메뉴 건너뛰기




Volumn 85, Issue 1, 2007, Pages 68-72

Rottlerin inhibits P2X7 receptor-stimulated phospholipase D activity in chronic lymphocytic leukaemia B-lymphocytes

Author keywords

B lymphocyte; Chronic lymphocytic leukaemia; P2X7 receptor; Phospholipase D; Rottlerin

Indexed keywords

2 [1 (3 DIMETHYLAMINOPROPYL) 3 INDOLYL] 3 (3 INDOLYL)MALEIMIDE; ADENOSINE TRIPHOSPHATE; ALANINE; GLUTAMIC ACID; ISOENZYME; MONOCLONAL ANTIBODY; PHORBOL 13 ACETATE 12 MYRISTATE; PHOSPHOLIPASE D; PROTEIN KINASE C ACTIVATOR; PROTEIN KINASE C INHIBITOR; PURINE P2X7 RECEPTOR; RECEPTOR ANTIBODY; ROTTLERIN;

EID: 33846048059     PISSN: 08189641     EISSN: 14401711     Source Type: Journal    
DOI: 10.1038/sj.icb.7100005     Document Type: Article
Times cited : (20)

References (41)
  • 1
    • 9144269934 scopus 로고    scopus 로고
    • Cellular distribution and functions of P2 receptor subtypes in different systems
    • Burnstock G, Knight GE. Cellular distribution and functions of P2 receptor subtypes in different systems. Int Rev Cytol 2004; 240: 31-304.
    • (2004) Int Rev Cytol , vol.240 , pp. 31-304
    • Burnstock, G.1    Knight, G.E.2
  • 2
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • North RA. Molecular physiology of P2X receptors. Physiol Rev 2002; 82: 1013-1067.
    • (2002) Physiol Rev , vol.82 , pp. 1013-1067
    • North, R.A.1
  • 3
    • 0027077621 scopus 로고
    • A novel pathway for the activation of phospholipase D by P2z purinergic receptors in BAC1.2F5 macrophages
    • el-Moatassim C, Dubyak GR. A novel pathway for the activation of phospholipase D by P2z purinergic receptors in BAC1.2F5 macrophages. J Biol Chem 1992; 267: 23664-23673.
    • (1992) J Biol Chem , vol.267 , pp. 23664-23673
    • el-Moatassim, C.1    Dubyak, G.R.2
  • 4
    • 0030070494 scopus 로고    scopus 로고
    • Phospholipase D activation by P2Z-purinoceptor agonists in human lymphocytes is dependent on bivalent cation influx
    • Gargett CE, Cornish EJ, Wiley JS. Phospholipase D activation by P2Z-purinoceptor agonists in human lymphocytes is dependent on bivalent cation influx. Biochem J 1996; 313: 529-535.
    • (1996) Biochem J , vol.313 , pp. 529-535
    • Gargett, C.E.1    Cornish, E.J.2    Wiley, J.S.3
  • 5
    • 2342639554 scopus 로고    scopus 로고
    • McDermott M, Morris AJ, Wakelam MJO. Phospholipase D. Biochem Cell Biol 2004; 82: 225-253.
    • McDermott M, Morris AJ, Wakelam MJO. Phospholipase D. Biochem Cell Biol 2004; 82: 225-253.
  • 6
    • 0033957426 scopus 로고    scopus 로고
    • ATP-induced killing of virulent Mycobacterium tuberculosis within human macrophages requires phospholipase D
    • Kusner DJ, Adams J. ATP-induced killing of virulent Mycobacterium tuberculosis within human macrophages requires phospholipase D. J Immunol 2000; 164: 379-388.
    • (2000) J Immunol , vol.164 , pp. 379-388
    • Kusner, D.J.1    Adams, J.2
  • 11
    • 0030977216 scopus 로고    scopus 로고
    • The isoquinoline derivative KN-62 a potent antagonist of the P2Z-receptor of human lymphocytes
    • Gargett CE, Wiley JS. The isoquinoline derivative KN-62 a potent antagonist of the P2Z-receptor of human lymphocytes. Br J Pharmacol 1997; 120: 1483-1490.
    • (1997) Br J Pharmacol , vol.120 , pp. 1483-1490
    • Gargett, C.E.1    Wiley, J.S.2
  • 12
    • 21544470248 scopus 로고    scopus 로고
    • Protein kinase C and phosphoipase D: Intimate interactions in intracellular signalling
    • Becker KP, Hannun YA. Protein kinase C and phosphoipase D: intimate interactions in intracellular signalling. Cell Mol Life Sci 2005; 62: 1448-1461.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1448-1461
    • Becker, K.P.1    Hannun, Y.A.2
  • 13
    • 3843066800 scopus 로고    scopus 로고
    • 7 receptor. Br J Pharm 2004; 142: 1015-1019.
    • 7 receptor. Br J Pharm 2004; 142: 1015-1019.
  • 14
    • 0032104245 scopus 로고    scopus 로고
