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Volumn 65, Issue 3, 1999, Pages 321-329

Multiple roles for PI 3-kinase in the regulation of PLCγ activity and Ca2+ mobilization in antigen-stimulated mast cells

Author keywords

Calcium; Fc RI; Phospholipase C; PI 3 kinase

Indexed keywords

ANTIGEN; CALCIUM ION; IMMUNOGLOBULIN E; INOSITOL 1,4,5 TRISPHOSPHATE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOLIPASE C; PROTEIN TYROSINE KINASE; THAPSIGARGIN; TYROSINE; WORTMANNIN;

EID: 0033052935     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: 10.1002/jlb.65.3.321     Document Type: Review
Times cited : (74)

References (55)
  • 1
    • 0028043846 scopus 로고
    • Biological function of PDGF-induced PI-3 kinase activity: Its role in PDGF receptor-mediated mitogenic signaling
    • Yu, J., Gutkind, J. S., Mahadevan, D., Li, W., Meyers, K. A., Pierce, J. H., Heidaran, M. A. (1994) Biological function of PDGF-induced PI-3 kinase activity: its role in PDGF receptor-mediated mitogenic signaling. J. Cell Biol. 127, 479-487.
    • (1994) J. Cell Biol. , vol.127 , pp. 479-487
    • Yu, J.1    Gutkind, J.S.2    Mahadevan, D.3    Li, W.4    Meyers, K.A.5    Pierce, J.H.6    Heidaran, M.A.7
  • 2
    • 0028260280 scopus 로고
    • Inhibition of the translocation of GLUT1 and GLUT4 in 3T3-L1 cells by the phosphatidylinositol 3-kinase inhibitor, wortmannin
    • Clarke, J. F., Young, P. W., Yonezawa, K., Kasuga, M., Holman, G. D. (1994) Inhibition of the translocation of GLUT1 and GLUT4 in 3T3-L1 cells by the phosphatidylinositol 3-kinase inhibitor, wortmannin. J. Biochem. 300, 631-635.
    • (1994) J. Biochem. , vol.300 , pp. 631-635
    • Clarke, J.F.1    Young, P.W.2    Yonezawa, K.3    Kasuga, M.4    Holman, G.D.5
  • 3
    • 0030993451 scopus 로고    scopus 로고
    • PH domains - A universal membrane adaptor
    • Hemmings, B. A. (1997) PH domains - a universal membrane adaptor. Science 275, 1899.
    • (1997) Science , vol.275 , pp. 1899
    • Hemmings, B.A.1
  • 4
    • 0028486018 scopus 로고
    • Phosphatidylinositol 3-kinase
    • Kapeller, R., Cantley, L. C. (1994) Phosphatidylinositol 3-kinase. BioEssays 16, 565-576.
    • (1994) BioEssays , vol.16 , pp. 565-576
    • Kapeller, R.1    Cantley, L.C.2
  • 5
    • 0029939448 scopus 로고    scopus 로고
    • PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface
    • Lemmon, M. A., Ferguson, K. M., Schlessinger, J. (1996) PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surface. Cell 85, 621-624.
    • (1996) Cell , vol.85 , pp. 621-624
    • Lemmon, M.A.1    Ferguson, K.M.2    Schlessinger, J.3
  • 6
    • 0028892253 scopus 로고
    • 3 interacts with SH2 domains and modulates PI 3-kinase association with tyrosine-phosphorylated proteins
    • 3 interacts with SH2 domains and modulates PI 3-kinase association with tyrosine-phosphorylated proteins. Cell 83, 821-830.
    • (1995) Cell , vol.83 , pp. 821-830
    • Rameh, L.E.1    Chen, S.-S.2    Cantley, L.C.3
  • 7
    • 0030992837 scopus 로고    scopus 로고
    • Signaling through the lipid products of phosphoinositide-3-OH kinase
    • Toker, A., Cantley, L. C. (1997) Signaling through the lipid products of phosphoinositide-3-OH kinase. Nature 387, 673-676.
