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Volumn 18, Issue 5, 1998, Pages 419-448

Ca2+ signaling in T-lymphocytes

Author keywords

Ca2+ signaling; Cyclic ADP ribose; Inositol 1,4,5 triphosphate; Second messenger; Signal transduction; T lymphocytes

Indexed keywords

1 [2 (4 METHOXYPHENYL) 2 [3 (4 METHOXYPHENYL)PROPOXY]ETHYL] 1H IMIDAZOLE; ADENOSINE DIPHOSPHATE RIBOSE; AMILORIDE; CALCIUM CHANNEL; CALCIUM ION; CALMODULIN INHIBITOR; CD4 ANTIGEN; CELL ADHESION MOLECULE; FORSKOLIN; INOSITOL 1,4,5 TRISPHOSPHATE; PHORBOL ESTER; RYANODINE RECEPTOR; CD3 ANTIGEN; LYMPHOCYTE ANTIGEN RECEPTOR; TOXIN;

EID: 0031596005     PISSN: 10408401     EISSN: None     Source Type: Journal    
DOI: 10.1615/critrevimmunol.v18.i5.20     Document Type: Review
Times cited : (62)

References (214)
  • 1
    • 0017729555 scopus 로고
    • Accelerated calcium ion uptake in murine thymocytes induced by concanavalin A
    • Ozato, K., Huang, L., and Ebert, J. D., Accelerated calcium ion uptake in murine thymocytes induced by concanavalin A, J. Cell. Physiol., 93, 153-160, 1977.
    • (1977) J. Cell. Physiol. , vol.93 , pp. 153-160
    • Ozato, K.1    Huang, L.2    Ebert, J.D.3
  • 2
    • 0020558256 scopus 로고
    • Free cytoplasmic calcium concentration and the mitogenic stimulation of lymphocytes
    • Hesketh, T. R., Smith, G. A., Moore, J. P., Taylor, M. V., and Metcalfe, J. C., Free cytoplasmic calcium concentration and the mitogenic stimulation of lymphocytes, J. Biol. Chem., 258, 4876-4882, 1983.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4876-4882
    • Hesketh, T.R.1    Smith, G.A.2    Moore, J.P.3    Taylor, M.V.4    Metcalfe, J.C.5
  • 3
    • 0001689806 scopus 로고
    • Crosslinking of surface antigens causes mobilization of intracellular ionized calcium in T lymphocytes
    • Ledbetter, J. A., June, C. H., Grosmaire, L. S., and Rabinovitch, P. S., Crosslinking of surface antigens causes mobilization of intracellular ionized calcium in T lymphocytes, Proc. Natl. Acad. Sci. U.S.A., 84, 1384-1388, 1987.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 1384-1388
    • Ledbetter, J.A.1    June, C.H.2    Grosmaire, L.S.3    Rabinovitch, P.S.4
  • 6
    • 0028260212 scopus 로고
    • Intracellular calcium dependence of gene expression in single T lymphocytes
    • Negulescu, P. A., Shastri, N., and Cahalan, M. D., Intracellular calcium dependence of gene expression in single T lymphocytes, Proc. Natl. Acad. Sci. U.S.A., 91, 2873-2877, 1994.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 2873-2877
    • Negulescu, P.A.1    Shastri, N.2    Cahalan, M.D.3
  • 7
    • 0025160020 scopus 로고
    • Differential CD3/T cell antigen receptor-mediated IL-2 production in Jurkat T cells. Dissociation of IL-2 response from total inositol phosphate and calcium responses
    • Stohl, W., Hofman, F. M., and Gray, J. D., Differential CD3/T cell antigen receptor-mediated IL-2 production in Jurkat T cells. Dissociation of IL-2 response from total inositol phosphate and calcium responses, J. Immunol., 145, 1078-1087, 1990.
    • (1990) J. Immunol. , vol.145 , pp. 1078-1087
    • Stohl, W.1    Hofman, F.M.2    Gray, J.D.3
  • 8
    • 0024439664 scopus 로고
    • Calcium and T lymphocyte activation
    • Gardner, P., Calcium and T lymphocyte activation, Cell, 59, 15-20, 1989.
    • (1989) Cell , vol.59 , pp. 15-20
    • Gardner, P.1
  • 9
    • 0027096253 scopus 로고
    • Signal transduction by T cell receptors: Mobilization of Ca and regulation of Ca-dependent effector molecules
    • Premack, B. A. and Gardner, P., Signal transduction by T cell receptors: mobilization of Ca and regulation of Ca-dependent effector molecules, Am. J. Physiol., 263, C1119-C1140, 1992.
    • (1992) Am. J. Physiol. , vol.263
    • Premack, B.A.1    Gardner, P.2
  • 10
    • 0025232561 scopus 로고
    • Patch clamp studies of lymphocyte activation
    • Gardner, P., Patch clamp studies of lymphocyte activation, Ann. Rev. Immunol., 8, 231-252, 1990.
    • (1990) Ann. Rev. Immunol. , vol.8 , pp. 231-252
    • Gardner, P.1
  • 11
  • 12
    • 0002052586 scopus 로고
    • The use of fluorescent indicators for measurements of cytosolic-free calcium concentration in cell populations and single cells
    • McCormack, J. G. and Cobbold, P. H., Eds., Oxford, New York, Tokyo: IRL Press
    • Thomas, A. P. and Delaville, F., The use of fluorescent indicators for measurements of cytosolic-free calcium concentration in cell populations and single cells, in Cellular Calcium - A Practical Approach, McCormack, J. G. and Cobbold, P. H., Eds., Oxford, New York, Tokyo: IRL Press, 1991, 1-54.
    • (1991) Cellular Calcium - A Practical Approach , pp. 1-54
    • Thomas, A.P.1    Delaville, F.2
  • 13
    • 0024488636 scopus 로고
    • Fluorescent probes of cell signaling
    • Tsien, R. Y., Fluorescent probes of cell signaling, Ann. Rev. Neurosci., 12, 227-253, 1989.
    • (1989) Ann. Rev. Neurosci. , vol.12 , pp. 227-253
    • Tsien, R.Y.1
  • 14
    • 0027983712 scopus 로고
    • Flow cytometric measurement of calcium influx in murine T cell hybrids using Fluo-3 and an organic-anion transport inhibitor
    • Baus, E., Urbain, J., Leo, O., and Andris, F., Flow cytometric measurement of calcium influx in murine T cell hybrids using Fluo-3 and an organic-anion transport inhibitor, J. Immunol. Methods, 173, 41-47, 1994.
