메뉴 건너뛰기




Volumn 162, Issue 4, 1999, Pages 2243-2250

The role of actin microfilaments in the down-regulation of the degranulation response in RBL-2H3 mast cells

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; BETA N ACETYLHEXOSAMINIDASE; CALCIUM; CYTOCHALASIN D; F ACTIN; INHIBITOR PROTEIN; LATRUNCULIN; PERVANADATE; PHOSPHOLIPASE; PHOSPHOLIPASE A2; PHOSPHOLIPASE C; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG;

EID: 0033558012     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (121)

References (50)
  • 1
    • 0011720768 scopus 로고
    • Structure and function of the high-affinity receptor for immunoglobulin E
    • Holowka, D., and B. Baird 1990. Structure and function of the high-affinity receptor for immunoglobulin E. Cell. Mol. Mech. Inflam. 1:173.
    • (1990) Cell. Mol. Mech. Inflam. , vol.1 , pp. 173
    • Holowka, D.1    Baird, B.2
  • 2
    • 0026611231 scopus 로고
    • The receptor with high affinity for IgE
    • Metzger, H. 1992. The receptor with high affinity for IgE. Immunol. Rev. 125:37.
    • (1992) Immunol. Rev. , vol.125 , pp. 37
    • Metzger, H.1
  • 3
    • 0028106207 scopus 로고
    • The high affinity receptor for immunoglobulin E
    • Adamczewski, M., and J. P. Kinet. 1994. The high affinity receptor for immunoglobulin E. Chem. Immunol. 59:173.
    • (1994) Chem. Immunol. , vol.59 , pp. 173
    • Adamczewski, M.1    Kinet, J.P.2
  • 4
    • 0029000726 scopus 로고
    • Early events in mast cell signal transduction
    • Scharenberg, A. M., and J. P. Kinet. 1995. Early events in mast cell signal transduction. Chem. Immunol. 61:72.
    • (1995) Chem. Immunol. , vol.61 , pp. 72
    • Scharenberg, A.M.1    Kinet, J.P.2
  • 5
    • 0029115648 scopus 로고
    • Protein tyrosine phosphorylation as a mechanism of signaling in mast cells and basophils
    • Hamawy, M. M., S. E. Mergehhagen, and R. P. Siraganian. 1995. Protein tyrosine phosphorylation as a mechanism of signaling in mast cells and basophils. Cell. Signalling 7:535.
    • (1995) Cell. Signalling , vol.7 , pp. 535
    • Hamawy, M.M.1    Mergehhagen, S.E.2    Siraganian, R.P.3
  • 6
    • 0029242504 scopus 로고
    • Signal transduction through the conserved motifs of the high affinity IgE receptor Fc∈RI
    • Jouvin, M. H., R. P. Numerof, and J. P. Kinet. 1995. Signal transduction through the conserved motifs of the high affinity IgE receptor Fc∈RI. Semin. Immunol. 7:29.
    • (1995) Semin. Immunol. , vol.7 , pp. 29
    • Jouvin, M.H.1    Numerof, R.P.2    Kinet, J.P.3
  • 7
    • 0030457522 scopus 로고    scopus 로고
    • Downstream signals initiated in mast cells by Fc∈RI and other receptors
    • Beaven, M. A. and R. A. Baumgartner. 1996. Downstream signals initiated in mast cells by Fc∈RI and other receptors. Curr. Opin. Immunol. 8:766.
    • (1996) Curr. Opin. Immunol. , vol.8 , pp. 766
    • Beaven, M.A.1    Baumgartner, R.A.2
  • 8
    • 0028035310 scopus 로고
    • Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation
    • Pribluda, V. S., C. Pribluda, and H. Metzger. 1994. Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation. Proc. Natl. Acad. Sci. USA 91:11246.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11246
    • Pribluda, V.S.1    Pribluda, C.2    Metzger, H.3
  • 10
    • 0029097912 scopus 로고
    • The role of actin filament barbed-end exposure in cytoskeletal dynamics and cell motility
    • Barkalow, K., and J. H. Hartwig. 1995. The role of actin filament barbed-end exposure in cytoskeletal dynamics and cell motility. Biochem. Soc. Trans. 23: 451.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 451
    • Barkalow, K.1    Hartwig, J.H.2
  • 12
    • 0031580210 scopus 로고    scopus 로고
    • Control of actin dynamics in cell motility
    • Carlier, M. F., and D. Pantaloni. 1997. Control of actin dynamics in cell motility. J. Mol. Biol. 269:459.