    • (1997) Nature , vol.387 , pp. 673-676
    • Toker, A.1    Cantley, L.C.2
  • 8
    • 0031471231 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase-γ activates Bruton's tyrosine kinase in concert with Src family kinases
    • Li, Z., Wahl, M. I. Eguinoa, A., Stephens, L. R., Hawkins, P. T., Witte, O. N. (1997) Phosphatidylinositol 3-kinase-γ activates Bruton's tyrosine kinase in concert with Src family kinases. Proc. Natl. Acad. Sci. USA 94, 13820-13825.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13820-13825
    • Li, Z.1    Wahl, M.I.2    Eguinoa, A.3    Stephens, L.R.4    Hawkins, P.T.5    Witte, O.N.6
  • 9
    • 0028883178 scopus 로고
    • Phospholipid signaling
    • Divecha, N., Irvine, R. (1995) Phospholipid signaling. Cell 80, 269-278.
    • (1995) Cell , vol.80 , pp. 269-278
    • Divecha, N.1    Irvine, R.2
  • 10
    • 0029965452 scopus 로고    scopus 로고
    • Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of Lys-802, a residue involved in the phosphate transfer reaction
    • Wymann, M. P., Bulgarell-Leva, G., Zvelebil, M. J., Pirola, L., Vanhaesebroechk, B., Waterfield, M. D., Panayolou, O. (1996) Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of Lys-802, a residue involved in the phosphate transfer reaction. Mol. Cell Biol. 16, 1722-1733.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 1722-1733
    • Wymann, M.P.1    Bulgarell-Leva, G.2    Zvelebil, M.J.3    Pirola, L.4    Vanhaesebroechk, B.5    Waterfield, M.D.6    Panayolou, O.7
  • 11
    • 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., Nonomura, Y., Matsuda, Y. (1993) Inhibition of histamine secretion by wortmannin through the blockade of phosphatidylinositol 3-kinase in RBL-2H3 cells. J. Biol. Chem. 268, 25846-25856.
    • (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    Nonomura, Y.7    Matsuda, Y.8
  • 12
    • 0026777051 scopus 로고
    • Certain inhibitors of protein serine/threonine kinases also inhibit tyrosin phosphorylation of phospholipase Cγ1 and other proteins and reveal distinct roles for tyrosine kinases and protein kinase C in stimulated rat basophilic RBL-2H3 cells
    • Yamada, K., Jelsema, C. L., Beaven, M. A. (1992) Certain inhibitors of protein serine/threonine kinases also inhibit tyrosin phosphorylation of phospholipase Cγ1 and other proteins and reveal distinct roles for tyrosine kinases and protein kinase C in stimulated rat basophilic RBL-2H3 cells. J. Biol. Chem. 149, 1031-1037.
    • (1992) J. Biol. Chem. , vol.149 , pp. 1031-1037
    • Yamada, K.1    Jelsema, C.L.2    Beaven, M.A.3
  • 13
    • 0029115917 scopus 로고
    • Wortmannin blocks lipid and protein kinase activities associated with PI 3-kinase and inhibits a specific subset of responses induced by FcεR1 crosslinking
    • Barker, S. A., Caldwell, K. K., Martinez, A. M., Pfeiffer, J. R., Oliver, J. M., Wilson, B. S. (1995) Wortmannin blocks lipid and protein kinase activities associated with PI 3-kinase and inhibits a specific subset of responses induced by FcεR1 crosslinking. Mol. Biol. Cell 6, 1145-1158.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1145-1158
    • Barker, S.A.1    Caldwell, K.K.2    Martinez, A.M.3    Pfeiffer, J.R.4    Oliver, J.M.5    Wilson, B.S.6
  • 14
    • 0031906691 scopus 로고    scopus 로고
    • Wortmannin-sensitive phosphorylation, translocation, and activation of PLCγ1, but not PLCγ2, in antigen-stimulated RBL-2H3 mast cells
    • Barker, S. A., Caldwell, K. K., Pfeiffer, J. R., Wilson, B. S. (1998) Wortmannin-sensitive phosphorylation, translocation, and activation of PLCγ1, but not PLCγ2, in antigen-stimulated RBL-2H3 mast cells. Mol. Biol. Cell 9, 483-496.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 483-496
    • Barker, S.A.1    Caldwell, K.K.2    Pfeiffer, J.R.3    Wilson, B.S.4
  • 15
    • 0032518666 scopus 로고    scopus 로고
    • Activation of phospholipase Cγ by PI 3-kinase-induced PH domain-mediated membrane targeting
    • Falasca, M., Logan, S. K., Lehto, V. P., Bacannte, G., Lemmon, M. A., Schlessinger, J. (1998) Activation of phospholipase Cγ by PI 3-kinase-induced PH domain-mediated membrane targeting. EMBO J. 17, 411-422.