    • (1994) J. Immunol. Methods , vol.173 , pp. 41-47
    • Baus, E.1    Urbain, J.2    Leo, O.3    Andris, F.4
  • 15
    • 0028247407 scopus 로고
    • Inexpensive techniques for measuring [Ca2+]j using a photomultiplier tube
    • Robinson, K. R., Keating, T. J., and Cork, R. J., Inexpensive techniques for measuring [Ca2+]j using a photomultiplier tube, Methods Cell Biol., 40, 287-303, 1994.
    • (1994) Methods Cell Biol. , vol.40 , pp. 287-303
    • Robinson, K.R.1    Keating, T.J.2    Cork, R.J.3
  • 16
    • 0021998316 scopus 로고
    • 2+ in individual small cells using fluorescence microscopy with dual excitation wavelengths
    • 2+ in individual small cells using fluorescence microscopy with dual excitation wavelengths, Cell. Calcium, 6, 145-147, 1985.
    • (1985) Cell. Calcium , vol.6 , pp. 145-147
    • Tsien, R.Y.1    Rink, T.J.2    Poenie, M.3
  • 17
    • 0026606454 scopus 로고
    • Imaging early steps of human T cell activation by antigen-presenting cells
    • Donnadieu, E., Cefai, D., Tan, Y. P., Paresys, G., Bismuth, G., and Trautmann, A., Imaging early steps of human T cell activation by antigen-presenting cells, J. Immunol., 148, 2643-2653, 1992.
    • (1992) J. Immunol. , vol.148 , pp. 2643-2653
    • Donnadieu, E.1    Cefai, D.2    Tan, Y.P.3    Paresys, G.4    Bismuth, G.5    Trautmann, A.6
  • 18
    • 0026452787 scopus 로고
    • ++ from crude microsomes and enriched vesicular plasma membranes but not from permeabilized T-lymphocytes and monocytes
    • ++ from crude microsomes and enriched vesicular plasma membranes but not from permeabilized T-lymphocytes and monocytes, Biochem. J., 288, 489-495, 1992.
    • (1992) Biochem. J. , vol.288 , pp. 489-495
    • Guse, A.H.1    Roth, E.2    Emmrich, F.3
  • 19
    • 0025296783 scopus 로고
    • Agonist-induced cytosolic calcium oscillations originate from a specific locus in single hepatocytes
    • Rooney, T. A., Sass, E. J., and Thomas, A. P., Agonist-induced cytosolic calcium oscillations originate from a specific locus in single hepatocytes, J. Biol. Chem., 265, 10792-10796, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10792-10796
    • Rooney, T.A.1    Sass, E.J.2    Thomas, A.P.3
  • 20
    • 0029893873 scopus 로고    scopus 로고
    • Laser scaning microscopy and calcium imaging
    • Schild, D., Laser scaning microscopy and calcium imaging, Cell. Calcium, 19, 281-296, 1996.
    • (1996) Cell. Calcium , vol.19 , pp. 281-296
    • Schild, D.1
  • 21
    • 0027200178 scopus 로고
    • 2+ measurements with visible wavelength indicators in isolated cardiac myocytes
    • 2+ measurements with visible wavelength indicators in isolated cardiac myocytes, Cell. Calcium, 14, 359-372, 1993.
    • (1993) Cell. Calcium , vol.14 , pp. 359-372
    • Lipp, P.1    Niggli, E.2
  • 22
    • 0027466815 scopus 로고
    • Flash photolysis of caged inositol 1,4,5-trisphosphate activates plasma membrane current in human T cells
    • McDonald, T. V., Premack, B. A., and Gardner, P., Flash photolysis of caged inositol 1,4,5-trisphosphate activates plasma membrane current in human T cells, J. Biol. Chem., 268, 3889-3896, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3889-3896
    • McDonald, T.V.1    Premack, B.A.2    Gardner, P.3
  • 24
    • 0028811179 scopus 로고
    • Nonradioactive, isomer-specifrc inositol phosphate mass determinations: Micro metal-dye detection-HPLC strongly Improves speed and sensitivity of analyses from cells: And micro-enzyme assays
    • Guse, A. H., Goldwich, A., Weber, K., and Mayr, G. W., Nonradioactive, isomer-specifrc inositol phosphate mass determinations: micro metal-dye detection-HPLC strongly Improves speed and sensitivity of analyses from cells: and micro-enzyme assays. J. Chromatogr. B, 672,189-198, 1995.
    • (1995) J. Chromatogr. B , vol.672 , pp. 189-198
    • Guse, A.H.1    Goldwich, A.2    Weber, K.3    Mayr, G.W.4
  • 25
    • 0016708461 scopus 로고
    • Cell cycle dependency of a T-cell marker on lymphoblasts
    • Schwenk, H. U. and Schneider, U., Cell cycle dependency of a T-cell marker on lymphoblasts, Blut, 31, 299-306, 1975.
    • (1975) Blut , vol.31 , pp. 299-306
    • Schwenk, H.U.1    Schneider, U.2
  • 27
    • 0027305396 scopus 로고
    • Immotalization of human T cell clones by Herpes virus saimiri. Signal transaction analysis reveals functional CD3, CD4, and IL-2 receptors
    • Bröker, B. M., Tsygankov, A. Y., Müller-Fleckenstein, I., Guse, A. H., Chitaev, N. A., Biesinger, B., Fleckenstein, B., and Emmrich, F., Immotalization of human T cell clones by Herpes virus saimiri. Signal transaction analysis reveals functional CD3, CD4, and IL-2 receptors, J. Immunol., 151, 1184-1192, 1993.
    • (1993) J. Immunol. , vol.151 , pp. 1184-1192
    • Bröker, B.M.1    Tsygankov, A.Y.2    Müller-Fleckenstein, I.3    Guse, A.H.4    Chitaev, N.A.5    Biesinger, B.6    Fleckenstein, B.7    Emmrich, F.8
  • 28
    • 0020030211 scopus 로고
    • Constitutive interleukin 2 production by the JURKAT human leukemic T cell line
    • Pawelec, G., Borowitz, A., Krammer, P. H., and Wernet, P., Constitutive interleukin 2 production by the JURKAT human leukemic T cell line, Eur. J. Immunol., 12, 387-392, 1982.