    • (1997) J. Mol. Biol. , vol.269 , pp. 459
    • Carlier, M.F.1    Pantaloni, D.2
  • 16
    • 0022371565 scopus 로고
    • Membrane and cytoskeletal changes associated with IgE-mediated serotonin release from rat basophilic leukemia cells
    • Pfeiffer, J. R., J. C. Seagrave, B H. Davis, G. G. Deanin, and J. M. Oliver. 1985. Membrane and cytoskeletal changes associated with IgE-mediated serotonin release from rat basophilic leukemia cells. J. Cell Biol. 101:2145.
    • (1985) J. Cell Biol. , vol.101 , pp. 2145
    • Pfeiffer, J.R.1    Seagrave, J.C.2    Davis, B.H.3    Deanin, G.G.4    Oliver, J.M.5
  • 17
    • 0026090189 scopus 로고
    • Regulation of the antigen-induced F-actin response in rat basophilic leukemia cells by protein kinase C
    • Apgar, J. R. 1991. Regulation of the antigen-induced F-actin response in rat basophilic leukemia cells by protein kinase C. J. Cell Biol. 112:1157.
    • (1991) J. Cell Biol. , vol.112 , pp. 1157
    • Apgar, J.R.1
  • 18
    • 0029013069 scopus 로고
    • Activation of protein kinase C in rat basophilic leukemia cells stimulates increased production of phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate: Correlation with actin polymerization
    • Apgar, J. 1995. Activation of protein kinase C in rat basophilic leukemia cells stimulates increased production of phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate: correlation with actin polymerization. Mol. Biol. Cell 6:97.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 97
    • Apgar, J.1
  • 19
    • 0028066617 scopus 로고
    • Tyrosine kinase-dependent assembly of actin plaques linking Fc∈RI cross-linking to increased cell substrate adhesion in RBL-2H3 tumor mast cells
    • Pfeiffer, J. R., and J. M. Oliver. 1994. Tyrosine kinase-dependent assembly of actin plaques linking Fc∈RI cross-linking to increased cell substrate adhesion in RBL-2H3 tumor mast cells. J. Immunol. 152:270.
    • (1994) J. Immunol. , vol.152 , pp. 270
    • Pfeiffer, J.R.1    Oliver, J.M.2
  • 20
    • 0029119988 scopus 로고
    • Focal adhesion formation is associated with secretion of allergic mediators
    • Kawasugi, K., P. W. French, R. Penny, and R. I. Ludowyke. 1995. Focal adhesion formation is associated with secretion of allergic mediators. Cell Motil. Cytoskeleton 31:215.
    • (1995) Cell Motil. Cytoskeleton , vol.31 , pp. 215
    • Kawasugi, K.1    French, P.W.2    Penny, R.3    Ludowyke, R.I.4
  • 22
    • 0026710617 scopus 로고
    • Peroxides of vanadate induce activation of phospholipase D in HL-60 cells: Role of tyrosine phosphorylation
    • Bourgoin, S., and S. Grinstein. 1992. Peroxides of vanadate induce activation of phospholipase D in HL-60 cells: role of tyrosine phosphorylation. J. Biol. Chem. 267:11908.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11908
    • Bourgoin, S.1    Grinstein, S.2
  • 23
    • 0026584237 scopus 로고
    • Evidence for a gelsolin-rich, labile F-actin pool in human polymorphonuclear leukocytes
    • Watts, R., and T. H. Howard. 1992. Evidence for a gelsolin-rich, labile F-actin pool in human polymorphonuclear leukocytes. Cell Motil. Cytoskel. 21:25.
    • (1992) Cell Motil. Cytoskel. , vol.21 , pp. 25
    • Watts, R.1    Howard, T.H.2
  • 24
    • 0031006342 scopus 로고    scopus 로고
    • 2, C, and D activity in RBL cells stimulated through Fc∈R1 is due to spreading and not simply adhesion
    • 2, C, and D activity in RBL cells stimulated through Fc∈R1 is due to spreading and not simply adhesion. J. Cell Sci. 110:771.
    • (1997) J. Cell Sci. , vol.110 , pp. 771
    • Apgar, J.R.1
  • 25
    • 0024208737 scopus 로고
    • T cell receptor-mediated signalling occurs in the absence of inositol phosphate production
    • O'Rourke, A. M., and M. F. Mescher. 1988. T cell receptor-mediated signalling occurs in the absence of inositol phosphate production. J. Biol. Chem. 263:18594.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18594
    • O'Rourke, A.M.1    Mescher, M.F.2
  • 26
    • 0020465411 scopus 로고
    • Lithium amplifies agonist-dependent phosphatidylinositol responses in brain and salivary glands
    • Berridge, M. J., C. P. Downes, and M. R. Hanley. 1982. Lithium amplifies agonist-dependent phosphatidylinositol responses in brain and salivary glands. Biochem. J. 206:587.
