메뉴 건너뛰기




Volumn 29, Issue 11, 2005, Pages 1325-1333

CD39-associated high ATPase activity contribute to the loss of P2X7-mediated calcium response in LCL cells

Author keywords

ATPase activity; Calcium response; CD39; Epstein Barr virus; P2X7 receptor

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CALCIUM; CD39 ANTIGEN; PURINE P2X7 RECEPTOR; ADENOSINE TRIPHOSPHATE; APYRASE; DRUG DERIVATIVE; LEUKOCYTE ANTIGEN; PURINE P2 RECEPTOR;

EID: 24744462289     PISSN: 01452126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.leukres.2005.03.017     Document Type: Article
Times cited : (5)

References (37)
  • 1
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • R.A. North Molecular physiology of P2X receptors Physiol Rev 82 2002 1013 1067
    • (2002) Physiol Rev , vol.82 , pp. 1013-1067
    • North, R.A.1
  • 2
    • 0034999161 scopus 로고    scopus 로고
    • Regulation of P2X7 nucleotide receptor function in human monocytes by extracellular ions and receptor density
    • L. Gudipaty, B.D. Humpherys, G. Buell, and G.R. Dubyak Regulation of P2X7 nucleotide receptor function in human monocytes by extracellular ions and receptor density Am J Physiol Cell Physiol 280 2001 c943 c953
    • (2001) Am J Physiol Cell Physiol , vol.280
    • Gudipaty, L.1    Humpherys, B.D.2    Buell, G.3    Dubyak, G.R.4
  • 4
    • 0035883160 scopus 로고    scopus 로고
    • Neuronal P2X7 receptors are targeted to presynaptic terminals in the central and peripheral nervous systems
    • S.A. Deuchars, L. Atkinson, R.E. Brooke, H. Musa, C.J. Milligan, and T.F. Battern Neuronal P2X7 receptors are targeted to presynaptic terminals in the central and peripheral nervous systems J Neurosci 21 2001 7143 7152
    • (2001) J Neurosci , vol.21 , pp. 7143-7152
    • Deuchars, S.A.1    Atkinson, L.2    Brooke, R.E.3    Musa, H.4    Milligan, C.J.5    Battern, T.F.6
  • 5
    • 4744363912 scopus 로고    scopus 로고
    • Expression of P2X7 in human hematopoietic cell lines and leukemia patients
    • X.J. Zhang, G.G. Zheng, X.T. Ma, Y.H. Yang, G. Li, and Q. Rao Expression of P2X7 in human hematopoietic cell lines and leukemia patients Leukemia Res 28 2004 1313 1322
    • (2004) Leukemia Res , vol.28 , pp. 1313-1322
    • Zhang, X.J.1    Zheng, G.G.2    Ma, X.T.3    Yang, Y.H.4    Li, G.5    Rao, Q.6
  • 6
    • 0037072748 scopus 로고    scopus 로고
    • Epithelial membrane proteins induce membrane blebbing and interact with the P2X7 receptor C-terminus
    • H.L. Wilson, S.A. Wilson, A. Surprenant, and R.A. North Epithelial membrane proteins induce membrane blebbing and interact with the P2X7 receptor C-terminus J Biol Chem 277 2002 34017 34023
    • (2002) J Biol Chem , vol.277 , pp. 34017-34023
    • Wilson, H.L.1    Wilson, S.A.2    Surprenant, A.3    North, R.A.4
  • 7
    • 0037931836 scopus 로고    scopus 로고
    • An Ile-568 to Asn polymorphism prevents normal trafficking and function of the human P2X7 receptor
    • J.S. Wiley, L.P. Dao-Ung, C. Li, A.N. Shemon, B.J. Gu, and M.L. Smart An Ile-568 to Asn polymorphism prevents normal trafficking and function of the human P2X7 receptor J Biol Chem 278 2003 17108 17113
    • (2003) J Biol Chem , vol.278 , pp. 17108-17113
    • Wiley, J.S.1    Dao-Ung, L.P.2    Li, C.3    Shemon, A.N.4    Gu, B.J.5    Smart, M.L.6
  • 8
    • 0037196958 scopus 로고    scopus 로고
    • A loss-of-function polymorphic mutation in the cytolytic P2X7 receptor gene and chronic lymphocytic leukaemia: A molecular study