    • (1998) EMBO J. , vol.17 , pp. 411-422
    • Falasca, M.1    Logan, S.K.2    Lehto, V.P.3    Bacannte, G.4    Lemmon, M.A.5    Schlessinger, J.6
  • 16
    • 0030995012 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C isozymes
    • Rhee, S. G., Bae, Y. S. (1997) Regulation of phosphoinositide-specific phospholipase C isozymes. J. Biol. Chem. 272, 15045-15048.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15045-15048
    • Rhee, S.G.1    Bae, Y.S.2
  • 17
    • 0025805394 scopus 로고
    • PDGF stimulation of inositol phospholipid hydrolysis requires PLC-γ1 phosphorylation on tyrosine residues 783 and 1254
    • Kim, H. K., Kim, J. W., Zilberstein, A., Margolis, B., Kim, J. G., Schlessinger, J., Rhee, S. G. (1991) PDGF stimulation of inositol phospholipid hydrolysis requires PLC-γ1 phosphorylation on tyrosine residues 783 and 1254. Cell 65, 435-441.
    • (1991) Cell , vol.65 , pp. 435-441
    • Kim, H.K.1    Kim, J.W.2    Zilberstein, A.3    Margolis, B.4    Kim, J.G.5    Schlessinger, J.6    Rhee, S.G.7
  • 18
    • 0025923860 scopus 로고
    • 1 isoform with tyrosine kinase
    • 1 isoform with tyrosine kinase. Trends Biol. Sci. 351, 297-301.
    • (1991) Trends Biol. Sci. , vol.351 , pp. 297-301
    • Rhee, S.G.1
  • 19
    • 0029946425 scopus 로고    scopus 로고
    • Lipid products of phosphoinositide 3-kinase bind human profilin with high affinity
    • Lu, P-J., Shieh, W-R., Rhee, S. G., Yin, H. L., Chen, C-S. (1996) Lipid products of phosphoinositide 3-kinase bind human profilin with high affinity. Biochemistry 33, 14027-14034.
    • (1996) Biochemistry , vol.33 , pp. 14027-14034
    • Lu, P.-J.1    Shieh, W.-R.2    Rhee, S.G.3    Yin, H.L.4    Chen, C.-S.5
  • 20
    • 0344653108 scopus 로고    scopus 로고
    • Activation of phospholipase C-γ by phosphatidylinositol 3,4,5-triphosphate
    • Bae, Y. S., Cantley, L. G., Chen, C. S., Seung-Ryul, K., Kwon, K. S., Rhee, S. G. (1998) Activation of phospholipase C-γ by phosphatidylinositol 3,4,5-triphosphate. J. Biol. Chem. 273, 4465-4469.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4465-4469
    • Bae, Y.S.1    Cantley, L.G.2    Chen, C.S.3    Seung-Ryul, K.4    Kwon, K.S.5    Rhee, S.G.6
  • 22
    • 14444287277 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase regulates phospholipase Cγ-mediated calcium signaling
    • Rameh, L. E., Rhee, S. G., Spokes, K., Kazlauskas, A., Cantley, L. C., Cantley, L. G. (1998) Phosphoinositide 3-kinase regulates phospholipase Cγ-mediated calcium signaling. J. Biol. Chem. 273, 23750-23757.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23750-23757
    • Rameh, L.E.1    Rhee, S.G.2    Spokes, K.3    Kazlauskas, A.4    Cantley, L.C.5    Cantley, L.G.6
  • 24
    • 0021136105 scopus 로고
    • The mechanism of the calcium signal and correlation with histamine release in 2H3 cell
    • Beaven, M. A., Roger, J., Moore, J. P., Hesketh, T. R., Smith, G. A., Metcalfe, J. C. (1984) The mechanism of the calcium signal and correlation with histamine release in 2H3 cell. J. Biol. Chem. 259, 7129-7136.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7129-7136