    • (1982) Biochem. J. , vol.206 , pp. 587
    • Berridge, M.J.1    Downes, C.P.2    Hanley, M.R.3
  • 27
    • 0026788301 scopus 로고
    • Phosphatidylcholine-specific phospholipase D-derived 1,2-diacylglycerol does not initiate protein kinase C activation in the RBL 2H3 mast-cell line
    • Lin, P., W. J. C. Fung, and A. M. Gilfillan. 1992. Phosphatidylcholine-specific phospholipase D-derived 1,2-diacylglycerol does not initiate protein kinase C activation in the RBL 2H3 mast-cell line. Biochem. J. 287:325.
    • (1992) Biochem. J. , vol.287 , pp. 325
    • Lin, P.1    Fung, W.J.C.2    Gilfillan, A.M.3
  • 28
    • 0025254238 scopus 로고
    • An indirect pathway of receptor-mediated 1,2-diacylglycerol formation in mast cell. I. IgE receptor-mediated activation of phospholipase D
    • Gruchalla, R. S., T. T. Dinh, and D. A. Kennerly. 1990. An indirect pathway of receptor-mediated 1,2-diacylglycerol formation in mast cell. I. IgE receptor-mediated activation of phospholipase D. J. Immunol. 144:2334.
    • (1990) J. Immunol. , vol.144 , pp. 2334
    • Gruchalla, R.S.1    Dinh, T.T.2    Kennerly, D.A.3
  • 29
    • 0024360298 scopus 로고
    • Latrunculins-novel marine macrolides that disrupt microfilament organization and affect cell growth. I. Comparison with cytochalasin D
    • Spector, I., N. R. Shochet, D. Blasberger, and Y. Kashman. 1989. Latrunculins-novel marine macrolides that disrupt microfilament organization and affect cell growth. I. Comparison with cytochalasin D. Cell Motil. Cytoskel. 13:127.
    • (1989) Cell Motil. Cytoskel. , vol.13 , pp. 127
    • Spector, I.1    Shochet, N.R.2    Blasberger, D.3    Kashman, Y.4
  • 30
    • 0023142377 scopus 로고
    • Inhibition of actin polymerization by latrunculin A
    • Coue, M., S. L. Brenner, I. Spector, and E. D. Korn. 1987. Inhibition of actin polymerization by latrunculin A. FEBS Lett. 213:316.
    • (1987) FEBS Lett. , vol.213 , pp. 316
    • Coue, M.1    Brenner, S.L.2    Spector, I.3    Korn, E.D.4
  • 31
    • 0027190844 scopus 로고
    • Mechanisms for actin reorganization in chemotactic factor-activated polymorphonuclear leukocytes
    • Watts, R. G., and T. H. Howard. 1993. Mechanisms for actin reorganization in chemotactic factor-activated polymorphonuclear leukocytes. Blood 81:2750.
    • (1993) Blood , vol.81 , pp. 2750
    • Watts, R.G.1    Howard, T.H.2
  • 32
    • 0028985349 scopus 로고
    • Dynamics of Triton-insoluble and Triton-soluble F-actin pools in calcium-activated human polymorphonuclear leukocytes: Evidence for regulation by gelsolin
    • Watts, R. G., J. D. Deaton, and T. H. Howard. 1995. Dynamics of Triton-insoluble and Triton-soluble F-actin pools in calcium-activated human polymorphonuclear leukocytes: evidence for regulation by gelsolin. Cell Motil. Cytoskel. 30:136.
    • (1995) Cell Motil. Cytoskel. , vol.30 , pp. 136
    • Watts, R.G.1    Deaton, J.D.2    Howard, T.H.3
  • 33
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • Cooper, J. A. 1987. Effects of cytochalasin and phalloidin on actin. J. Cell Biol. 105:1473.
    • (1987) J. Cell Biol. , vol.105 , pp. 1473
    • Cooper, J.A.1
  • 34
    • 0028177358 scopus 로고
    • Role of tropomyosin, α-actinin, and actin binding protein 280 in stabilizing Triton insoluble F-actin in basal and chemotactic factor activated neutrophils
    • Watts, R. G., and T. H. Howard. 1994. Role of tropomyosin, α-actinin, and actin binding protein 280 in stabilizing Triton insoluble F-actin in basal and chemotactic factor activated neutrophils. Cell Motil. Cytoskel. 28:155.
