메뉴 건너뛰기




Volumn 25, Issue 6, 2009, Pages 256-260

Purinergic signaling and immune modulation at the schistosome surface?

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; ALKALINE PHOSPHATASE; PHOSPHODIESTERASE;

EID: 66149171633     PISSN: 14714922     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pt.2009.03.004     Document Type: Article
Times cited : (59)

References (49)
  • 1
    • 33749261659 scopus 로고    scopus 로고
    • Adenosine 5′-triphosphate and adenosine as endogenous signaling molecules in immunity and inflammation
    • Bours M.J., et al. Adenosine 5′-triphosphate and adenosine as endogenous signaling molecules in immunity and inflammation. Pharmacol. Ther. 112 (2006) 358-404
    • (2006) Pharmacol. Ther. , vol.112 , pp. 358-404
    • Bours, M.J.1
  • 2
    • 3042634614 scopus 로고    scopus 로고
    • 2+ and membrane potential and promotes transcription of IL-6 in macrophages
    • 2+ and membrane potential and promotes transcription of IL-6 in macrophages. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 9479-9484
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 9479-9484
    • Hanley, P.J.1
  • 3
    • 29644433257 scopus 로고    scopus 로고
    • The priming effect of extracellular UTP on human neutrophils: role of calcium released from thapsigargin-sensitive intracellular stores
    • Tuluc F., et al. The priming effect of extracellular UTP on human neutrophils: role of calcium released from thapsigargin-sensitive intracellular stores. Purinergic Signal. 1 (2005) 359-368
    • (2005) Purinergic Signal. , vol.1 , pp. 359-368
    • Tuluc, F.1
  • 5
    • 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
    • Marteau F., et al. 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
  • 6
    • 0034667802 scopus 로고    scopus 로고
    • Extracellular ATP and TNF-α synergize in the activation and maturation of human dendritic cells
    • Schnurr M., et al. Extracellular ATP and TNF-α synergize in the activation and maturation of human dendritic cells. J. Immunol. 165 (2000) 4704-4709
    • (2000) J. Immunol. , vol.165 , pp. 4704-4709
    • Schnurr, M.1
  • 7
    • 0348222661 scopus 로고    scopus 로고
    • Adenosine: an endogenous regulator of innate immunity
    • Hasko G., and Cronstein B.N. Adenosine: an endogenous regulator of innate immunity. Trends Immunol. 25 (2004) 33-39
    • (2004) Trends Immunol. , vol.25 , pp. 33-39
    • Hasko, G.1    Cronstein, B.N.2
  • 8
    • 0034011526 scopus 로고    scopus 로고
    • Adenosine, a potent natural suppressor of arachidonic acid release and leukotriene biosynthesis in human neutrophils
    • Flamand N., et al. Adenosine, a potent natural suppressor of arachidonic acid release and leukotriene biosynthesis in human neutrophils. Am. J. Respir. Crit. Care Med. 161 (2000) S88-S94
    • (2000) Am. J. Respir. Crit. Care Med. , vol.161
    • Flamand, N.1
  • 9
    • 0021991004 scopus 로고
    • Regulation of macrophage lysosomal secretion by adenosine, adenosine phosphate esters, and related structural analogues of adenosine
    • Riches D.W., et al. Regulation of macrophage lysosomal secretion by adenosine, adenosine phosphate esters, and related structural analogues of adenosine. J. Leukoc. Biol. 37 (1985) 545-557
    • (1985) J. Leukoc. Biol. , vol.37 , pp. 545-557
    • Riches, D.W.1
  • 10
    • 1342281409 scopus 로고    scopus 로고
    • Regulation of adenosine receptor subtypes during cultivation of human monocytes: role of receptors in preventing lipopolysaccharide-triggered respiratory burst
    • Thiele A., et al. Regulation of adenosine receptor subtypes during cultivation of human monocytes: role of receptors in preventing lipopolysaccharide-triggered respiratory burst. Infect. Immun. 72 (2004) 1349-1357