    • (1982) Eur. J. Immunol. , vol.12 , pp. 387-392
    • Pawelec, G.1    Borowitz, A.2    Krammer, P.H.3    Wernet, P.4
  • 29
    • 0025828930 scopus 로고
    • Calcium signals in single T cells on activation by lectin
    • Tregear, R. T., Hoyland, J., and Mason, W. T., Calcium signals in single T cells on activation by lectin, Eur. J. Immunol., 21, 1283-1288, 1991.
    • (1991) Eur. J. Immunol. , vol.21 , pp. 1283-1288
    • Tregear, R.T.1    Hoyland, J.2    Mason, W.T.3
  • 30
    • 0026338871 scopus 로고
    • Molecular and genetic insights into T cell antigen receptor structure and function
    • Weiss, A., Molecular and genetic insights into T cell antigen receptor structure and function, Annu. Rev. Genet., 25, 487-510, 1991.
    • (1991) Annu. Rev. Genet. , vol.25 , pp. 487-510
    • Weiss, A.1
  • 31
    • 0025966241 scopus 로고
    • T-cell development and transmembrane signaling: Changing biological responses through an unchanging receptor
    • Finkel, T. H., Kubo, R. T., and Cambier, J. C., T-cell development and transmembrane signaling: changing biological responses through an unchanging receptor, Immunol. Today, 12, 79-85, 1991.
    • (1991) Immunol. Today , vol.12 , pp. 79-85
    • Finkel, T.H.1    Kubo, R.T.2    Cambier, J.C.3
  • 32
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss, A. and Littman, D. R., Signal transduction by lymphocyte antigen receptors, Cell, 76, 263-274, 1994.
    • (1994) Cell , vol.76 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 33
    • 0026681679 scopus 로고
    • The T cell receptor as a multicomponent signaling machine: CD4/CD8 coreceptors and CD45 in T cell activation
    • Janeway C. A., Jr., The T cell receptor as a multicomponent signaling machine: CD4/CD8 coreceptors and CD45 in T cell activation, Annu. Rev. Immunol., 10, 645-674, 1992.
    • (1992) Annu. Rev. Immunol. , vol.10 , pp. 645-674
    • Janeway Jr., C.A.1
  • 34
    • 0000810666 scopus 로고
    • Role of T3 surface molecules in human T-cell activation: T3-dependent activation results in an increase in cytoplasmic free calcium
    • Weiss, A., Imboden, J., Shoback, D., and Stobo, J., Role of T3 surface molecules in human T-cell activation: T3-dependent activation results in an increase in cytoplasmic free calcium, Proc. Natl. Acad. Sci. U.S.A., 81, 4169-4173, 1984.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 4169-4173
    • Weiss, A.1    Imboden, J.2    Shoback, D.3    Stobo, J.4
  • 35
    • 0023908650 scopus 로고
    • Early signal transduction by the antigen receptor without commitment to T cell activation
    • Goldsmith, A. and Weiss, A., Early signal transduction by the antigen receptor without commitment to T cell activation, Science, 240, 1029-1031, 1988.
    • (1988) Science , vol.240 , pp. 1029-1031
    • Goldsmith, A.1    Weiss, A.2
  • 36
    • 0024755604 scopus 로고
    • 2+ current in human leukemic T cells
    • 2+ current in human leukemic T cells, Cell Reg., 1, 99-112, 1989.
    • (1989) Cell Reg. , vol.1 , pp. 99-112
    • Lewis, R.S.1    Cahalan, M.D.2
  • 38
    • 0028467150 scopus 로고
    • Antigen recognition by helper T cells elicits a sequence of distinct changes of their shape and intracellular calcium
    • Donnadieu, E., Bismuth, G., and Trautmann, A., Antigen recognition by helper T cells elicits a sequence of distinct changes of their shape and intracellular calcium, Curr. Biol., 4, 584-595, 1994.
    • (1994) Curr. Biol. , vol.4 , pp. 584-595
    • Donnadieu, E.1    Bismuth, G.2    Trautmann, A.3
  • 39
    • 0025297050 scopus 로고
    • Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyl inositol pathway
    • Koretzky, G. A., Picus, J., Thomas, M. L., and Weiss, A., Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyl inositol pathway, Nature, 346, 66-68, 1990.
    • (1990) Nature , vol.346 , pp. 66-68
    • Koretzky, G.A.1    Picus, J.2    Thomas, M.L.3    Weiss, A.4
  • 40
    • 0028887998 scopus 로고
    • Multiple kinases mediate T-cell receptor signaling
    • Howe, L. R. and Weiss, A., Multiple kinases mediate T-cell receptor signaling, Trends Biochem. Sci., 20, 59-64, 1995.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 59-64
    • Howe, L.R.1    Weiss, A.2
  • 41
    • 0025332477 scopus 로고
    • T cell antigen receptor-mediated activation of phospholipase C requires tyrosine phosphorylation
    • Mustelin, T., Coggeshall, M., Isakov, N., and Altman, A., T cell antigen receptor-mediated activation of phospholipase C requires tyrosine phosphorylation, Science, 247, 1584-1587, 1990.
    • (1990) Science , vol.247 , pp. 1584-1587
    • Mustelin, T.1    Coggeshall, M.2    Isakov, N.3    Altman, A.4
  • 42
    • 0021988801 scopus 로고
    • Kinetics of long-term (72 hr) calcium content during mitogen activation of cultured human T-lymphocytes
    • Wolff, C. H., Akerman, K. E., and Andersson, L. C., Kinetics of long-term (72 hr) calcium content during mitogen activation of cultured human T-lymphocytes, J. Cell. Physiol., 123, 46-50,1985.
    • (1985) J. Cell. Physiol. , vol.123 , pp. 46-50
    • Wolff, C.H.1    Akerman, K.E.2    Andersson, L.C.3
  • 44
    • 0027156266 scopus 로고
    • 2+ signal in individual human peripheral T cells
    • 2+ signal in individual human peripheral T cells, J. Immunol., 150, 5338-5349, 1993.
