메뉴 건너뛰기




Volumn 102, Issue 2, 1998, Pages 304-315

Identification of the FcεRI-activated tyrosine kinases Lyn, Syk, and Zap-70 in human basophils

Author keywords

Allergy; Basophils; IgE; IgE receptor; Signal transduction; Tyrosine kinases

Indexed keywords

FC RECEPTOR; PROTEIN TYROSINE KINASE; 3,3',4,5'-TETRAHYDROXYSTILBENE; ENZYME INHIBITOR; IMMUNOGLOBULIN E RECEPTOR; LYN PROTEIN-TYROSINE KINASE; PICEATANNOL; PROTEIN KINASE LYN; PROTEIN KINASE ZAP 70; STILBENE DERIVATIVE; TYRO3 PROTEIN, HUMAN; ZAP70 PROTEIN, HUMAN;

EID: 0031595219     PISSN: 00916749     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0091-6749(98)70100-9     Document Type: Article
Times cited : (60)

References (89)
  • 1
    • 0028118817 scopus 로고
    • Expression of functional high affinity inimunoglobulin E receptors (FcεRI) on monocytes of atopic individuals
    • Maurer D, Fiebiger E, Reininger B, WolffoWiniski B, Jouvin M-H, Kilgus O, et al. Expression of functional high affinity inimunoglobulin E receptors (FcεRI) on monocytes of atopic individuals. J Exp Med 1994;179:745-50.
    • (1994) J Exp Med , vol.179 , pp. 745-750
    • Maurer, D.1    Fiebiger, E.2    Reininger, B.3    Wolffowiniski, B.4    Jouvin, M.-H.5    Kilgus, O.6
  • 2
    • 0039820128 scopus 로고
    • High-affinity IgE receptor on eosinophils is involved in defense against parasites
    • Gounni AS, Lamkhioued B, Ochiai K, Tanaka Y, Delaporte E, Capron A, et al. High-affinity IgE receptor on eosinophils is involved in defense against parasites. Nature 1994;367:183-6.
    • (1994) Nature , vol.367 , pp. 183-186
    • Gounni, A.S.1    Lamkhioued, B.2    Ochiai, K.3    Tanaka, Y.4    Delaporte, E.5    Capron, A.6
  • 3
    • 0026583666 scopus 로고
    • Epidermal Langerhans cells from normal human skin bind monomeric IgE via FcεRI
    • Wang B, Rieger A, Kilgus O, Ochiai K, Maurer D, Fodinger D, et al. Epidermal Langerhans cells from normal human skin bind monomeric IgE via FcεRI. J Exp Med 1992;175:1353-65.
    • (1992) J Exp Med , vol.175 , pp. 1353-1365
    • Wang, B.1    Rieger, A.2    Kilgus, O.3    Ochiai, K.4    Maurer, D.5    Fodinger, D.6
  • 4
    • 8944239404 scopus 로고    scopus 로고
    • Peripheral blood dendritic cells express FcεRI as a complex composed of FcεRIα- And FcεRI-gamma-chains and can use this receptor for IgE-mediated allergen presentation
    • Maurer D, Fiebiger E, Ebner C, Reininger B, Fischer GF, Wichlas S, et al. Peripheral blood dendritic cells express FcεRI as a complex composed of FcεRIα- and FcεRI-gamma-chains and can use this receptor for IgE-mediated allergen presentation. J Immunol 1996;157:607-16.
    • (1996) J Immunol , vol.157 , pp. 607-616
    • Maurer, D.1    Fiebiger, E.2    Ebner, C.3    Reininger, B.4    Fischer, G.F.5    Wichlas, S.6
  • 5
    • 0026514978 scopus 로고
    • Human epidermal Langerhans cells express the high affinity receptor for immunoglobulin E (FcεRI)
    • Bieber T, Salle H, Wollenberg A, Hakimi J, Chizzonite R, Ring J, et al. Human epidermal Langerhans cells express the high affinity receptor for immunoglobulin E (FcεRI). J Exp Med 1992;175:1285-90.
    • (1992) J Exp Med , vol.175 , pp. 1285-1290
    • Bieber, T.1    Salle, H.2    Wollenberg, A.3    Hakimi, J.4    Chizzonite, R.5    Ring, J.6
  • 6
    • 0026601947 scopus 로고
    • Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases
    • Eiseman E, Bolen JB. Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases. Nature 1992;355:78-80.
    • (1992) Nature , vol.355 , pp. 78-80
    • Eiseman, E.1    Bolen, J.B.2
  • 7
    • 0026611481 scopus 로고
    • FcεRI-mediated tyrosine phosphorylation and activation of the 72-kDa protein-tyrosine kinase, PTK72, in RBL-2H3 rat tumor mast cells
    • Hutchcroft JE, Geahlen RL, Deanin GG, Oliver JM. FcεRI-mediated tyrosine phosphorylation and activation of the 72-kDa protein-tyrosine kinase, PTK72, in RBL-2H3 rat tumor mast cells. Proc Natl Acad Sci U S A 1992;89:9107-11.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 9107-9111
    • Hutchcroft, J.E.1    Geahlen, R.L.2    Deanin, G.G.3    Oliver, J.M.4
  • 8
    • 0027433055 scopus 로고
    • Protein-tyrosine kinase p72syk in high affinity IgE receptor signaling: Identification as a component of pp72 and association with the receptor gamma chain after receptor aggregation
    • Benhamou M, Ryba NJ, Kihara H, Nishikata H, Siraganian RP. Protein-tyrosine kinase p72syk in high affinity IgE receptor signaling: identification as a component of pp72 and association with the receptor gamma chain after receptor aggregation. J Biol Chem 1993;268:23318-24.