    • (2004) Infect. Immun. , vol.72 , pp. 1349-1357
    • Thiele, A.1
  • 11
    • 34250719722 scopus 로고    scopus 로고
    • Purine and pyrimidine receptors
    • Burnstock G. Purine and pyrimidine receptors. Cell. Mol. Life Sci. 64 (2007) 1471-1483
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 1471-1483
    • Burnstock, G.1
  • 12
    • 33644607461 scopus 로고    scopus 로고
    • Pathophysiology and therapeutic potential of purinergic signaling
    • Burnstock G. Pathophysiology and therapeutic potential of purinergic signaling. Pharmacol. Rev. 58 (2006) 58-86
    • (2006) Pharmacol. Rev. , vol.58 , pp. 58-86
    • Burnstock, G.1
  • 13
    • 0042386007 scopus 로고    scopus 로고
    • Coordinated adenine nucleotide phosphohydrolysis and nucleoside signaling in posthypoxic endothelium: role of ectonucleotidases and adenosine A2B receptors
    • Eltzschig H.K., et al. Coordinated adenine nucleotide phosphohydrolysis and nucleoside signaling in posthypoxic endothelium: role of ectonucleotidases and adenosine A2B receptors. J. Exp. Med. 198 (2003) 783-796
    • (2003) J. Exp. Med. , vol.198 , pp. 783-796
    • Eltzschig, H.K.1
  • 14
    • 6344283049 scopus 로고    scopus 로고
    • Targeted disruption of cd73/ecto-5′-nucleotidase alters thromboregulation and augments vascular inflammatory response
    • Koszalka P., et al. Targeted disruption of cd73/ecto-5′-nucleotidase alters thromboregulation and augments vascular inflammatory response. Circ. Res. 95 (2004) 814-821
    • (2004) Circ. Res. , vol.95 , pp. 814-821
    • Koszalka, P.1
  • 15
    • 33144479358 scopus 로고    scopus 로고
    • Regulation of platelet functions by P2 receptors
    • Gachet C. Regulation of platelet functions by P2 receptors. Annu. Rev. Pharmacol. Toxicol. 46 (2006) 277-300
    • (2006) Annu. Rev. Pharmacol. Toxicol. , vol.46 , pp. 277-300
    • Gachet, C.1
  • 16
    • 1542346410 scopus 로고    scopus 로고
    • Clinical and molecular pharmacologic characteristics of adenosine-induced vasodilation
    • Biaggioni I. Clinical and molecular pharmacologic characteristics of adenosine-induced vasodilation. Clin. Pharmacol. Ther. 75 (2004) 137-139
    • (2004) Clin. Pharmacol. Ther. , vol.75 , pp. 137-139
    • Biaggioni, I.1
  • 17
    • 0019781379 scopus 로고
    • Properties of a series of tegumental membrane-bound phosphohydrolase activities of Schistosoma mansoni
    • Cesari I.M., et al. Properties of a series of tegumental membrane-bound phosphohydrolase activities of Schistosoma mansoni. Biochem. J. 198 (1981) 467-473
    • (1981) Biochem. J. , vol.198 , pp. 467-473
    • Cesari, I.M.1
  • 18
    • 0038982065 scopus 로고
    • Histochemical observations of alkaline phosphatase in Schistosoma mansoni
    • Dusanic D.G. Histochemical observations of alkaline phosphatase in Schistosoma mansoni. J. Infect. Dis. 105 (1959) 1-8
    • (1959) J. Infect. Dis. , vol.105 , pp. 1-8
    • Dusanic, D.G.1
  • 19
    • 0014251105 scopus 로고
    • Ultrastructure of the tegument of adult Schistosoma mansoni
    • Morris G.P., and Threadgold L.T. Ultrastructure of the tegument of adult Schistosoma mansoni. J. Parasitol. 54 (1968) 15-27
    • (1968) J. Parasitol. , vol.54 , pp. 15-27
    • Morris, G.P.1    Threadgold, L.T.2
  • 20
    • 0016311235 scopus 로고
    • Schistosoma mansoni: distribution and characteristics of alkaline and acid phosphatase
    • Cesari I.M. Schistosoma mansoni: distribution and characteristics of alkaline and acid phosphatase. Exp. Parasitol. 36 (1974) 405-414
    • (1974) Exp. Parasitol. , vol.36 , pp. 405-414
    • Cesari, I.M.1
  • 21
    • 0022002875 scopus 로고
    • Antigenicity and immunogenicity of the tegumental outer membrane of adult Schistosoma mansoni
