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Volumn 208, Issue 9, 2011, Pages 1823-1834

Extracellular ATP acts on P2Y2 purinergic receptors to facilitate HIV-1 infection

(32)  Séror, Claire a,c,d   Melki, Marie Thérèse e   Subra, Frédéric f   Raza, Syed Qasim a,c,d   Bras, Marlène e   Saïdi, Héla e   Nardacci, Roberta g   Voisin, Laurent a,c,d   Paoletti, Audrey a,c,d   Law, Frédéric a,c,d   Martins, Isabelle a,c,d   Amendola, Alessandra g   Abdul Sater, Ali A h   Ciccosanti, Fabiola g   Delelis, Olivier f   Niedergang, Florence j,k,l   Thierry, Sylvain f   Said Sadier, Najwane h   Lamaze, Christophe m   Métivier, Didier a,c,d   more..

a INSERM   (France)

Author keywords

[No Author keywords available]

Indexed keywords

4 ACETAMIDO 4' ISOTHIOCYANATOSTILBENE 2,2' DISULFONIC ACID; 4,4' DIISOTHIOCYANATOSTILBENE 2,2' DISULFONIC ACID; ADENOSINE TRIPHOSPHATE; ANTIRETROVIRUS AGENT; APYRASE; CARBENOXOLONE; CD4 ANTIGEN; CELL RECEPTOR; COMPLEMENTARY DNA; ENVELOPE PROTEIN; FOCAL ADHESION KINASE 2; PLERIXAFOR; PURINERGIC P2Y2 RECEPTOR; PYRIDOXAL PHOSPHATE 6 AZOPHENYL 2',4' DISULFONIC ACID; SHORT HAIRPIN RNA; SMALL INTERFERING RNA; SURAMIN; VIRUS RNA; GAP JUNCTION PROTEIN; NERVE PROTEIN; PANX1 PROTEIN, HUMAN;

EID: 80054840705     PISSN: 00221007     EISSN: 15409538     Source Type: Journal    
DOI: 10.1084/jem.20101805     Document Type: Article
Times cited : (146)