    • (1993) J. Immunol. , vol.150 , pp. 5338-5349
    • Wacholtz, M.C.1    Lipsky, P.E.2
  • 47
    • 0021849733 scopus 로고
    • Stimulation of the T3 T cell receptor complex induces a membrane-potential-sensitive calcium influx
    • Oettgen, H. C., Terhorst, C., Cantley, L. C., and Rosoff, P. M., Stimulation of the T3 T cell receptor complex induces a membrane-potential-sensitive calcium influx, Cell, 40, 583-590, 1985.
    • (1985) Cell , vol.40 , pp. 583-590
    • Oettgen, H.C.1    Terhorst, C.2    Cantley, L.C.3    Rosoff, P.M.4
  • 50
    • 0024453294 scopus 로고
    • Inositol phosphates and cell signaling
    • Berridge, M. J. and Irvine, R. F., Inositol phosphates and cell signaling, Nature, 341, 197-205, 1989.
    • (1989) Nature , vol.341 , pp. 197-205
    • Berridge, M.J.1    Irvine, R.F.2
  • 51
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signaling
    • Berridge, M. J., Inositol trisphosphate and calcium signaling, Nature, 361, 315-325, 1993.
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 52
    • 0020643801 scopus 로고
    • 2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate
    • 2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate, Nature, 306, 67-68, 1983.
    • (1983) Nature , vol.306 , pp. 67-68
    • Streb, H.1    Irvine, R.F.2    Berridge, M.J.3    Schulz, L.4
  • 53
    • 0028307952 scopus 로고
    • Calcium release activity and metabolism of inositol 1,4,5-trisphosphate in T cells. Modulation by novel inositol 1,4,5-trisphosphate 5-phosphatase inhibitors
    • Ward, S. G., Lampe, D., Liu, C., Potter, B. V. L., and Westwick, J., Calcium release activity and metabolism of inositol 1,4,5-trisphosphate in T cells. Modulation by novel inositol 1,4,5-trisphosphate 5-phosphatase inhibitors, Eur. J. Biochem., 222, 515-523, 1994.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 515-523
    • Ward, S.G.1    Lampe, D.2    Liu, C.3    Potter, B.V.L.4    Westwick, J.5
  • 54
    • 0025294823 scopus 로고
    • Regulation of calcium influx across the plasma membrane of the human T-leukemic cell line, JURKAT: Dependence on a rise in cytosolic free calcium can be dissociated from formation of inositol phosphates
    • Ng, J., Gustavsson, J., Jondal, M., and Andersson, T., Regulation of calcium influx across the plasma membrane of the human T-leukemic cell line, JURKAT: dependence on a rise in cytosolic free calcium can be dissociated from formation of inositol phosphates, Biochim. Biophys. Acta, 1053, 97-105, 1990.
    • (1990) Biochim. Biophys. Acta , vol.1053 , pp. 97-105
    • Ng, J.1    Gustavsson, J.2    Jondal, M.3    Andersson, T.4
  • 55
    • 0025301875 scopus 로고
    • Signal transduction through the T cell receptor-CD3 complex. Evidence for heterogeneity in receptor coupling
    • Brattsand, G., Cantrell, D. A., Ward, S., Ivars, F., and Gullberg, M., Signal transduction through the T cell receptor-CD3 complex. Evidence for heterogeneity in receptor coupling, J. Immunol., 144, 3651-3658, 1990.
    • (1990) J. Immunol. , vol.144 , pp. 3651-3658
    • Brattsand, G.1    Cantrell, D.A.2    Ward, S.3    Ivars, F.4    Gullberg, M.5
  • 56
    • 0026541202 scopus 로고
    • Analysis of inositol polyphosphates from human T-lymphocyte cell lines by anion-exchangeHPLC and post-column derivatization
    • Guse, A. H. and Emmrich, F., Analysis of inositol polyphosphates from human T-lymphocyte cell lines by anion-exchangeHPLC and post-column derivatization, J. Chromatogr., 593, 157-163, 1992.
    • (1992) J. Chromatogr. , vol.593 , pp. 157-163
    • Guse, A.H.1    Emmrich, F.2
  • 57
    • 0028364596 scopus 로고
    • Identification of high molecular weight forms of inositol 1,4,5-trisphosphate 3-kinase in rat thymus and human lymphocytes
    • D'Santos, C. S., Communi, D., Ludgate, M., Vanweyenberg, V., V.,Takazawa, K., and Erneux, C., Identification of high molecular weight forms of inositol 1,4,5-trisphosphate 3-kinase in rat thymus and human lymphocytes, Cell. Signal., 6, 335-344, 1994.
    • (1994) Cell. Signal. , vol.6 , pp. 335-344
    • D'Santos, C.S.1    Communi, D.2    Ludgate, M.3    Vanweyenberg, V.V.4    Takazawa, K.5    Erneux, C.6
  • 58
    • 0028011094 scopus 로고
    • The control of intracellular signal molecules at the level of their hydrolysis: The example of inositol 1,4,5-trisphosphate 5-phosphatase
    • Verjans, B., Moreau, C., and Erneux, C, The control of intracellular signal molecules at the level of their hydrolysis: the example of inositol 1,4,5-trisphosphate 5-phosphatase, Mol. Cell. Endokrinol., 98, 167-171, 1994.
    • (1994) Mol. Cell. Endokrinol. , vol.98 , pp. 167-171
    • Verjans, B.1    Moreau, C.2    Erneux, C.3
  • 60
    • 0026340591 scopus 로고
    • T-cell receptor-mediated metabolism of inositol polyphosphates in Jurkat T- lymphocytes
    • Guse, A. H. and Emmrich, F., T-cell receptor-mediated metabolism of inositol polyphosphates in Jurkat T- lymphocytes, J. Biol. Chem., 266, 24498-24502, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24498-24502
    • Guse, A.H.1    Emmrich, F.2
  • 61
    • 0027400907 scopus 로고
    • Mass changes of inositol 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate during cell cycle progression in rat thymocytes
    • Guse, A. H., Greiner, E., Emmrich, F., and Brand, K., Mass changes of inositol 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate during cell cycle progression in rat thymocytes, J. Biol. Chem., 268, 7129-7133, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7129-7133
    • Guse, A.H.1    Greiner, E.2    Emmrich, F.3    Brand, K.4
  • 64
    • 0025301475 scopus 로고
    • Inositol 1,3,4,5-tetrakisphosphate stimulates calcium release from bovine adrenal microsomes by a mechanism independent of the inositol 1,4,5-trisphosphate receptor
    • Ely, J. A., Hunyady, L., Baukal, A. J., and Catt, K. J., Inositol 1,3,4,5-tetrakisphosphate stimulates calcium release from bovine adrenal microsomes by a mechanism independent of the inositol 1,4,5-trisphosphate receptor, Biochem. J., 268, 333-338, 1990.