    • Payares G., et al. Antigenicity and immunogenicity of the tegumental outer membrane of adult Schistosoma mansoni. Parasite Immunol. 7 (1985) 45-61
    • (1985) Parasite Immunol. , vol.7 , pp. 45-61
    • Payares, G.1
  • 22
    • 33644674090 scopus 로고    scopus 로고
    • The tegument surface membranes of the human blood parasite Schistosoma mansoni: a proteomic analysis after differential extraction
    • Braschi S., et al. The tegument surface membranes of the human blood parasite Schistosoma mansoni: a proteomic analysis after differential extraction. Proteomics 6 (2006) 1471-1482
    • (2006) Proteomics , vol.6 , pp. 1471-1482
    • Braschi, S.1
  • 23
    • 0025341848 scopus 로고
    • Production of a mouse monoclonal antibody against the alkaline phosphatase of adult Schistosoma mansoni
    • Pujol F.H., et al. Production of a mouse monoclonal antibody against the alkaline phosphatase of adult Schistosoma mansoni. Mol. Biochem. Parasitol. 40 (1990) 43-52
    • (1990) Mol. Biochem. Parasitol. , vol.40 , pp. 43-52
    • Pujol, F.H.1
  • 24
    • 0021737870 scopus 로고
    • Isolation and partial characterization of the tegumental outer membrane of schistosomula of Schistosoma mansoni
    • Levi-Schaffer F., et al. Isolation and partial characterization of the tegumental outer membrane of schistosomula of Schistosoma mansoni. Mol. Biochem. Parasitol. 13 (1984) 283-300
    • (1984) Mol. Biochem. Parasitol. , vol.13 , pp. 283-300
    • Levi-Schaffer, F.1
  • 25
    • 0023921972 scopus 로고
    • Acetylcholinesterase in Schistosoma mansoni is anchored to the membrane via covalently attached phosphatidylinositol
    • Espinoza B., et al. Acetylcholinesterase in Schistosoma mansoni is anchored to the membrane via covalently attached phosphatidylinositol. Mol. Biochem. Parasitol. 29 (1988) 171-179
    • (1988) Mol. Biochem. Parasitol. , vol.29 , pp. 171-179
    • Espinoza, B.1
  • 26
    • 20844458058 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the Schistosoma mansoni tegumental sub-proteome
    • van Balkom B.W., et al. Mass spectrometric analysis of the Schistosoma mansoni tegumental sub-proteome. J. Proteome Res. 4 (2005) 958-966
    • (2005) J. Proteome Res. , vol.4 , pp. 958-966
    • van Balkom, B.W.1
  • 27
    • 33644696623 scopus 로고    scopus 로고
    • Proteins exposed at the adult schistosome surface revealed by biotinylation
    • Braschi S., and Wilson R.A. Proteins exposed at the adult schistosome surface revealed by biotinylation. Mol. Cell. Proteomics 5 (2005) 347-356
    • (2005) Mol. Cell. Proteomics , vol.5 , pp. 347-356
    • Braschi, S.1    Wilson, R.A.2
  • 28
    • 0027411290 scopus 로고
    • Characterization and localization of an ATP diphosphohydrolase on the external surface of the tegument of Schistosoma mansoni
    • Vasconcelos E.G., et al. Characterization and localization of an ATP diphosphohydrolase on the external surface of the tegument of Schistosoma mansoni. Mol. Biochem. Parasitol. 58 (1993) 205-214
    • (1993) Mol. Biochem. Parasitol. , vol.58 , pp. 205-214
    • Vasconcelos, E.G.1
  • 29
    • 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 E.G., et al. 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 (1996) 22139-22145
    • (1996) J. Biol. Chem. , vol.271 , pp. 22139-22145
    • Vasconcelos, E.G.1
  • 30
    • 0141507054 scopus 로고    scopus 로고
    • Transcriptome analysis of the acoelomate human parasite Schistosoma mansoni
    • Verjovski-Almeida S., et al. Transcriptome analysis of the acoelomate human parasite Schistosoma mansoni. Nat. Genet. 35 (2003) 148-157
    • (2003) Nat. Genet. , vol.35 , pp. 148-157
    • Verjovski-Almeida, S.1
  • 31
    • 0037767919 scopus 로고    scopus 로고
