메뉴 건너뛰기




Volumn 2, Issue 2, 2006, Pages 409-430

The E-NTPDase family of ectonucleotidases: Structure function relationships and pathophysiological significance

Author keywords

Apyrase; Brain; CD39; Ecto ATPase; Immunology; Ischemia; Kidney; Liver; Nervous tissue; NTPDase; Platelet; Vasculature

Indexed keywords


EID: 33846436678     PISSN: 15739538     EISSN: 15739546     Source Type: Journal    
DOI: 10.1007/s11302-006-9003-5     Document Type: Article
Times cited : (769)

References (262)
  • 1
    • 18044366615 scopus 로고
    • Origin, metabolism and function of extracellular adenine nucleotides in the blood
    • Luthje J (1989) Origin, metabolism and function of extracellular adenine nucleotides in the blood. Klin Wochenschr 67:317-327
    • (1989) Klin Wochenschr , vol.67 , pp. 317-327
    • Luthje, J.1
  • 2
    • 9144269934 scopus 로고    scopus 로고
    • Cellular distribution and functions of P2 receptor subtypes in different systems
    • Burnstock G, Knight GE (2004) Cellular distribution and functions of P2 receptor subtypes in different systems. Int Rev Cytol 240:31-304
    • (2004) Int Rev Cytol , vol.240 , pp. 31-304
    • Burnstock, G.1    Knight, G.E.2
  • 4
    • 0031081539 scopus 로고    scopus 로고
    • Release, metabolism and interconversion of adenine and uridine nucleotides: Implications for G protein-coupled P2 receptor agonist selectivity Trends
    • Harden TK, Lazarowski ER, Boucher RC (1997) Release, metabolism and interconversion of adenine and uridine nucleotides: Implications for G protein-coupled P2 receptor agonist selectivity. Trends Pharmacol Sci 18:43-46
    • (1997) Pharmacol Sci , vol.18 , pp. 43-46
    • Harden, T.K.1    Lazarowski, E.R.2    Boucher, R.C.3
  • 6
    • 0028985704 scopus 로고
    • Characterisation of an ATP receptor mediating mitogenesis in vascular smooth muscle cells
    • Erlinge D, You JP, Wahlestedt C et al (1995) Characterisation of an ATP receptor mediating mitogenesis in vascular smooth muscle cells. Eur J Pharmacol-Molec Pharm 289:135-149
    • (1995) Eur J Pharmacol-Molec Pharm , vol.289 , pp. 135-149
    • Erlinge, D.1    You, J.P.2    Wahlestedt, C.3
  • 7
    • 0031812161 scopus 로고    scopus 로고
    • Extracellular ATP: A growth factor for vascular smooth muscle cells
    • Erlinge D (1998) Extracellular ATP: A growth factor for vascular smooth muscle cells. Gen Pharmacol 31:1-8
    • (1998) Gen Pharmacol , vol.31 , pp. 1-8
    • Erlinge, D.1
  • 9
    • 0028116924 scopus 로고
    • Desensitization of angiotensin receptor function
    • Sasamura H, Dza VJ, Pratt RE (1994) Desensitization of angiotensin receptor function. Kidney Int 46:1499-1501
    • (1994) Kidney Int , vol.46 , pp. 1499-1501
    • Sasamura, H.1    Dza, V.J.2    Pratt, R.E.3
  • 10
    • 0031908460 scopus 로고    scopus 로고
    • Ecto-enzymes of lymphoid cells
    • Goding JW, Howard MC (1998) Ecto-enzymes of lymphoid cells. Immunol Rev 161:5-10
    • (1998) Immunol Rev , vol.161 , pp. 5-10
    • Goding, J.W.1    Howard, M.C.2
  • 12
    • 0027661421 scopus 로고
    • Signal transduction via P2 purinergic receptors for extracellular ATP and other nucleotides
    • Dubyak GR, El-Moatassim C (1993) Signal transduction via P2 purinergic receptors for extracellular ATP and other nucleotides. Am J Physiol 265:C577-C606
    • (1993) Am J Physiol , vol.265
    • Dubyak, G.R.1    El-Moatassim, C.2
  • 15
    • 0029995730 scopus 로고    scopus 로고
    • P2X receptors: An emerging channel family
    • Buell G, Collo G, Rassendren F (1996) P2X receptors: An emerging channel family. Eur J Neurosci 8:2221-2228
    • (1996) Eur J Neurosci , vol.8 , pp. 2221-2228
    • Buell, G.1    Collo, G.2    Rassendren, F.3
  • 16
    • 0033058757 scopus 로고    scopus 로고
    • Emerging roles of purinergic signalling in gastrointestinal epithelial secretion and hepatobiliary function
    • Roman RM, Fitz JG (1999) Emerging roles of purinergic signalling in gastrointestinal epithelial secretion and hepatobiliary function. Gastroenterology 116:964-979
    • (1999) Gastroenterology , vol.116 , pp. 964-979
    • Roman, R.M.1    Fitz, J.G.2
  • 17
    • 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
  • 18
    • 0030437695 scopus 로고    scopus 로고
    • Extracellular purine metabolism
    • Zimmermann H (1996) Extracellular purine metabolism. Drug Dev Res 39:337-352
    • (1996) Drug Dev Res , vol.39 , pp. 337-352
    • Zimmermann, H.1
  • 19
    • 0034855050 scopus 로고    scopus 로고
    • Modulation of extracellular nucleotide-mediated signaling by CD39/ nucleoside triphosphate diphosphohydrolase-1
    • Robson SC, Enjyoji K, Goepfert C et al (2001) Modulation of extracellular nucleotide-mediated signaling by CD39/nucleoside triphosphate diphosphohydrolase-1. Drug Dev Res 53:193-207
    • (2001) Drug Dev Res , vol.53 , pp. 193-207
    • Robson, S.C.1    Enjyoji, K.2    Goepfert, C.3
  • 20
    • 18044366362 scopus 로고    scopus 로고
    • Ectonucleotidases of CD39 family modulate vascular inflammation and thrombosis in transplantation
    • Robson SC, Wu Y, Sun XF et al (2005) Ectonucleotidases of CD39 family modulate vascular inflammation and thrombosis in transplantation. Semin Thromb Hemost 31:217-233
    • (2005) Semin Thromb Hemost , vol.31 , pp. 217-233
    • Robson, S.C.1    Wu, Y.2    Sun, X.F.3
  • 21
    • 0033816854 scopus 로고    scopus 로고
    • Ecto-enzymes: Physiology meets pathology
    • Goding JW (2000) Ecto-enzymes: Physiology meets pathology. J Leukoc Biol 67:285-311
    • (2000) J Leukoc Biol , vol.67 , pp. 285-311
    • Goding, J.W.1
  • 23
    • 0035810936 scopus 로고    scopus 로고
    • o ATP synthase is active in ATP synthesis and is inhibited by angiostatin
    • o ATP synthase is active in ATP synthesis and is inhibited by angiostatin. Proc Natl Acad Sci USA 98:6656-6661
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6656-6661
    • Moser, T.L.1    Kenan, D.J.2    Ashley, T.A.3
  • 24
    • 0344011492 scopus 로고    scopus 로고
    • + -ATP synthase in the extracellular ATP synthesis and proliferation of human umbilical vein endothelial cells
    • + -ATP synthase in the extracellular ATP synthesis and proliferation of human umbilical vein endothelial cells. Mol Cancer Res 1:931-939
    • (2003) Mol Cancer Res , vol.1 , pp. 931-939
    • Arakaki, N.1    Nagao, T.2    Niki, R.3
  • 25
    • 25144473903 scopus 로고    scopus 로고
    • NPP-type ectophosphodiesterases: Unity in diversity
    • Stefan C, Jansen S, Bollen M (2005) NPP-type ectophosphodiesterases: Unity in diversity. Trends Biochem Sci 30:542-550
    • (2005) Trends Biochem Sci , vol.30 , pp. 542-550
    • Stefan, C.1    Jansen, S.2    Bollen, M.3
  • 26
    • 0026729643 scopus 로고
    • 5′-nucleotidase-molecular structure and functional aspects
    • Zimmermann H (1992) 5′-nucleotidase-molecular structure and functional aspects. Biochem J 285:345-365
    • (1992) Biochem J , vol.285 , pp. 345-365
    • Zimmermann, H.1
  • 27
    • 0031933227 scopus 로고    scopus 로고
    • Ecto-enzyme and signaling functions of lymphocyte CD73
    • Resta R, Yamashita Y, Thompson LF (1998) Ecto-enzyme and signaling functions of lymphocyte CD73. Immunol Rev 161:95-109
    • (1998) Immunol Rev , vol.161 , pp. 95-109
    • Resta, R.1    Yamashita, Y.2    Thompson, L.F.3
  • 28
    • 35549006392 scopus 로고    scopus 로고
    • E-NTPDases in human airways regulation and relevance for chronic lung diseases
    • (PUSI 2:1; this issue)
    • Burch LH, Picher M (2006) E-NTPDases in human airways regulation and relevance for chronic lung diseases. Purinergic Signalling (PUSI 2:1; this issue)
    • (2006) Purinergic Signalling
    • Burch, L.H.1    Picher, M.2
  • 29
    • 33846081115 scopus 로고    scopus 로고
    • CD39, NTPDase1, is attached to the plasma membrane by two transmembrane domains. Why?
    • (PUSI 2:1; this issue)
    • Grinthal A, Guidotti G (2006) CD39, NTPDase1, is attached to the plasma membrane by two transmembrane domains. Why? Purinergic Signalling (PUSI 2:1; this issue)
    • (2006) Purinergic Signalling
    • Grinthal, A.1    Guidotti, G.2
  • 30
    • 33845702620 scopus 로고    scopus 로고
    • The structure of the nucleoside triphosphate diphosphohydrolases (NTPDases) as revealed by mutagenic and comptational modeling analyses
    • (PUSI 2:1; this issue)
    • Kirley TL, Crawford PA, Smith TM (2006) The structure of the nucleoside triphosphate diphosphohydrolases (NTPDases) as revealed by mutagenic and comptational modeling analyses. Purinergic Signalling (PUSI 2:1; this issue)
    • (2006) Purinergic Signalling
    • Kirley, T.L.1    Crawford, P.A.2    Smith, T.M.3
  • 31
    • 0030221465 scopus 로고    scopus 로고
    • Biochemistry, localization and functional roles of ecto-nucleotidases in the nervous system
    • Zimmermann H (1996) Biochemistry, localization and functional roles of ecto-nucleotidases in the nervous system. Prog Neurobiol 49:589-618
    • (1996) Prog Neurobiol , vol.49 , pp. 589-618
    • Zimmermann, H.1
  • 32
    • 0033152549 scopus 로고    scopus 로고
    • Two novel families of ecto-nucleotidases: Molecular structures, catalytic properties, and a search for function
    • Zimmermann H (1999) Two novel families of ecto-nucleotidases: Molecular structures, catalytic properties, and a search for function. Trends Pharmacol Sci 20:231-236
    • (1999) Trends Pharmacol Sci , vol.20 , pp. 231-236
    • Zimmermann, H.1
  • 33
    • 0033766981 scopus 로고    scopus 로고
    • Extracellular metabolism of ATP and other nucleotides
    • Zimmermann H (2000) Extracellular metabolism of ATP and other nucleotides. Naunyn-Schmiedeberg's Arch Pharmacol 362:299-309
    • (2000) Naunyn-Schmiedeberg's Arch Pharmacol , vol.362 , pp. 299-309
    • Zimmermann, H.1
  • 34
    • 0035033156 scopus 로고    scopus 로고
    • Ectonucleotidases: Some recent developments and a note on nomenclature
    • Zimmermann H (2001) Ectonucleotidases: Some recent developments and a note on nomenclature. Drug Dev Res 52:44-56
    • (2001) Drug Dev Res , vol.52 , pp. 44-56
    • Zimmermann, H.1
  • 35
    • 0032462074 scopus 로고    scopus 로고
    • Structure and function of ectoapyrase (CD39)
    • Wang TF, Handa M, Guidotti G (1998) Structure and function of ectoapyrase (CD39). Drug Dev Res 45:245-252
    • (1998) Drug Dev Res , vol.45 , pp. 245-252
    • Wang, T.F.1    Handa, M.2    Guidotti, G.3
  • 36
    • 0032869899 scopus 로고    scopus 로고
    • Ecto-nucleotidases: Molecular structures, catalytic properties, and functional roles in the nervous system
    • Zimmermann H, Braun N (1999) Ecto-nucleotidases: Molecular structures, catalytic properties, and functional roles in the nervous system. Prog Brain Res 120:371-385
    • (1999) Prog Brain Res , vol.120 , pp. 371-385
    • Zimmermann, H.1    Braun, N.2
  • 37
    • 0000612708 scopus 로고
    • Ectonucleotidases. Measurememt of activities and use of inhibitors
    • In: Paton DM (ed) Plenum, New York
    • Pearson JD (1985) Ectonucleotidases. Measurememt of activities and use of inhibitors. In: Paton DM (ed) Methods in pharmacology 6. Plenum, New York, pp 83-107
    • (1985) Methods in Pharmacology , vol.6 , pp. 83-107
    • Pearson, J.D.1
  • 39
    • 77957057275 scopus 로고    scopus 로고
    • ATP-diphosphohydrolases, apyrases, and nucleotide phosphohydrolases: Biochemical properties and functions
    • In: Lee AG (ed) JAI, Greenwich, London
    • Beaudoin AR, Sévigny J, Picher M (1996) ATP-diphosphohydrolases, apyrases, and nucleotide phosphohydrolases: Biochemical properties and functions. In: Lee AG (ed) Biomembranes. JAI, Greenwich, London, pp 369-401
    • (1996) Biomembranes , pp. 369-401
    • Beaudoin, A.R.1    Sévigny, J.2    Picher, M.3
  • 40
    • 0001955370 scopus 로고    scopus 로고
    • Extracellular metabolism of nucleotides and adenosine in the cardiovascular system
    • In: Burnstock G, Dobson JG, Liang BT et al (eds) Kluwer, Dordrecht, Boston, London