    • (1990) Biochem. J. , vol.268 , pp. 333-338
    • Ely, J.A.1    Hunyady, L.2    Baukal, A.J.3    Catt, K.J.4
  • 65
    • 0025951503 scopus 로고
    • Inositol tetrakisphosphates as second messengers induce calcium-dependent chloride currents in Xenopus laevis oocytes
    • Guse, A. H., Gercken, G., Boysen, H., Schwarz, J. R., and Meyerhof, W., Inositol tetrakisphosphates as second messengers induce calcium-dependent chloride currents in Xenopus laevis oocytes, Biochem. Biophys. Res. Commun., 179, 641-647, 1991.
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 641-647
    • Guse, A.H.1    Gercken, G.2    Boysen, H.3    Schwarz, J.R.4    Meyerhof, W.5
  • 68
    • 0030971842 scopus 로고    scopus 로고
    • Modulation of endoplasmicc reliculum calcium pump expression during T lymphocyte activation
    • Launay, S., Bobe, R., Lacabaratz-Porret, C., Bredoux, R., Kovacs, T., Enouf, J., and Papp, B., Modulation of endoplasmicc reliculum calcium pump expression during T lymphocyte activation, J. Biol. Chem., 272, 10746-10750, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10746-10750
    • Launay, S.1    Bobe, R.2    Lacabaratz-Porret, C.3    Bredoux, R.4    Kovacs, T.5    Enouf, J.6    Papp, B.7
  • 69
    • 0028853108 scopus 로고
    • The human type 1 ru inositol 1,4,5-trisphosphate receptor from T-lymphocytes
    • Harnick, D. J., Jayaraman, T., Ma, Y., Mulieri, P., Go, L. O., and Marks, A. R., The human type 1 ru inositol 1,4,5-trisphosphate receptor from T-lymphocytes, J. Biol. Chem., 270, 2833-2840, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2833-2840
    • Harnick, D.J.1    Jayaraman, T.2    Ma, Y.3    Mulieri, P.4    Go, L.O.5    Marks, A.R.6
  • 71
    • 0029975479 scopus 로고    scopus 로고
    • Regulation of the inositol 1,4,5-trisphosphate receptor by tyrosine phosphorylation
    • Jayaraman, T., Ondrias, K., Ondriasova, E., and Marks, A. R., Regulation of the inositol 1,4,5-trisphosphate receptor by tyrosine phosphorylation, Science, 272, 1492-1494, 1996.
    • (1996) Science , vol.272 , pp. 1492-1494
    • Jayaraman, T.1    Ondrias, K.2    Ondriasova, E.3    Marks, A.R.4
  • 75
    • 0026510372 scopus 로고
    • Plasma membrane inositol 1,4,5-trisphosphate receptor of lymphocytes: Selective enrichment in sialic acid and unique binding specificity
    • Khan, A. A., Steiner, J. P., and Snyder, S. H., Plasma membrane inositol 1,4,5-trisphosphate receptor of lymphocytes: selective enrichment in sialic acid and unique binding specificity, Proc. Natl. Acad. Sci. U.S.A., 89, 2849-2853, 1992.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 2849-2853
    • Khan, A.A.1    Steiner, J.P.2    Snyder, S.H.3
  • 78
    • 0030973158 scopus 로고    scopus 로고
    • T cells deficient in inositol 1,4,5-trisphosphate receptor are resistant to apoptosis
    • Jayaraman, T. and Marks, A. R., T cells deficient in inositol 1,4,5-trisphosphate receptor are resistant to apoptosis, Mol. Cell. Biol., 17, 3005-3012, 1997.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3005-3012
    • Jayaraman, T.1    Marks, A.R.2
  • 80
    • 0027461582 scopus 로고
    • Ryanodine receptors: How many, where and Why?
    • Sorrentino, V. and Volpe, P., Ryanodine receptors: how many, where and Why?, Trend. Pharmacol. Sci., 14, 98-105, 1903.
    • (1903) Trend. Pharmacol. Sci. , vol.14 , pp. 98-105
    • Sorrentino, V.1    Volpe, P.2
  • 82
    • 0028925223 scopus 로고
    • The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues
    • Giannini, G., Conti,A., Mammarella, S., Scrobogna, M., and Sorrentino, V., The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues, J. Cell Biol., 128, 893-904, 1995.
    • (1995) J. Cell Biol. , vol.128 , pp. 893-904
    • Giannini, G.1    Conti, A.2    Mammarella, S.3    Scrobogna, M.4    Sorrentino, V.5
  • 84
    • 0026418298 scopus 로고
    • 2+ release in sea urchin egg homogenates: Modulation by cyclic ADP-ribose
    • 2+ release in sea urchin egg homogenates: modulation by cyclic ADP-ribose, Science, 253,1143-1146, 1991.
    • (1991) Science , vol.253 , pp. 1143-1146
    • Gallone, A.1    Lee, H.C.2    Busa, W.B.3
  • 89
    • 0028897336 scopus 로고
    • Magnesium ions but not ATP inhibit cyclic ADP-ribose-induced calcium release
    • Graeff, R. M., Podein, R. J., Aarhus, R., and Lee, H. C., Magnesium ions but not ATP inhibit cyclic ADP-ribose-induced calcium release, Biochem. Biophys. Res. Commun., 206, 786-791, 1995.
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 786-791
    • Graeff, R.M.1    Podein, R.J.2    Aarhus, R.3    Lee, H.C.4
  • 90
    • 0028822308 scopus 로고
    • Enzymatic cyclization of nicotinamide adenine dinucleotide phosphate (NADP)
    • Zhang, F.-J., Gu, Q.-M., Jing, P., and Sih, C. J., Enzymatic cyclization of nicotinamide adenine dinucleotide phosphate (NADP), Bioorg. Med. Chem. Lett., 5, 2267-2272, 1995.