References (51)
  • 4
    • 4143127920 scopus 로고    scopus 로고
    • Pannexin membrane channels are mechanosensitive conduits for ATP
    • Bao, L., S. Locovei, and G. Dahl. 2004. Pannexin membrane channels are mechanosensitive conduits for ATP. FEBS Lett. 572:65-68.
    • (2004) FEBS Lett , vol.572 , pp. 65-68
    • Bao, L.1    Locovei, S.2    Dahl, G.3
  • 5
    • 77951608957 scopus 로고    scopus 로고
    • Pyk2 activation triggers epidermal growth factor receptor signaling and cell motility after wounding sheets of epithelial cells
    • Block, E.R., M.A. Tolino, and J.K. Klarlund. 2010. Pyk2 activation triggers epidermal growth factor receptor signaling and cell motility after wounding sheets of epithelial cells. J. Biol. Chem. 285:13372-13379.
    • (2010) J. Biol. Chem. , vol.285 , pp. 13372-13379
    • Block, E.R.1    Tolino, M.A.2    Klarlund, J.K.3
  • 7
    • 77951638914 scopus 로고    scopus 로고
    • Basal release of ATP: an autocrine-paracrine mechanism for cell regulation
    • re1
    • Corriden, R., and P.A. Insel. 2010. Basal release of ATP: an autocrine-paracrine mechanism for cell regulation. Sci. Signal. 3:re1.
    • (2010) Sci. Signal. , vol.3
    • Corriden, R.1    Insel, P.A.2
  • 10
  • 12
    • 1142286425 scopus 로고    scopus 로고
    • Charged polymers modulate retrovirus transduction via membrane charge neutralization and virus aggregation
    • Davis, H.E., M. Rosinski, J.R. Morgan, and M.L. Yarmush. 2004. Charged polymers modulate retrovirus transduction via membrane charge neutralization and virus aggregation. Biophys. J. 86:1234-1242.
    • (2004) Biophys. J. , vol.86 , pp. 1234-1242
    • Davis, H.E.1    Rosinski, M.2    Morgan, J.R.3    Yarmush, M.L.4
  • 13
    • 62149093020 scopus 로고    scopus 로고
    • The G140S mutation in HIV integrases from raltegravir-resistant patients rescues catalytic defect due to the resistance Q148H mutation
    • Delelis, O., I. Malet, L. Na, L. Tchertanov, V. Calvez, A.G. Marcelin, F. Subra, E. Deprez, and J.F. Mouscadet. 2009. The G140S mutation in HIV integrases from raltegravir-resistant patients rescues catalytic defect due to the resistance Q148H mutation. Nucleic Acids Res. 37:1193-1201.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1193-1201
    • Delelis, O.1    Malet, I.2    Na, L.3    Tchertanov, L.4    Calvez, V.5    Marcelin, A.G.6    Subra, F.7    Deprez, E.8    Mouscadet, J.F.9
  • 14
    • 0030002637 scopus 로고    scopus 로고
    • HIV- 1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng, Y., C.C. Broder, P.E. Kennedy, and E.A. Berger. 1996. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science. 272:872-877.
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 15
    • 0035139983 scopus 로고    scopus 로고
    • Danger signals: SOS to the immune system
    • Gallucci, S., and P. Matzinger. 2001. Danger signals: SOS to the immune system. Curr. Opin. Immunol. 13:114-119.
    • (2001) Curr. Opin. Immunol. , vol.13 , pp. 114-119
    • Gallucci, S.1    Matzinger, P.2
  • 17
    • 0035398022 scopus 로고    scopus 로고
    • Toxicity, efficacy, and pharmacology of suramin in adults with recurrent high-grade gliomas
    • New Approaches to Brain Tumor Therapy CNS. Consortium
    • Grossman, S.A., S. Phuphanich, G. Lesser, J. Rozental, L.B. Grochow, J. Fisher, and S. Piantadosi; New Approaches to Brain Tumor Therapy CNS Consortium. 2001. Toxicity, efficacy, and pharmacology of suramin in adults with recurrent high-grade gliomas. J. Clin. Oncol. 19:3260-3266.
    • (2001) J. Clin. Oncol. , vol.19 , pp. 3260-3266
    • Grossman, S.A.1    Phuphanich, S.2    Lesser, G.3    Rozental, J.4    Grochow, L.B.5    Fisher, J.6    Piantadosi, S.7
  • 18
    • 77949409948 scopus 로고    scopus 로고
    • Targeting early infection to prevent HIV-1 mucosal transmission
    • Haase, A.T. 2010. Targeting early infection to prevent HIV-1 mucosal transmission. Nature. 464:217-223.
    • (2010) Nature , vol.464 , pp. 217-223
    • Haase, A.T.1
  • 19
    • 50949123789 scopus 로고    scopus 로고
    • Induction of the Galpha(q) signaling cascade by the human immunodeficiency virus envelope is required for virus entry