    • Zimmermann H, Pearson J (1998) Extracellular metabolism of nucleotides and adenosine in the cardiovascular system. In: Burnstock G, Dobson JG, Liang BT et al (eds) Cardiovascular Biology of Purines. Kluwer, Dordrecht, Boston, London, pp 342-358
    • (1998) Cardiovascular Biology of Purines , pp. 342-358
    • Zimmermann, H.1    Pearson, J.2
  • 41
    • 0027938206 scopus 로고
    • The CD39 lymphoid cell activation antigen: Molecular cloning and structural characterization
    • Maliszewski CR, DeLepesse GJT, Schoenborn MA et al (1994) The CD39 lymphoid cell activation antigen: Molecular cloning and structural characterization. J Immunol 153:3574-3583
    • (1994) J Immunol , vol.153 , pp. 3574-3583
    • Maliszewski, C.R.1    DeLepesse, G.J.T.2    Schoenborn, M.A.3
  • 42
    • 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
  • 44
    • 12644288616 scopus 로고    scopus 로고
    • Identification and characterization of CD39 vascular ATP diphosphohydrolase
    • Kaczmarek E, Koziak K, Sévigny J et al (1996) Identification and characterization of CD39 vascular ATP diphosphohydrolase. J Biol Chem 271:33116-33122
    • (1996) J Biol Chem , vol.271 , pp. 33116-33122
    • Kaczmarek, E.1    Koziak, K.2    Sévigny, J.3
  • 45
    • 0028828430 scopus 로고
    • Purification and properties of human placental ATP diphosphohydrolase
    • Christoforidis S, Papamarcaki T, Galaris D et al (1995) Purification and properties of human placental ATP diphosphohydrolase. Eur J Biochem 234:66-74
    • (1995) Eur J Biochem , vol.234 , pp. 66-74
    • Christoforidis, S.1    Papamarcaki, T.2    Galaris, D.3
  • 46
    • 0030984844 scopus 로고    scopus 로고
    • Characterization of brain ecto-apyrase: Evidence for only one ecto-apyrase (CD39) gene
    • Wang TF, Rosenberg PA, Guidotti G (1997) Characterization of brain ecto-apyrase: Evidence for only one ecto-apyrase (CD39) gene. Mol Brain Res 47:295-302
    • (1997) Mol Brain Res , vol.47 , pp. 295-302
    • Wang, T.F.1    Rosenberg, P.A.2    Guidotti, G.3
  • 47
    • 0030721511 scopus 로고    scopus 로고
    • An ecto-ATPase and an ecto-ATP diphosphohydrolase are expressed in rat brain
    • Kegel B, Braun N, Heine P et al (1997) An ecto-ATPase and an ecto-ATP diphosphohydrolase are expressed in rat brain. Neuropharmacology 36:1189-1200
    • (1997) Neuropharmacology , vol.36 , pp. 1189-1200
    • Kegel, B.1    Braun, N.2    Heine, P.3
  • 48
    • 0031012542 scopus 로고    scopus 로고
    • Complementary DNA cloning and sequencing of the chicken muscle ecto-ATPase-homology with the lymphoid cell activation antigen CD39
    • Kirley TL (1997) Complementary DNA cloning and sequencing of the chicken muscle ecto-ATPase-homology with the lymphoid cell activation antigen CD39. J Biol Chem 272:1076-1081
    • (1997) J Biol Chem , vol.272 , pp. 1076-1081
    • Kirley, T.L.1
  • 49
    • 0031229572 scopus 로고    scopus 로고
    • Cloning and mapping of a human and mouse gene with homology to ecto-ATPase genes
    • Chadwick BP, Frischauf AM (1997) Cloning and mapping of a human and mouse gene with homology to ecto-ATPase genes. Mamm Genome 8:668-672
    • (1997) Mamm Genome , vol.8 , pp. 668-672
    • Chadwick, B.P.1    Frischauf, A.M.2
  • 50
    • 0032526486 scopus 로고    scopus 로고
    • The CD39-like gene family: Identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster
    • Chadwick BP, Frischauf AM (1998) The CD39-like gene family: Identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics 50:357-367
    • (1998) Genomics , vol.50 , pp. 357-367
    • Chadwick, B.P.1    Frischauf, A.M.2
  • 51
    • 15644364846 scopus 로고    scopus 로고
    • cDNA cloning and chromosomal mapping of a mouse gene with homology to NTPases
    • Chadwick BP, Williamson J, Sheer D et al (1998) cDNA cloning and chromosomal mapping of a mouse gene with homology to NTPases. Mamm Genome 9:162-164
    • (1998) Mamm Genome , vol.9 , pp. 162-164
    • Chadwick, B.P.1    Williamson, J.2    Sheer, D.3
  • 52
    • 2442534085 scopus 로고    scopus 로고
    • Cloning and characterization of mouse nucleoside triphosphate diphosphohydrolase-8
    • Bigonnesse F, Lévesque SA, Kukulski F et al (2004) Cloning and characterization of mouse nucleoside triphosphate diphosphohydrolase-8. Biochemistry USA 43:5511-5519
    • (2004) Biochemistry USA , vol.43 , pp. 5511-5519
    • Bigonnesse, F.1    Lévesque, S.A.2    Kukulski, F.3
  • 53
    • 13444278752 scopus 로고    scopus 로고
    • C-terininal splicing of NTPDase2 provides distinctive catalytic properties, cellular distribution and enzyme regulation
    • Wang CJF, Vlajkovic SM, Housley GD et al (2005) C-terininal splicing of NTPDase2 provides distinctive catalytic properties, cellular distribution and enzyme regulation. Biochem J 385:729-736
    • (2005) Biochem J , vol.385 , pp. 729-736
    • Wang, C.J.F.1    Vlajkovic, S.M.2    Housley, G.D.3
  • 54
    • 0141994772 scopus 로고    scopus 로고
    • Requirement of Cys(399) for processing of the human ecto-ATPase (NTPDase2) and its implications for determination of the activities of splice variants of the enzyme
    • Mateo J, Kreda S, Henry CE et al (2003) Requirement of Cys(399) for processing of the human ecto-ATPase (NTPDase2) and its implications for determination of the activities of splice variants of the enzyme. J Biol Chem 278:39960-39968
    • (2003) J Biol Chem , vol.278 , pp. 39960-39968
    • Mateo, J.1    Kreda, S.2    Henry, C.E.3
  • 55
    • 24744447579 scopus 로고    scopus 로고
    • CD molecules 2005: Human cell differentiation molecules
    • Zola H, Swart B, Nicholson I et al (2005) CD molecules 2005: Human cell differentiation molecules. Blood 106:3123-3126
    • (2005) Blood , vol.106 , pp. 3123-3126
    • Zola, H.1    Swart, B.2    Nicholson, I.3
  • 56
    • 0001951142 scopus 로고    scopus 로고
    • Proposed nomenclature for two novel nucleotide hydrolyzing enzyme families expressed on the cell surface
    • In: vanDuffel L, Lemmens R (eds) Shaker BV, Maastricht
    • Zimmermann H, Beaudoin AR, Bollen M et al (2000) Proposed nomenclature for two novel nucleotide hydrolyzing enzyme families expressed on the cell surface. In: VanDuffel L, Lemmens R (eds) Ecto-ATPases and related ectonucleotidases, Shaker BV, Maastricht, pp 1-8
    • (2000) Ecto-ATPases and Related Ectonucleotidases , pp. 1-8
    • Zimmermann, H.1    Beaudoin, A.R.2    Bollen, M.3
  • 57
    • 16444369930 scopus 로고    scopus 로고
    • Comparative hydrolysis of P2 receptor agonists by NTPDase 1, 2, 3 and 8
    • Kukulski F, Lévesque SA, Lavoie ÉG et al (2005) Comparative hydrolysis of P2 receptor agonists by NTPDase 1, 2, 3 and 8. Purinergic Signalling 1:193-204
    • (2005) Purinergic Signalling , vol.1 , pp. 193-204
    • Kukulski, F.1    Lévesque, S.A.2    Lavoie, É.G.3
  • 58
    • 2342455143 scopus 로고    scopus 로고
    • Cloning and characterization of mouse nucleoside triphosphate diphosphohydrolase-3
    • Lavoie É.G, Kukulski F, Lévesque SA et al (2004) Cloning and characterization of mouse nucleoside triphosphate diphosphohydrolase-3. Biochem Pharmacol 67:1917-1926
    • (2004) Biochem Pharmacol , vol.67 , pp. 1917-1926
    • Lavoie, É.G.1    Kukulski, F.2    Lévesque, S.A.3
  • 59
    • 23844501100 scopus 로고    scopus 로고
    • Cloning and characterization of the ecto-nucleotidase NTPDase3 from rat brain: Predicted secondary structure and relation to members of the E-NTPDase family and actin
    • Vorhoff T, Zimmermann H, Pelletier J et al (2005) Cloning and characterization of the ecto-nucleotidase NTPDase3 from rat brain: Predicted secondary structure and relation to members of the E-NTPDase family and actin. Purinergic Signaling 1:259-270
    • (2005) Purinergic Signaling , vol.1 , pp. 259-270
    • Vorhoff, T.1    Zimmermann, H.2    Pelletier, J.3
  • 60
    • 0003740712 scopus 로고    scopus 로고
    • The C-terminal cysteine-rich region dictates specific catalytic properties in chimeras of the ecto-nucleotidases NTPDase1 and NTPDase2
    • Heine P, Braun N, Sévigny J et al (2001) The C-terminal cysteine-rich region dictates specific catalytic properties in chimeras of the ecto-nucleotidases NTPDase1 and NTPDase2. Eur J Biochem 262:102-107
    • (2001) Eur J Biochem , vol.262 , pp. 102-107
    • Heine, P.1    Braun, N.2    Sévigny, J.3
  • 61
    • 7244243728 scopus 로고    scopus 로고
    • Dynamic motions of CD39 transmembrane domains regulate and are regulated by the enzymatic active site
    • Grinthal A, Guidotti G (2004) Dynamic motions of CD39 transmembrane domains regulate and are regulated by the enzymatic active site. Biochemistry USA 43:13849-13858
    • (2004) Biochemistry USA , vol.43 , pp. 13849-13858
    • Grinthal, A.1    Guidotti, G.2
  • 62
    • 0037089425 scopus 로고    scopus 로고
    • Differential catalytic properties and vascular topography of murine nucleoside triphosphate diphosphohydrolase 1 (NTPDase1) and NTPDase2 have implications for thromboregulation
    • Sévigny J, Sundberg C, Braun N et al (2002) Differential catalytic properties and vascular topography of murine nucleoside triphosphate diphosphohydrolase 1 (NTPDase1) and NTPDase2 have implications for thromboregulation. Blood 99:2801-2809
    • (2002) Blood , vol.99 , pp. 2801-2809
    • Sévigny, J.1    Sundberg, C.2    Braun, N.3
  • 63
    • 0029811585 scopus 로고    scopus 로고
    • Partial purification and immunohistochemical localization of ATP diphosphohydrolase from Schistosoma mansoni - Immunological cross-reactivities with potato apyrase and Toxoplasma gondii nucleoside triphosphate hydrolase
    • Vasconcelos EG, Ferreira ST, de Carvalho TMU et al (1996) Partial purification and immunohistochemical localization of ATP diphosphohydrolase from Schistosoma mansoni - Immunological cross-reactivities with potato apyrase and Toxoplasma gondii nucleoside triphosphate hydrolase. J Biol Chem 271:22139-22145
    • (1996) J Biol Chem , vol.271 , pp. 22139-22145
    • Vasconcelos, E.G.1    Ferreira, S.T.2    de Carvalho, T.M.U.3
  • 64
    • 0000048169 scopus 로고    scopus 로고
    • Structural elements and limited proteolysis of CD39 influence ATP diphosphohydrolase activity
    • Schulte am Esch J, Sévigny J, Kaczmarek E et al (1999) Structural elements and limited proteolysis of CD39 influence ATP diphosphohydrolase activity. Biochemistry USA 38:2248-2258
    • (1999) Biochemistry USA , vol.38 , pp. 2248-2258
    • Schulte am Esch, J.1    Sévigny, J.2    Kaczmarek, E.3
  • 65
    • 23844520981 scopus 로고    scopus 로고
    • Expression, characterization, and site-directed mutagenesis of a human E-type ATPase
    • In: vanDuffel L, Lemmens R (eds) Shaker BV, Maastricht
    • Smith TM, Kirley TL (2000) Expression, characterization, and site-directed mutagenesis of a human E-type ATPase. In: VanDuffel L, Lemmens R (eds) Ecto-ATPases and Related Ectonucleotidases. Shaker BV, Maastricht, pp. 90-105
    • (2000) Ecto-ATPases and Related Ectonucleotidases , pp. 90-105
    • Smith, T.M.1    Kirley, T.L.2
  • 66
    • 0035810654 scopus 로고    scopus 로고
    • The importance of histidine residues in human ecto-nucleoside triphosphate diphosphohydrolase-3 as determined by site-directed mutagenesis
    • Hicks-Berger CA, Yang F, Smith TM et al (2001) The importance of histidine residues in human ecto-nucleoside triphosphate diphosphohydrolase-3 as determined by site-directed mutagenesis. BBA Protein Struct Mol Enzym 1547:72-81
    • (2001) BBA Protein Struct Mol Enzym , vol.1547 , pp. 72-81
    • Hicks-Berger, C.A.1    Yang, F.2    Smith, T.M.3
  • 67
    • 0035799316 scopus 로고    scopus 로고
    • Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: The importance of residues in the apyrase conserved regions
    • Yang F, Hicks-Berger CA, Smith TM et al (2001) Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: The importance of residues in the apyrase conserved regions. Biochemistry USA 40:3943-3950
    • (2001) Biochemistry USA , vol.40 , pp. 3943-3950
    • Yang, F.1    Hicks-Berger, C.A.2    Smith, T.M.3
  • 68
    • 0037404803 scopus 로고    scopus 로고
    • Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3