    • (1993) J Biol Chem , vol.268 , pp. 23318-23324
    • Benhamou, M.1    Ryba, N.J.2    Kihara, H.3    Nishikata, H.4    Siraganian, R.P.5
  • 10
    • 0026611231 scopus 로고
    • The receptor with high affinity for IgE
    • Metzger H. The receptor with high affinity for IgE. Immunol Rev 1992;125:37-48.
    • (1992) Immunol Rev , vol.125 , pp. 37-48
    • Metzger, H.1
  • 12
    • 3042769995 scopus 로고    scopus 로고
    • Wortmannin-sensitive phosphorylation, translocation and activation of PLCγl, but not PLCγ2, in antigen-stimulated RBL-2H3 mast cells
    • Barker SA, Caldwell KK, Pfeiffer JR, Wilson BS. Wortmannin-sensitive phosphorylation, translocation and activation of PLCγl, but not PLCγ2, in antigen-stimulated RBL-2H3 mast cells. Mol Cell Biol 1998;6:1145-58.
    • (1998) Mol Cell Biol , vol.6 , pp. 1145-1158
    • Barker, S.A.1    Caldwell, K.K.2    Pfeiffer, J.R.3    Wilson, B.S.4
  • 13
    • 0026352438 scopus 로고
    • IgE-induced tyrosine phosphorylation of phospholipase C-γ 1 in rat basophilic leukemia cells
    • Park DJ, Min HK, Rhee SG. IgE-induced tyrosine phosphorylation of phospholipase C-γ 1 in rat basophilic leukemia cells. J Biol Chem 1991;266:24237-40.
    • (1991) J Biol Chem , vol.266 , pp. 24237-24240
    • Park, D.J.1    Min, H.K.2    Rhee, S.G.3
  • 14
    • 0029115917 scopus 로고
    • Wortmannin blocks lipid and protein kinase activities associated with PI-3-kinase and inhibits a specific subset of responses induced by FcεRI crosslinking
    • Barker S, Caldwell K, Hall A, Martinez AM, Pfeiffer JR, Oliver JM, et al. Wortmannin blocks lipid and protein kinase activities associated with PI-3-kinase and inhibits a specific subset of responses induced by FcεRI crosslinking. Mol Biol Cell 1995;6:1145-58.
    • (1995) Mol Biol Cell , vol.6 , pp. 1145-1158
    • Barker, S.1    Caldwell, K.2    Hall, A.3    Martinez, A.M.4    Pfeiffer, J.R.5    Oliver, J.M.6
  • 15
    • 0027374488 scopus 로고
    • Inhibition of histamine secretion by Wortmannin through the blockade of phosphatidylinositol 3-kinase in RBL-2H3 cells
    • Yano H, Nakanishi S, Kimura K, Hanai N, Saitoh Y, Fukui Y, et al. Inhibition of histamine secretion by Wortmannin through the blockade of phosphatidylinositol 3-kinase in RBL-2H3 cells. J Biol Chem 1993;268:25846-56.
    • (1993) J Biol Chem , vol.268 , pp. 25846-25856
    • Yano, H.1    Nakanishi, S.2    Kimura, K.3    Hanai, N.4    Saitoh, Y.5    Fukui, Y.6
  • 16
    • 0028968081 scopus 로고
    • Purification of a major tyrosine kinase from RBL-2H3 cells phosphorylating FcεRI γ-cytoplasmic domain and identification as the Btk tyrosine kinase
    • Price DJ, Kawakami Y, Kawakami T, Rivnay B. Purification of a major tyrosine kinase from RBL-2H3 cells phosphorylating FcεRI γ-cytoplasmic domain and identification as the Btk tyrosine kinase. Biochim Biophys Acta 1995;1265:133-42.
    • (1995) Biochim Biophys Acta , vol.1265 , pp. 133-142
    • Price, D.J.1    Kawakami, Y.2    Kawakami, T.3    Rivnay, B.4
  • 17
    • 0026535589 scopus 로고
    • Tyrosine phosphorylation of vav proto-oncogene product containing SH2 domain and transcription factor motifs
    • Margolis B, Hu P, Katzav S, Li W, Oliver JM, Ullrich A, et al. Tyrosine phosphorylation of vav proto-oncogene product containing SH2 domain and transcription factor motifs. Nature 1992;356:71-4.
    • (1992) Nature , vol.356 , pp. 71-74
    • Margolis, B.1    Hu, P.2    Katzav, S.3    Li, W.4    Oliver, J.M.5    Ullrich, A.6
  • 18
    • 0028897659 scopus 로고
    • Regulation of the adapter molecule Grb2 by the FcεRI in the mast cell line RBL2H3
    • Turner H, Reif K, Rivera J, Cantrell DA. Regulation of the adapter molecule Grb2 by the FcεRI in the mast cell line RBL2H3. J Biol Chem 1995;270:9500-6.
    • (1995) J Biol Chem , vol.270 , pp. 9500-9506
    • Turner, H.1    Reif, K.2    Rivera, J.3    Cantrell, D.A.4
  • 19
    • 0027496310 scopus 로고
    • rsk and pp70-S6 kinases in mouse mast cells by signaling through the c-kit receptor tyrosine kinase or FcεRI: Rapamycin inhibits activation of pp70-S6 kinase and proliferation in mouse mast cells
    • rsk and pp70-S6 kinases in mouse mast cells by signaling through the c-kit receptor tyrosine kinase or FcεRI: rapamycin inhibits activation of pp70-S6 kinase and proliferation in mouse mast cells. Eur J Immunol 1993;23:3286-91.
    • (1993) Eur J Immunol , vol.23 , pp. 3286-3291
    • Tsai, M.1    Chen, R.-H.2    Tam, S.-Y.3    Blenis, J.4    Galli, S.J.5
  • 20
    • 0027975334 scopus 로고
    • Stimulation of mitogen-activated protein kinase activity by different secretory stimuli in rat basophilic leukemia cells
    • Offermanns S, Jones SVP, Bombien E, Schultz G. Stimulation of mitogen-activated protein kinase activity by different secretory stimuli in rat basophilic leukemia cells. J Immunol 1994;152:250-61.