    • The extended protein kinase C superfamily
    • Mellor H, Parker PJ. The extended protein kinase C superfamily. Biochem J 1998; 332: 281-292.
    • (1998) Biochem J , vol.332 , pp. 281-292
    • Mellor, H.1    Parker, P.J.2
  • 15
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies SP, Reddy H, Caivano M, Cohen P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J 2000; 351: 95-105.
    • (2000) Biochem J , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 16
    • 0026538078 scopus 로고
    • Inhibitors of protein kinase C. 2. Substituted bisindoylmaleimides with improved potency and selectivity
    • Davis PD, Elliot LH, Harris W, Hill CH, Hurst SA, Keech E et al. Inhibitors of protein kinase C. 2. Substituted bisindoylmaleimides with improved potency and selectivity. J Med Chem 1992; 35: 994-1001.
    • (1992) J Med Chem , vol.35 , pp. 994-1001
    • Davis, P.D.1    Elliot, L.H.2    Harris, W.3    Hill, C.H.4    Hurst, S.A.5    Keech, E.6
  • 22
    • 1542619335 scopus 로고    scopus 로고
    • 7 receptor impairs ATP-induced IL-1b release from human monocytes
    • 7 receptor impairs ATP-induced IL-1b release from human monocytes. J Immunol 2004; 172: 3399-3405.
    • (2004) J Immunol , vol.172 , pp. 3399-3405
    • Sluyter, R.1    Shemon, A.N.2    Wiley, J.S.3
  • 23
    • 0027248964 scopus 로고
    • Isoenzyme specificity of bisindolylmaleimides, selective inhibitors of protein kinase C
    • Wilkinson SE, Parker PJ, Nixon JS. Isoenzyme specificity of bisindolylmaleimides, selective inhibitors of protein kinase C. Biochem J 1993; 294: 335-337.
    • (1993) Biochem J , vol.294 , pp. 335-337
    • Wilkinson, S.E.1    Parker, P.J.2    Nixon, J.S.3
  • 25
    • 0037111661 scopus 로고    scopus 로고
    • Constitutively activated phosphatidylinositol-3 kinase (PI-3 K) is involved in the defect of apoptosis in B-CLL: Association with protein kinase Cdelta
    • Ringshausen I, Schneller F, Bogner C, Hipp S, Duyster J, Peschel C et al. Constitutively activated phosphatidylinositol-3 kinase (PI-3 K) is involved in the defect of apoptosis in B-CLL: association with protein kinase Cdelta. Blood 2002; 100: 3741-3748.
    • (2002) Blood , vol.100 , pp. 3741-3748
    • Ringshausen, I.1    Schneller, F.2    Bogner, C.3    Hipp, S.4    Duyster, J.5    Peschel, C.6
  • 26
    • 20044363128 scopus 로고    scopus 로고
    • Survival role of protein kinase C (PKC) in chronic lymphocytic leukemia and determination of isoform expression pattern and genes altered by PKC inhibition
    • Alkan S, Huang Q, Ergin M, Denning F, Nand S, Maududi T et al. Survival role of protein kinase C (PKC) in chronic lymphocytic leukemia and determination of isoform expression pattern and genes altered by PKC inhibition. Am J Hematol 2005; 79: 97-106.
    • (2005) Am J Hematol , vol.79 , pp. 97-106
    • Alkan, S.1    Huang, Q.2    Ergin, M.3    Denning, F.4    Nand, S.5    Maududi, T.6
  • 27
    • 0034651539 scopus 로고    scopus 로고
    • Multiple pathways control protein kinase C phosphorylation
    • Parekh DB, Ziegler W, Parker PJ. Multiple pathways control protein kinase C phosphorylation. EMBO J 2000; 19: 496-503.
    • (2000) EMBO J , vol.19 , pp. 496-503
    • Parekh, D.B.1    Ziegler, W.2    Parker, P.J.3
  • 28
    • 0032566691 scopus 로고    scopus 로고
    • Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1
    • Le Good JA, Ziegler WH, Parekh DB, Alessi DR, Cohen P, Parker PJ. Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. Science 1998; 281: 2042-2045.
    • (1998) Science , vol.281 , pp. 2042-2045
    • Le Good, J.A.1    Ziegler, W.H.2    Parekh, D.B.3    Alessi, D.R.4    Cohen, P.5    Parker, P.J.6
  • 29
    • 0037105040 scopus 로고    scopus 로고
    • 7 receptors activate protein kinase D and p42/p44 mitogen activated kinase (MAPK) downstream of protein kinase C