    • Murphy DM, Kirley TL (2003) Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3. Arch Biochem Biophys 413:107-115
    • (2003) Arch Biochem Biophys , vol.413 , pp. 107-115
    • Murphy, D.M.1    Kirley, T.L.2
  • 69
    • 0025753142 scopus 로고
    • Similarity of the three dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein
    • Flaherty KM, Mckay DB, Kabsch W et al (1991) Similarity of the three dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Proc Natl Acad Sci U S A 88:5041-5045
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 5041-5045
    • Flaherty, K.M.1    Mckay, D.B.2    Kabsch, W.3
  • 70
    • 0033524467 scopus 로고    scopus 로고
    • Site-directed mutagenesis of a human brain ecto-apyrase: Evidence that the E-type ATPases are related to the actin/heat shock 70/sugar kinase superfamily
    • Smith TM, Kirley TL (1999) Site-directed mutagenesis of a human brain ecto-apyrase: Evidence that the E-type ATPases are related to the actin/ heat shock 70/sugar kinase superfamily. Biochemistry USA 38:321-328
    • (1999) Biochemistry USA , vol.38 , pp. 321-328
    • Smith, T.M.1    Kirley, T.L.2
  • 71
    • 0141988880 scopus 로고    scopus 로고
    • Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: Implications for structure and function
    • Ivanenkov VV, Murphy-Piedmonte DM, Kirley TL (2003) Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: Implications for structure and function. Biochemistry USA 42:11726-11735
    • (2003) Biochemistry USA , vol.42 , pp. 11726-11735
    • Ivanenkov, V.V.1    Murphy-Piedmonte, D.M.2    Kirley, T.L.3
  • 72
    • 21744436486 scopus 로고    scopus 로고
    • Characterization of disulfide bonds in human nucleoside triphosphate diphosphohydrolase 3 (NTPDase3): Implications for NTPDase structural modeling
    • Ivanenkov VV, Meller J, Kirley TL (2005) Characterization of disulfide bonds in human nucleoside triphosphate diphosphohydrolase 3 (NTPDase3): Implications for NTPDase structural modeling. Biochemistry USA 44:8998-9012
    • (2005) Biochemistry USA , vol.44 , pp. 8998-9012
    • Ivanenkov, V.V.1    Meller, J.2    Kirley, T.L.3
  • 73
    • 0030018168 scopus 로고    scopus 로고
    • Control of cell membrane ecto-ATPase by oligomerization state: Intermolecular cross-linking modulates ATPase activity
    • Stout JG, Kirley TL (1996) Control of cell membrane ecto-ATPase by oligomerization state: Intermolecular cross-linking modulates ATPase activity. Biochemistry USA 35:8289-8298
    • (1996) Biochemistry USA , vol.35 , pp. 8289-8298
    • Stout, J.G.1    Kirley, T.L.2
  • 74
    • 0032016497 scopus 로고    scopus 로고
    • Cross-linking induces homodimer formation and inhibits enzymatic activity of chicken stomach ecto-apyrase
    • Carl SAL, Smith TM, Kirley TL (1998) Cross-linking induces homodimer formation and inhibits enzymatic activity of chicken stomach ecto-apyrase. Biochem Mol Biol Int 44:463-470
    • (1998) Biochem Mol Biol Int , vol.44 , pp. 463-470
    • Carl, S.A.L.1    Smith, T.M.2    Kirley, T.L.3
  • 75
    • 0032544580 scopus 로고    scopus 로고
    • The transmembrane domains of ectoapyrase (CD39) affect its enzymatic activity and quaternary structure
    • Wang TF, Ou Y, Guidotti G (1998) The transmembrane domains of ectoapyrase (CD39) affect its enzymatic activity and quaternary structure. J Biol Chem 273:24814-24821
    • (1998) J Biol Chem , vol.273 , pp. 24814-24821
    • Wang, T.F.1    Ou, Y.2    Guidotti, G.3
  • 76
    • 0033514375 scopus 로고    scopus 로고
    • Glycosylation is essential for functional expression of a human brain ecto-apyrase
    • Smith TM, Kirley TL (1999) Glycosylation is essential for functional expression of a human brain ecto-apyrase. Biochemistry USA 38:1509-1516
    • (1999) Biochemistry USA , vol.38 , pp. 1509-1516
    • Smith, T.M.1    Kirley, T.L.2
  • 77
    • 0034635168 scopus 로고    scopus 로고
    • Substitution of His59 converts CD39 into an ADPase in a quarternary structure dependent manner
    • Grinthal A, Guidotti G (2000) Substitution of His59 converts CD39 into an ADPase in a quarternary structure dependent manner. Biochemistry USA 39:9-16
    • (2000) Biochemistry USA , vol.39 , pp. 9-16
    • Grinthal, A.1    Guidotti, G.2
  • 78
    • 0038070596 scopus 로고    scopus 로고
    • Determination of native oligomeric state and substrate specificity of rat NTPDase1 and NTPDase2 after heterologous expression in Xenopus oocytes
    • Failer BU, Aschrafi A, Schmalzing G et al (2003) Determination of native oligomeric state and substrate specificity of rat NTPDase1 and NTPDase2 after heterologous expression in Xenopus oocytes. Eur J Biochem 270:1802-1809
    • (2003) Eur J Biochem , vol.270 , pp. 1802-1809
    • Failer, B.U.1    Aschrafi, A.2    Schmalzing, G.3
  • 79
    • 0037065699 scopus 로고    scopus 로고
    • Transmembrane domains confer different substrate specificities and adenosine diphosphate hydrolysis mechanisms on CD39, CD39L1, and chimeras
    • Grinthal A, Guidotti G (2002) Transmembrane domains confer different substrate specificities and adenosine diphosphate hydrolysis mechanisms on CD39, CD39L1, and chimeras. Biochemistry USA 41:1947-1956
    • (2002) Biochemistry USA , vol.41 , pp. 1947-1956
    • Grinthal, A.1    Guidotti, G.2
  • 80
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock protein
    • Bork P, Sander C, Valencia A (1992) An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock protein. Proc Natl Acad Sci USA 89:7290-7294
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 81
    • 0031016802 scopus 로고    scopus 로고
    • Loss of ATP diphosphohydrolase activity with endothelial cell activation
    • Robson SC, Kaczmarek E, Siegel JB et al (1997) Loss of ATP diphosphohydrolase activity with endothelial cell activation. J Exp Med 185:153-163
    • (1997) J Exp Med , vol.185 , pp. 153-163
    • Robson, S.C.1    Kaczmarek, E.2    Siegel, J.B.3
  • 82
    • 0030912495 scopus 로고    scopus 로고
    • Modulation of vascular ATP diphosphohydrolase by fatty acids
    • Robson SC, Daoud S, Begin M et al (1997) Modulation of vascular ATP diphosphohydrolase by fatty acids. Blood Coagul Fibrinolysis 8:21-27
    • (1997) Blood Coagul Fibrinolysis , vol.8 , pp. 21-27
    • Robson, S.C.1    Daoud, S.2    Begin, M.3
  • 83
    • 0035798558 scopus 로고    scopus 로고
    • Mammalian plasma membrane ecto-nucleoside triphosphate diphosphohydrolase 1, CD39, is not active intracellularly - The N -glycosylation state of CD39 correlates with surface activity and localization
    • Zhong XT, Malhotra R, Woodruff R et al (2001) Mammalian plasma membrane ecto-nucleoside triphosphate diphosphohydrolase 1, CD39, is not active intracellularly - The N -glycosylation state of CD39 correlates with surface activity and localization. J Biol Chem 276:41518-41525
    • (2001) J Biol Chem , vol.276 , pp. 41518-41525
    • Zhong, X.T.1    Malhotra, R.2    Woodruff, R.3
  • 84
    • 0034695487 scopus 로고    scopus 로고
    • Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae
    • Koziak K, Kaczmarek E, Kittel A et al (2000) Palmitoylation targets CD39/ endothelial ATP diphosphohydrolase to caveolae. J Biol Chem 275:2057-2062
    • (2000) J Biol Chem , vol.275 , pp. 2057-2062
    • Koziak, K.1    Kaczmarek, E.2    Kittel, A.3
  • 86
    • 22544484227 scopus 로고    scopus 로고
    • Cholesterol-dependent lipid assemblies regulate the activity of the ecto-nucleotidase CD39
    • Papanikolaou A, Papafotika A, Murphy C et al (2005) Cholesterol-dependent lipid assemblies regulate the activity of the ecto-nucleotidase CD39. J Biol Chem 280:26406-26414
    • (2005) J Biol Chem , vol.280 , pp. 26406-26414
    • Papanikolaou, A.1    Papafotika, A.2    Murphy, C.3
  • 88
    • 0033525077 scopus 로고    scopus 로고
    • Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts - Many raft proteins are acylated, while few are prenylated
    • Melkonian KA, Ostermeyer AG, Chen JZ et al (1999) Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts - Many raft proteins are acylated, while few are prenylated. J Biol Chem 274:3910-3917
    • (1999) J Biol Chem , vol.274 , pp. 3910-3917
    • Melkonian, K.A.1    Ostermeyer, A.G.2    Chen, J.Z.3
  • 89
    • 0036102125 scopus 로고    scopus 로고
    • CD39 is the dominant Langerhans cell associated ecto-NTPDase: Modulatory roles in inflammation and immune responsiveness
    • Mizumoto N, Kumamoto T, Robson SC et al (2002) CD39 is the dominant Langerhans cell associated ecto-NTPDase: Modulatory roles in inflammation and immune responsiveness. Nat Med 8:358-365
    • (2002) Nat Med , vol.8 , pp. 358-365
    • Mizumoto, N.1    Kumamoto, T.2    Robson, S.C.3
  • 91
    • 0032479195 scopus 로고    scopus 로고
    • Ecto-ATP diphosphohydrolase/CD39 is overexpressed in differentiated human melanomas
    • Dzhandzhugazyan KN, Kirkin AF, Straten PT et al (1998) Ecto-ATP diphosphohydrolase/CD39 is overexpressed in differentiated human melanomas. FEBS Lett 430:227-230
    • (1998) FEBS Lett , vol.430 , pp. 227-230
    • Dzhandzhugazyan, K.N.1    Kirkin, A.F.2    Straten, P.T.3
  • 92
    • 4644269260 scopus 로고    scopus 로고
    • Enhanced ecto-apyrase activity of stimulated endothelial or mesangial cells is downregulated by glucocorticolds in vitro
    • Kapojos JJ, VandenBerg A, Borghuis T et al (2004) Enhanced ecto-apyrase activity of stimulated endothelial or mesangial cells is downregulated by glucocorticolds in vitro. Eur J Pharmacol 501:191-198
    • (2004) Eur J Pharmacol , vol.501 , pp. 191-198
    • Kapojos, J.J.1    VandenBerg, A.2    Borghuis, T.3
  • 93
    • 0028556471 scopus 로고
    • Upregulation of antithrombotic ectonucleotidases by aspirin in human endothelial cells in-vitro
    • Cheung PK, Visser J, Bakker WW (1994) Upregulation of antithrombotic ectonucleotidases by aspirin in human endothelial cells in-vitro. J Pharm Pharmacol 46:1032-1034
    • (1994) J Pharm Pharmacol , vol.46 , pp. 1032-1034
    • Cheung, P.K.1    Visser, J.2    Bakker, W.W.3
  • 94
    • 0030974576 scopus 로고    scopus 로고
    • Modulation of glomerular ecto-ADPase expression by oestradiol - A histochemical study
    • Faas MM, Bakker WW, Klok PA et al (1997) Modulation of glomerular ecto-ADPase expression by oestradiol - A histochemical study. Thromb Haemost 77:767-771
    • (1997) Thromb Haemost , vol.77 , pp. 767-771
    • Faas, M.M.1    Bakker, W.W.2    Klok, P.A.3
  • 95
    • 0032547062 scopus 로고    scopus 로고
    • A novel response to dioxin - Induction of ecto-ATPase gene expression
    • Gao L, Dong LQ, Whitlock JP (1998) A novel response to dioxin - Induction of ecto-ATPase gene expression. J Biol Chem 273:15358-15365
    • (1998) J Biol Chem , vol.273 , pp. 15358-15365
    • Gao, L.1    Dong, L.Q.2    Whitlock, J.P.3
  • 96
    • 0035881219 scopus 로고    scopus 로고
    • Accessibility and activity of the promoter for a dioxin-inducible ecto-ATPase gene
    • Gao L, Whitlock JP (2001) Accessibility and activity of the promoter for a dioxin-inducible ecto-ATPase gene. Arch Biochem Biophys 392:270-278
    • (2001) Arch Biochem Biophys , vol.392 , pp. 270-278
    • Gao, L.1    Whitlock, J.P.2
  • 97
    • 18644375290 scopus 로고    scopus 로고
    • Cell-type specificity of ectonucleotidase expression and upregulation by 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Wood E, Broekman MJ, Kirley TL et al (2002) Cell-type specificity of ectonucleotidase expression and upregulation by 2,3,7,8-tetrachlorodibenzo- p -dioxin. Arch Biochem Biophys 407:49-62
    • (2002) Arch Biochem Biophys , vol.407 , pp. 49-62
    • Wood, E.1    Broekman, M.J.2    Kirley, T.L.3
  • 98
    • 0035110533 scopus 로고    scopus 로고
    • Ecto-ATPase mRNA is regulated by FSH in Sertoli cells
    • Lu QX, Porter LD, Cui XM et al (2001) Ecto-ATPase mRNA is regulated by FSH in Sertoli cells. J Androl 22:289-301
    • (2001) J Androl , vol.22 , pp. 289-301
    • Lu, Q.X.1    Porter, L.D.2    Cui, X.M.3
  • 99
    • 11244334380 scopus 로고    scopus 로고
    • Ectonucleotidase NTPDase2 is selectively down-regulated in biliary cirrhosis