    • (1994) J Immunol , vol.152 , pp. 250-261
    • Offermanns, S.1    Jones, S.V.P.2    Bombien, E.3    Schultz, G.4
  • 21
    • 0027374512 scopus 로고
    • Tyrosine phosphorylation of a mitogen-activated protein kinase-like protein occurs at a late step in exocytosis: Studies with tyrosine phosphatase inhibitors and various secretagogues in rat RBL-2H3 cells
    • Santini F, Beaven MA. Tyrosine phosphorylation of a mitogen-activated protein kinase-like protein occurs at a late step in exocytosis: studies with tyrosine phosphatase inhibitors and various secretagogues in rat RBL-2H3 cells. J Biol Chem 1993;268:22716-22.
    • (1993) J Biol Chem , vol.268 , pp. 22716-22722
    • Santini, F.1    Beaven, M.A.2
  • 22
    • 0005928594 scopus 로고    scopus 로고
    • Regulation and roles of the membrane, cytoskeletal and adhesive responses of RBL-2H3 rat tumor mast cells to FcεRI crosslinking
    • Hamawy MM, editor. Austin, Tex.: R.G. Landes
    • Oliver JM, Pfeiffer JR, Wilson BS. Regulation and roles of the membrane, cytoskeletal and adhesive responses of RBL-2H3 rat tumor mast cells to FcεRI crosslinking. In: Hamawy MM, editor. IgE receptor (FcεRI) in mast cells and basophils. Austin, Tex.: R.G. Landes; 1997. p. 139-66.
    • (1997) IgE Receptor (FcεRI) in Mast Cells and Basophils , pp. 139-166
    • Oliver, J.M.1    Pfeiffer, J.R.2    Wilson, B.S.3
  • 23
    • 0025116160 scopus 로고
    • Signal transduction events in human basophils: A comparative study of the role of protein kinase C in basophils activated by anti-IgE antibody and formyl-methionyl-leucylphenylalanine
    • Warner JA, MacGlashan DW Jr. Signal transduction events in human basophils: a comparative study of the role of protein kinase C in basophils activated by anti-IgE antibody and formyl-methionyl-leucylphenylalanine. J Immunol 1990;145:1897-905.
    • (1990) J Immunol , vol.145 , pp. 1897-1905
    • Warner, J.A.1    MacGlashan Jr., D.W.2
  • 24
    • 0026055094 scopus 로고
    • Oscillations in free cytosolic calcium during IgE-mediated stimulation distinguish human basophils from human mast cells
    • MacGlashan D Jr, Guo C-B. Oscillations in free cytosolic calcium during IgE-mediated stimulation distinguish human basophils from human mast cells. J Immunol 1991;147:2259-69.
    • (1991) J Immunol , vol.147 , pp. 2259-2269
    • MacGlashan Jr., D.1    Guo, C.-B.2
  • 25
    • 0024502165 scopus 로고
    • Protein kinase C (PKC) changes in human basophils: IgE-mediated activation is accompanied by an increase in total PKC activity
    • Warner JA, MacGlashan DW Jr. Protein kinase C (PKC) changes in human basophils: IgE-mediated activation is accompanied by an increase in total PKC activity. J Immunol 1989;142:1669-77.
    • (1989) J Immunol , vol.142 , pp. 1669-1677
    • Warner, J.A.1    MacGlashan Jr., D.W.2
  • 26
    • 0025275159 scopus 로고
    • Differential mechanisms in the stimulus-secretion coupling in human basophils: Evidence for a protein-kinase-C-dependent and a protein-kinase-C-independent route
    • Knol EF, Koenderman L, Mul E, Verhoeven AJ, Roos D. Differential mechanisms in the stimulus-secretion coupling in human basophils: evidence for a protein-kinase-C-dependent and a protein-kinase-C-independent route. Agents Actions 1990;30:49-52.
    • (1990) Agents Actions , vol.30 , pp. 49-52
    • Knol, E.F.1    Koenderman, L.2    Mul, E.3    Verhoeven, A.J.4    Roos, D.5
  • 27
    • 0028078912 scopus 로고
    • Graded changes in the response of individual human basophils to stimulation: Distributional behavior of early activation events
    • MacGlashan DW Jr, Bochner BS, Warner JA. Graded changes in the response of individual human basophils to stimulation: distributional behavior of early activation events. J Leukoc Biol 1994;55:13-23.
    • (1994) J Leukoc Biol , vol.55 , pp. 13-23
    • MacGlashan Jr., D.W.1    Bochner, B.S.2    Warner, J.A.3
  • 28
    • 0021299354 scopus 로고
    • Basophils and mast cells: Morphologic insights into their biology, secretory patterns, and function
    • Galli SJ, Dvorak AM, Dvorak HE. Basophils and mast cells: morphologic insights into their biology, secretory patterns, and function. Prog Allergy 1984;34:1-141.
    • (1984) Prog Allergy , vol.34 , pp. 1-141
    • Galli, S.J.1    Dvorak, A.M.2    Dvorak, H.E.3
  • 31
    • 0028999779 scopus 로고
    • Signal transduction and cytokine production by human basophils
    • MacGlashan DW Jr. Signal transduction and cytokine production by human basophils. Chem Immunol 1995;61:88-113.
    • (1995) Chem Immunol , vol.61 , pp. 88-113
    • MacGlashan Jr., D.W.1
  • 33
    • 0020537586 scopus 로고
    • Studies of antigen binding on human basophils, I: Antigen binding and functional consequences
    • MacGlashan DW, Lichtenstein LM. Studies of antigen binding on human basophils, I: antigen binding and functional consequences. J Immunol 1983;130:2330-6.