    • J.S. Wiley, L.P. Dao-Ung, B.J. Gu, R. Sluyter, A.N. Shemon, and C. Li A loss-of-function polymorphic mutation in the cytolytic P2X7 receptor gene and chronic lymphocytic leukaemia: a molecular study Lancet 359 2002 1114 1119
    • (2002) Lancet , vol.359 , pp. 1114-1119
    • Wiley, J.S.1    Dao-Ung, L.P.2    Gu, B.J.3    Sluyter, R.4    Shemon, A.N.5    Li, C.6
  • 9
    • 4544309949 scopus 로고    scopus 로고
    • An Arg307 to Gln polymorphism within the ATP-binding site causes loss of function of the human P2X7 receptor
    • B.J. Gu, R. Sluyter, K.K. Skarratt, A.N. Shemon, L.P. Dao-Ung, and S.J. Fuller An Arg307 to Gln polymorphism within the ATP-binding site causes loss of function of the human P2X7 receptor J Biol Chem 279 2004 31287 31295
    • (2004) J Biol Chem , vol.279 , pp. 31287-31295
    • Gu, B.J.1    Sluyter, R.2    Skarratt, K.K.3    Shemon, A.N.4    Dao-Ung, L.P.5    Fuller, S.J.6
  • 10
    • 3042757217 scopus 로고    scopus 로고
    • The mechanism of ATP release as an autocrine/paracrine molecule
    • T. Katsuragi, and K. Migita The mechanism of ATP release as an autocrine/paracrine molecule Nippon Yakurigaku Zasshi 123 2004 382 388
    • (2004) Nippon Yakurigaku Zasshi , vol.123 , pp. 382-388
    • Katsuragi, T.1    Migita, K.2
  • 11
    • 0036102125 scopus 로고    scopus 로고
    • CD39 is the dominant Langerhans cell-associated ecto-NTPDase: Modulatory roles in inflammation and immune responsiveness
    • N. Mizumoto, T. Kumamoto, S.C. Robson, J. Sevigny, H. Matsue, and K. Enjyoji CD39 is the dominant Langerhans cell-associated ecto-NTPDase: modulatory roles in inflammation and immune responsiveness Nat Med 8 2002 358 365
    • (2002) Nat Med , vol.8 , pp. 358-365
    • Mizumoto, N.1    Kumamoto, T.2    Robson, S.C.3    Sevigny, J.4    Matsue, H.5    Enjyoji, K.6
  • 12
    • 0029664401 scopus 로고    scopus 로고
    • CD39 is an ecto-apyrase
    • T.F. Wang, and G. Guidotti CD39 is an ecto-apyrase J Biol Chem 271 1996 9898 9901
    • (1996) J Biol Chem , vol.271 , pp. 9898-9901
    • Wang, T.F.1    Guidotti, G.2
  • 13
    • 0032753671 scopus 로고    scopus 로고
    • Analysis of CD39/ATP diphosphohydrolsae expression in endothelial cells, platelets and leukocytes
    • E. Koziak, J. Sevigny, S.C. Robson, J.B. Siegel, and E. Kaczmarek Analysis of CD39/ATP diphosphohydrolsae expression in endothelial cells, platelets and leukocytes Thromb Haemost 82 1999 1538 1544
    • (1999) Thromb Haemost , vol.82 , pp. 1538-1544
    • Koziak, E.1    Sevigny, J.2    Robson, S.C.3    Siegel, J.B.4    Kaczmarek, E.5
  • 14
    • 0034855050 scopus 로고    scopus 로고
    • Modulation of extracellular nucleotide-mediated signaling by CD39/nucleoside triphosphate diphosphohydrolase-1
    • S.C. Robson, K. Enjyoji, C. Goepfert, M. Imai, E. Kaczmarek, and Y. Lin Modulation of extracellular nucleotide-mediated signaling by CD39/nucleoside triphosphate diphosphohydrolase-1 Drug Dev Res 53 2001 193 207
    • (2001) Drug Dev Res , vol.53 , pp. 193-207
    • Robson, S.C.1    Enjyoji, K.2    Goepfert, C.3    Imai, M.4    Kaczmarek, E.5    Lin, Y.6
  • 15
    • 0024497851 scopus 로고
    • A phenotypic study of cell from Burkit lymphoma and EBV-B-lymphoblastoid lines and their relation to cells in normal lymphoid tissues