    • Beaven, M.A.1    Roger, J.2    Moore, J.P.3    Hesketh, T.R.4    Smith, G.A.5    Metcalfe, J.C.6
  • 25
    • 0023664863 scopus 로고
    • The kinetics of phosphoinositide hydrolysis in rat basophilic leukemia (RBL-2H3) cells varies with the type of IgE cross-linking agent used
    • Cunha-Melo, J. R., Dean, N. M., Moyer, J. D., Maeyama, K., Beaven, M. A. (1987) The kinetics of phosphoinositide hydrolysis in rat basophilic leukemia (RBL-2H3) cells varies with the type of IgE cross-linking agent used. J. Biol. Chem. 262, 11455-11463.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11455-11463
    • Cunha-Melo, J.R.1    Dean, N.M.2    Moyer, J.D.3    Maeyama, K.4    Beaven, M.A.5
  • 26
    • 0023664901 scopus 로고
    • Evidence for an early rise in inositol 1,4,5-trisphosphate which precedes the rise in other inositol phosphates and in cytoplasmic calcium
    • Pribluda, V. S., Metzger, H. (1987) Evidence for an early rise in inositol 1,4,5-trisphosphate which precedes the rise in other inositol phosphates and in cytoplasmic calcium. J. Biol. Chem. 262, 11449-11454.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11449-11454
    • Pribluda, V.S.1    Metzger, H.2
  • 27
    • 0023879739 scopus 로고
    • Highly cooperative opening of calcium channels by inositol 1,4,5-trisphosphate
    • Meyer, T., Holowka, D., Stryer, L. (1988) Highly cooperative opening of calcium channels by inositol 1,4,5-trisphosphate. Science 240, 653-656.
    • (1988) Science , vol.240 , pp. 653-656
    • Meyer, T.1    Holowka, D.2    Stryer, L.3
  • 28
    • 0024385998 scopus 로고
    • Depletion of guanine nucleotides with mycophenolic acid supresses IgE receptor-mediated degranulation in rat basophilic leukemia cells
    • Wilson, B. S., Deanin, G. G., Standefer, J. D, Vanderjagt, D., Oliver, J. M. (1989) Depletion of guanine nucleotides with mycophenolic acid supresses IgE receptor-mediated degranulation in rat basophilic leukemia cells. J. Immunol. 143, 259-265.
    • (1989) J. Immunol. , vol.143 , pp. 259-265
    • Wilson, B.S.1    Deanin, G.G.2    Standefer, J.D.3    Vanderjagt, D.4    Oliver, J.M.5
  • 29
    • 0023767034 scopus 로고
    • Regulation of calcium influx by second messengers in rat mast cells
    • Penner, R., Matthews, G., Neher, E. (1988) Regulation of calcium influx by second messengers in rat mast cells. Nature 334, 499-504.
    • (1988) Nature , vol.334 , pp. 499-504
    • Penner, R.1    Matthews, G.2    Neher, E.3
  • 30
    • 0027175061 scopus 로고
    • Calcium release-activated calcium current in rat mast cells
    • Hoth, M., Penner, R. (1993) Calcium release-activated calcium current in rat mast cells. J. Physiol. 465, 359-386.
    • (1993) J. Physiol. , vol.465 , pp. 359-386
    • Hoth, M.1    Penner, R.2
  • 31
    • 0029996127 scopus 로고    scopus 로고
    • Calcium mobilization via sphingosine kinase in signaling by the FcεR1 antigen receptor
    • Choi O. H., Kim J. H., Kinet J. P. (1996) Calcium mobilization via sphingosine kinase in signaling by the FcεR1 antigen receptor. Nature 380, 634-636.