    • (1994) Cell Motil. Cytoskel. , vol.28 , pp. 155
    • Watts, R.G.1    Howard, T.H.2
  • 35
    • 0023341187 scopus 로고
    • DNP-phycobiliproteins, fluorescent antigens to study dynamic properties of antigen-IgE receptor complexes on RBL-2H3 rat mast cells
    • Seagrave, J. C., G. G. Deanin, J. C. Martin, B. H. Davis, and J. M. Oliver. 1987. DNP-phycobiliproteins, fluorescent antigens to study dynamic properties of antigen-IgE receptor complexes on RBL-2H3 rat mast cells. Cytometry 8:287.
    • (1987) Cytometry , vol.8 , pp. 287
    • Seagrave, J.C.1    Deanin, G.G.2    Martin, J.C.3    Davis, B.H.4    Oliver, J.M.5
  • 36
    • 0023548004 scopus 로고
    • Regulation of the affinity state of the N-formylated peptide receptor of neutrophils: Role of guanine nucleotide-binding proteins and the cytoskeleton
    • Painter, R. G., K. Zahler-Bentz, and R. E. Dukes. 1987. Regulation of the affinity state of the N-formylated peptide receptor of neutrophils: role of guanine nucleotide-binding proteins and the cytoskeleton. J. Cell Biol. 105:2959.
    • (1987) J. Cell Biol. , vol.105 , pp. 2959
    • Painter, R.G.1    Zahler-Bentz, K.2    Dukes, R.E.3
  • 37
    • 0023690739 scopus 로고
    • Lateral segregation of neutrophil chemotactic receptors into actin- and fodrin-rich membrane microdomains depleted in guanyl nucleotide regulatory proteins
    • Jesaitis, A. J., G. M. Bokoch, J. O. Tolley, and R. A. Allen. 1988. Lateral segregation of neutrophil chemotactic receptors into actin- and fodrin-rich membrane microdomains depleted in guanyl nucleotide regulatory proteins. J. Cell Biol. 107:921.
    • (1988) J. Cell Biol. , vol.107 , pp. 921
    • Jesaitis, A.J.1    Bokoch, G.M.2    Tolley, J.O.3    Allen, R.A.4
  • 38
    • 0024787850 scopus 로고
    • Regulation of chemoattractant receptor interaction with transducing proteins by organizational control in the plasma membrane of human neutrophils
    • Jesaitis, A. J., J. O. Tolley, G. M. Bokoch, and R. A. Allen. 1989. Regulation of chemoattractant receptor interaction with transducing proteins by organizational control in the plasma membrane of human neutrophils. J. Cell Biol. 109:2783.
    • (1989) J. Cell Biol. , vol.109 , pp. 2783
    • Jesaitis, A.J.1    Tolley, J.O.2    Bokoch, G.M.3    Allen, R.A.4
  • 39
    • 0027998862 scopus 로고
    • Differential control of the tyrosine kinases Lyn and Syk by the two signaling chains of the high affinity immunoglobulin E receptor
    • Jouvin, M. H. E., M. Adamczewski, R. Numerof, O. Letourneur, A. Valle, and J. P. Kinet. 1994. Differential control of the tyrosine kinases Lyn and Syk by the two signaling chains of the high affinity immunoglobulin E receptor. J. Biol. Chem. 269:5918.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5918
    • Jouvin, M.H.E.1    Adamczewski, M.2    Numerof, R.3    Letourneur, O.4    Valle, A.5    Kinet, J.P.6
  • 40
    • 0030849446 scopus 로고    scopus 로고
    • The unique domain as the site on Lyn kinase for its constitutive association with the high affinity receptor for IgE
    • Vonakis, B. M., H. Chen, H. Haleem-Smith, and H. Metzger. 1997. The unique domain as the site on Lyn kinase for its constitutive association with the high affinity receptor for IgE. J. Biol. Chem. 272:24072.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24072
    • Vonakis, B.M.1    Chen, H.2    Haleem-Smith, H.3    Metzger, H.4
  • 41
    • 0030604541 scopus 로고    scopus 로고
    • The Fc∈RIβ subunit functions as an amplifier of Fc∈RIγ-mediated cell activation signals
    • Lin, S., C. Cicala, A. M. Scharenberg, and J. P. Kinet. 1996. The Fc∈RIβ subunit functions as an amplifier of Fc∈RIγ-mediated cell activation signals. Cell 85:985.