    • N.R. Ling, D. Hardie, L. Lowe, G.D. Jonson, M. Khan, and I.C. Maclennan A phenotypic study of cell from Burkit lymphoma and EBV-B-lymphoblastoid lines and their relation to cells in normal lymphoid tissues Int J Cancer 43 1989 112 118
    • (1989) Int J Cancer , vol.43 , pp. 112-118
    • Ling, N.R.1    Hardie, D.2    Lowe, L.3    Jonson, G.D.4    Khan, M.5    MacLennan, I.C.6
  • 16
    • 0028034865 scopus 로고
    • Enhancement of J6-1 human leukemic cell proliferation by cell-cell contact: Role of an M-CSF-like membrane-associated growth factor MAF-J6-1
    • K.F. Wu, Q. Rao, G.G. Zheng, Y.Q. Geng, M. Li, and J. Kong Enhancement of J6-1 human leukemic cell proliferation by cell-cell contact: Role of an M-CSF-like membrane-associated growth factor MAF-J6-1 Leukemia Res 18 1994 843 849
    • (1994) Leukemia Res , vol.18 , pp. 843-849
    • Wu, K.F.1    Rao, Q.2    Zheng, G.G.3    Geng, Y.Q.4    Li, M.5    Kong, J.6
  • 17
    • 0031960730 scopus 로고    scopus 로고
    • Enhancement of J6-1 human leukemic cell proliferation by membrane-bound M-CSF through a cell-cell contact mechanism II. Role of an M-CSF receptor-like membrane protein
    • K.F. Wu, Q. Rao, G.G. Zheng, Z.H. He, H.G. Ying, and Y.H. Song Enhancement of J6-1 human leukemic cell proliferation by membrane-bound M-CSF through a cell-cell contact mechanism II. Role of an M-CSF receptor-like membrane protein Leukemia Res 22 1998 55 60
    • (1998) Leukemia Res , vol.22 , pp. 55-60
    • Wu, K.F.1    Rao, Q.2    Zheng, G.G.3    He, Z.H.4    Ying, H.G.5    Song, Y.H.6
  • 18
    • 0033999678 scopus 로고    scopus 로고
    • Membrane-bound macrophage colony stimulating factor and its receptor play adhesion molecule-like role in leukemic cells
    • G.G. Zheng, Q. Rao, K.F. Wu, Z.H. He, and Y.Q. Geng Membrane-bound macrophage colony stimulating factor and its receptor play adhesion molecule-like role in leukemic cells Leukemia Res 24 2000 375 383
    • (2000) Leukemia Res , vol.24 , pp. 375-383
    • Zheng, G.G.1    Rao, Q.2    Wu, K.F.3    He, Z.H.4    Geng, Y.Q.5
  • 19
    • 0032479195 scopus 로고    scopus 로고
    • Ecto-ATP diphosphohydrolase/CD39 is overexpressed in differentiated human melanomas
    • K.N. Dzhandzhugazyan, A.F. Kirkin, P. thor Straten, and J. Zeuthen Ecto-ATP diphosphohydrolase/CD39 is overexpressed in differentiated human melanomas FEBS Lett 430 1998 227 230
    • (1998) FEBS Lett , vol.430 , pp. 227-230
    • Dzhandzhugazyan, K.N.1    Kirkin, A.F.2    Thor Straten, P.3    Zeuthen, J.4
  • 20
    • 0030668613 scopus 로고    scopus 로고
    • Demonstration of an extracellular ATP-binding site in NCAM: Functional implications of nucleotide binding
    • K. Dzhandzhugazyan, and E. Bock Demonstration of an extracellular ATP-binding site in NCAM: functional implications of nucleotide binding Biochemistry 36 1997 15381 15395
    • (1997) Biochemistry , vol.36 , pp. 15381-15395
    • Dzhandzhugazyan, K.1    Bock, E.2
  • 21
    • 0025177280 scopus 로고
    • Ecto-ATPase activity in cytolytic T-lymphocytes. Protection from the cytolytic effects of extracellular ATP
    • A. Filippini, R.E. Taffs, T. Agui, and M.V. Sitkovsky Ecto-ATPase activity in cytolytic T-lymphocytes. Protection from the cytolytic effects of extracellular ATP J Biol Chem 265 1990 334 340
    • (1990) J Biol Chem , vol.265 , pp. 334-340
    • Filippini, A.1    Taffs, R.E.2    Agui, T.3    Sitkovsky, M.V.4
  • 23
    • 0034599539 scopus 로고    scopus 로고
    • Synthesis of conformationally constrained analogues of KN-62, a potent antagonist of the P2X7-receptor