    • Harmon, B., and L. Ratner. 2008. Induction of the Galpha(q) signaling cascade by the human immunodeficiency virus envelope is required for virus entry. J. Virol. 82:9191-9205.
    • (2008) J. Virol. , vol.82 , pp. 9191-9205
    • Harmon, B.1    Ratner, L.2
  • 20
    • 42249114677 scopus 로고    scopus 로고
    • OppA, the ecto-ATPase of Mycoplasma hominis induces ATP release and cell death in HeLa cells
    • Hopfe, M., and B. Henrich. 2008. OppA, the ecto-ATPase of Mycoplasma hominis induces ATP release and cell death in HeLa cells. BMC Microbiol. 8:55.
    • (2008) BMC Microbiol , vol.8 , pp. 55
    • Hopfe, M.1    Henrich, B.2
  • 24
    • 37049018852 scopus 로고    scopus 로고
    • Adhesion molecule interactions facilitate human immunodeficiency virus type 1-induced virological synapse formation between T cells
    • Jolly, C., I. Mitar, and Q.J. Sattentau. 2007. Adhesion molecule interactions facilitate human immunodeficiency virus type 1-induced virological synapse formation between T cells. J. Virol. 81:13916-13921.
    • (2007) J. Virol. , vol.81 , pp. 13916-13921
    • Jolly, C.1    Mitar, I.2    Sattentau, Q.J.3
  • 25
    • 0038312107 scopus 로고    scopus 로고
    • Flavonoids -novel lead compounds for the development of P2Y2 receptor antagonists
    • Kaulich, M., F. Streicher, R. Mayer, I. Müller, and C.E. Müller. 2003. Flavonoids - novel lead compounds for the development of P2Y2 receptor antagonists. Drug Dev. Res. 59:72-81.
    • (2003) Drug Dev. Res. , vol.59 , pp. 72-81
    • Kaulich, M.1    Streicher, F.2    Mayer, R.3    Müller, I.4    Müller, C.E.5
  • 26
    • 33746701380 scopus 로고    scopus 로고
    • P2X receptors as cell-surface ATP sensors in health and disease
    • Khakh, B.S., and R.A. North. 2006. P2X receptors as cell-surface ATP sensors in health and disease. Nature. 442:527-532.
    • (2006) Nature , vol.442 , pp. 527-532
    • Khakh, B.S.1    North, R.A.2
  • 28
    • 0030840444 scopus 로고    scopus 로고
    • ATP- induced killing of mycobacteria by human macrophages is mediated by purinergic P2Z(P2X7) receptors
    • Lammas, D.A., C. Stober, C.J. Harvey, N. Kendrick, S. Panchalingam, and D.S. Kumararatne. 1997. ATP-induced killing of mycobacteria by human macrophages is mediated by purinergic P2Z(P2X7) receptors. Immunity. 7:433-444.
    • (1997) Immunity , vol.7 , pp. 433-444
    • Lammas, D.A.1    Stober, C.2    Harvey, C.J.3    Kendrick, N.4    Panchalingam, S.5    Kumararatne, D.S.6
  • 29
    • 0036644013 scopus 로고    scopus 로고
    • Multiparametric flow cytometric analysis of biochemical and functional events associated with apoptosis and oncosis using the 7-aminoactinomycin D assay
    • Lecoeur, H., L.M. de Oliveira-Pinto, and M.L. Gougeon. 2002. Multiparametric flow cytometric analysis of biochemical and functional events associated with apoptosis and oncosis using the 7-aminoactinomycin D assay. J. Immunol. Methods. 265:81-96.
    • (2002) J. Immunol. Methods. , vol.265 , pp. 81-96
    • Lecoeur, H.1    de Oliveira-Pinto, L.M.2    Gougeon, M.L.3
  • 31
    • 10744232199 scopus 로고    scopus 로고
    • Src homology 3 binding sites in the P2Y2 nucleotide receptor interact with Src and regulate activities of Src, proline-rich tyrosine kinase 2, and growth factor receptors
    • Liu, J., Z. Liao, J. Camden, K.D. Griffin, R.C. Garrad, L.I. Santiago-Pérez, F.A. González, C.I. Seye, G.A. Weisman, and L. Erb. 2004. Src homology 3 binding sites in the P2Y2 nucleotide receptor interact with Src and regulate activities of Src, proline-rich tyrosine kinase 2, and growth factor receptors. J. Biol. Chem. 279:8212-8218.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8212-8218
    • Liu, J.1    Liao, Z.2    Camden, J.3    Griffin, K.D.4    Garrad, R.C.5    Santiago-Pérez, L.I.6    González, F.A.7    Seye, C.I.8    Weisman, G.A.9    Erb, L.10
  • 34
    • 59849107898 scopus 로고    scopus 로고
    • Common principles and intermediates of viral proteinmediated fusion: the HIV-1 paradigm
    • Melikyan, G.B. 2008. Common principles and intermediates of viral proteinmediated fusion: the HIV-1 paradigm. Retrovirology. 5:111.
    • (2008) Retrovirology , vol.5 , pp. 111
    • Melikyan, G.B.1
  • 35
    • 77954044097 scopus 로고    scopus 로고