    • Dranoff JA, Kruglov EA, Toure J et al (2004) Ectonucleotidase NTPDase2 is selectively down-regulated in biliary cirrhosis. J Investig Med 52:475-482
    • (2004) J Investig Med , vol.52 , pp. 475-482
    • Dranoff, J.A.1    Kruglov, E.A.2    Toure, J.3
  • 100
    • 0032538046 scopus 로고    scopus 로고
    • Nucleotide metabolizing ectoenzymes are upregulated in A431 cells periodically treated with cytostatic ATP leading to partial resistance without preventing apoptosis
    • Wiendl HS, Schneider C, Ogilvie A (1998) Nucleotide metabolizing ectoenzymes are upregulated in A431 cells periodically treated with cytostatic ATP leading to partial resistance without preventing apoptosis. Biochim Biophys Acta Mol Cell Res 1404:282-298
    • (1998) Biochim Biophys Acta Mol Cell Res , vol.1404 , pp. 282-298
    • Wiendl, H.S.1    Schneider, C.2    Ogilvie, A.3
  • 101
    • 0036001053 scopus 로고    scopus 로고
    • Purine signaling and potential new therapeutic approach: Possible outcome of NTPDase inhibition
    • Gendron FP, Benrezzak O, Krugh BW et al (2002) Purine signaling and potential new therapeutic approach: Possible outcome of NTPDase inhibition. Current Drug Targets 3:229-245
    • (2002) Current Drug Targets , vol.3 , pp. 229-245
    • Gendron, F.P.1    Benrezzak, O.2    Krugh, B.W.3
  • 103
    • 0030221110 scopus 로고    scopus 로고
    • Modulation of purinergic neurotransmission by ecto-ATPase
    • Kennedy C, Westfall TD, Sneddon P (1996) Modulation of purinergic neurotransmission by ecto-ATPase. Semin Neurosci 8:195-199
    • (1996) Semin Neurosci , vol.8 , pp. 195-199
    • Kennedy, C.1    Westfall, T.D.2    Sneddon, P.3
  • 104
    • 0030986228 scopus 로고    scopus 로고
    • The ecto-ATPase inhibitor ARL 67156 enhances parasympathetic neurotransmission in the guinea-pig urinary bladder
    • Westfall TD, Kennedy C, Sneddon P (1997) The ecto-ATPase inhibitor ARL 67156 enhances parasympathetic neurotransmission in the guinea-pig urinary bladder. Eur J Pharmacol 329:169-173
    • (1997) Eur J Pharmacol , vol.329 , pp. 169-173
    • Westfall, T.D.1    Kennedy, C.2    Sneddon, P.3
  • 105
    • 1642456586 scopus 로고    scopus 로고
    • Effect of the ecto-ATPase inhibitor, ARL 67156, on the bovine chromaffin cell response to ATP
    • Drakulich DA, Spellmon C, Hexum TD (2004) Effect of the ecto-ATPase inhibitor, ARL 67156, on the bovine chromaffin cell response to ATP. Eur J Pharmacol 485:137-140
    • (2004) Eur J Pharmacol , vol.485 , pp. 137-140
    • Drakulich, D.A.1    Spellmon, C.2    Hexum, T.D.3
  • 106
    • 0034214125 scopus 로고    scopus 로고
    • Novel inhibitors of nucleoside triphosphate diphosphohydrolases: Chemical synthesis and biochemical and pharmacological characterizations
    • Gendron FP, Halbfinger E, Fischer B et al (2000) Novel inhibitors of nucleoside triphosphate diphosphohydrolases: Chemical synthesis and biochemical and pharmacological characterizations. J Med Chem 43:2239-2247
    • (2000) J Med Chem , vol.43 , pp. 2239-2247
    • Gendron, F.P.1    Halbfinger, E.2    Fischer, B.3
  • 107
    • 0142184953 scopus 로고    scopus 로고
    • Oxidized ATP (OATP) attenuates proinflammatory signaling via P2 receptor-independent mechanisms
    • Beigi RD, Kertesy SB, Aquilina G et al (2003) Oxidized ATP (OATP) attenuates proinflammatory signaling via P2 receptor-independent mechanisms. Brit J Pharmacol 140:507-519
    • (2003) Brit J Pharmacol , vol.140 , pp. 507-519
    • Beigi, R.D.1    Kertesy, S.B.2    Aquilina, G.3
  • 108
    • 4043128177 scopus 로고    scopus 로고
    • Gadolinium inhibition of ecto-nucleoside triphosphate diphosphohydrolase activity in Torpedo electric organ
    • Escalada A, Navarro P, Ros E et al (2004) Gadolinium inhibition of ecto-nucleoside triphosphate diphosphohydrolase activity in Torpedo electric organ. Neurochem Res 29:1711-1714
    • (2004) Neurochem Res , vol.29 , pp. 1711-1714
    • Escalada, A.1    Navarro, P.2    Ros, E.3
  • 109
    • 0033563017 scopus 로고    scopus 로고
    • Functional characterization of rat ecto-ATPase and ecto-ATP diphosphohydrolase after heterologous expression in CHO cells
    • Heine P, Braun N, Zimmermann H (1999) Functional characterization of rat ecto-ATPase and ecto-ATP diphosphohydrolase after heterologous expression in CHO cells. Eur J Biochem 262:102-107
    • (1999) Eur J Biochem , vol.262 , pp. 102-107
    • Heine, P.1    Braun, N.2    Zimmermann, H.3
  • 110
    • 0034492841 scopus 로고    scopus 로고
    • Inhibition of ecto-apyrase and ecto-ATPase by pyridoxal phosphate-related compounds
    • Hoffmann C, Heine P, Pradel G et al (2000) Inhibition of ecto-apyrase and ecto-ATPase by pyridoxal phosphate-related compounds. Drug Dev Res 51:153-158
    • (2000) Drug Dev Res , vol.51 , pp. 153-158
    • Hoffmann, C.1    Heine, P.2    Pradel, G.3
  • 111
    • 29744434583 scopus 로고    scopus 로고
    • A capillary electrophoresis method for the characterization of ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) and the screening of inhibitors by in-capillary enzymatic microreactions
    • Iqbal J, Vollmayer P, Braun N et al (2005) A capillary electrophoresis method for the characterization of ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) and the screening of inhibitors by in-capillary enzymatic microreactions. Purinergic Signalling 1:349-358
    • (2005) Purinergic Signalling , vol.1 , pp. 349-358
    • Iqbal, J.1    Vollmayer, P.2    Braun, N.3
  • 112
    • 0345540629 scopus 로고    scopus 로고
    • Targeted disruption of cd39/ATP diphosphohydrolase results in disordered hemostasis and thromboregulation
    • Enjyoji K, Sévigny J, Lin Y et al (1999) Targeted disruption of cd39/ATP diphosphohydrolase results in disordered hemostasis and thromboregulation. Nat. Med 5:1010-1017
    • (1999) Nat Med , vol.5 , pp. 1010-1017
    • Enjyoji, K.1    Sévigny, J.2    Lin, Y.3
  • 113
    • 0034218231 scopus 로고    scopus 로고
    • CD39 modulates endothelial cell activation and apoptosis
    • Goepfert C, Imai M, Brouard S et al (2000) CD39 modulates endothelial cell activation and apoptosis. Mol Med 6:591-603
    • (2000) Mol Med , vol.6 , pp. 591-603
    • Goepfert, C.1    Imai, M.2    Brouard, S.3
  • 115
    • 11244333374 scopus 로고    scopus 로고
    • Regulation of P2Y 1 receptor-mediated signaling by the ectonucleoside triphosphate diphosphohydrolase isozymes NTPDase1 and NTPDase2
    • Alvarado-Castillo C, Harden TK, Boyer JL (2005) Regulation of P2Y 1 receptor-mediated signaling by the ectonucleoside triphosphate diphosphohydrolase isozymes NTPDase1 and NTPDase2. Mol Pharmacol 67:114-122
    • (2005) Mol Pharmacol , vol.67 , pp. 114-122
    • Alvarado-Castillo, C.1    Harden, T.K.2    Boyer, J.L.3
  • 116
    • 16344375453 scopus 로고    scopus 로고
    • Release and extracellular metabolism of ATP by ecto-nucleotidase eNTPDase 1-3 in hypothalamic and pituitary cells
    • He ML, Gonzales-Iglesias AE, Tomic M et al (2005) Release and extracellular metabolism of ATP by ecto-nucleotidase eNTPDase 1-3 in hypothalamic and pituitary cells. Purinergic Signalling 1:135-144
    • (2005) Purinergic Signalling , vol.1 , pp. 135-144
    • He, M.L.1    Gonzales-Iglesias, A.E.2    Tomic, M.3
  • 117
    • 20744441669 scopus 로고    scopus 로고
    • Portal fibroblasts regulate the proliferation of bile duct epithelia via expression of NTPDase2
    • Jhandier MN, Kruglov EA, Lavoie ÉG et al (2005) Portal fibroblasts regulate the proliferation of bile duct epithelia via expression of NTPDase2. J Biol Chem 280:22986-22992
    • (2005) J Biol Chem , vol.280 , pp. 22986-22992
    • Jhandier, M.N.1    Kruglov, E.A.2    Lavoie, É.G.3
  • 118
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • Anderson RGW (1998) The caveolae membrane system. Annu Rev Biochem 67:199-225
    • (1998) Annu Rev Biochem , vol.67 , pp. 199-225
    • Anderson, R.G.W.1
  • 121
  • 123
    • 33646799779 scopus 로고    scopus 로고
    • Ran BPM associates with CD39 and modulates ecto-nucleotidase activity
    • Epub ahead of print
    • Wu Y, Sun X, Kaczmarek E et al (2006) Ran BPM associates with CD39 and modulates ecto-nucleotidase activity. Biochem J, Epub ahead of print.
    • (2006) Biochem J
    • Wu, Y.1    Sun, X.2    Kaczmarek, E.3
  • 124
    • 0037183982 scopus 로고    scopus 로고
    • Activation of Ras/Erk pathway by a novel MET-interacting protein RanBPM
    • Wang DK, Li ZB, Messing EM et al (2002) Activation of Ras/Erk pathway by a novel MET-interacting protein RanBPM. J Biol Chem 277:36216-36222
    • (2002) J Biol Chem , vol.277 , pp. 36216-36222
    • Wang, D.K.1    Li, Z.B.2    Messing, E.M.3
  • 125
    • 33646760052 scopus 로고    scopus 로고
    • NTPDase1 interacts with RanBPM to directly modulate Ras activation and cellular proliferation in liver regeneration following partial hepatectomy
    • Wu Y, Sun X, Enjyoji K et al (2004) NTPDase1 interacts with RanBPM to directly modulate Ras activation and cellular proliferation in liver regeneration following partial hepatectomy. Hepatology 135:222
    • (2004) Hepatology , vol.135 , pp. 222
    • Wu, Y.1    Sun, X.2    Enjyoji, K.3
  • 127
    • 0030473797 scopus 로고    scopus 로고
    • PDZ domains bind carboxy-terminal sequences of target proteins
    • Saras J, Heldin CH (1996) PDZ domains bind carboxy-terminal sequences of target proteins. Trends Biochem Sci 21:455-458
    • (1996) Trends Biochem Sci , vol.21 , pp. 455-458
    • Saras, J.1    Heldin, C.H.2
  • 128
    • 0036876382 scopus 로고    scopus 로고
    • Signalling complex organization by PDZ domain proteins
    • Fan JS, Zhang M (2002) Signalling complex organization by PDZ domain proteins. NeuroSignals 11:315-321
    • (2002) NeuroSignals , vol.11 , pp. 315-321
    • Fan, J.S.1    Zhang, M.2
  • 129
    • 0037155199 scopus 로고    scopus 로고
    • PDZ domains: Structural modules for protein complex assembly
    • Hung AY, Sheng M (2002) PDZ domains: Structural modules for protein complex assembly. J Biol Chem 277:5699-5702
    • (2002) J Biol Chem , vol.277 , pp. 5699-5702
    • Hung, A.Y.1    Sheng, M.2
  • 130
    • 0030220611 scopus 로고    scopus 로고
    • P2X purinoceptor plethora
    • North RA (1996) P2X purinoceptor plethora. Semin Neurosci 8:187-194
    • (1996) Semin Neurosci , vol.8 , pp. 187-194
    • North, R.A.1
  • 131
    • 0034617279 scopus 로고    scopus 로고
    • ATP crossing the cell plasma membrane generates an ionic current in Xenopus oocytes
    • Bodas E, Aleu J, Pujol G et al (2000) ATP crossing the cell plasma membrane generates an ionic current in Xenopus oocytes. J Biol Chem 275:20268-20273
    • (2000) J Biol Chem , vol.275 , pp. 20268-20273
    • Bodas, E.1    Aleu, J.2    Pujol, G.3
  • 132
    • 0028970042 scopus 로고
    • Cell biology of atherosclerosis
    • Ross R (1995) Cell biology of atherosclerosis. Annu Rev Physiol 57:791-804
    • (1995) Annu Rev Physiol , vol.57 , pp. 791-804
    • Ross, R.1
  • 133
    • 0025838808 scopus 로고
    • Inhibition of platelet function by an aspirin-insensitive endothelial cell ADPase. Thromboregulation by endothelial cells
    • Marcus AJ, Safier LB, Hajjar KA et al (1991) Inhibition of platelet function by an aspirin-insensitive endothelial cell ADPase. Thromboregulation by endothelial cells. J Clin Invest 88:1690-1696
    • (1991) J Clin Invest , vol.88 , pp. 1690-1696
    • Marcus, A.J.1    Safier, L.B.2    Hajjar, K.A.3
  • 134
    • 0037381237 scopus 로고    scopus 로고
    • Metabolic control of excessive extracellular nucleotide accumulation by CD39/ecto-nucleotidase-1: Implications for ischemic vascular diseases
    • Marcus AJ, Broekman MJ, Drosopoulos JHF et al (2003) Metabolic control of excessive extracellular nucleotide accumulation by CD39/ ecto-nucleotidase-1: Implications for ischemic vascular diseases. J Pharmacol Exp Ther 305:9-16
    • (2003) J Pharmacol Exp Ther , vol.305 , pp. 9-16
    • Marcus, A.J.1    Broekman, M.J.2    Drosopoulos, J.H.F.3
  • 135
    • 0035910015 scopus 로고    scopus 로고
    • Disordered cellular migration and angiogenesis in cd39-null mice