    • (1996) Cell , vol.85 , pp. 985
    • Lin, S.1    Cicala, C.2    Scharenberg, A.M.3    Kinet, J.P.4
  • 43
    • 0031041581 scopus 로고    scopus 로고
    • Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains
    • Field, K. A., D. Holowka, and B. Baird. 1997. Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains. J. Biol. Chem. 272:4276.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4276
    • Field, K.A.1    Holowka, D.2    Baird, B.3
  • 44
    • 0031452944 scopus 로고    scopus 로고
    • Compartmentalized IgE receptor-mediated signal transduction in living cells
    • Stauffer, T. P., and T. Meyer. 1997. Compartmentalized IgE receptor-mediated signal transduction in living cells. J. Cell Biol. 139:1447.
    • (1997) J. Cell Biol. , vol.139 , pp. 1447
    • Stauffer, T.P.1    Meyer, T.2
  • 45
    • 0025951923 scopus 로고
    • Phosphorylation and dephosphorylation of the high-affinity receptor for immunoglobulin E immediately after receptor engagement and disengagement
    • Paolini, R., M. H. Jouvin, and J. P. Kinet. 1991. Phosphorylation and dephosphorylation of the high-affinity receptor for immunoglobulin E immediately after receptor engagement and disengagement. Nature 353:855.
    • (1991) Nature , vol.353 , pp. 855
    • Paolini, R.1    Jouvin, M.H.2    Kinet, J.P.3
  • 46
    • 0024241284 scopus 로고
    • A monoclonal antibody that inhibits secretion from rat basophilic leukemia cells and binds to a novel membrane component
    • Soto, E. O., and I. Pecht. 1988. A monoclonal antibody that inhibits secretion from rat basophilic leukemia cells and binds to a novel membrane component. J. Immunol 141:4324.
    • (1988) J. Immunol. , vol.141 , pp. 4324
    • Soto, E.O.1    Pecht, I.2
  • 47
    • 0028842110 scopus 로고
    • Regulation of high-affinity IgE receptor-mediated mast cell activation by murine low-affinity IgG receptors
    • Daeron, M., O. Malbec, S. Latour, M. Arock, and W. H. Fridman. 1995. Regulation of high-affinity IgE receptor-mediated mast cell activation by murine low-affinity IgG receptors. J. Clin. Invest. 95:577.
    • (1995) J. Clin. Invest. , vol.95 , pp. 577
    • Daeron, M.1    Malbec, O.2    Latour, S.3    Arock, M.4    Fridman, W.H.5
  • 48
    • 0031157104 scopus 로고    scopus 로고
    • A newly recognized pathway for the negative regulation of mast cell-dependent hypersensitivity and inflammation mediated by an endogenous cell surface receptor of the gp49 family
    • Katz, H. R., and K. F. Austen. 1997 A newly recognized pathway for the negative regulation of mast cell-dependent hypersensitivity and inflammation mediated by an endogenous cell surface receptor of the gp49 family. J. Immunol. 158:5065.
    • (1997) J. Immunol. , vol.158 , pp. 5065
    • Katz, H.R.1    Austen, K.F.2
  • 49
    • 0031030037 scopus 로고    scopus 로고
    • Shuttling of initiating kinase between discrete aggregates of the high affinity receptor for IgE regulates the cellular response
    • Torigoe, C., B. Goldstein, C. Wofsy, and H. Metzger. 1997. Shuttling of initiating kinase between discrete aggregates of the high affinity receptor for IgE regulates the cellular response. Proc Natl. Acad Sci. USA 94:1372.
    • (1997) Proc Natl. Acad Sci. USA , vol.94 , pp. 1372
    • Torigoe, C.1    Goldstein, B.2    Wofsy, C.3    Metzger, H.4
  • 50
    • 0026777097 scopus 로고
    • Adherence of rat basophilic leukemia (RBL-2H3) cells to fibronectin-coated surfaces enhances secretion
    • Hamawy, M. M., C. Oliver, S. E. Mergenhagen, and R. P. Siraganian. 1992. Adherence of rat basophilic leukemia (RBL-2H3) cells to fibronectin-coated surfaces enhances secretion. J. Immunol. 149:615.
    • (1992) J. Immunol. , vol.149 , pp. 615
    • Hamawy, M.M.1    Oliver, C.2    Mergenhagen, S.E.3    Siraganian, R.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.