    • (1995) Bioorg. Med. Chem. Lett. , vol.5 , pp. 2267-2272
    • Zhang, F.-J.1    Gu, Q.-M.2    Jing, P.3    Sih, C.J.4
  • 91
    • 0029916751 scopus 로고    scopus 로고
    • 2Prime;-Phospho-cyclic ADP-ribose, a calcium mobilizing agent derived from NADP
    • Vu, C. Q., Lu, P.-J., Chen, C.-S., and Jacobson, M. K., 2Prime;-Phospho-cyclic ADP-ribose, a calcium mobilizing agent derived from NADP, J. Biol. Chem., 271, 4747-4754, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4747-4754
    • Vu, C.Q.1    Lu, P.-J.2    Chen, C.-S.3    Jacobson, M.K.4
  • 92
    • 0029616337 scopus 로고
    • ADP-ribosyl cyclase and CD38 catalyze the synthesis of a calcium mobilizing metabolite from NADP
    • Aarhus, R., Graeff, R. M., Dickey, D. M., Walseth, T. F., and Lee, H. C., ADP-ribosyl cyclase and CD38 catalyze the synthesis of a calcium mobilizing metabolite from NADP, J. Biol. Chem., 270, 30327-30333, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30327-30333
    • Aarhus, R.1    Graeff, R.M.2    Dickey, D.M.3    Walseth, T.F.4    Lee, H.C.5
  • 94
    • 0025384609 scopus 로고
    • 2+ mobilizing activities of cyclic ADP-ribose inositol trisphosphate
    • 2+ mobilizing activities of cyclic ADP-ribose inositol trisphosphate, Cell Reg., 1, 279-290, 1990.
    • (1990) Cell Reg. , vol.1 , pp. 279-290
    • Dargie, P.J.1    Agre, M.C.2    Lee, H.C.3
  • 95
    • 0028131433 scopus 로고
    • Cyclic ADP ribose activation of the ryanodine receptor is mediated by calmodulin
    • Lee, H. C., Aarhus, R., Graeff, R., Gurnack, M., and Walseth, T. F., Cyclic ADP ribose activation of the ryanodine receptor is mediated by calmodulin, Nature, 370, 307-309, 1994.
    • (1994) Nature , vol.370 , pp. 307-309
    • Lee, H.C.1    Aarhus, R.2    Graeff, R.3    Gurnack, M.4    Walseth, T.F.5
  • 98
    • 0026575932 scopus 로고
    • The mechanism of action of cyclosporin A and FK506
    • Schreiber, S. L. and Crabtree, G. R., The mechanism of action of cyclosporin A and FK506, Immunol. Today, 13, 136-142, 1992.
    • (1992) Immunol. Today , vol.13 , pp. 136-142
    • Schreiber, S.L.1    Crabtree, G.R.2
  • 100
    • 0028087898 scopus 로고
    • Involvement of the brain type of ryanodine receptor in T-cell proliferation
    • Hakamata, Y., Nishimura, S., Nakai, J., Nakashima, Y., Kita, T., and Imoto, K., Involvement of the brain type of ryanodine receptor in T-cell proliferation, FEBS Lett., 352, 206-210, 1994.
    • (1994) FEBS Lett. , vol.352 , pp. 206-210
    • Hakamata, Y.1    Nishimura, S.2    Nakai, J.3    Nakashima, Y.4    Kita, T.5    Imoto, K.6
  • 101
    • 0028972692 scopus 로고
    • Ruthenium Red potently inhibits immune responses both in vitro and in vivo
    • Dwyer, D. S., Gordon, K., and Jones, B., Ruthenium Red potently inhibits immune responses both in vitro and in vivo, Int. J. Immunopharmacol., 17, 931-940, 1995.
    • (1995) Int. J. Immunopharmacol. , vol.17 , pp. 931-940
    • Dwyer, D.S.1    Gordon, K.2    Jones, B.3
  • 104
    • 0025831860 scopus 로고
    • Determination of endogenous levels of cyclic ADP-ribose in rat tissues
    • Walseth, T. F. and Lee, H. C., Determination of endogenous levels of cyclic ADP-ribose in rat tissues, Biochim. Biophys. Acta, 1094, 113-120, 1991.
    • (1991) Biochim. Biophys. Acta , vol.1094 , pp. 113-120
    • Walseth, T.F.1    Lee, H.C.2
  • 105
    • 0028875421 scopus 로고
    • 2+ release in intestinal longitudinal muscle
    • 2+ release in intestinal longitudinal muscle, J. Biol. Chem., 270, 25488-25494, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25488-25494
    • Kuemmerle, J.F.1    Makhlouf, G.M.2
  • 106
    • 0029143465 scopus 로고
    • Accumulation of cyclic ADP-ribose measured by a specific radioimmunoassay in differentiated human leukemic HL-60 cells with all-trans-retinoic acid
    • Takahashi, K., Kukimoto, I., Tokita, K.-I., Inageda, K., Inoue, S.-I., Kontani, K., Hoshino, S.-I., Nishina, H., Kanaho, Y., and Katada, T., Accumulation of cyclic ADP-ribose measured by a specific radioimmunoassay in differentiated human leukemic HL-60 cells with all-trans-retinoic acid, FEBS Lett., 371, 204-208, 1995.
    • (1995) FEBS Lett. , vol.371 , pp. 204-208
    • Takahashi, K.1    Kukimoto, I.2    Tokita, K.-I.3    Inageda, K.4    Inoue, S.-I.5    Kontani, K.6    Hoshino, S.-I.7    Nishina, H.8    Kanaho, Y.9    Katada, T.10
  • 107
    • 0032502851 scopus 로고    scopus 로고
    • Quantification of intracellular levels of cyclic ADP-ribose by high-performance liquid chromatography
    • da Silva, C. P., Potter, B. V. L., Mayr, G. W., and Guse, A. H., Quantification of intracellular levels of cyclic ADP-ribose by high-performance liquid chromatography, J. Chromatogr. B, 707, 43-50, 1998.
    • (1998) J. Chromatogr. B , vol.707 , pp. 43-50
    • Da Silva, C.P.1    Potter, B.V.L.2    Mayr, G.W.3    Guse, A.H.4
  • 108
    • 0000785554 scopus 로고
    • Human CD38: A versatile leukocyte molecule with emerging clinical prospectives
    • Funaro, A., Horenstein, A. L., and Malavasi, F., Human CD38: a versatile leukocyte molecule with emerging clinical prospectives, Fund. Clin. Immunol., 3, 101-114, 1995.