    • (1996) Nature , vol.380 , pp. 634-636
    • Choi, O.H.1    Kim, J.H.2    Kinet, J.P.3
  • 34
    • 0024346141 scopus 로고
    • Activation of calcium entry by the tumor promoter, thapsigargin, in parotid acinar cells
    • Takemura, H., Hughes, A. R., Thastrup, O., Putney, J. W. (1989) Activation of calcium entry by the tumor promoter, thapsigargin, in parotid acinar cells. J. Biol. Chem. 264, 12266-12271.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12266-12271
    • Takemura, H.1    Hughes, A.R.2    Thastrup, O.3    Putney, J.W.4
  • 36
    • 0026352438 scopus 로고
    • IgE-induced tyrosine phosphorylation of phospholipase C-γ1 in rat basophilic leukemia cells
    • Park, D. J., Min, H. K., Rhee, S. G. (1991) IgE-induced tyrosine phosphorylation of phospholipase C-γ1 in rat basophilic leukemia cells. J. Biol. Chem. 266, 24237-24240.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24237-24240
    • Park, D.J.1    Min, H.K.2    Rhee, S.G.3
  • 37
    • 0026612253 scopus 로고
    • FcεR1-mediated tyrosine phosphorylation of multiple proteins, including phospholipase Cγ1 and the receptor βγ2 complex, in RBL-2H3 rat basophilic leukemia cells
    • Li, W., Deanin, G. G., Margolis, B., Schlessinger, J., Oliver, J. M. (1992) FcεR1-mediated tyrosine phosphorylation of multiple proteins, including phospholipase Cγ1 and the receptor βγ2 complex, in RBL-2H3 rat basophilic leukemia cells. Mol. Cell. Biol. 12, 3176-3182.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3176-3182
    • Li, W.1    Deanin, G.G.2    Margolis, B.3    Schlessinger, J.4    Oliver, J.M.5
  • 38
    • 0026600298 scopus 로고
    • Phospholipase C-γ1 is translocated to the membrane of rat basophilic leukemia cells in response to aggregation of IgE receptors
    • Atkinson, T. P., Kaliner, M. A., Hohman, R. J. (1992) Phospholipase C-γ1 is translocated to the membrane of rat basophilic leukemia cells in response to aggregation of IgE receptors. J. Immunol. 148, 94-122.
    • (1992) J. Immunol. , vol.148 , pp. 94-122
    • Atkinson, T.P.1    Kaliner, M.A.2    Hohman, R.J.3
  • 39
    • 0027165809 scopus 로고
    • Orthovanadate induces translocation of phospholipase C-γ1 and -γ2 in permeabilized mast cells
    • Atkinson, T. P., Lee, C-W. Rhee, S. G., Hohman, R. J. (1993) Orthovanadate induces translocation of phospholipase C-γ1 and -γ2 in permeabilized mast cells. J. Immunol. 151, 1448-1455.
    • (1993) J. Immunol. , vol.151 , pp. 1448-1455
    • Atkinson, T.P.1    Lee, C.-W.2    Rhee, S.G.3    Hohman, R.J.4
  • 40
    • 2642612273 scopus 로고    scopus 로고
    • FcεR1-induced protein tyrosine phosphorylation
    • (M. M. Hamawy, ed.) Austin, TX: R. G. Landes
    • Benhamou, M. (1997) FcεR1-induced protein tyrosine phosphorylation. In IgE Receptor (FcεR1) Function in Mast Cells and Basophils (M. M. Hamawy, ed.) Austin, TX: R. G. Landes.
    • (1997) IgE Receptor (FcεR1) Function in Mast Cells and Basophils
    • Benhamou, M.1
  • 41
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss, A., Littman, D. R. (1994) Signal transduction by lymphocyte antigen receptors. Cell 76, 263-274.
    • (1994) Cell , vol.76 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 42
    • 0028072499 scopus 로고
    • Inhibition of mast cell FcεRI-mediated signalling and effector function by the Syk-selective inhibitor, piceatannol
    • Oliver, J. M., Burg, D. L., Wilson, B. S., McLaughlin, J. L., Geahlen, R. L. (1994) Inhibition of mast cell FcεRI-mediated signalling and effector function by the Syk-selective inhibitor, piceatannol. J. Biol. Chem. 269, 29697-29703.
    • (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
  • 43
    • 3743054628 scopus 로고    scopus 로고
    • Transfection of Syk reconstitutes high-affinity IgE mediated degranulation in Syk negative variants of rat basophilic leukemia RBL-2H3 cells
    • Zhang, J., Bernenstein, E. H., Evans, R. L., Siraganian, R. P. (1996) Transfection of Syk reconstitutes high-affinity IgE mediated degranulation in Syk negative variants of rat basophilic leukemia RBL-2H3 cells. FASEB J. 10, 59.
