Cryptococcus neoformans Can. J. Microbiol. 20 1974 833 838
    • (1974) Can. J. Microbiol. , vol.20 , pp. 833-838
    • Mahvi, T.A.1    Spicer, S.S.2    Wright, N.J.3
  • 47
    • 0031147739 scopus 로고    scopus 로고
    • Trypanosoma brucei: Ecto-phosphatase activity present on the surface of intact procyclic forms
    • E.C. Fernandes, J.R. Meyer-Fernandes, M.A.C. Silva-Neto, and A.E. Vercesi Trypanosoma brucei: ecto-phosphatase activity present on the surface of intact procyclic forms Z. Naturforsch. 52 1997 351 358
    • (1997) Z. Naturforsch. , vol.52 , pp. 351-358
    • Fernandes, E.C.1    Meyer-Fernandes, J.R.2    Silva-Neto, M.A.C.3    Vercesi, A.E.4
  • 51
    • 0017170293 scopus 로고
    • Alkaline phosphatase. I. Kinetics and inhibition by levamisole of purified isoenzymes from humans
    • H. Van-Belle Alkaline phosphatase. I. Kinetics and inhibition by levamisole of purified isoenzymes from humans Clin. Chem. 22 1976 972 976
    • (1976) Clin. Chem. , vol.22 , pp. 972-976
    • Van-Belle, H.1
  • 52
    • 0011913143 scopus 로고
    • Bafilomycins: A class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • E.J. Bowman, A. Siebers, and K. Altendorf Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells Proc. Natl. Acad. Sci. 85 1988 7972 7976
    • (1988) Proc. Natl. Acad. Sci. , vol.85 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 56
    • 0033949271 scopus 로고    scopus 로고
    • Distribution, cloning, and characterization of porcine nucleoside triphosphate diphosphohydrolase-1
    • R. Lemmens, L. Vanduffel, A. Kittel, A.R. Beaudoin, O. Benrezzak, and J. Sévigny Distribution, cloning, and characterization of porcine nucleoside triphosphate diphosphohydrolase-1 Eur. J. Biochem. 267 2000 4106 4114
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4106-4114
    • Lemmens, R.1    Vanduffel, L.2    Kittel, A.3    Beaudoin, A.R.4    Benrezzak, O.5    Sévigny, J.6
  • 59
    • 0020571977 scopus 로고
    • Evidence for distinct 5′- and 3′-nucleotidase activities in the surface membrane fraction of Leishmania donovani promastigotes
    • M. Gottlieb, and D.M. Dwyer Evidence for distinct 5′- and 3′-nucleotidase activities in the surface membrane fraction of Leishmania donovani promastigotes Mol. Biochem. Parasitol. 7 1983 303 317
    • (1983) Mol. Biochem. Parasitol. , vol.7 , pp. 303-317
    • Gottlieb, M.1    Dwyer, D.M.2
  • 63
    • 0031229572 scopus 로고    scopus 로고
    • Cloning and mapping of a human and mouse gene with homology to ecto-ATPase genes
    • B.P. Chadwick, and A.M. Frischauf Cloning and mapping of a human and mouse gene with homology to ecto-ATPase genes Mamm. Genome 8 1997 668 672
    • (1997) Mamm. Genome , vol.8 , pp. 668-672
    • Chadwick, B.P.1    Frischauf, A.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.