    • (1995) Fund. Clin. Immunol. , vol.3 , pp. 101-114
    • Funaro, A.1    Horenstein, A.L.2    Malavasi, F.3
  • 110
    • 0029909008 scopus 로고    scopus 로고
    • Human CD38, a cell-surface protein with multiple functions
    • Mehta, K., Shahid, U., and Malavasi, F., Human CD38, a cell-surface protein with multiple functions, FASEB J., 10, 1408-1417, 1996.
    • (1996) FASEB J. , vol.10 , pp. 1408-1417
    • Mehta, K.1    Shahid, U.2    Malavasi, F.3
  • 114
    • 0030057816 scopus 로고    scopus 로고
    • Posttranslational modification of CD38 protein into a high molecular weight form alters its catalytic properties
    • Umar, S., Malavasi, F., and Mehta, K., Posttranslational modification of CD38 protein into a high molecular weight form alters its catalytic properties, J. Biol. Chem. 271, 15922-15927, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15922-15927
    • Umar, S.1    Malavasi, F.2    Mehta, K.3
  • 115
    • 0030586618 scopus 로고    scopus 로고
    • Coordinated regulation in human T cells of nucleotide-hydrolyzing ecto-enzymatic activities, including CD38 and PC-1. Possible role in the recycling of nicotinamide adenine dinucleotide metabolites
    • Deterre, P., Gelman, L., Gary-Gouy, H., Arrieumerlou, C., Berthelier, V., Tixier, J.-M., Ktorza, S., Coding, J., Schmitt, C., and Bismuth, G., Coordinated regulation in human T cells of nucleotide-hydrolyzing ecto-enzymatic activities, including CD38 and PC-1. Possible role in the recycling of nicotinamide adenine dinucleotide metabolites, J. Immunol., 157, 1381-1388, 1996.
    • (1996) J. Immunol. , vol.157 , pp. 1381-1388
    • Deterre, P.1    Gelman, L.2    Gary-Gouy, H.3    Arrieumerlou, C.4    Berthelier, V.5    Tixier, J.-M.6    Ktorza, S.7    Coding, J.8    Schmitt, C.9    Bismuth, G.10
  • 118
    • 0023136482 scopus 로고
    • Ion channels activated by inositol 1,4,5-trisphosphate in plasma membrane of human T-lymphocytes
    • Kuno, M. and Gardner, P., Ion channels activated by inositol 1,4,5-trisphosphate in plasma membrane of human T-lymphocytes, Nature, 326,301-304, 1987.
    • (1987) Nature , vol.326 , pp. 301-304
    • Kuno, M.1    Gardner, P.2
  • 120
    • 0025195367 scopus 로고
    • 2+ entry by inositol phosphates - A possible mechanism
    • 2+ entry by inositol phosphates - a possible mechanism, FEBS Lett., 263, 5-9, 1990.
    • (1990) FEBS Lett. , vol.263 , pp. 5-9
    • Irvine, R.F.1
  • 121
    • 0022575011 scopus 로고
    • A model for receptor-regulated calcium entry
    • Putney J. W., Jr., A model for receptor-regulated calcium entry, Cell. Calcium, 7, 1-12, 1986.
    • (1986) Cell. Calcium , vol.7 , pp. 1-12
    • Putney Jr., J.W.1
  • 125
    • 0026594980 scopus 로고
    • 2+ stores activates a calcium current in mast cells
    • 2+ stores activates a calcium current in mast cells, Nature, 355, 353-356, 1992.
    • (1992) Nature , vol.355 , pp. 353-356
    • Hoth, M.1    Penner, R.2
  • 132
    • 0022339544 scopus 로고
    • Control of free cytoplasmic calcium by intracellular pH in rat lymphocytes, Biochim
    • 132: Grinstein, S. and Goetz, J. D., Control of free cytoplasmic calcium by intracellular pH in rat lymphocytes, Biochim. Biophys. Acta, 819, 267-270, 1985.
    • (1985) Biophys. Acta , vol.819 , pp. 267-270
    • Grinstein, S.1    Goetz, J.D.2
  • 133
    • 0028180362 scopus 로고
    • ++-entry induced by rapid cytosolic alkalinization in Jurkat T-lymphocytes
    • ++-entry induced by rapid cytosolic alkalinization in Jurkat T-lymphocytes, Biochem. J., 301, 83-88, 1994.
    • (1994) Biochem. J. , vol.301 , pp. 83-88
    • Guse, A.H.1    Roth, E.2    Emmrich, F.3
  • 135
    • 0028589615 scopus 로고
    • The calcium current activated by the T cell receptor and store depletion in human lymphocytes is absent in a primary immunodeficiency
    • Partiseti, M., LeDeist, F., Hivroz, C., Fischer, A., Korn, H., and Choquet, D., The calcium current activated by the T cell receptor and store depletion in human lymphocytes is absent in a primary immunodeficiency, J. Biol. Chem., 269, 32327-32335, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32327-32335
    • Partiseti, M.1    LeDeist, F.2    Hivroz, C.3    Fischer, A.4    Korn, H.5    Choquet, D.6
  • 136
    • 0028801217 scopus 로고
    • Characterization of T cell mutants with defects in capacitative calcium entry: Genetic evidence for the physiological roles of CRAC channels
    • Fanger, C. M., Hoth, M., Crabtree, G. R., and Lewis, R. S., Characterization of T cell mutants with defects in capacitative calcium entry: genetic evidence for the physiological roles of CRAC channels, J. Cell. Biol., 131, 655-667, 1995.
    • (1995) J. Cell. Biol. , vol.131 , pp. 655-667
    • Fanger, C.M.1    Hoth, M.2    Crabtree, G.R.3    Lewis, R.S.4
  • 138
    • 0029006156 scopus 로고
    • Slow calcium-dependent inactivation of depletion-activated calcium current
    • Zweifach, A. and Lewis, R. S., Slow calcium-dependent inactivation of depletion-activated calcium current, J. Biol. Chem., 270, 14445-14451, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14445-14451
    • Zweifach, A.1    Lewis, R.S.2
  • 139
    • 0029986107 scopus 로고    scopus 로고
    • Calcium-dependent enhancement of depletion-activated calcium current in Jurkat T lymphocytes
    • Christian E. P., Spence, K. T., Togo, J. A., Dargis, P. G., and Patel, J., Calcium-dependent enhancement of depletion-activated calcium current in Jurkat T lymphocytes, J. Membrane Biol., 150, 63-71, 1996.