    • (1996) FASEB J. , vol.10 , pp. 59
    • Zhang, J.1    Bernenstein, E.H.2    Evans, R.L.3    Siraganian, R.P.4
  • 44
    • 0028800756 scopus 로고
    • Clustering of Syk is sufficient to induce tyrosine phosphorylation and release of allergic mediators from rat basophilic leukemia cells
    • Rivera, V. M., Brugge, J. S. (1995) Clustering of Syk is sufficient to induce tyrosine phosphorylation and release of allergic mediators from rat basophilic leukemia cells. Mol. Cell. Biol. 15, 582-590.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 582-590
    • Rivera, V.M.1    Brugge, J.S.2
  • 45
    • 0030018304 scopus 로고    scopus 로고
    • A role for Bruton's tyrosine kinase in B cell antigen receptor-mediated activation of phospholipase C-γ2
    • Takata, M., Kurosaki, T. (1996) A role for Bruton's tyrosine kinase in B cell antigen receptor-mediated activation of phospholipase C-γ2. J. Exp. Med. 184, 31-40.
    • (1996) J. Exp. Med. , vol.184 , pp. 31-40
    • Takata, M.1    Kurosaki, T.2
  • 48
    • 0030822605 scopus 로고    scopus 로고
    • Phosphorylation of two regulatory tyrosine residues in the activation of Bruton's tyrosine kinase via alternative receptors
    • Wahl, M. I., Fluckiger, A-C., Kato, R. M., Park, H., Witte, O., Rawlings, D. J. (1997) Phosphorylation of two regulatory tyrosine residues in the activation of Bruton's tyrosine kinase via alternative receptors. Proc. Natl. Acad. Sci. USA 94, 11526-11533.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11526-11533
    • Wahl, M.I.1    Fluckiger, A.-C.2    Kato, R.M.3    Park, H.4    Witte, O.5    Rawlings, D.J.6
  • 49
    • 0029348814 scopus 로고
    • The Btk subfamily of cytoplasmic tyrosine kinases: Structure, regulation and function
    • Rawlings, D. J., Witte, O. N. (1995) The Btk subfamily of cytoplasmic tyrosine kinases: structure, regulation and function. Semin. Immunol. 7, 237-246.
    • (1995) Semin. Immunol. , vol.7 , pp. 237-246
    • Rawlings, D.J.1    Witte, O.N.2
  • 50
    • 0025763863 scopus 로고
    • Differential activation of human basophils by anti-IgE and formyl-methionylleucyl-phenylalanine: Indications for protein kinase C-dependent and -independent pathways
    • Knol, E. F., Koenderman, L., Mul, F. P., Verhoeven, A. J., Roos, D. (1991) Differential activation of human basophils by anti-IgE and formyl-methionylleucyl-phenylalanine: indications for protein kinase C-dependent and -independent pathways. Eur. J. Immunol. 21, 881-885.
    • (1991) Eur. J. Immunol. , vol.21 , pp. 881-885
    • Knol, E.F.1    Koenderman, L.2    Mul, F.P.3    Verhoeven, A.J.4    Roos, D.5
  • 51
    • 0028175590 scopus 로고
    • 2+ influx: How many mechanisms for how many channels?
    • 2+ influx: how many mechanisms for how many channels? TIPS 15, 76-83.
    • (1994) TIPS , vol.15 , pp. 76-83
    • Fasolato, C.1    Innocenti, B.2    Pozzan, T.3
  • 52
    • 0026209437 scopus 로고
    • Inositol tetrakisphosphate as a second messenger: Confusions, contradictions and a potential resolution
    • Irvine, R. F. (1991) Inositol tetrakisphosphate as a second messenger: confusions, contradictions and a potential resolution. BioEssays 13, 419-426.
    • (1991) BioEssays , vol.13 , pp. 419-426
    • Irvine, R.F.1
  • 53
    • 0028302065 scopus 로고
    • Inhibition of agonist-stimulated inositol 1,4,5-trisphosphate productions and calcium signaling by the myosin light chain kinase inhibitor, wortmannin
    • Nakanish, S., Catt, K. J., Balla, T. (1994) Inhibition of agonist-stimulated inositol 1,4,5-trisphosphate productions and calcium signaling by the myosin light chain kinase inhibitor, wortmannin. J. Biol. Chem. 269, 6528-6535.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6528-6535
    • Nakanish, S.1    Catt, K.J.2    Balla, T.3


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