    • Goepfert C, Sundberg C, Sévigny J et al (2001) Disordered cellular migration and angiogenesis in cd39-null mice. Circulation 104:3109-3115
    • (2001) Circulation , vol.104 , pp. 3109-3115
    • Goepfert, C.1    Sundberg, C.2    Sévigny, J.3
  • 136
    • 0043235654 scopus 로고    scopus 로고
    • Increased mitogenic and decreased contractile P2 receptors in smooth muscle cells by shear stress in human vessels with intact endothelium
    • Wang LW, Andersson M, Karlsson L et al (2003) Increased mitogenic and decreased contractile P2 receptors in smooth muscle cells by shear stress in human vessels with intact endothelium. Arterioscler Thromb Vasc Biol 23:1370-1376
    • (2003) Arterioscler Thromb Vasc Biol , vol.23 , pp. 1370-1376
    • Wang, L.W.1    Andersson, M.2    Karlsson, L.3
  • 137
    • 5344257562 scopus 로고    scopus 로고
    • 12 is expressed in vascular smooth muscle cells and stimulates contraction in human blood vessels
    • 12 is expressed in vascular smooth muscle cells and stimulates contraction in human blood vessels. Arterioscler Thromb Vasc Biol 24:1810-1815
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , pp. 1810-1815
    • Wihlborg, A.K.1    Wang, L.W.2    Braun, O.O.3
  • 138
    • 0033575280 scopus 로고    scopus 로고
    • CD39-L4 is a secreted human apyrase, specific for the hydrolysis of nucleoside diphosphates
    • Mulero JJ, Yeung G, Nelken ST et al (1999) CD39-L4 is a secreted human apyrase, specific for the hydrolysis of nucleoside diphosphates. J Biol Chem 29:20064-20067
    • (1999) J Biol Chem , vol.29 , pp. 20064-20067
    • Mulero, J.J.1    Yeung, G.2    Nelken, S.T.3
  • 139
    • 0000303572 scopus 로고    scopus 로고
    • Thromboregulatory potential of endothelial CD39/nucleoside triphosphate diphosphohydrolase: Modulation of purinergic signalling in platelets
    • Robson SC, Sévigny J, Imai M et al (2000) Thromboregulatory potential of endothelial CD39/nucleoside triphosphate diphosphohydrolase: Modulation of purinergic signalling in platelets. Emerg Ther Targets 4:155-171
    • (2000) Emerg Ther Targets , vol.4 , pp. 155-171
    • Robson, S.C.1    Sévigny, J.2    Imai, M.3
  • 140
    • 0035146418 scopus 로고    scopus 로고
    • Thromboregulation by endothelial cells: Significance for occlusive vascular diseases
    • Robson SC (2001) Thromboregulation by endothelial cells: Significance for occlusive vascular diseases. Arterioscler Thromb Vasc Biol 21:1251
    • (2001) Arterioscler Thromb Vasc Biol , vol.21 , pp. 1251
    • Robson, S.C.1
  • 141
    • 0027982162 scopus 로고
    • Integrins as dynamic regulators of vascular function
    • Luscinskas FW, Lawler J (1994) Integrins as dynamic regulators of vascular function. FASEB J 8:929-938
    • (1994) FASEB J , vol.8 , pp. 929-938
    • Luscinskas, F.W.1    Lawler, J.2
  • 143
    • 0032698162 scopus 로고    scopus 로고
    • 3: Inside-out, outside-in, and sideways
    • 3: Inside-out, outside-in, and sideways. Thromb Haemost 82:318-325
    • (1999) Thromb Haemost , vol.82 , pp. 318-325
    • Shattil, S.J.1
  • 144
    • 20144389797 scopus 로고    scopus 로고
    • Modulation of endothelial cell migration by extracellular nucleotides - Involvement of focal adhesion kinase and phosphatidylinositol 3-kinase-mediated pathways
    • Kaczmarek E, Erb L, Koziak K et al (2005) Modulation of endothelial cell migration by extracellular nucleotides - Involvement of focal adhesion kinase and phosphatidylinositol 3-kinase-mediated pathways. Thromb Haemost 93:735-742
    • (2005) Thromb Haemost , vol.93 , pp. 735-742
    • Kaczmarek, E.1    Erb, L.2    Koziak, K.3
  • 145
    • 5044241341 scopus 로고    scopus 로고
    • Integrin signalling
    • Giancotti F, Ruoslahti E (1999) Integrin signalling. Science 285:102-104
    • (1999) Science , vol.285 , pp. 102-104
    • Giancotti, F.1    Ruoslahti, E.2
  • 146
    • 0036121594 scopus 로고    scopus 로고
    • Elucidation of the thromboregulatory role of CD39/ectoapyrase in the ischemic brain
    • Pinsky DJ, Broekman MJ, Peschon JJ et al (2002) Elucidation of the thromboregulatory role of CD39/ectoapyrase in the ischemic brain. J Clin Invest 109:1031-1040
    • (2002) J Clin Invest , vol.109 , pp. 1031-1040
    • Pinsky, D.J.1    Broekman, M.J.2    Peschon, J.J.3
  • 147
    • 85047692190 scopus 로고    scopus 로고
    • Thromboregulatory manifestations in human CD39 transgenic mice and the implications for thrombotic disease and transplantation
    • Dwyer KM, Robson SC, Nandurkar HH et al (2004) Thromboregulatory manifestations in human CD39 transgenic mice and the implications for thrombotic disease and transplantation. J Clin Invest 113:1440-1446
    • (2004) J Clin Invest , vol.113 , pp. 1440-1446
    • Dwyer, K.M.1    Robson, S.C.2    Nandurkar, H.H.3
  • 148
    • 0034721480 scopus 로고    scopus 로고
    • Recombinant adenoviral mediated CD39 gene transfer prolongs cardiac xenograft survival
    • Imai M, Takigami K, Guckelberger O et al (2000) Recombinant adenoviral mediated CD39 gene transfer prolongs cardiac xenograft survival. Transplantation 70:864-870
    • (2000) Transplantation , vol.70 , pp. 864-870
    • Imai, M.1    Takigami, K.2    Guckelberger, O.3
  • 149
    • 0030475414 scopus 로고    scopus 로고
    • Apyrase administration prolongs discordant xenograft survival
    • Koyamada N, Miyatake T, Candinas D et al (1996) Apyrase administration prolongs discordant xenograft survival. Transplantation 62:1739-1743
    • (1996) Transplantation , vol.62 , pp. 1739-1743
    • Koyamada, N.1    Miyatake, T.2    Candinas, D.3
  • 150
    • 0029859062 scopus 로고    scopus 로고
    • Loss of rat glomerular ATP diphosphohydrolase activity during reperfusion injury is associated with oxidative stress reactions
    • Candinas D, Koyamada N, Miyatake T et al (1996) Loss of rat glomerular ATP diphosphohydrolase activity during reperfusion injury is associated with oxidative stress reactions. Thromb Haemost 76:807-812
    • (1996) Thromb Haemost , vol.76 , pp. 807-812
    • Candinas, D.1    Koyamada, N.2    Miyatake, T.3
  • 151
    • 1642281919 scopus 로고    scopus 로고
    • Beneficial effects of CD39/ecto-nucleoside triphosphate diphosphohydrolase-I in murine intestinal ischemia-reperfusion injury
    • Guckelberger O, Sun XF, Sévigny J et al (2004) Beneficial effects of CD39/ecto-nucleoside triphosphate diphosphohydrolase-I in murine intestinal ischemia-reperfusion injury. Thromb Haemost 91:576-586
    • (2004) Thromb Haemost , vol.91 , pp. 576-586
    • Guckelberger, O.1    Sun, X.F.2    Sévigny, J.3
  • 153
    • 0030270961 scopus 로고    scopus 로고
    • Pericytes in the microvasculature
    • Hirschi KK, Damore PA (1996) Pericytes in the microvasculature. Cardiovasc Res 32:687-698
    • (1996) Cardiovasc Res , vol.32 , pp. 687-698
    • Hirschi, K.K.1    Damore, P.A.2
  • 154
    • 1842407860 scopus 로고    scopus 로고
    • Vascular development-cellular and molecular regulation
    • Beck L, Damore PA (1997) Vascular development-cellular and molecular regulation. FASEB J 11:365-373
    • (1997) FASEB J , vol.11 , pp. 365-373
    • Beck, L.1    Damore, P.A.2
  • 155
    • 1842505718 scopus 로고    scopus 로고
    • In vitro verification of antithrombotic effect of recombinant soluble nucleotide triphosphate diphosphohydrolase 1
    • Sampram ES, Ouriel K (2004) In vitro verification of antithrombotic effect of recombinant soluble nucleotide triphosphate diphosphohydrolase 1. J Vasc Interv Radiol 15:379-384
    • (2004) J Vasc Interv Radiol , vol.15 , pp. 379-384
    • Sampram, E.S.1    Ouriel, K.2
  • 156
    • 13844296449 scopus 로고    scopus 로고
    • Relation of CD39 to plaque instability and thrombus formation in directional atherectomy specimens from patients with stable and unstable angina pectoris
    • Hatakeyama H, Hao H, Imamura T et al (2005) Relation of CD39 to plaque instability and thrombus formation in directional atherectomy specimens from patients with stable and unstable angina pectoris. Am J Cardiol 95:632-635
    • (2005) Am J Cardiol , vol.95 , pp. 632-635
    • Hatakeyama, H.1    Hao, H.2    Imamura, T.3
  • 157
    • 0025903550 scopus 로고
    • Expression, distribution, and biochemistry of human CD39: Role in activation-associatied homotypic adhesion of lymphocytes
    • Kansas GS, Wood GS, Tedder TF (1991) Expression, distribution, and biochemistry of human CD39: Role in activation-associatied homotypic adhesion of lymphocytes. J Immunol 146:2235-2244
    • (1991) J Immunol , vol.146 , pp. 2235-2244
    • Kansas, G.S.1    Wood, G.S.2    Tedder, T.F.3
  • 158
    • 0035451422 scopus 로고    scopus 로고
    • Monomorphic molecules function as additional recognition structures on haptenated target cells for HLA-A1-restricted, hapten-specific CTL
    • Stockl J, Majdic O, Fischer G et al (2001) Monomorphic molecules function as additional recognition structures on haptenated target cells for HLA-A1-restricted, hapten-specific CTL. J Immunol 167:2724-2733
    • (2001) J Immunol , vol.167 , pp. 2724-2733
    • Stockl, J.1    Majdic, O.2    Fischer, G.3
  • 159
    • 0032846934 scopus 로고    scopus 로고
    • Human monocyte derived dendritic cells express functional P2X and P2Y receptors as well as ecto-nucleotidases
    • Berchtold S, Ogilvie ALJ, Bogdan C et al (1999) Human monocyte derived dendritic cells express functional P2X and P2Y receptors as well as ecto-nucleotidases. FEBS Lett 458:424-428
    • (1999) FEBS Lett , vol.458 , pp. 424-428
    • Berchtold, S.1    Ogilvie, A.L.J.2    Bogdan, C.3
  • 160
    • 25844523991 scopus 로고    scopus 로고
    • Cell-surface enzymes in control of leukocyte trafficking
    • Salmi M, Jalkanen S (2005) Cell-surface enzymes in control of leukocyte trafficking. Nat Rev Immunol 5:760-771
    • (2005) Nat Rev Immunol , vol.5 , pp. 760-771
    • Salmi, M.1    Jalkanen, S.2
  • 161
    • 11944273124 scopus 로고    scopus 로고
    • + regulatory T cells: I. Phenotype and physiology
    • +regulatory T cells: I. Phenotype and physiology. APMIS 112:629-641
    • (2004) APMIS , vol.112 , pp. 629-641
    • Holm, T.1    Nielsson, J.2    Claesson, M.3
  • 162
    • 0036697257 scopus 로고    scopus 로고
    • Adenosine triphosphate release and purinergic regulation of cholangiocyte transport
    • Feranchak AP, Fitz JG (2002) Adenosine triphosphate release and purinergic regulation of cholangiocyte transport. Semin Liver Dis 22:251-262
    • (2002) Semin Liver Dis , vol.22 , pp. 251-262
    • Feranchak, A.P.1    Fitz, J.G.2
  • 163
    • 10644226074 scopus 로고    scopus 로고
    • Cell swelling-induced ATP release is tightly dependent on intracellular calcium elevations
    • Boudreault F, Grygorczyk R (2004) Cell swelling-induced ATP release is tightly dependent on intracellular calcium elevations. J Physiol London 561:499-513
    • (2004) J Physiol London , vol.561 , pp. 499-513
    • Boudreault, F.1    Grygorczyk, R.2
  • 164
    • 0037370966 scopus 로고    scopus 로고
    • Control of epithelial transport via luminal P2 receptors
    • Leipziger J (2003) Control of epithelial transport via luminal P2 receptors. Am J Physiol Renal Physiol 284:F419-F432
    • (2003) Am J Physiol Renal Physiol , vol.284
    • Leipziger, J.1
  • 165
    • 0037380778 scopus 로고    scopus 로고
    • Knock-out mice reveal tissue-specific roles of P2Y receptor subtypes in different epithelia
    • Dubyak GR (2003) Knock-out mice reveal tissue-specific roles of P2Y receptor subtypes in different epithelia. Mol Pharmacol 63:773-776
    • (2003) Mol Pharmacol , vol.63 , pp. 773-776
    • Dubyak, G.R.1
  • 166
    • 0024510031 scopus 로고
    • Characterization of purinoceptors present on human liver plasma membranes
    • Keppens S, VandeKerckhove J, De Wulf H (1989) Characterization of purinoceptors present on human liver plasma membranes. FEBS Lett 248:137-140
    • (1989) FEBS Lett , vol.248 , pp. 137-140
    • Keppens, S.1    VandeKerckhove, J.2    de Wulf, H.3
  • 167
    • 0027411196 scopus 로고
    • The complex interaction of ATP and UTP with isolated hepatocytes. How many receptors?