    • (1983) J Immunol , vol.130 , pp. 2330-2336
    • MacGlashan, D.W.1    Lichtenstein, L.M.2
  • 34
    • 0027417128 scopus 로고
    • Releasability of human basophils: Cellular sensitivity and maximal histamine release are independent variables
    • MacGlashan DW Jr. Releasability of human basophils: cellular sensitivity and maximal histamine release are independent variables. J Allergy Clin Immunol 1993;91:605-15.
    • (1993) J Allergy Clin Immunol , vol.91 , pp. 605-615
    • MacGlashan Jr., D.W.1
  • 36
    • 0018908440 scopus 로고
    • Receptor cross-linking and histamine release in basophils
    • Chabay R, DeLisi C, Hook WA, Siraganian RP. Receptor cross-linking and histamine release in basophils. J Biol Chem 1980;255:4628-35.
    • (1980) J Biol Chem , vol.255 , pp. 4628-4635
    • Chabay, R.1    DeLisi, C.2    Hook, W.A.3    Siraganian, R.P.4
  • 37
    • 0025336023 scopus 로고
    • A comparative study of releasing and nonreleasing human basophils: Nonreleasing basophils lack an early component of the signal transduction pathway that follows IgE cross-linking
    • Nguyen K-L, Gillis S, MacGlashan DW Jr. A comparative study of releasing and nonreleasing human basophils: nonreleasing basophils lack an early component of the signal transduction pathway that follows IgE cross-linking. J Allergy Clin Immunol 1990;85:1020-9.
    • (1990) J Allergy Clin Immunol , vol.85 , pp. 1020-1029
    • Nguyen, K.-L.1    Gillis, S.2    MacGlashan Jr., D.W.3
  • 38
  • 39
    • 0015846644 scopus 로고
    • Mechanisms of passive sensitization, III: Number of IgE molecules and their receptor sites on human basophil granulocytes
    • Ishizaka T, Soto CS, Ishizaka K. Mechanisms of passive sensitization, III: number of IgE molecules and their receptor sites on human basophil granulocytes. J Immunol 1973;111:500-11.
    • (1973) J Immunol , vol.111 , pp. 500-511
    • Ishizaka, T.1    Soto, C.S.2    Ishizaka, K.3
  • 40
    • 0024364046 scopus 로고
    • Differential release of mediators from human basophils: Differences in arachidonic acid metabolism following activation by unrelated stimuli
    • Warner JA, Peters SP, Lichtenstein LM, Hubbard W, Yancey KB, Stevenson HC, et al. Differential release of mediators from human basophils: differences in arachidonic acid metabolism following activation by unrelated stimuli. J Leukocyte Biol 1989;45:558-71.
    • (1989) J Leukocyte Biol , vol.45 , pp. 558-571
    • Warner, J.A.1    Peters, S.P.2    Lichtenstein, L.M.3    Hubbard, W.4    Yancey, K.B.5    Stevenson, H.C.6
  • 41
    • 0024440150 scopus 로고
    • Recombinant human IL-1α and -1β potentiate IgE-mediated histamine release from human basophils
    • Massey WA, Randall TC, Kagey-Sobotka A, Warner JA, MacDonald SM, Gillis S, et al. Recombinant human IL-1α and -1β potentiate IgE-mediated histamine release from human basophils. J Immunol 1989;143:1875-80.
    • (1989) J Immunol , vol.143 , pp. 1875-1880
    • Massey, W.A.1    Randall, T.C.2    Kagey-Sobotka, A.3    Warner, J.A.4    MacDonald, S.M.5    Gillis, S.6
  • 42
    • 0025133290 scopus 로고
    • Interleukin 3 and granulocyte/macrophage-colony-stimulating factor render human basophils responsive to low concentrations of complement component C3a
    • Bischoff SC, De Weck AL, Dahinden CA. Interleukin 3 and granulocyte/macrophage-colony-stimulating factor render human basophils responsive to low concentrations of complement component C3a. Proc Natl Acad Sci U S A 1990;87:6813-7.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 6813-6817
    • Bischoff, S.C.1    De Weck, A.L.2    Dahinden, C.A.3
  • 43
    • 0025647484 scopus 로고
    • Interleukin 5 modifies histamine release and leukotriene generation by human basophils in response to diverse agonists
    • Bischoff SC, Brunner T, De Weck AL, Dahinden CA. Interleukin 5 modifies histamine release and leukotriene generation by human basophils in response to diverse agonists. J Exp Med 1990;172:1577-82.
    • (1990) J Exp Med , vol.172 , pp. 1577-1582
    • Bischoff, S.C.1    Brunner, T.2    De Weck, A.L.3    Dahinden, C.A.4
  • 44
    • 0027511738 scopus 로고
    • RANTES and related chemokines activate human basophil granulocytes through different G protein-coupled receptors
    • Bischoff SC, Krieger M, Brunner T, Rot A, Tscharner V, Baggiolini M, et al. RANTES and related chemokines activate human basophil granulocytes through different G protein-coupled receptors. Eur J Immunol 1993;23:761-7.
    • (1993) Eur J Immunol , vol.23 , pp. 761-767
    • Bischoff, S.C.1    Krieger, M.2    Brunner, T.3    Rot, A.4    Tscharner, V.5    Baggiolini, M.6
  • 47
    • 0026543877 scopus 로고
    • Monocyte chemotactic and activating factor is a potent histamine-releasing factor forhuman basophils
    • Kuna P, Reddigari SR, Rucinski D, Oppenheim JJ, Kaplan AP. Monocyte chemotactic and activating factor is a potent histamine-releasing factor forhuman basophils. J Exp Med 1992;175:489-93.