    • P.G. Baraldi, R. Romagnoli, M.A. Tabrizi, S. Falzoni, and F. di Virgilio Synthesis of conformationally constrained analogues of KN-62, a potent antagonist of the P2X7-receptor Bioorg Med Chem Lett 10 2000 681 684
    • (2000) Bioorg Med Chem Lett , vol.10 , pp. 681-684
    • Baraldi, P.G.1    Romagnoli, R.2    Tabrizi, M.A.3    Falzoni, S.4    Di Virgilio, F.5
  • 24
    • 0141925639 scopus 로고    scopus 로고
    • Increased vesicle recycling in response to osmotic cell swelling: Cause and consequence of hypotonicity-provoked ATP release
    • T. van der Wijk, S.F. Tomassen, A.B. Houtsmuller, H.R. de Jonge, and B.C. Tilly Increased vesicle recycling in response to osmotic cell swelling: cause and consequence of hypotonicity-provoked ATP release J Biol Chem 278 2003 40020 40025
    • (2003) J Biol Chem , vol.278 , pp. 40020-40025
    • Van Der Wijk, T.1    Tomassen, S.F.2    Houtsmuller, A.B.3    De Jonge, H.R.4    Tilly, B.C.5
  • 25
    • 0032577474 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane regulator-independent release of ATP: Its implications for the regulation of P2Y2 receptors in airway epithelial
    • W.C. Watt, E.R. Lazarowski, and R.C. Boucher Cystic fibrosis transmembrane regulator-independent release of ATP: its implications for the regulation of P2Y2 receptors in airway epithelial J Biol Chem 273 1998 14053 14058
    • (1998) J Biol Chem , vol.273 , pp. 14053-14058
    • Watt, W.C.1    Lazarowski, E.R.2    Boucher, R.C.3
  • 26
    • 0037593535 scopus 로고    scopus 로고
    • Colocalization of ATP release sites and ecto-ATPase activity at the extracellular surface of human astrocytes
    • S.M. Joseph, M.R. Buchakjian, and G.R. Dubyak Colocalization of ATP release sites and ecto-ATPase activity at the extracellular surface of human astrocytes J Biol Chem 278 2003 23331 23342
    • (2003) J Biol Chem , vol.278 , pp. 23331-23342
    • Joseph, S.M.1    Buchakjian, M.R.2    Dubyak, G.R.3
  • 27
    • 0029664380 scopus 로고    scopus 로고
    • Hydrolysis of P2-purinoceptor agonists by a purified ectonucleotidase from the bovine aorta, the ATP-diphosphohydrolase
    • M. Picher, J. Sevigny, P. D'Orleans-Juste, and A.R. Beaudoin Hydrolysis of P2-purinoceptor agonists by a purified ectonucleotidase from the bovine aorta, the ATP-diphosphohydrolase Biochem Pharmacol 51 11 1996 1453 1460
    • (1996) Biochem Pharmacol , vol.51 , Issue.11 , pp. 1453-1460
    • Picher, M.1    Sevigny, J.2    D'Orleans-Juste, P.3    Beaudoin, A.R.4
  • 28
    • 0033198604 scopus 로고    scopus 로고
    • Two different ionotropic receptors are activated by ATP in rat microglia
    • S. Visentin, M. Renzi, C. Frank, A. Greco, and G. Levi Two different ionotropic receptors are activated by ATP in rat microglia J Physiol 519 Pt 3 1999 723 736
    • (1999) J Physiol , vol.519 , Issue.PART 3 , pp. 723-736
    • Visentin, S.1    Renzi, M.2    Frank, C.3    Greco, A.4    Levi, G.5
  • 29
    • 0041845127 scopus 로고    scopus 로고
    • Mutation of a dibasic amino acid motif within the C terminus of the P2X7 nucleotide receptor results in trafficking defects and impaired function
    • L.C. Denlinger, J.A. Sommer, K. Parker, L. Gudipaty, P.L. Fisette, and J.W. Watters Mutation of a dibasic amino acid motif within the C terminus of the P2X7 nucleotide receptor results in trafficking defects and impaired function J Immunol 171 2003 1304 1311
