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Volumn 22, Issue 10, 2000, Pages 747-754

Stimulation of Ca2+-dependent exocytosis and release of arachidonic acid in cultured mast cells (RBL-2H3) by quercetin

Author keywords

Allergy; Mast cells; Quercetin; RBL 2H3 cells; Signal transduction

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ARACHIDONIC ACID; CALCIUM; GUANOSINE TRIPHOSPHATASE; QUERCETIN;

EID: 0033852582     PISSN: 01920561     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0192-0561(00)00034-5     Document Type: Article
Times cited : (12)

References (30)
  • 1
    • 0024461089 scopus 로고
    • Recent advance in the cellular and molecular biology of mast cells
    • Stevens R.L., Austen K.F. Recent advance in the cellular and molecular biology of mast cells. Immunol. Today. 10:1989;381-385.
    • (1989) Immunol. Today , vol.10 , pp. 381-385
    • Stevens, R.L.1    Austen, K.F.2
  • 3
    • 0029892080 scopus 로고    scopus 로고
    • Critical protective role of mast cells in a model of acute septic peritonitis
    • Echtenacher B., Mannel D.N., Hultner L. Critical protective role of mast cells in a model of acute septic peritonitis. Nature. 381:1996;75-77.
    • (1996) Nature , vol.381 , pp. 75-77
    • Echtenacher, B.1    Mannel, D.N.2    Hultner, L.3
  • 4
    • 0029981928 scopus 로고    scopus 로고
    • Mast cell modulation of neutrophil influx and bacterial clearance at sites of infection through TNF-alpha
    • Malaviya R., Ikeda T., Ross E., Abraham S.N. Mast cell modulation of neutrophil influx and bacterial clearance at sites of infection through TNF-alpha. Nature. 381:1996;77-80.
    • (1996) Nature , vol.381 , pp. 77-80
    • Malaviya, R.1    Ikeda, T.2    Ross, E.3    Abraham, S.N.4
  • 5
    • 0030930693 scopus 로고    scopus 로고
    • Mast cells in infection and immunity
    • Abraham S.N., Malaviya R. Mast cells in infection and immunity. Infect. Immunol. 65:1997;3501-3508.
    • (1997) Infect. Immunol. , vol.65 , pp. 3501-3508
    • Abraham, S.N.1    Malaviya, R.2
  • 6
    • 0031132767 scopus 로고    scopus 로고
    • The mast cell. A versatile effector cell for a challenging world
    • Galli S.J. The mast cell. A versatile effector cell for a challenging world. Int. Arch. Allergy Immunol. 113:1997;14-22.
    • (1997) Int. Arch. Allergy Immunol. , vol.113 , pp. 14-22
    • Galli, S.J.1
  • 7
    • 0030718543 scopus 로고    scopus 로고
    • Impaired mast cell-dependent natural immunity in complement C3-deficient mice
    • Prodeus A.P., Zhou X., Maurer M., Galli S.J., Carroll M.C. Impaired mast cell-dependent natural immunity in complement C3-deficient mice. Nature. 390:1997;172-175.
    • (1997) Nature , vol.390 , pp. 172-175
    • Prodeus, A.P.1    Zhou, X.2    Maurer, M.3    Galli, S.J.4    Carroll, M.C.5
  • 8
    • 0024348298 scopus 로고
    • Heterogeneity of mast cells and phenotype changes between subpopulations
    • Kitamura Y. Heterogeneity of mast cells and phenotype changes between subpopulations. Ann. Rev. Immunol. 7:1989;59-76.
    • (1989) Ann. Rev. Immunol. , vol.7 , pp. 59-76
    • Kitamura, Y.1
  • 9
    • 0030024349 scopus 로고    scopus 로고
    • Identification of a committed precursor for the mast cell lineage
    • Rodewald H.R., Dessing M., Dvorak A.M., Galli S.J. Identification of a committed precursor for the mast cell lineage. Science. 271:1996;818-822.
    • (1996) Science , vol.271 , pp. 818-822
    • Rodewald, H.R.1    Dessing, M.2    Dvorak, A.M.3    Galli, S.J.4
  • 10
    • 0000457253 scopus 로고
    • Dimeric immunoglobulin E serves as a unit signal for mast cell degranulation
    • Segal D.M., Taurog J., Metzger H. Dimeric immunoglobulin E serves as a unit signal for mast cell degranulation. Proc. Natl. Acad. Sci. USA. 74:1977;2993-2997.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 2993-2997