    • (1992) J Exp Med , vol.175 , pp. 489-493
    • Kuna, P.1    Reddigari, S.R.2    Rucinski, D.3    Oppenheim, J.J.4    Kaplan, A.P.5
  • 48
    • 0026506889 scopus 로고
    • Connective tissue-activating peptide-III and its derivative, neu-trophil-activating peptide-2, release histamine from human basophils
    • Reddigari SR, Kuna P, Miragliotta GF, Kornfeld D, Baeza ML, Castor CW, et al. Connective tissue-activating peptide-III and its derivative, neu-trophil-activating peptide-2, release histamine from human basophils. J Allergy Clin Immunol 1992;89:666-72.
    • (1992) J Allergy Clin Immunol , vol.89 , pp. 666-672
    • Reddigari, S.R.1    Kuna, P.2    Miragliotta, G.F.3    Kornfeld, D.4    Baeza, M.L.5    Castor, C.W.6
  • 49
    • 0027159569 scopus 로고
    • Characterization of the human basophil response to cytokines, growth factors, and histamine releasing factors of the intercrine/chemokine family
    • Kuna P, Reddigari SR, Schall TJ, Rucinski D, Sadick M, Kaplan AP. Characterization of the human basophil response to cytokines, growth factors, and histamine releasing factors of the intercrine/chemokine family. J Immunol 1993;150:1932-43.
    • (1993) J Immunol , vol.150 , pp. 1932-1943
    • Kuna, P.1    Reddigari, S.R.2    Schall, T.J.3    Rucinski, D.4    Sadick, M.5    Kaplan, A.P.6
  • 50
    • 0029029377 scopus 로고
    • Identification and partial characterization of a unique marker for human basophils
    • Kepley CL, Craig SS, Schwartz LB. Identification and partial characterization of a unique marker for human basophils. J Immunol 1995;154:6548-55.
    • (1995) J Immunol , vol.154 , pp. 6548-6555
    • Kepley, C.L.1    Craig, S.S.2    Schwartz, L.B.3
  • 51
    • 0026079536 scopus 로고
    • Generation and use of anti-phosphotyrosine antibodies for immun ob lotting
    • Kamps MP. Generation and use of anti-phosphotyrosine antibodies for immun ob lotting. Methods Enzymol 1991;201:101-10.
    • (1991) Methods Enzymol , vol.201 , pp. 101-110
    • Kamps, M.P.1
  • 52
    • 0025822648 scopus 로고
    • High affinity human IgE receptor (FcεRI): Analysis of functional domains of the α-subunit with monoclonal antibodies
    • Riske F, Hakim J, Mallamaci M, Griffin M, Pilson B, Tobkes N, et al. High affinity human IgE receptor (FcεRI): analysis of functional domains of the α-subunit with monoclonal antibodies. J Biol Chem 1991;266:11245-51.
    • (1991) J Biol Chem , vol.266 , pp. 11245-11251
    • Riske, F.1    Hakim, J.2    Mallamaci, M.3    Griffin, M.4    Pilson, B.5    Tobkes, N.6
  • 53
    • 0025946132 scopus 로고
    • Molecular cloning of a porcine gene syk that encodes a 72-kDa protein-tyrosine kinase showing high susceptibility to proteolysis
    • Taniguchi T, Kobayashi T, Kondo J, Takahashi K, Nakamura H, Suzuki J, et al. Molecular cloning of a porcine gene syk that encodes a 72-kDa protein-tyrosine kinase showing high susceptibility to proteolysis. J Biol Chem 1991;266:15790-6.
    • (1991) J Biol Chem , vol.266 , pp. 15790-15796
    • Taniguchi, T.1    Kobayashi, T.2    Kondo, J.3    Takahashi, K.4    Nakamura, H.5    Suzuki, J.6
  • 54
    • 0027990449 scopus 로고
    • Purification of human basophils by density and size alone
    • Kepley C, Craig S, Schwartz L. Purification of human basophils by density and size alone. J Immunol Methods 1994;175:1-9.
    • (1994) J Immunol Methods , vol.175 , pp. 1-9
    • Kepley, C.1    Craig, S.2    Schwartz, L.3
  • 55
    • 0027472874 scopus 로고
    • Purification of human blood basophils by negative selection using immunomagnetic beads
    • Bjerke T, Nielsen S, Helgestad J, Nielsen BW, Schiotz PO. Purification of human blood basophils by negative selection using immunomagnetic beads. J Immunol Methods 1993;157:49-56.
    • (1993) J Immunol Methods , vol.157 , pp. 49-56
    • Bjerke, T.1    Nielsen, S.2    Helgestad, J.3    Nielsen, B.W.4    Schiotz, P.O.5
  • 56
    • 0015289322 scopus 로고
    • The relationship of the chemotactic behavior of the complement-derived factors, C3a, C5a, and C567, and a bacterial chemotactic factor to their ability to activate the proesterase 1 of rabbit polymorphonuclear leukocytes
    • Becker EL. The relationship of the chemotactic behavior of the complement-derived factors, C3a, C5a, and C567, and a bacterial chemotactic factor to their ability to activate the proesterase 1 of rabbit polymorphonuclear leukocytes. J Exp Med 1972;135:376-87.
    • (1972) J Exp Med , vol.135 , pp. 376-387
    • Becker, E.L.1
  • 57
    • 0028072499 scopus 로고
    • Inhibition of mast cell FcεRI-mediated signaling and effector function by the Syk-selective inhibitor, piceatannol
    • Oliver JM, Burg DL, Wilson BS, McLaughlin JL, Geahlen RL. Inhibition of mast cell FcεRI-mediated signaling and effector function by the Syk-selective inhibitor, piceatannol. J Biol Chem 1994;269:29697-703.