    • Molecular characterization and immunolocalization of Schistosoma mansoni ATP-diphosphohydrolase
    • DeMarco R., et al. Molecular characterization and immunolocalization of Schistosoma mansoni ATP-diphosphohydrolase. Biochem. Biophys. Res. Commun. 307 (2003) 831-838
    • (2003) Biochem. Biophys. Res. Commun. , vol.307 , pp. 831-838
    • DeMarco, R.1
  • 32
    • 33751547252 scopus 로고    scopus 로고
    • Characterization of Schistosoma mansoni ATPDase2 gene, a novel apyrase family member
    • Levano-Garcia J., et al. Characterization of Schistosoma mansoni ATPDase2 gene, a novel apyrase family member. Biochem. Biophys. Res. Commun. 352 (2007) 384-389
    • (2007) Biochem. Biophys. Res. Commun. , vol.352 , pp. 384-389
    • Levano-Garcia, J.1
  • 33
    • 33644696623 scopus 로고    scopus 로고
    • Proteins exposed at the adult schistosome surface revealed by biotinylation
    • Braschi S., and Wilson R.A. Proteins exposed at the adult schistosome surface revealed by biotinylation. Mol. Cell. Proteomics 5 (2006) 347-356
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 347-356
    • Braschi, S.1    Wilson, R.A.2
  • 34
    • 0015166804 scopus 로고
    • Schistosoma mansoni and Haematoloechus medioplexus: nuclosidediphosphatase localization in tegument
    • Bogitsh B.J., and Krupa P.L. Schistosoma mansoni and Haematoloechus medioplexus: nuclosidediphosphatase localization in tegument. Exp. Parasitol. 30 (1971) 418-425
    • (1971) Exp. Parasitol. , vol.30 , pp. 418-425
    • Bogitsh, B.J.1    Krupa, P.L.2
  • 35
    • 33846944693 scopus 로고    scopus 로고
    • No overt cellular inflammation around intravascular schistosomes in vivo
    • Keating J.H., et al. No overt cellular inflammation around intravascular schistosomes in vivo. J. Parasitol. 92 (2006) 1365-1369
    • (2006) J. Parasitol. , vol.92 , pp. 1365-1369
    • Keating, J.H.1
  • 36
    • 0031714870 scopus 로고    scopus 로고
    • Increased reactivity to 5-hydroxytryptamine of portal veins from mice infected with Schistosoma mansoni
    • Silva C.L., et al. Increased reactivity to 5-hydroxytryptamine of portal veins from mice infected with Schistosoma mansoni. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 120 (1998) 417-423
    • (1998) Comp. Biochem. Physiol. A Mol. Integr. Physiol. , vol.120 , pp. 417-423
    • Silva, C.L.1
  • 37
    • 18744396721 scopus 로고    scopus 로고
    • Cellular mechanisms involved in the increased contraction of portal veins from Schistosoma mansoni-infected mice
    • Silva C.L., et al. Cellular mechanisms involved in the increased contraction of portal veins from Schistosoma mansoni-infected mice. Parasitol. Res. 89 (2003) 16-22
    • (2003) Parasitol. Res. , vol.89 , pp. 16-22
    • Silva, C.L.1
  • 38
    • 0036010756 scopus 로고    scopus 로고
    • Regulation of ecto-5′-nucleotidase by TNF-α in human endothelial cells
    • Kalsi K., et al. Regulation of ecto-5′-nucleotidase by TNF-α in human endothelial cells. Mol. Cell. Biochem. 232 (2002) 113-119
    • (2002) Mol. Cell. Biochem. , vol.232 , pp. 113-119
    • Kalsi, K.1
  • 39
    • 34548862888 scopus 로고    scopus 로고
    • Differential platelet adhesion to distinct life-cycle stages of the parasitic helminth Schistosoma mansoni
    • Wu Y.P., et al. Differential platelet adhesion to distinct life-cycle stages of the parasitic helminth Schistosoma mansoni. J. Thromb. Haemost. 5 (2007) 2146-2148
    • (2007) J. Thromb. Haemost. , vol.5 , pp. 2146-2148
    • Wu, Y.P.1
  • 40
    • 0031848298 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase-deficient mice develop enhanced type 1 cytokine-associated cellular and humoral immune responses after vaccination with attenuated Schistosoma mansoni cercariae but display partially reduced resistance