    • Keppens S (1993) The complex interaction of ATP and UTP with isolated hepatocytes. How many receptors? Gen Pharmacol 24:283-289
    • (1993) Gen Pharmacol , vol.24 , pp. 283-289
    • Keppens, S.1
  • 168
    • 0026767460 scopus 로고
    • A nucleoside transporter is functionally linked to ectonucleotidases in rat liver canalicular membrane
    • Che MX, Nishida T, Gatmaitan Z et al (1992) A nucleoside transporter is functionally linked to ectonucleotidases in rat liver canalicular membrane. J Biol Chem 267:9684-9688
    • (1992) J Biol Chem , vol.267 , pp. 9684-9688
    • Che, M.X.1    Nishida, T.2    Gatmaitan, Z.3
  • 170
    • 0030638506 scopus 로고    scopus 로고
    • Introduction - Transport across the hepatocyte canalicular membrane
    • Keppler D, Arias IM (1997) Introduction - Transport across the hepatocyte canalicular membrane. FASEB J 11:15-18
    • (1997) FASEB J , vol.11 , pp. 15-18
    • Keppler, D.1    Arias, I.M.2
  • 171
    • 0029815856 scopus 로고    scopus 로고
    • Isolated rat hepatocytes can signal to other hepatocytes and bile duct cells by release of nucleotides
    • Schlosser SF, Burgstahler AD, Nathanson JA (1996) Isolated rat hepatocytes can signal to other hepatocytes and bile duct cells by release of nucleotides. Proc Natl Acad Sci USA 93:9948-9953
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9948-9953
    • Schlosser, S.F.1    Burgstahler, A.D.2    Nathanson, J.A.3
  • 172
    • 1242314389 scopus 로고    scopus 로고
    • Extracellular ATP activates c- Jun N-terminal kinase signalling and cell cycle progression in hepatocytes
    • Thevananther S, Sun H, Li D et al (2004) Extracellular ATP activates c- Jun N-terminal kinase signalling and cell cycle progression in hepatocytes. Hepatology 39:393-402
    • (2004) Hepatology , vol.39 , pp. 393-402
    • Thevananther, S.1    Sun, H.2    Li, D.3
  • 173
    • 0030980919 scopus 로고    scopus 로고
    • Biochemical and molecular identification of distinct forms of alkaline phosphodiesterase I expressed on the apical and basolateral plasma membrane surfaces of rat hepatocytes
    • Scott LJ, Delautier D, Meerson NR et al (1997) Biochemical and molecular identification of distinct forms of alkaline phosphodiesterase I expressed on the apical and basolateral plasma membrane surfaces of rat hepatocytes. Hepatology 25:995-1002
    • (1999) Hepatology , vol.25 , pp. 995-1002
    • Scott, L.J.1    Delautier, D.2    Meerson, N.R.3
  • 174
    • 0031885056 scopus 로고    scopus 로고
    • Ecto-phosphodiesterase/pyrophosphatase of lymphocytes and non-lymphoid cells: Structure and function of the PC-1 family
    • Goding JW, Terkeltaub R, Maurice M et al (1998) Ecto-phosphodiesterase/ pyrophosphatase of lymphocytes and non-lymphoid cells: Structure and function of the PC-1 family. Immunol Rev 161:11-26
    • (1998) Immunol Rev , vol.161 , pp. 11-26
    • Goding, J.W.1    Terkeltaub, R.2    Maurice, M.3
  • 175
    • 0039765232 scopus 로고    scopus 로고
    • Identification and characterization of a novel hepatic canalicular ATP diphosphohydrolase
    • Séigny J, Robson SC, Waelkens E et al (2000) Identification and characterization of a novel hepatic canalicular ATP diphosphohydrolase. J Biol Chem 275:5640-5647
    • (2000) J Biol Chem , vol.275 , pp. 5640-5647
    • Sévigny, J.1    Robson, S.C.2    Waelkens, E.3
  • 176
    • 0036828987 scopus 로고    scopus 로고
    • The ecto-nucleoside triphosphate diphosphohydrolase NTPDase2/CD39L1 is expressed in a novel functional compartment within the liver
    • Dranoff JA, Kruglov EA, Robson SC et al (2002) The ecto-nucleoside triphosphate diphosphohydrolase NTPDase2/CD39L1 is expressed in a novel functional compartment within the liver. Hepatology 36:1135-1144
    • (2002) Hepatology , vol.36 , pp. 1135-1144
    • Dranoff, J.A.1    Kruglov, E.A.2    Robson, S.C.3
  • 177
    • 3242673389 scopus 로고    scopus 로고
    • Expression of P2Y nucleotide receptors and ectonucleotidases in quiescent and activated rat hepatic stellate cells
    • Dranoff JA, Ogawa M, Kruglov EA et al (2004) Expression of P2Y nucleotide receptors and ectonucleotidases in quiescent and activated rat hepatic stellate cells. Am J Physiol Gastrointest Liver Physiol 287:G417-G424
    • (2004) Am J Physiol Gastrointest Liver Physiol , vol.287
    • Dranoff, J.A.1    Ogawa, M.2    Kruglov, E.A.3
  • 178
    • 0032575263 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases
    • Smith TM, Kirley TL (1998) Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases. Biochim Biophys Acta 1386:65-78
    • (1998) Biochim Biophys Acta , vol.1386 , pp. 65-78
    • Smith, T.M.1    Kirley, T.L.2
  • 179
    • 0001307318 scopus 로고
    • The liver cell: Some new approaches to its study
    • Novikoff AB, Essner E (1960) The liver cell: Some new approaches to its study. Am J Med 29:102-131
    • (1960) Am J Med , vol.29 , pp. 102-131
    • Novikoff, A.B.1    Essner, E.2
  • 180
    • 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 I
    • Lin S-H, Guidotti G (1989) 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 I. J Biol Chem 264:14408-1414
    • (1989) J Biol Chem , vol.264 , pp. 14408-14414
    • Lin, S.-H.1    Guidotti, G.2
  • 182
    • 0028840189 scopus 로고
    • The rat liver 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 liver 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
  • 183
    • 0034658349 scopus 로고    scopus 로고
    • Identification, characterization, and immunolocalization of a nucleoside triphosphate diphosphohydrolase in pig liver
    • Leclerc MC, Grondin G, Gendron FP et al (2000) Identification, characterization, and immunolocalization of a nucleoside triphosphate diphosphohydrolase in pig liver. Arch Biochem Biophys 377:372-378
    • (2000) Arch Biochem Biophys , vol.377 , pp. 372-378
    • Leclerc, M.C.1    Grondin, G.2    Gendron, F.P.3
  • 184
    • 0032568833 scopus 로고    scopus 로고
    • Molecular cloning of the chicken oviduct ecto-ATP-diphosphohydrolase
    • Nagy AK, Knowles AF, Nagami GT (1998) Molecular cloning of the chicken
    • (1998) J Biol Chem , vol.273 , pp. 16043-16049
    • Nagy, A.K.1    Knowles, A.F.2    Nagami, G.T.3
  • 185
    • 0036094468 scopus 로고    scopus 로고
    • Purification, characterization, cloning, and expression of the chicken liver ecto-ATP-diphosphohydrolase
    • Knowles AF, Nagy AK, Strobel RS et al (2002) Purification, characterization, cloning, and expression of the chicken liver ecto-ATP-diphosphohydrolase. Eur J Biochem 269:2373-2382
    • (2002) Eur J Biochem , vol.269 , pp. 2373-2382
    • Knowles, A.F.1    Nagy, A.K.2    Strobel, R.S.3
  • 186
    • 0031020196 scopus 로고    scopus 로고
    • Ectonucleotidases, purine nucleoside transporter, and function of the bile canalicular plasma membrane of the hepatocyte
    • Che MX, Gatmaitan Z, Arias IM (1997) Ectonucleotidases, purine nucleoside transporter, and function of the bile canalicular plasma membrane of the hepatocyte. FASEB J 11:101-108
    • (1997) FASEB J , vol.11 , pp. 101-108
    • Che, M.X.1    Gatmaitan, Z.2    Arias, I.M.3
  • 187
    • 0009501259 scopus 로고
    • Dependence of bone marrow cells on the liver for purine salvage
    • Lajtha LG, Vane JR (1958) Dependence of bone marrow cells on the liver for purine salvage. Nature 182:191-192
    • (1958) Nature , vol.182 , pp. 191-192
    • Lajtha, L.G.1    Vane, J.R.2
  • 189
    • 0141758434 scopus 로고    scopus 로고
    • Rat pancreas secretes particulate ecto-nucleotidase CD39
    • Sorensen CE, Amstrup J, Rasmussen HN et al (2003) Rat pancreas secretes particulate ecto-nucleotidase CD39. J Physiol London 551:881-892
    • (2003) J Physiol London , vol.551 , pp. 881-892
    • Sorensen, C.E.1    Amstrup, J.2    Rasmussen, H.N.3
  • 190
    • 0018117271 scopus 로고
    • Characterization of (Mg,Ca)-ATPase activity in rat pancreatic plasma membranes
    • Lambert M, Christophe J (1978) Characterization of (Mg,Ca)-ATPase activity in rat pancreatic plasma membranes. Eur J Biochem 91:485-492
    • (1978) Eur J Biochem , vol.91 , pp. 485-492
    • Lambert, M.1    Christophe, J.2
  • 191
    • 0019136197 scopus 로고
    • Membrane adenosine triphosphatase activities in rat pancreas
    • Martin SS, Senior AE (1980) Membrane adenosine triphosphatase activities in rat pancreas. Biochim Biophys Acta 602:401-418
    • (1980) Biochim Biophys Acta , vol.602 , pp. 401-418
    • Martin, S.S.1    Senior, A.E.2
  • 192
    • 0019320639 scopus 로고
    • Characterization and purification of a calcium-sensitive ATP diphosphohydrolase from pig pancreas
    • LeBel D, Poirier GG, Phaneuf S et al (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
  • 194
    • 3042803608 scopus 로고
    • Localization and physiological role of the ATP-diphosphohydrolase in the pancreatic acinar cell
    • In: Ribet A, Pradayrol L, Susini C (eds) Elsevier, Elsevier
    • Beaudoin AR, Laliberté JF, LeBel D et al (1980) Localization and physiological role of the ATP-diphosphohydrolase in the pancreatic acinar cell. In: Ribet A, Pradayrol L, Susini C (eds) Biology of normal and cancerous exocrine pancreatic cells. Elsevier, Elsevier, pp 273-218
    • (1980) Biology of Normal and Cancerous Exocrine Pancreatic Cells , pp. 218-273
    • Beaudoin, A.R.1    Laliberté, J.F.2    LeBel, D.3
  • 195
    • 3042699600 scopus 로고    scopus 로고
    • Localization of nucleoside triphosphate diphosphohydrolase-1 (NTPDase1) and NTPDase2 in pancreas and salivary gland
    • Kittel A, Pelletier J, Bigonnesse F et al (2004) Localization of nucleoside triphosphate diphosphohydrolase-1 (NTPDase1) and NTPDase2 in pancreas and salivary gland. J Histochem Cytochem 52:861-871
    • (2004) J Histochem Cytochem , vol.52 , pp. 861-871
    • Kittel, A.1    Pelletier, J.2    Bigonnesse, F.3
  • 196
    • 3042813752 scopus 로고    scopus 로고
    • ATP and ATPase secretion by exocrine pancreas in rat, guinea pig, and human
    • Kordas KS, Sperlagh B, Tihanyi T et al (2004) ATP and ATPase secretion by exocrine pancreas in rat, guinea pig, and human. Pancreas 29:53-60
    • (2004) Pancreas , vol.29 , pp. 53-60
    • Kordas, K.S.1    Sperlagh, B.2    Tihanyi, T.3
  • 197
    • 0031677813 scopus 로고    scopus 로고
    • Demonstration and immunolocalization of ATP diphosphohydrolase in the pig digestive system
    • Sévigny J, Grondin G, Gendron FP et al (1998) Demonstration and immunolocalization of ATP diphosphohydrolase in the pig digestive system. Am J Physiol Gastrointest Liver Physiol 38:G473-G482
    • (1998) Am J Physiol Gastrointest Liver Physiol , vol.38
    • Sévigny, J.1    Grondin, G.2    Gendron, F.P.3
  • 198
    • 0037704152 scopus 로고    scopus 로고
    • Paracrine factors in tubuloglomerular feedback: Adenosine, ATP, and nitric oxide
    • Schnermann J, Levine DZ (2003) Paracrine factors in tubuloglomerular feedback: Adenosine, ATP, and nitric oxide. Annu Rev Physiol 65:501-529
    • (2003) Annu Rev Physiol , vol.65 , pp. 501-529
    • Schnermann, J.1    Levine, D.Z.2
  • 199
    • 18244393473 scopus 로고    scopus 로고
    • Renal cell-to-cell communication via extracellular ATP
    • Komlosi P, Fintha A, Bell PD (2005) Renal cell-to-cell communication via extracellular ATP. Physiology 20:86- 90
    • (2005) Physiology , vol.20
    • Komlosi, P.1    Fintha, A.2    Bell, P.D.3
  • 200
    • 20244376494 scopus 로고    scopus 로고
    • Expression of NTPDase1 and NTPDase2 in murine kidney: Relevance to regulation of P2 receptor signaling
    • Kishore BK, Isaac J, Fausther M et al (2005) Expression of NTPDase1 and NTPDase2 in murine kidney: Relevance to regulation of P2 receptor signaling. Am J Physiol Renal Physiol 288:F1032-F1043
    • (2005) Am J Physiol Renal Physiol , vol.288
    • Kishore, B.K.1    Isaac, J.2    Fausther, M.3
  • 201
    • 0033937869 scopus 로고    scopus 로고
    • Purification, characterization, and localization of an ATP diphosphohydrolase in porcine kidney
    • Lemmens R, Kupers L, Sévigny J et al (2000) Purification, characterization, and localization of an ATP diphosphohydrolase in porcine kidney. Am J Physiol Renal Physiol 278:F978-F988
    • (2000) Am J Physiol Renal Physiol , vol.278
    • Lemmens, R.1    Kupers, L.2    Sévigny, J.3
  • 202
  • 204
    • 4344693268 scopus 로고    scopus 로고
    • Glial modulation of synaptic transmission in culture