    • (1994) J Biol Chem , vol.269 , pp. 29697-29703
    • Oliver, J.M.1    Burg, D.L.2    Wilson, B.S.3    McLaughlin, J.L.4    Geahlen, R.L.5
  • 58
    • 0028985471 scopus 로고
    • Distinct functions of the FcεRI γ and β subunits in the control of FcεRI-mediated tyrosine kinase activation and signaling responses in RBL-2H3 mast cells
    • Wilson BS, Kapp N, Lee RJ, Pfeiffer JR, Martinez AM, Platt Y, et al. Distinct functions of the FcεRI γ and β subunits in the control of FcεRI-mediated tyrosine kinase activation and signaling responses in RBL-2H3 mast cells. J Biol Chem 1995;270:4013-22.
    • (1995) J Biol Chem , vol.270 , pp. 4013-4022
    • Wilson, B.S.1    Kapp, N.2    Lee, R.J.3    Pfeiffer, J.R.4    Martinez, A.M.5    Platt, Y.6
  • 59
    • 0028321540 scopus 로고
    • Molecular cloning of human Syk: A B cell protein-tyrosine kinase associated with the surface immunoglobulin M-B cell receptor complex
    • Law CL, Sidorenko SP, Chandran KA, Draves KE, Chan AC, Weiss A, et al. Molecular cloning of human Syk: A B cell protein-tyrosine kinase associated with the surface immunoglobulin M-B cell receptor complex. J Biol Chem 1994;269:12310-9.
    • (1994) J Biol Chem , vol.269 , pp. 12310-12319
    • Law, C.L.1    Sidorenko, S.P.2    Chandran, K.A.3    Draves, K.E.4    Chan, A.C.5    Weiss, A.6
  • 60
    • 0026688237 scopus 로고
    • The B cell antigen receptor complex: Association of Ig-alpha and Ig-beta with distinct cytoplasmic effectors
    • Clark MR, Campbell KS, Kazlauskas A, Johnson SA, Hertz M, Potter TA, et al. The B cell antigen receptor complex: association of Ig-alpha and Ig-beta with distinct cytoplasmic effectors. Science 1992;258:123-6.
    • (1992) Science , vol.258 , pp. 123-126
    • Clark, M.R.1    Campbell, K.S.2    Kazlauskas, A.3    Johnson, S.A.4    Hertz, M.5    Potter, T.A.6
  • 61
    • 0030996848 scopus 로고    scopus 로고
    • ZAP-70 protein tyrosine kinase is constitutively targeted to the T cell cortex independently of its SH2 domains
    • Huby RDJ, Iwashima M, Weiss A, Ley SC. ZAP-70 protein tyrosine kinase is constitutively targeted to the T cell cortex independently of its SH2 domains. J Cell Biol 1997;137:1639-49.
    • (1997) J Cell Biol , vol.137 , pp. 1639-1649
    • Huby, R.D.J.1    Iwashima, M.2    Weiss, A.3    Ley, S.C.4
  • 62
    • 0029115648 scopus 로고
    • Protein tyrosine phosphorylation as a mechanism of signalling in mast cells and basophils
    • Hamawy MM, Mergenhagen SE, Siraganian RP Protein tyrosine phosphorylation as a mechanism of signalling in mast cells and basophils. Cell Signal 1995;7:535-44.
    • (1995) Cell Signal , vol.7 , pp. 535-544
    • Hamawy, M.M.1    Mergenhagen, S.E.2    Siraganian, R.P.3
  • 63
    • 0019141549 scopus 로고
    • A model of cell activation and desensitization by surface immunoglobin: The case of histamine release from human basophils
    • Dembo M, Goldstein B. A model of cell activation and desensitization by surface immunoglobin: the case of histamine release from human basophils. Cell 1980;22:59-67.
    • (1980) Cell , vol.22 , pp. 59-67
    • Dembo, M.1    Goldstein, B.2
  • 64
    • 0020049819 scopus 로고
    • Role of receptor aggregation in triggering IgE-mediated reactions
    • Kagey-Sobotka A, MacGlashan DW, Lichtenstein LM. Role of receptor aggregation in triggering IgE-mediated reactions. Fed Proc 1982;41:12-6.
    • (1982) Fed Proc , vol.41 , pp. 12-16
    • Kagey-Sobotka, A.1    MacGlashan, D.W.2    Lichtenstein, L.M.3
  • 66
    • 0026350671 scopus 로고
    • Hematopoietic cells express two forms of lyn kinase differing by 21 amino acids in the amino terminus
    • Yi TL, Bolen JB, Ihle JN. Hematopoietic cells express two forms of lyn kinase differing by 21 amino acids in the amino terminus. Mol Cell Biol 1991;11:2391-8.
    • (1991) Mol Cell Biol , vol.11 , pp. 2391-2398
    • Yi, T.L.1    Bolen, J.B.2    Ihle, J.N.3
  • 67
    • 0025185003 scopus 로고
    • Src-related tyrosine protein kinases as signaling components in hematopoietic cells
    • Eiseman E, Bolen JB. src-related tyrosine protein kinases as signaling components in hematopoietic cells. Cancer Cells 1990;2:303-10.
    • (1990) Cancer Cells , vol.2 , pp. 303-310
    • Eiseman, E.1    Bolen, J.B.2
  • 68
    • 0024313880 scopus 로고
    • Selective expression of a protein-tyrosine kinase, p561yn, in hematopoietic cells and association with production of human T-cell lymphotropic virus type I
    • Yamanashi Y, Mori S, Yoshida M, Kishimoto T, Inoue K, Yamamoto T, et al. Selective expression of a protein-tyrosine kinase, p561yn, in hematopoietic cells and association with production of human T-cell lymphotropic virus type I. Proc Natl Acad Sci U S A 1989;86:6538-42.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 6538-6542
    • Yamanashi, Y.1    Mori, S.2    Yoshida, M.3    Kishimoto, T.4    Inoue, K.5    Yamamoto, T.6
  • 69
    • 0026656317 scopus 로고
    • Association of the 72-kDa protein-tyrosine kinase PTK72 with the B cell antigen receptor
    • Hutchcroft JE, Harrison ML, Geahlen RL. Association of the 72-kDa protein-tyrosine kinase PTK72 with the B cell antigen receptor. J Biol Chem 1992;267:8613-9.