    • Escape of HIV-1-infected dendritic cells from TRAIL-mediated NK cell cytotoxicity during NK-DC cross-talk-a pivotal role of HMGB1
    • Melki, M.T., H. Saïdi, A. Dufour, J.C. Olivo-Marin, and M.L. Gougeon. 2010. Escape of HIV-1-infected dendritic cells from TRAIL-mediated NK cell cytotoxicity during NK-DC cross-talk-a pivotal role of HMGB1. PLoS Pathog. 6:e1000862.
    • (2010) PLoS Pathog , vol.6
    • Melki, M.T.1    Saïdi, H.2    Dufour, A.3    Olivo-Marin, J.C.4    Gougeon, M.L.5
  • 40
    • 0031754497 scopus 로고    scopus 로고
    • Receptors for purines and pyrimidines
    • Ralevic, V., and G. Burnstock. 1998. Receptors for purines and pyrimidines. Pharmacol. Rev. 50:413-492.
    • (1998) Pharmacol. Rev. , vol.50 , pp. 413-492
    • Ralevic, V.1    Burnstock, G.2
  • 42
    • 56349127521 scopus 로고    scopus 로고
    • HMGB1-dependent triggering of HIV-1 replication and persistence in dendritic cells as a consequence of NK-DC cross-talk
    • Saïdi, H., M.T. Melki, and M.L. Gougeon. 2008. HMGB1-dependent triggering of HIV-1 replication and persistence in dendritic cells as a consequence of NK-DC cross-talk. PLoS ONE. 3:e3601.
    • (2008) PLoS ONE , vol.3
    • Saïdi, H.1    Melki, M.T.2    Gougeon, M.L.3
  • 44
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • Schroder, K., and J. Tschopp. 2010. The inflammasomes. Cell. 140:821-832.
    • (2010) Cell , vol.140 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 45
    • 0036086930 scopus 로고    scopus 로고
    • Extracellular ATP signaling and P2X nucleotide receptors in monolayers of primary human vascular endothelial cells
    • Schwiebert, L.M., W.C. Rice, B.A. Kudlow, A.L. Taylor, and E.M. Schwiebert. 2002. Extracellular ATP signaling and P2X nucleotide receptors in monolayers of primary human vascular endothelial cells. Am. J. Physiol. Cell Physiol. 282:C289-C301.
    • (2002) Am. J. Physiol. Cell Physiol. , vol.282
    • Schwiebert, L.M.1    Rice, W.C.2    Kudlow, B.A.3    Taylor, A.L.4    Schwiebert, E.M.5
  • 46
    • 4143053858 scopus 로고    scopus 로고
    • The P2Y2 nucleotide receptor mediates vascular cell adhesion molecule-1 expression through interaction with VEGF receptor-2 (KDR/Flk-1)
    • Seye, C.I., N. Yu, F.A. González, L. Erb, and G.A. Weisman. 2004. The P2Y2 nucleotide receptor mediates vascular cell adhesion molecule-1 expression through interaction with VEGF receptor-2 (KDR/Flk-1). J. Biol. Chem. 279:35679-35686.
    • (2004) J. Biol. Chem. , vol.279 , pp. 35679-35686
    • Seye, C.I.1    Yu, N.2    González, F.A.3    Erb, L.4    Weisman, G.A.5
  • 47
    • 67649639047 scopus 로고    scopus 로고
    • Signaling at purinergic P2X receptors
    • Surprenant, A., and R.A. North. 2009. Signaling at purinergic P2X receptors. Annu. Rev. Physiol. 71:333-359.
    • (2009) Annu. Rev. Physiol. , vol.71 , pp. 333-359
    • Surprenant, A.1    North, R.A.2
  • 48
    • 77949384495 scopus 로고    scopus 로고
    • Immunology and the elusive AIDS vaccine
    • Virgin, H.W., and B.D. Walker. 2010. Immunology and the elusive AIDS vaccine. Nature. 464:224-231.
    • (2010) Nature , vol.464 , pp. 224-231
    • Virgin, H.W.1    Walker, B.D.2
  • 49
    • 55949096011 scopus 로고    scopus 로고
    • Dynamics of shear-induced ATP release from red blood cells
    • Wan, J., W.D. Ristenpart, and H.A. Stone. 2008. Dynamics of shear-induced ATP release from red blood cells. Proc. Natl. Acad. Sci. USA. 105:16432-16437.
    • (2008) Proc. Natl. Acad. Sci. USA. , vol.105 , pp. 16432-16437
    • Wan, J.1    Ristenpart, W.D.2    Stone, H.A.3
  • 51
    • 34948851977 scopus 로고    scopus 로고
    • Extracellular ATP is cytotoxic to mononuclear phagocytes but does not induce killing of intracellular Mycobacterium avium subsp. paratuberculosis
    • Woo, S.R., R.G. Barletta, and C.J. Czuprynski. 2007. Extracellular ATP is cytotoxic to mononuclear phagocytes but does not induce killing of intracellular Mycobacterium avium subsp. paratuberculosis. Clin. Vaccine Immunol. 14:1078-1083.
    • (2007) Clin. Vaccine Immunol. , vol.14 , pp. 1078-1083
    • Woo, S.R.1    Barletta, R.G.2    Czuprynski, C.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.