    • Araque A, Perea G (2004) Glial modulation of synaptic transmission in culture. Glia 47:241-248
    • (2004) Glia , vol.47 , pp. 241-248
    • Araque, A.1    Perea, G.2
  • 205
    • 24644473520 scopus 로고    scopus 로고
    • 2 nucleotide receptor function: Implications for proliferative and inflammatory pathways in astrocytes
    • 2 nucleotide receptor function: Implications for proliferative and inflammatory pathways in astrocytes. Mol Neurobiol 31:1-15
    • (2005) Mol Neurobiol , vol.31 , pp. 1-15
    • Weisman, G.A.1    Wang, M.2    Kong, Q.3
  • 206
    • 22244464662 scopus 로고    scopus 로고
    • ATP mediates rapid microglial response to local brain injury in vivo
    • Davalos D, Grutzendler J, Yang G et al (2005) ATP mediates rapid microglial response to local brain injury in vivo. Nat Neurosci 8:752-758
    • (2005) Nat Neurosci , vol.8 , pp. 752-758
    • Davalos, D.1    Grutzendler, J.2    Yang, G.3
  • 207
    • 0029560273 scopus 로고
    • Noradrenaline and ATP: Cotransmitters and neuromodulators
    • Burnstock G (1995) Noradrenaline and ATP: Cotransmitters and neuromodulators. J Physiol Pharmacol 365-384
    • (1995) J Physiol Pharmacol , pp. 365-384
    • Burnstock, G.1
  • 208
    • 1642421811 scopus 로고    scopus 로고
    • ATP is a key mediator of central and peripheral chemosensory transduction
    • Spyer KM, Dale N, Gourine AV (2004) ATP is a key mediator of central and peripheral chemosensory transduction. Exp Physiol 89:53-59
    • (2004) Exp Physiol , vol.89 , pp. 53-59
    • Spyer, K.M.1    Dale, N.2    Gourine, A.V.3
  • 209
    • 0034708818 scopus 로고    scopus 로고
    • Response of Schwann cells to action potentials in development
    • Stevens B, Fields RD (2000) Response of Schwann cells to action potentials in development. Science 287:2267-2271
    • (2000) Science , vol.287 , pp. 2267-2271
    • Stevens, B.1    Fields, R.D.2
  • 210
    • 0030875738 scopus 로고    scopus 로고
    • Adenine nucleotides undergo rapid, quantitative conversion to adenosine in the extracellular space in rat hippocampus
    • Dunwiddie TV, Diao LH, Proctor WR (1997) Adenine nucleotides undergo rapid, quantitative conversion to adenosine in the extracellular space in rat hippocampus. J Neurosci 17:7673-7682
    • (1997) J Neurosci , vol.17 , pp. 7673-7682
    • Dunwiddie, T.V.1    Diao, L.H.2    Proctor, W.R.3
  • 211
    • 0032521330 scopus 로고    scopus 로고
    • Inhibition by ATP of hippocampal synaptic transmission requires localized extracellular catabolism by ecto-nucleotidases into adenosine and channeling to adenosine A1 receptors
    • Cunha RA, Sebastiao AM, Ribeiro JA (1998) Inhibition by ATP of hippocampal synaptic transmission requires localized extracellular catabolism by ecto-nucleotidases into adenosine and channeling to adenosine A1 receptors. J Neurosci 18:1987-1995
    • (1998) J Neurosci , vol.18 , pp. 1987-1995
    • Cunha, R.A.1    Sebastiao, A.M.2    Ribeiro, J.A.3
  • 212
    • 1642463439 scopus 로고    scopus 로고
    • ATP- and adenosine-mediated signaling in the central nervous system: Synaptic purinoceptors: The stage for ATP to play its "dual-role"
    • Kato F, Kawamura M, Shigetomi E et al (2004) ATP- and adenosine-mediated signaling in the cTntral nervous system: Synaptic purinoceptors: the stage for ATP to play its "dual-role". J Pharmacol Sci 94:107-111
    • (2004) J Pharmacol Sci , vol.94 , pp. 107-111
    • Kato, F.1    Kawamura, M.2    Shigetomi, E.3
  • 213
    • 0032550212 scopus 로고    scopus 로고
    • Widespread expression of ecto-apyrase (CD39) in the central nervous system
    • Wang TF, Guidotti G (1998) Widespread expression of ecto-apyrase (CD39) in the central nervous system. Brain Res 790:318-322
    • (1998) Brain Res , vol.790 , pp. 318-322
    • Wang, T.F.1    Guidotti, G.2
  • 214
    • 0042928440 scopus 로고    scopus 로고
    • Purification and characterization of NTPDase1 (Ecto-apyrase) and NTPDase2 (Ecto-ATPase) from porcine brain cortex synaptosomes
    • Kukulski F, Komoszynski M (2003) Purification and characterization of NTPDase1 (Ecto-apyrase) and NTPDase2 (Ecto-ATPase) from porcine brain cortex synaptosomes. Eur J Biochem 270:3447-3454
    • (2003) Eur J Biochem , vol.270 , pp. 3447-3454
    • Kukulski, F.1    Komoszynski, M.2
  • 215
    • 9544221643 scopus 로고    scopus 로고
    • Comparative hydrolysis of extracellular adenine nucleotides and adenosine in synaptic membranes from porcine brain cortex, hippocampus, cerebellum and medulla oblongata
    • Kukulski F, Sévigny J, Komoszynski M (2004) Comparative hydrolysis of extracellular adenine nucleotides and adenosine in synaptic membranes from porcine brain cortex, hippocampus, cerebellum and medulla oblongata. Brain Res 1030:49-56
    • (2004) Brain Res , vol.1030 , pp. 49-56
    • Kukulski, F.1    Sévigny, J.2    Komoszynski, M.3
  • 216
    • 0002359246 scopus 로고    scopus 로고
    • Ecto-ATPases of the nervous system
    • In: Plesner L, Kirley TL, Knowles AF (eds) Plenum, New York
    • Nagy AK (1997) Ecto-ATPases of the nervous system. In: Plesner L, Kirley TL, Knowles AF (eds) Ecto-ATPases: Recent progress in structure and function. Plenum, New York, pp 1-13
    • (1997) Ecto-ATPases: Recent Progress in Structure and Function , pp. 1-13
    • Nagy, A.K.1
  • 217
    • 0027393389 scopus 로고
    • Production of adenosine from extracellular ATP at the striatal cholinergic synapse
    • James S, Richardson PJ (1993) Production of adenosine from extracellular ATP at the striatal cholinergic synapse. J Neurochem 60:219-227
    • (1993) J Neurochem , vol.60 , pp. 219-227
    • James, S.1    Richardson, P.J.2
  • 218
    • 0034753234 scopus 로고    scopus 로고
    • Regulation of the ecto-nucleotidase pathway in rat hippocampal nerve terminals
    • Cunha RA (2001) Regulation of the ecto-nucleotidase pathway in rat hippocampal nerve terminals. Neurochem Res 26:979-991
    • (2001) Neurochem Res , vol.26 , pp. 979-991
    • Cunha, R.A.1
  • 219
    • 31144457368 scopus 로고    scopus 로고
    • Immunolocalization of ecto-nucleoside triphosphate diphosphohydrolase 3 in rat brain: Implications for modulation of multiple homeostatic systems including feeding and sleep wake behaviors
    • Belcher SM, Zsarnovzky A, Crawford PA et al (2006) Immunolocalization of ecto-nucleoside triphosphate diphosphohydrolase 3 in rat brain: Implications for modulation of multiple homeostatic systems including feeding and sleep wake behaviors. Neuroscience 137: 1331-1346
    • (2006) Neuroscience , vol.137 , pp. 1331-1346
    • Belcher, S.M.1    Zsarnovzky, A.2    Crawford, P.A.3
  • 220
    • 0041707786 scopus 로고    scopus 로고
    • Extracellular adenine nucleotides metabolism in astrocyte cultures from different brain regions
    • Wink MR, Braganhol E, Tamajusuku ASK et al (2003) Extracellular adenine nucleotides metabolism in astrocyte cultures from different brain regions. Neurochem Int 43:621-628
    • (2003) Neurochem Int , vol.43 , pp. 621-628
    • Wink, M.R.1    Braganhol, E.2    Tamajusuku, A.S.K.3
  • 221
    • 0025940228 scopus 로고
    • Metabolism of extracellular adenine nucleotides by cultured rat brain astrocytes
    • Lai KM, Wong PCL (1991) Metabolism of extracellular adenine nucleotides by cultured rat brain astrocytes. J Neurochem 57:1510-1515
    • (1991) J Neurochem , vol.57 , pp. 1510-1515
    • Lai, K.M.1    Wong, P.C.L.2
  • 222
    • 0038029796 scopus 로고    scopus 로고
    • Expression of the ecto-ATPase NTPDase2 in the germinal zones of the developing and adult rat brain
    • Braun N, Sévigny J, Mishra S et al (2003) Expression of the ecto-ATPase NTPDase2 in the germinal zones of the developing and adult rat brain. Eur J Neurosci 17:1355-1364
    • (2003) Eur J Neurosci , vol.17 , pp. 1355-1364
    • Braun, N.1    Sévigny, J.2    Mishra, S.3
  • 223
    • 21244444660 scopus 로고    scopus 로고
    • Functional expression of the ecto-ATPase NTPDase2 and of nucleotide receptors by neuronal progenitor cells in the adult murine hippocampus
    • Shukla V, Zimmermann H, Wang L et al (2005) Functional expression of the ecto-ATPase NTPDase2 and of nucleotide receptors by neuronal progenitor cells in the adult murine hippocampus. J Neurosci Res 80:600-610
    • (2005) J Neurosci Res , vol.80 , pp. 600-610
    • Shukla, V.1    Zimmermann, H.2    Wang, L.3
  • 224
    • 1242271263 scopus 로고    scopus 로고
    • Localization of SNARE proteins and secretory organelle proteins in astrocytes in vitro and in situ
    • Wilhelm A, Volknandt W, Langer D et al (2004) Localization of SNARE proteins and secretory organelle proteins in astrocytes in vitro and in situ. Neurosci Res 48: 249-257
    • (2004) Neurosci Res , vol.48 , pp. 249-257
    • Wilhelm, A.1    Volknandt, W.2    Langer, D.3
  • 225
    • 0034842447 scopus 로고    scopus 로고
    • Microglial ectonucleotidases: Identification and functional roles
    • Braun N, Zimmermann H (2001) Microglial ectonucleotidases: Identification and functional roles. Drug Dev Res 53:208-217
    • (2001) Drug Dev Res , vol.53 , pp. 208-217
    • Braun, N.1    Zimmermann, H.2
  • 226
    • 0034515728 scopus 로고    scopus 로고
    • Assignment of ecto-nucleoside triphosphate diphosphohydrolase-1/cd39 expression to microglia and vasculature of the brain
    • Braun N, Sévigny J, Robson SC et al (2000) Assignment of ecto-nucleoside triphosphate diphosphohydrolase-1/cd39 expression to microglia and vasculature of the brain. Eur J Neurosci 12:4357-4366
    • (2000) Eur J Neurosci , vol.12 , pp. 4357-4366
    • Braun, N.1    Sévigny, J.2    Robson, S.C.3
  • 227
    • 0038643444 scopus 로고    scopus 로고
    • Astrocytes as stem cells: Nomenclature, phenotype and translation
    • Steindler DA, Laywell ED (2003) Astrocytes as stem cells: Nomenclature, phenotype and translation. Glia 43:62-69
    • (2003) Glia , vol.43 , pp. 62-69
    • Steindler, D.A.1    Laywell, E.D.2
  • 228
    • 33645105355 scopus 로고    scopus 로고
    • Extracellular nucleotide signaling in adult neural stem cells: Synergism with growth factor-mediated cellular proliferation
    • Mishra SK, Braun N, Shukla V et al (2006) Extracellular nucleotide signaling in adult neural stem cells: Synergism with growth factor-mediated cellular proliferation. Development 133: 675-684
    • (2006) Development , vol.133 , pp. 675-684
    • Mishra, S.K.1    Braun, N.2    Shukla, V.3
  • 229
    • 0034844594 scopus 로고    scopus 로고
    • Multiple ecto-nucleotidases in PC12 cells: Identification and cellular distribution after heterologous expression
    • Vollmayer P, Koch M, Braun N et al (2001) Multiple ecto-nucleotidases in PC12 cells: Identification and cellular distribution after heterologous expression. J Neurochem 78:1019-1028
    • (2001) J Neurochem , vol.78 , pp. 1019-1028
    • Vollmayer, P.1    Koch, M.2    Braun, N.3
  • 230
    • 18044396559 scopus 로고    scopus 로고
    • Ectonucleoside triphosphate diphosphohydrolase1/CD39, localized in neurons of human and porcine heart, modulates ATP-induced norepinephrine exocytosis
    • Machida T, Heerdt PM, Reid AC et al (2005) Ectonucleoside triphosphate diphosphohydrolase1/CD39, localized in neurons of human and porcine heart, modulates ATP-induced norepinephrine exocytosis. J Pharmacol Exp Ther 313:570-577
    • (2005) J Pharmacol Exp Ther , vol.313 , pp. 570-577
    • Machida, T.1    Heerdt, P.M.2    Reid, A.C.3
  • 231
    • 0036721467 scopus 로고    scopus 로고
    • Enzyme kinetics and pharmacological characterization of nucleotidases released from the guinea pig isolated vas deferens during nerve stimulation: Evidence for a soluble ecto-nucleoside triphosphate diphosphohydrolase-like ATPase and a soluble ecto-5′-nucleotidase-like AMPase
    • Mihaylova-Todorova ST, Todorov LD, Westfall DP (2002) Enzyme kinetics and pharmacological characterization of nucleotidases released from the guinea pig isolated vas deferens during nerve stimulation: Evidence for a soluble ecto-nucleoside triphosphate diphosphohydrolase-like ATPase and a soluble ecto-5′-nucleotidase-like AMPase. J Pharmacol Exp Ther 302:992-1001
    • (2002) J Pharmacol Exp Ther , vol.302 , pp. 992-1001
    • Mihaylova-Todorova, S.T.1    Todorov, L.D.2    Westfall, D.P.3
  • 232
    • 1042291303 scopus 로고    scopus 로고
    • Association of the ecto-ATPase NTPDase2 with glial cells of the peripheral nervous system