    • (1992) J Biol Chem , vol.267 , pp. 8613-8619
    • Hutchcroft, J.E.1    Harrison, M.L.2    Geahlen, R.L.3
  • 70
    • 0027338195 scopus 로고
    • Involvement of p72syk, a protein-tyrosine kinase, in Fcγ receptor signaling
    • Agarwal A, Salem P, Robbins KC. Involvement of p72syk, a protein-tyrosine kinase, in Fcγ receptor signaling. J Biol Chem 1993;268:15900-5.
    • (1993) J Biol Chem , vol.268 , pp. 15900-15905
    • Agarwal, A.1    Salem, P.2    Robbins, K.C.3
  • 71
    • 0027406756 scopus 로고
    • Protein-tyrosine kinase p72syk is activated by thrombin and is negatively regulated through Ca2+ mobilization in platelets
    • Taniguchi T, Kitagawa H, Yasue S, Yanagi S, Sakai K, Asahi M, et al. Protein-tyrosine kinase p72syk is activated by thrombin and is negatively regulated through Ca2+ mobilization in platelets. J Biol Chem 1993;268:2277-9.
    • (1993) J Biol Chem , vol.268 , pp. 2277-2279
    • Taniguchi, T.1    Kitagawa, H.2    Yasue, S.3    Yanagi, S.4    Sakai, K.5    Asahi, M.6
  • 72
    • 0025942245 scopus 로고
    • The zeta chain is associated with a tyrosine kinase and upon T-cell antigen receptor stimulation associates with ZAP-70, a 70-kDa tyrosine phosphoprotein
    • Chan AC, Irving BA, Fraser JD, Weiss A. The zeta chain is associated with a tyrosine kinase and upon T-cell antigen receptor stimulation associates with ZAP-70, a 70-kDa tyrosine phosphoprotein. Proc Natl Acad Sci USA 1991;88:9166-70.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9166-9170
    • Chan, A.C.1    Irving, B.A.2    Fraser, J.D.3    Weiss, A.4
  • 73
    • 0028216232 scopus 로고
    • Differential expression of ZAP-70 and Syk protein tyrosine kinases, and the role of this family of protein tyrosine kinases in TCR signaling
    • Chan AC, van Oers NS, Tran A, Turka L, Law CL, Ryan JC, et al. Differential expression of ZAP-70 and Syk protein tyrosine kinases, and the role of this family of protein tyrosine kinases in TCR signaling. J Immunol 1994;152:4758-66.
    • (1994) J Immunol , vol.152 , pp. 4758-4766
    • Chan, A.C.1    Van Oers, N.S.2    Tran, A.3    Turka, L.4    Law, C.L.5    Ryan, J.C.6
  • 74
    • 0026483786 scopus 로고
    • ZAP-70: A 70 kd protein-tyrosine kinase that associates with the TCR-ζ chain
    • Chan AC, Iwashima M, Turck CW, Weiss A. ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR-ζ chain. Cell 1992;71:649-62.
    • (1992) Cell , vol.71 , pp. 649-662
    • Chan, A.C.1    Iwashima, M.2    Turck, C.W.3    Weiss, A.4
  • 75
    • 0029063151 scopus 로고
    • Analysis of the interaction of ZAP-70 and syk protein-tyrosine kinases with the T-cell antigen receptor by plasmon resonance
    • Bu JY, Shaw AS, Chan AC. Analysis of the interaction of ZAP-70 and syk protein-tyrosine kinases with the T-cell antigen receptor by plasmon resonance. Proc Natl Acad Sci U S A 1995;92:5106-10.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 5106-5110
    • Bu, J.Y.1    Shaw, A.S.2    Chan, A.C.3
  • 76
    • 0029114537 scopus 로고
    • Determinants of the phagocytic signal mediated by the type IIIA Fcγ receptor, FcγRIIIA: Sequence requirements and interaction with protein-tyrosine kinases
    • Park JG, Schreiber AD. Determinants of the phagocytic signal mediated by the type IIIA Fcγ receptor, FcγRIIIA: sequence requirements and interaction with protein-tyrosine kinases. Proc Natl Acad Sci USA 1995;92:7381-5.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7381-7385
    • Park, J.G.1    Schreiber, A.D.2
  • 77
    • 0025007179 scopus 로고
    • CD3 ζ subunit can substitute for the subunit of Fcε receptor type I in assembly and functional expression of the high-affinity IgE receptor: Evidence for inter-receptor complementation
    • Howard FD, Rodewald HR, Kinet JP, Reinherz EL. CD3 ζ subunit can substitute for the subunit of Fcε receptor type I in assembly and functional expression of the high-affinity IgE receptor: evidence for inter-receptor complementation. Proc Natl Acad Sci U S A 1990;87:7015-9.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 7015-7019
    • Howard, F.D.1    Rodewald, H.R.2    Kinet, J.P.3    Reinherz, E.L.4
  • 78
    • 0031181191 scopus 로고    scopus 로고
    • FcεRI γ can support T cell development and function in mice lacking endogenous TCR ζ-chain
    • Shores E, Flamand V, Tran T, Grinberg A, Kinet JP, Love PE. FcεRI γ can support T cell development and function in mice lacking endogenous TCR ζ-chain. J Immunol 1997;159:222-30.
    • (1997) J Immunol , vol.159 , pp. 222-230
    • Shores, E.1    Flamand, V.2    Tran, T.3    Grinberg, A.4    Kinet, J.P.5    Love, P.E.6
  • 79
    • 9244246767 scopus 로고    scopus 로고
    • Protein tyrosine kinases in activation signal of human basophils through the immunoglobulin E receptor type 1
    • Benhamou M, Feuillard J, Lortholary O, Bourgeois C, Michel L, LeGoff, L, et al. Protein tyrosine kinases in activation signal of human basophils through the immunoglobulin E receptor type 1. J Leukoc Biol 1996;59:461-70.