    • Segal, D.M.1    Taurog, J.2    Metzger, H.3
  • 12
    • 0025642479 scopus 로고
    • Neomycin is a potent secretagogue of mast cells that directly activates a GTP-binding protein that involved in exocytosis
    • Aridor M., Sagi-Eisenberg R. Neomycin is a potent secretagogue of mast cells that directly activates a GTP-binding protein that involved in exocytosis. J. Cell Biol. 111:1990;2885-2891.
    • (1990) J. Cell Biol. , vol.111 , pp. 2885-2891
    • Aridor, M.1    Sagi-Eisenberg, R.2
  • 13
    • 0025075352 scopus 로고
    • Exocytosis in mast cells by basic secretagogues: Evidence for direct activation of GTP-binding proteins
    • Aridor M., Traub L.M., Sagi-Eisenberg R. Exocytosis in mast cells by basic secretagogues: evidence for direct activation of GTP-binding proteins. J. Cell Biol. 111:1990;909-917.
    • (1990) J. Cell Biol. , vol.111 , pp. 909-917
    • Aridor, M.1    Traub, L.M.2    Sagi-Eisenberg, R.3
  • 14
    • 0025162326 scopus 로고
    • G protein activation: A receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides
    • Mousli M., Bueb J.L., Bronner C., Rouot B., Landry Y. G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides. TIPS. 11:1990;358-362.
    • (1990) TIPS , vol.11 , pp. 358-362
    • Mousli, M.1    Bueb, J.L.2    Bronner, C.3    Rouot, B.4    Landry, Y.5
  • 16
    • 0032532945 scopus 로고    scopus 로고
    • 2+-dependent exocytosis and arachidonic acid release in cultured mast cells (RBL-2H3) by a GTPase-deficient mutant of Gαi3
    • 2+-dependent exocytosis and arachidonic acid release in cultured mast cells (RBL-2H3) by a GTPase-deficient mutant of Gαi3. Eur. J. Biochem. 258:1998;144-149.
    • (1998) Eur. J. Biochem. , vol.258 , pp. 144-149
    • Zussman, A.1    Hermuet, S.2    Sagi-Eisenberg, R.3
  • 17
    • 0032524984 scopus 로고    scopus 로고
    • Quercetin sensitizes RBL-2H3 cells to polybasic mast cell secretagogues through increased expression of Gi GTP-binding proteins linked to phospholipase C signaling pathway
    • Senyshyn J., Baumgartner R.A., Beaven M.A. Quercetin sensitizes RBL-2H3 cells to polybasic mast cell secretagogues through increased expression of Gi GTP-binding proteins linked to phospholipase C signaling pathway. J. Immunol. 160:1998;5136-5144.
    • (1998) J. Immunol. , vol.160 , pp. 5136-5144
    • Senyshyn, J.1    Baumgartner, R.A.2    Beaven, M.A.3
  • 18
    • 0027143916 scopus 로고
    • Quercetin-induced expression of rat mast cell protease II and accumulation of secretory granules in rat basophilic leukemia cells
    • Trnovsky J., Letourneau R., Haggag E., Boucher W., Theoharides T.C. Quercetin-induced expression of rat mast cell protease II and accumulation of secretory granules in rat basophilic leukemia cells. Biochem. Pharmacol. 46:1993;2315-2326.
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 2315-2326
    • Trnovsky, J.1    Letourneau, R.2    Haggag, E.3    Boucher, W.4    Theoharides, T.C.5
  • 19
    • 0017903789 scopus 로고
    • Selective precipitation of 32[P] onto filter papers
    • Reimann E.M., Umfleet R.A. Selective precipitation of 32[P] onto filter papers. Biochem. Biophys. Acta. 523:1978;516-521.
    • (1978) Biochem. Biophys. Acta , vol.523 , pp. 516-521
    • Reimann, E.M.1    Umfleet, R.A.2
  • 21
    • 0031041306 scopus 로고    scopus 로고
    • RGS proteins and signaling by heterotrimeric G proteins
    • Dohlman H.G., Thorner J. RGS proteins and signaling by heterotrimeric G proteins. J. Biol. Chem. 272:1997;3871-3874.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3871-3874
    • Dohlman, H.G.1    Thorner, J.2
  • 22
    • 0030907376 scopus 로고    scopus 로고
    • A new family of G-protein regulators - The RGS proteins