    • Braun N, Sévigny J, Robson SC et al (2004) Association of the ecto-ATPase NTPDase2 with glial cells of the peripheral nervous system. Glia 45:124-132
    • (2004) Glia , vol.45 , pp. 124-132
    • Braun, N.1    Sévigny, J.2    Robson, S.C.3
  • 233
    • 0030587104 scopus 로고    scopus 로고
    • Ectonucleotidase activity in the perilymphatic compartment of the guinea pig cochlea
    • Vlajkovic SM, Thorne PR, Munoz DJB et al (1996) Ectonucleotidase activity in the perilymphatic compartment of the guinea pig cochlea. Hear Res 99:31-37
    • (1996) Hear Res , vol.99 , pp. 31-37
    • Vlajkovic, S.M.1    Thorne, P.R.2    Munoz, D.J.B.3
  • 234
    • 0031892914 scopus 로고    scopus 로고
    • The pharmacology and kinetics of ecto-nucleotidases in the perilymphatic compartment of the guinea-pig cochlea
    • Vlajkovic SM, Thorne PR, Housley GD et al (1998) The pharmacology and kinetics of ecto-nucleotidases in the perilymphatic compartment of the guinea-pig cochlea. Hear Res 117:71-80
    • (1998) Hear Res , vol.117 , pp. 71-80
    • Vlajkovic, S.M.1    Thorne, P.R.2    Housley, G.D.3
  • 235
    • 0036696146 scopus 로고    scopus 로고
    • Distribution of ectonucleoside triphosphate diphosphohydrolases 1 and 2 in rat cochlea
    • Vlajkovic SM, Thorne PR, Sévigny J et al (2002) Distribution of ectonucleoside triphosphate diphosphohydrolases 1 and 2 in rat cochlea. Hear Res 170:127-138
    • (2002) Hear Res , vol.170 , pp. 127-138
    • Vlajkovic, S.M.1    Thorne, P.R.2    Sévigny, J.3
  • 236
    • 0036868211 scopus 로고    scopus 로고
    • NTPDase1 and NTPDase2 immunolocalization in mouse cochlea: Implications for regulation of P2 receptor signaling
    • Vlajkovic SM, Thorne PR, Sévigny J et al (2002) NTPDase1 and NTPDase2 immunolocalization in mouse cochlea: Implications for regulation of P2 receptor signaling. J Histochem Cytochem 50:1435-1441
    • (2002) J Histochem Cytochem , vol.50 , pp. 1435-1441
    • Vlajkovic, S.M.1    Thorne, P.R.2    Sévigny, J.3
  • 237
    • 2942585271 scopus 로고    scopus 로고
    • Noise exposure induces up-regulation of ecto-nucleoside triphosphate diphosphohydrolases 1 and 2 in rat cochlea
    • Vlajkovic SM, Housley GD, Munoz DJB et al (2004) Noise exposure induces up-regulation of ecto-nucleoside triphosphate diphosphohydrolases 1 and 2 in rat cochlea. Neuroscience 126:763-773
    • (2004) Neuroscience , vol.126 , pp. 763-773
    • Vlajkovic, S.M.1    Housley, G.D.2    Munoz, D.J.B.3
  • 238
    • 0033528777 scopus 로고    scopus 로고
    • 3 receptor immunoreactive nerves in rat taste buds
    • 3 receptor immunoreactive nerves in rat taste buds. Neuroreport 10:1107-1111
    • (1999) Neuroreport , vol.10 , pp. 1107-1111
    • Bo, X.N.1    Alavi, A.2    Xiang, Z.H.3
  • 241
    • 28544448048 scopus 로고    scopus 로고
    • ATP signaling is crucial for communication from taste buds to gustatory nerves
    • Finger TE, Danilova V, Barrows J et al (2005) ATP signaling is crucial for communication from taste buds to gustatory nerves. Science 310:1495-1499
    • (2005) Science , vol.310 , pp. 1495-1499
    • Finger, T.E.1    Danilova, V.2    Barrows, J.3
  • 242
    • 61449224264 scopus 로고    scopus 로고
    • Nucleoside triphosphate diphosphohydrolase-2 (NTPDase2) is the ecto-ATPase of taste buds
    • (in press)
    • Bartel DL, Sullivan SL, Lavoie ÉG et al (2006) Nucleoside triphosphate diphosphohydrolase-2 (NTPDase2) is the ecto-ATPase of taste buds. J Comp Neurol 499 (in press)
    • (2006) J Comp Neurol , pp. 499
    • Bartel, D.L.1    Sullivan, S.L.2    Lavoie, É.G.3
  • 243
    • 0032125217 scopus 로고    scopus 로고
    • Upregulation of the enzyme chain hydrolyzing extracellular ATP following transient forebrain ischemia in the rat
    • Braun N, Zhu Y, Krieglstein J et al (1998) Upregulation of the enzyme chain hydrolyzing extracellular ATP following transient forebrain ischemia in the rat. J Neurosci 18:4891-4900
    • (1998) J Neurosci , vol.18 , pp. 4891-4900
    • Braun, N.1    Zhu, Y.2    Krieglstein, J.3
  • 244
    • 0000521486 scopus 로고    scopus 로고
    • Nucleotide hydrolysis in rats submitted to global cerebral ischemia: A possible link between preconditioning and adenosine production
    • Schetinger MRC, Bonan CD, Schierholt R et al (1998) Nucleotide hydrolysis in rats submitted to global cerebral ischemia: A possible link between preconditioning and adenosine production. J Stroke Cerebrovasc Dis 7:281-286
    • (1998) J Stroke Cerebrovasc Dis , vol.7 , pp. 281-286
    • Schetinger, M.R.C.1    Bonan, C.D.2    Schierholt, R.3
  • 246
    • 17844385044 scopus 로고    scopus 로고
    • Pathophysiological roles of extracellular nucleotides in glial cells: Differential expression of purinergic receptors in resting and activated microglia
    • Bianco F, Fumagalli M, Pravettoni E et al (2005) Pathophysiological roles of extracellular nucleotides in glial cells: Differential expression of purinergic receptors in resting and activated microglia. Brain Res Rev 48:144-156
    • (2005) Brain Res Rev , vol.48 , pp. 144-156
    • Bianco, F.1    Fumagalli, M.2    Pravettoni, E.3
  • 247
    • 0033959173 scopus 로고    scopus 로고
    • Learning-specific decrease in synaptosomal ATP diphosphohydrolase activity from hippocampus and entorhinal cortex of adult rats
    • Bonan CD, Roesler R, Pereira GS et al (2000) Learning-specific decrease in synaptosomal ATP diphosphohydrolase activity from hippocampus and entorhinal cortex of adult rats. Brain Res 854:253-256
    • (2000) Brain Res , vol.854 , pp. 253-256
    • Bonan, C.D.1    Roesler, R.2    Pereira, G.S.3
  • 248
    • 0025149532 scopus 로고
    • Synaptosomal ATPase activities in temporal cortex and hippocampal formation of humans with focal epilepsy
    • Nagy AK, Houser CR, Delgado-Escueta AV (1990) Synaptosomal ATPase activities in temporal cortex and hippocampal formation of humans with focal epilepsy. Brain Res 529:192-201
    • (1990) Brain Res , vol.529 , pp. 192-201
    • Nagy, A.K.1    Houser, C.R.2    Delgado-Escueta, A.V.3
  • 249
    • 0030767799 scopus 로고    scopus 로고
    • Reduced cortical ecto-ATPase activity in rat brains during prolonged status epilepticus induced by sequential administration of lithium and pilocarpine
    • Nagy AK, Walton NY, Treiman DM (1997) Reduced cortical ecto-ATPase activity in rat brains during prolonged status epilepticus induced by sequential administration of lithium and pilocarpine. Mol Chem Neuropathol 31:135-147
    • (1997) Mol Chem Neuropathol , vol.31 , pp. 135-147
    • Nagy, A.K.1    Walton, N.Y.2    Treiman, D.M.3
  • 250
    • 0034087454 scopus 로고    scopus 로고
    • Changes in synaptosomal ectonucleotidase activities in two rat models of temporal lobe epilepsy
    • Bonan CD, Walz R, Pereira GS et al (2000) Changes in synaptosomal ectonucleotidase activities in two rat models of temporal lobe epilepsy. Epilepsy Res 39:229-238
    • (2000) Epilepsy Res , vol.39 , pp. 229-238
    • Bonan, C.D.1    Walz, R.2    Pereira, G.S.3
  • 251
    • 0033895263 scopus 로고    scopus 로고
    • Altered ATP hydrolysis induced by pentylenetetrazol kindling in rat brain synaptosomes
    • Bonan CD, Amaral OB, Rockenbach IC et al (2000) Altered ATP hydrolysis induced by pentylenetetrazol kindling in rat brain synaptosomes. Neurochem Res 25:775-779
    • (2000) Neurochem Res , vol.25 , pp. 775-779
    • Bonan, C.D.1    Amaral, O.B.2    Rockenbach, I.C.3
  • 252
    • 0038047531 scopus 로고    scopus 로고
    • Acute caffeine treatment increases extracellular nucleotide hydrolysis from rat striatal and hippocampal synaptosomes
    • Da Silva RS, Bruno AN, Battastini AMO et al (2003) Acute caffeine treatment increases extracellular nucleotide hydrolysis from rat striatal and hippocampal synaptosomes. Neurochem Res 28:1249-1254
    • (2003) Neurochem Res , vol.28 , pp. 1249-1254
    • da Silva, R.S.1    Bruno, A.N.2    Battastini, A.M.O.3
  • 253
    • 0032862590 scopus 로고    scopus 로고
    • Functional expression of a cDNA encoding a human ecto-ATPase
    • Mateo J, Harden TK, Boyer JL (1999) Functional expression of a cDNA encoding a human ecto-ATPase. Brit J Pharmacol 128:396-402
    • (1999) Brit J Pharmacol , vol.128 , pp. 396-402
    • Mateo, J.1    Harden, T.K.2    Boyer, J.L.3
  • 254
    • 0032079546 scopus 로고    scopus 로고
    • Golgi localization and functional expression of human uridine diphosphatase
    • Wang TF, Guidotti G (1998) Golgi localization and functional expression of human uridine diphosphatase. J Biol Chem 273:11392-1139
    • (1998) J Biol Chem , vol.273 , pp. 1139-11392
    • Wang, T.F.1    Guidotti, G.2
  • 255
    • 0034705522 scopus 로고    scopus 로고
    • First apyrase splice variants have different enzymatic properties
    • Biederbick A, Kosan C, Kunz J et al (2000) First apyrase splice variants have different enzymatic properties. J Biol Chem 275:19018-19024
    • (2000) J Biol Chem , vol.275 , pp. 19018-19024
    • Biederbick, A.1    Kosan, C.2    Kunz, J.3
  • 256
    • 0033564879 scopus 로고    scopus 로고
    • Glycoprotein reglycosylation and nucleotide sugar utilization in the secretory pathway: Identification of a nucleoside diphosphatase in the endoplasmic reticulum
    • Trombetta ES, Helenius A (1999) Glycoprotein reglycosylation and nucleotide sugar utilization in the secretory pathway: Identification of a nucleoside diphosphatase in the endoplasmic reticulum. EMBO J 18:3282-3292
    • (1999) EMBO J , vol.18 , pp. 3282-3292
    • Trombetta, E.S.1    Helenius, A.2
  • 257
    • 0035656529 scopus 로고    scopus 로고
    • Identity between the PCPH proto-oncogene and the CD39L4 (ENTPD5) ectonucleoside triphosphate diphosphohydrolase gen
    • Páez JG, Recio JA, Rouzaut A et al (2001) Identity between the PCPH proto-oncogene and the CD39L4 (ENTPD5) ectonucleoside triphosphate diphosphohydrolase gene. Int J Oncol 19:1249-1254
    • (2001) Int J Oncol , vol.19 , pp. 1249-1254
    • Páez, J.G.1    Recio, J.A.2    Rouzaut, A.3
  • 258
    • 0034711043 scopus 로고    scopus 로고
    • CD39L2, a gene encoding a human nucleoside diphosphatase, predominantly expresssed in the heart
    • Yeung G, Mulero JJ, McGowan DW et al (2000) CD39L2, a gene encoding a human nucleoside diphosphatase, predominantly expresssed in the heart. Biochemistry USA 39:12916-12923
    • (2000) Biochemistry USA , vol.39 , pp. 12916-12923
    • Yeung, G.1    Mulero, J.J.2    McGowan, D.W.3
  • 259
    • 0034602379 scopus 로고    scopus 로고
    • Expression and characterization of soluble and membrane-bound human nucleoside triphosphate diphosphohydrolase 6 (CD39L2)
    • Hicks-Berger CA, Chadwick BP, Frischauf AM et al (2000) Expression and characterization of soluble and membrane-bound human nucleoside triphosphate diphosphohydrolase 6 (CD39L2). J Biol Chem 275:34041-34045
    • (2000) J Biol Chem , vol.275 , pp. 34041-34045
    • Hicks-Berger, C.A.1    Chadwick, B.P.2    Frischauf, A.M.3
  • 260
    • 0034329660 scopus 로고    scopus 로고
    • Sequencing, functional expression and characterization of NTPDase6, a nucleoside diphosphatase and novel member of the ecto-nucleoside triphosphate diphosphohydrolase family
    • Braun N, Fengler S, Ebeling C et al (2000) Sequencing, functional expression and characterization of NTPDase6, a nucleoside diphosphatase and novel member of the ecto-nucleoside triphosphate diphosphohydrolase family. Biochem J 351:639-647
    • (2000) Biochem J , vol.351 , pp. 639-647
    • Braun, N.1    Fengler, S.2    Ebeling, C.3
  • 261
    • 0035907276 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel mammalian endo-apyrase (LALP1)
    • Shi JD, Kukar T, Wang CY et al (2001) Molecular cloning and characterization of a novel mammalian endo-apyrase (LALP1). J Biol Chem 276:17474-17478
    • (2001) J Biol Chem , vol.276 , pp. 17474-17478
    • Shi, J.D.1    Kukar, T.2    Wang, C.Y.3
  • 262
    • 0037184806 scopus 로고    scopus 로고
    • Prevention of autoimmune diabetes by FTY720 in nonobese diabetic mice
    • Maki T, Gottschalk R, Monaco AP (2002) Prevention of autoimmune diabetes by FTY720 in nonobese diabetic mice. Transplantation 74:1684-1686
    • (2002) Transplantation , vol.74 , pp. 1684-1686
    • Maki, T.1    Gottschalk, R.2    Monaco, A.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.