    • (1996) J Leukoc Biol , vol.59 , pp. 461-470
    • Benhamou, M.1    Feuillard, J.2    Lortholary, O.3    Bourgeois, C.4    Michel, L.5    LeGoff, L.6
  • 80
    • 0019792538 scopus 로고
    • IgE-mediated histamine release from human basophils: Differences between antigen E- And anti-IgE-induced secretion
    • Marone G, Kagey-Sobotka A, Lichtenstein LM. IgE-mediated histamine release from human basophils: differences between antigen E- and anti-IgE-induced secretion. Int Arch Allergy Appl Immunol 1981;65:339-48.
    • (1981) Int Arch Allergy Appl Immunol , vol.65 , pp. 339-348
    • Marone, G.1    Kagey-Sobotka, A.2    Lichtenstein, L.M.3
  • 81
    • 0022615314 scopus 로고
    • Characteristics of human basophil sulfidopeptide leukotreine release: Releasability defined as the ability of basophils to respond to dimeric cross-links
    • MacGlashan DW Jr, Peters SP, Warner J, Lichtenstein LM. Characteristics of human basophil sulfidopeptide leukotreine release: releasability defined as the ability of basophils to respond to dimeric cross-links. J Immunol 1986;136:2231-9.
    • (1986) J Immunol , vol.136 , pp. 2231-2239
    • MacGlashan Jr., D.W.1    Peters, S.P.2    Warner, J.3    Lichtenstein, L.M.4
  • 82
    • 0014873793 scopus 로고
    • In vitro reversed anaphylaxis: Characteristics of anti-IgE mediated histamine release
    • Lichtenstein LM, Levy DA, Ishizaka K. In vitro reversed anaphylaxis: characteristics of anti-IgE mediated histamine release. Immunology 1970;19:831-42.
    • (1970) Immunology , vol.19 , pp. 831-842
    • Lichtenstein, L.M.1    Levy, D.A.2    Ishizaka, K.3
  • 83
    • 0023903732 scopus 로고
    • Assessment of IgE-receptor function through measurement of hydrolysis of membrane inositol phospholipids: New insights on the phenomena of biphasic antigen concentration-response curves and desensitization
    • Maeyama K, Hohman RJ, Ali H, Cunha-Melo JR, Beaven MA. Assessment of IgE-receptor function through measurement of hydrolysis of membrane inositol phospholipids: new insights on the phenomena of biphasic antigen concentration-response curves and desensitization. J Immunol 1988;140:3919-27.
    • (1988) J Immunol , vol.140 , pp. 3919-3927
    • Maeyama, K.1    Hohman, R.J.2    Ali, H.3    Cunha-Melo, J.R.4    Beaven, M.A.5
  • 84
    • 0027270134 scopus 로고
    • Heterologous desensitization of the high affinity receptor for IgE (FcεRI) on RBL cells
    • Weetall M, Holowka D, Baird B. Heterologous desensitization of the high affinity receptor for IgE (FcεRI) on RBL cells. J Immunol 1993;150:4072-83.
    • (1993) J Immunol , vol.150 , pp. 4072-4083
    • Weetall, M.1    Holowka, D.2    Baird, B.3
  • 85
    • 0027338322 scopus 로고
    • Immobilization of Fcε receptors by wheat germ agglutinin: Receptor dynamics in IgE-mediated signal transduction
    • McCloskey MA. Immobilization of Fcε receptors by wheat germ agglutinin: receptor dynamics in IgE-mediated signal transduction. J Immunol 1993;151:3237-51.
    • (1993) J Immunol , vol.151 , pp. 3237-3251
    • McCloskey, M.A.1
  • 86
    • 0029154906 scopus 로고
    • Kinetics of tyrosine phosphorylation when IgE dimers bind to Fc-ε receptors on rat basophilic leukemia cells
    • Wofsy C, Kent UM, Mao SY, Metzger H, Goldstein B. Kinetics of tyrosine phosphorylation when IgE dimers bind to Fc-ε receptors on rat basophilic leukemia cells. J Biol Chem 1995;270:20264-72.
    • (1995) J Biol Chem , vol.270 , pp. 20264-20272
    • Wofsy, C.1    Kent, U.M.2    Mao, S.Y.3    Metzger, H.4    Goldstein, B.5
  • 87
    • 0030058977 scopus 로고    scopus 로고
    • Persistence of tyrosine-phosphorylated FcεRI in deactivated cells
    • Paolini R, Serra A, Kinet JP. Persistence of tyrosine-phosphorylated FcεRI in deactivated cells. J Biol Chem 1996;271:15987-92.
    • (1996) J Biol Chem , vol.271 , pp. 15987-15992
    • Paolini, R.1    Serra, A.2    Kinet, J.P.3
  • 88
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of src
    • Brown MT, Cooper JA. Regulation, substrates and functions of src. Biochim Biophys Acta 1996;1287:121-49.
    • (1996) Biochim Biophys Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 89
    • 0029803010 scopus 로고    scopus 로고
    • The inositol 5′-phosphatase SHIP binds to immunoreceptor signaling motifs and responds to high affinity IgE receptor aggregation
    • Osborne MA, Zenner G, Lubinus M, Zhang X, Songyang Z, Cantley LC, et al. The inositol 5′-phosphatase SHIP binds to immunoreceptor signaling motifs and responds to high affinity IgE receptor aggregation. J Biol Chem 1996;271:29271-8.
    • (1996) J Biol Chem , vol.271 , pp. 29271-29278
    • Osborne, M.A.1    Zenner, G.2    Lubinus, M.3    Zhang, X.4    Songyang, Z.5    Cantley, L.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.