    • 7 receptors activate protein kinase D and p42/p44 mitogen activated kinase (MAPK) downstream of protein kinase C. Biochem J 2002; 366: 745-755.
    • (2002) Biochem J , vol.366 , pp. 745-755
    • Bradford, M.D.1    Soltoff, S.P.2
  • 30
    • 0036135941 scopus 로고    scopus 로고
    • 7 receptor-mediated phospholipase D activation is regulated by both PKC-dependent and PKC-independent pathways in a rat brain-derived Type-2 astrocyte cell line, RBA-2
    • 7 receptor-mediated phospholipase D activation is regulated by both PKC-dependent and PKC-independent pathways in a rat brain-derived Type-2 astrocyte cell line, RBA-2. Cell Signal 2002; 14: 83-92.
    • (2002) Cell Signal , vol.14 , pp. 83-92
    • Hung, A.C.1    Sun, S.H.2
  • 31
    • 0035851112 scopus 로고    scopus 로고
    • Rottlerin is a mitochondrial uncoupler that decreases cellular ATP levels and indirectly blocks protein kinase C delta tyrosine phosphorylation
    • Soltoff SP. Rottlerin is a mitochondrial uncoupler that decreases cellular ATP levels and indirectly blocks protein kinase C delta tyrosine phosphorylation. J Biol Chem 2001; 276: 37986-37992.
    • (2001) J Biol Chem , vol.276 , pp. 37986-37992
    • Soltoff, S.P.1
  • 34
    • 0027304738 scopus 로고
    • 2z purinergic receptors in BAC1.2F5 macrophages. Product inhibition of phospholipase D enzyme activity
    • 2z purinergic receptors in BAC1.2F5 macrophages. Product inhibition of phospholipase D enzyme activity. J Biol Chem 1993; 268: 15571-15578.
    • (1993) J Biol Chem , vol.268 , pp. 15571-15578
    • el-Moatassim, C.1    Dubyak, G.R.2
  • 35
    • 0030589244 scopus 로고    scopus 로고
    • 7 nucleotide receptor and associated phospholipase D activity by lipopolysaccharide and INF-gamma in the human THP-1 monocytic cell line
    • 7 nucleotide receptor and associated phospholipase D activity by lipopolysaccharide and INF-gamma in the human THP-1 monocytic cell line. J Immunol 1996; 157: 5627-5637.
    • (1996) J Immunol , vol.157 , pp. 5627-5637
    • Humphreys, B.D.1    Dubyak, G.R.2
  • 36
    • 0036727667 scopus 로고    scopus 로고
    • Regulation of phospholipase D in human placental trophoblasts by the P(2) purinergic receptor
    • Divald A, Karl PI, Fisher SE. Regulation of phospholipase D in human placental trophoblasts by the P(2) purinergic receptor. Placenta 2002; 23: 584-593.
    • (2002) Placenta , vol.23 , pp. 584-593
    • Divald, A.1    Karl, P.I.2    Fisher, S.E.3
  • 37
    • 0035031568 scopus 로고    scopus 로고
    • Detection of P2X purinergic receptors on human B lymphocytes
    • Sluyter R, Barden JA, Wiley JS. Detection of P2X purinergic receptors on human B lymphocytes. Cell Tissue Res 2001; 304: 231-236.
    • (2001) Cell Tissue Res , vol.304 , pp. 231-236
    • Sluyter, R.1    Barden, J.A.2    Wiley, J.S.3
  • 38
    • 0035884993 scopus 로고    scopus 로고
    • ATP stimulates human macrophages to kill intracellular virulent mycobacterium tuberculosis via calcium-dependent phagosome-lysosome fusion
    • Kusner DJ, Barton JA. ATP stimulates human macrophages to kill intracellular virulent mycobacterium tuberculosis via calcium-dependent phagosome-lysosome fusion. J Immunol 2001; 167: 3308-3315.
    • (2001) J Immunol , vol.167 , pp. 3308-3315
    • Kusner, D.J.1    Barton, J.A.2
  • 39
    • 0035884935 scopus 로고    scopus 로고
    • ATP-mediated killing of intracellular mycobacteria by macrophages is a P2X(7)-dependent process inducing bacterial death by phagosome-lysosome fusion
    • Fairbairn IP, Stober CB, Kumararatne DS, Lammas DA. ATP-mediated killing of intracellular mycobacteria by macrophages is a P2X(7)-dependent process inducing bacterial death by phagosome-lysosome fusion. J Immunol 2001; 167: 3300-3307.
    • (2001) J Immunol , vol.167 , pp. 3300-3307
    • Fairbairn, I.P.1    Stober, C.B.2    Kumararatne, D.S.3    Lammas, D.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.