    • (2003) J Immunol , vol.171 , pp. 1304-1311
    • Denlinger, L.C.1    Sommer, J.A.2    Parker, K.3    Gudipaty, L.4    Fisette, P.L.5    Watters, J.W.6
  • 30
    • 0037424417 scopus 로고    scopus 로고
    • P2X7 receptor cell surface expression and cytolitic pore formation are regulated by a distal C-terminal region
    • M.L. Smart, B. Gu, R.G. Panchal, J. Wiley, B. Cromer, and D.A. Williams P2X7 receptor cell surface expression and cytolitic pore formation are regulated by a distal C-terminal region J Biol Chem 278 2003 8853 8860
    • (2003) J Biol Chem , vol.278 , pp. 8853-8860
    • Smart, M.L.1    Gu, B.2    Panchal, R.G.3    Wiley, J.4    Cromer, B.5    Williams, D.A.6
  • 31
    • 4744352568 scopus 로고    scopus 로고
    • Involvement of multiple P2Y receptors and signaling pathways in the action of adenine nucleotides diphosphates on human monocyte-derived dendritic cells
    • F. Marteau, D. Communi, J.M. Boeynaems, and N. Suarez-Gonzalez Involvement of multiple P2Y receptors and signaling pathways in the action of adenine nucleotides diphosphates on human monocyte-derived dendritic cells J Leukoc Biol 76 2004 796 803
    • (2004) J Leukoc Biol , vol.76 , pp. 796-803
    • Marteau, F.1    Communi, D.2    Boeynaems, J.M.3    Suarez-Gonzalez, N.4
  • 32
    • 0025177280 scopus 로고
    • Ecto-ATPase activity in cytolytic T-lymphocytes. Protection from the cytolytic effects of extracellular ATP
    • A. Filippini, R.E. Taffs, T. Agui, and M.V. Sitkovsky Ecto-ATPase activity in cytolytic T-lymphocytes. Protection from the cytolytic effects of extracellular ATP J Biol Chem 265 1990 334 340
    • (1990) J Biol Chem , vol.265 , pp. 334-340
    • Filippini, A.1    Taffs, R.E.2    Agui, T.3    Sitkovsky, M.V.4
  • 34
    • 0035669827 scopus 로고    scopus 로고
    • Inhibition of platelet recruitment by endothelial cell CD39/ecto-ADPase: Significance for occlusive vascular diseases
    • A.J. Marcus, M.J. Broekman, J.H. Drosopoulos, D.J. Pinsky, N. Islam, and C.R. Maliszewsk Inhibition of platelet recruitment by endothelial cell CD39/ecto-ADPase: significance for occlusive vascular diseases Ital Heart J 2 2001 824 830
    • (2001) Ital Heart J , vol.2 , pp. 824-830
    • Marcus, A.J.1    Broekman, M.J.2    Drosopoulos, J.H.3    Pinsky, D.J.4    Islam, N.5    Maliszewsk, C.R.6
  • 36
    • 0142188258 scopus 로고    scopus 로고
    • NAD-induced T cell death: ADP-ribosylation of cell surface proteins by ART2 activates the cytolytic P2X7 purinoceptor
    • M. Seman, S. Adriouch, F. Scheuplein, C. Krebs, D. Freese, and G. Glowacki NAD-induced T cell death: ADP-ribosylation of cell surface proteins by ART2 activates the cytolytic P2X7 purinoceptor Immunity 19 2003 571 582
    • (2003) Immunity , vol.19 , pp. 571-582
    • Seman, M.1    Adriouch, S.2    Scheuplein, F.3    Krebs, C.4    Freese, D.5    Glowacki, G.6
  • 37
    • 51249161806 scopus 로고
    • Characterization of a human herpes virus-6 (HHV-6) and Epstein-Barr virus (EBV) associated leukemic cell line, J6-1
    • K.F. Wu, J. Luka, S.S. Joshi, S.J. Pirruccello, A. Masih, and J.G. Sharp Characterization of a human herpes virus-6 (HHV-6) and Epstein-Barr virus (EBV) associated leukemic cell line, J6-1 Chin J Cancer Res 6 1994 157 168
    • (1994) Chin J Cancer Res , vol.6 , pp. 157-168
    • Wu, K.F.1    Luka, J.2    Joshi, S.S.3    Pirruccello, S.J.4    Masih, A.5    Sharp, J.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.