    • James S.L., et al. Inducible nitric oxide synthase-deficient mice develop enhanced type 1 cytokine-associated cellular and humoral immune responses after vaccination with attenuated Schistosoma mansoni cercariae but display partially reduced resistance. Infect. Immun. 66 (1998) 3510-3518
    • (1998) Infect. Immun. , vol.66 , pp. 3510-3518
    • James, S.L.1
  • 41
    • 4744370354 scopus 로고    scopus 로고
    • Functional characterization of a P2X receptor from Schistosoma mansoni
    • Agboh K.C., et al. Functional characterization of a P2X receptor from Schistosoma mansoni. J. Biol. Chem. 279 (2004) 41650-41657
    • (2004) J. Biol. Chem. , vol.279 , pp. 41650-41657
    • Agboh, K.C.1
  • 42
    • 0033021847 scopus 로고    scopus 로고
    • ATP reception and chemosensory adaptation in Tetrahymena thermophila
    • Kim M.Y., et al. ATP reception and chemosensory adaptation in Tetrahymena thermophila. J. Exp. Biol. 202 (1999) 407-416
    • (1999) J. Exp. Biol. , vol.202 , pp. 407-416
    • Kim, M.Y.1
  • 43
    • 0021436447 scopus 로고
    • ATP and the autonomy of the contractile vacuole in Amoeba proteus
    • Pothier F., et al. ATP and the autonomy of the contractile vacuole in Amoeba proteus. J. Exp. Zool. 230 (1984) 211-218
    • (1984) J. Exp. Zool. , vol.230 , pp. 211-218
    • Pothier, F.1
  • 44
    • 11444268861 scopus 로고    scopus 로고
    • Parasite nucleotide-metabolizing enzymes and host purinergic signaling
    • Gounaris K., and Selkirk M.E. Parasite nucleotide-metabolizing enzymes and host purinergic signaling. Trends Parasitol. 21 (2005) 17-21
    • (2005) Trends Parasitol. , vol.21 , pp. 17-21
    • Gounaris, K.1    Selkirk, M.E.2
  • 45
    • 0036720235 scopus 로고    scopus 로고
    • Nucleotidase cascades are catalyzed by secreted proteins of the parasitic nematode Trichinella spiralis
    • Gounaris K. Nucleotidase cascades are catalyzed by secreted proteins of the parasitic nematode Trichinella spiralis. Infect. Immun. 70 (2002) 4917-4924
    • (2002) Infect. Immun. , vol.70 , pp. 4917-4924
    • Gounaris, K.1
  • 46
    • 0033021431 scopus 로고    scopus 로고
    • Secretion of ATP-utilizing enzymes, nucleoside diphosphate kinase and ATPase, by Mycobacterium bovis BCG: sequestration of ATP from macrophage P2Z receptors? Mol
    • Zaborina O., et al. Secretion of ATP-utilizing enzymes, nucleoside diphosphate kinase and ATPase, by Mycobacterium bovis BCG: sequestration of ATP from macrophage P2Z receptors? Mol. Microbiol. 31 (1999) 1333-1343
    • (1999) Microbiol. , vol.31 , pp. 1333-1343
    • Zaborina, O.1
  • 47
    • 34249057208 scopus 로고    scopus 로고
    • An insight into the sialome of the oriental rat flea, Xenopsylla cheopis (Rots)
    • Andersen J.F., et al. An insight into the sialome of the oriental rat flea, Xenopsylla cheopis (Rots). BMC Genomics 8 (2007) 102-119
    • (2007) BMC Genomics , vol.8 , pp. 102-119
    • Andersen, J.F.1
  • 48
    • 33947702519 scopus 로고    scopus 로고
    • Adenosine and lymphocyte regulation
    • Gessi S., et al. Adenosine and lymphocyte regulation. Purinergic Signal. 3 (2007) 109-116
    • (2007) Purinergic Signal. , vol.3 , pp. 109-116
    • Gessi, S.1
  • 49
    • 0032518553 scopus 로고    scopus 로고
    • Divalent cation dependence and inhibition of Schistosoma mansoni ATP diphosphohydrolase by fluorosulfonylbenzoyl adenosine
    • Torres C.R., et al. Divalent cation dependence and inhibition of Schistosoma mansoni ATP diphosphohydrolase by fluorosulfonylbenzoyl adenosine. Eur. J. Biochem. 251 (1998) 516-521
    • (1998) Eur. J. Biochem. , vol.251 , pp. 516-521
    • Torres, C.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.