    • Koelle M.R. A new family of G-protein regulators - the RGS proteins. Curr. Opin. Cell. Biol. 9:1997;143-147.
    • (1997) Curr. Opin. Cell. Biol. , vol.9 , pp. 143-147
    • Koelle, M.R.1
  • 23
    • 0031916822 scopus 로고    scopus 로고
    • Mammalian RGS proteins: Barbarians at the gate
    • Berman D.M., Gilman A.G. Mammalian RGS proteins: barbarians at the gate. J. Biol. Chem. 273:1998;1269-1272.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1269-1272
    • Berman, D.M.1    Gilman, A.G.2
  • 24
    • 0031931196 scopus 로고    scopus 로고
    • Heterotrimeric G protein signaling: Roles in immune function and fine-tuning by RGS proteins
    • Kehrl J.H. Heterotrimeric G protein signaling: roles in immune function and fine-tuning by RGS proteins. Immunity. 8:1998;1-10.
    • (1998) Immunity , vol.8 , pp. 1-10
    • Kehrl, J.H.1
  • 25
    • 0029559788 scopus 로고
    • GAIP, a protein that specifically interacts with the trimeric G protein Gαi3, is a member of a protein family with a highly conserved core domain
    • de Vries L., Mousli M., Wurmser A., Farquhar M.G. GAIP, a protein that specifically interacts with the trimeric G protein Gαi3, is a member of a protein family with a highly conserved core domain. Proc. Natl. Acad. Sci. USA. 92:1995;11916-11920.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11916-11920
    • De Vries, L.1    Mousli, M.2    Wurmser, A.3    Farquhar, M.G.4
  • 26
    • 0022615827 scopus 로고
    • Effect of quercetin on ATP-driven pumps and glycolysis
    • Racker E. Effect of quercetin on ATP-driven pumps and glycolysis. Prog. Clin. Biol. Res. 213:1986;257-271.
    • (1986) Prog. Clin. Biol. Res. , vol.213 , pp. 257-271
    • Racker, E.1
  • 27
    • 0029148577 scopus 로고
    • Role for phosphatidylinositol 3-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells
    • Brown W.J., de Wald D.B., Emr S.D., Plutner H., Balch W.E. Role for phosphatidylinositol 3-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells. J. Cell. Biol. 130:1995;781-796.
    • (1995) J. Cell. Biol. , vol.130 , pp. 781-796
    • Brown, W.J.1    De Wald, D.B.2    Emr, S.D.3    Plutner, H.4    Balch, W.E.5
  • 28
    • 0029014963 scopus 로고
    • Activation of the mitogen-activated protein kinase/cytosolic phospholipase A2 pathway in a rat mast cell line. Indications of different pathways for release of arachidonic acid and secretory granules
    • Hirasawa N., Santini F., Beaven M.A. Activation of the mitogen-activated protein kinase/cytosolic phospholipase A2 pathway in a rat mast cell line. Indications of different pathways for release of arachidonic acid and secretory granules. J. Immunol. 154:1995;5391-5402.
    • (1995) J. Immunol. , vol.154 , pp. 5391-5402
    • Hirasawa, N.1    Santini, F.2    Beaven, M.A.3
  • 29
    • 0030842112 scopus 로고    scopus 로고
    • Relationship between flavonoid structure and inhibition of phosphatidylinositol 3-kinase: A comparison with tyrosine kinase and protein kinase C inhibition
    • Agullo G., Gamet P.L., Manenti S., Viala C., Remesy C., Chap H., Payrastre B. Relationship between flavonoid structure and inhibition of phosphatidylinositol 3-kinase: a comparison with tyrosine kinase and protein kinase C inhibition. Biochem. Pharmacol. 53:1997;1649-1657.
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 1649-1657
    • Agullo, G.1    Gamet, P.L.2    Manenti, S.3    Viala, C.4    Remesy, C.5    Chap, H.6    Payrastre, B.7
  • 30
    • 0025195169 scopus 로고
    • Ge: A GTP-binding protein mediating exocytosis
    • Gomperts B.D. Ge: a GTP-binding protein mediating exocytosis. Annu. Rev. Physiol. 52:1990;591-606.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 591-606
    • Gomperts, B.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.