    • (1996) J. Membrane Biol. , vol.150 , pp. 63-71
    • Christian, E.P.1    Spence, K.T.2    Togo, J.A.3    Dargis, P.G.4    Patel, J.5
  • 140
    • 0030982181 scopus 로고    scopus 로고
    • Mitochondrial regulation of store-operated calcium signaling in T-lymphocytes
    • Hoth, M., Fanger, C. M., and Lewis, R. S., Mitochondrial regulation of store-operated calcium signaling in T-lymphocytes, J. Cell. Biol., 137, 633-648, 1997.
    • (1997) J. Cell. Biol. , vol.137 , pp. 633-648
    • Hoth, M.1    Fanger, C.M.2    Lewis, R.S.3
  • 143
    • 0028967010 scopus 로고
    • Evaluation of calcium influx factors from stimulated Jurkat T-lymphocytes by microinjection into Xenopus oocytes
    • Thomas, D. and Hanley, M. R., Evaluation of calcium influx factors from stimulated Jurkat T-lymphocytes by microinjection into Xenopus oocytes, J. Biol. Chem., 270, 6429-6432, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6429-6432
    • Thomas, D.1    Hanley, M.R.2
  • 145
    • 0028899481 scopus 로고
    • Chromatographic resolution of an intracellular calcium influx factor from thapsigargin-activated Jurkat cells
    • Kim, H. Y., Thomas, D., and Hanley, M. R., Chromatographic resolution of an intracellular calcium influx factor from thapsigargin-activated Jurkat cells, J. Biol. Chem., 270, 9706-9708, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9706-9708
    • Kim, H.Y.1    Thomas, D.2    Hanley, M.R.3
  • 146
    • 0029792366 scopus 로고    scopus 로고
    • Regulation of inositol trisphosphate-induced membrane currents in Xenopus-oocytes by a Jurkat cell calcium Influx factor
    • Thomas, D., Kim, H. Y., and Hanley, M. R., Regulation of inositol trisphosphate-induced membrane currents in Xenopus-oocytes by a Jurkat cell calcium Influx factor, Biochem. J., 318, 649-656, 1996.
    • (1996) Biochem. J. , vol.318 , pp. 649-656
    • Thomas, D.1    Kim, H.Y.2    Hanley, M.R.3
  • 148
    • 0028124715 scopus 로고
    • Calcium signaling in T cells stimulated by a cyclophilin B-bindmg protein
    • Bram, R. J. and Crabtree, G.R., Calcium signaling in T cells stimulated by a cyclophilin B-bindmg protein, Nature, 371, 355-358, 1994.
    • (1994) Nature , vol.371 , pp. 355-358
    • Bram, R.J.1    Crabtree, G.R.2
  • 149
    • 0028826727 scopus 로고
    • Capacitative calcium entry
    • Berridge, M. J., Capacitative calcium entry, Biochem. J., 312, 1-11, 1995.
    • (1995) Biochem. J. , vol.312 , pp. 1-11
    • Berridge, M.J.1
  • 151
    • 0030586619 scopus 로고    scopus 로고
    • Tyrphostin A9 inhibits calcium release-dependent phosphorylations and calcium entry via calcium release activated channel in Jurkat T cells
    • Marhaba, R., Mary, F., Pelassy, C., Stanescu, A. T., Aussel, C., and Breittmayer, J.-P., Tyrphostin A9 inhibits calcium release-dependent phosphorylations and calcium entry via calcium release activated channel in Jurkat T cells, J. Immunol., 1996; 157:1468-1473.
    • (1996) J. Immunol. , vol.157 , pp. 1468-1473
    • Marhaba, R.1    Mary, F.2    Pelassy, C.3    Stanescu, A.T.4    Aussel, C.5    Breittmayer, J.-P.6
  • 154
    • 0025727028 scopus 로고
    • Nitrendipine-induced inhibition of calcium influx in a human T-cell clone: Role of cell depolarization
    • Randriamampita, C., Bismuth, G., Debré, P., and Trautmann, A., Nitrendipine-induced inhibition of calcium influx in a human T-cell clone: role of cell depolarization, Cell. Calcium, 12, 313-323, 1991.
    • (1991) Cell. Calcium , vol.12 , pp. 313-323
    • Randriamampita, C.1    Bismuth, G.2    Debré, P.3    Trautmann, A.4
  • 155
    • 0030766877 scopus 로고    scopus 로고
    • 2+ entry antagonist LU 52396: Its inhibitory activity depends on the activation state of the cells
    • 2+ entry antagonist LU 52396: its inhibitory activity depends on the activation state of the cells, Cell. Calcium, 22, 91-97, 1997.
    • (1997) Cell. Calcium , vol.22 , pp. 91-97
    • Guse, A.H.1    De Wit, C.2    Klokow, T.3    Schweitzer, K.4    Mayr, G.W.5
  • 160
    • 0027234026 scopus 로고
    • 2+ entry mechanisms coexist in Jurkat T cells during T cell receptor antigen activation
    • 2+ entry mechanisms coexist in Jurkat T cells during T cell receptor antigen activation, Biochem. J., 293, 395-398, 1993.
    • (1993) Biochem. J. , vol.293 , pp. 395-398
    • Chow, S.C.1    Kass, E.N.2    Orrenius, S.3
  • 163
    • 0024326855 scopus 로고
    • Phorbol esters regulate CD2- and CD3-mediateed calcium responses in peripheral blood-derived human T cells
    • Cantrell, D. A., Lucas, S. C., Ward, S., Westwick, J., and Gulberg, M., Phorbol esters regulate CD2- and CD3-mediateed calcium responses in peripheral blood-derived human T cells, J. Immunol., 143, 3653-3658, 1989.
    • (1989) J. Immunol. , vol.143 , pp. 3653-3658
    • Cantrell, D.A.1    Lucas, S.C.2    Ward, S.3    Westwick, J.4    Gulberg, M.5
  • 165
    • 0028885203 scopus 로고
    • Protein kinase C activation inhibits TCR-mediated calcium influx but not inositol trisphosphate production in HPB-ALL T cells
    • Shivnan, E. and Alexander, D. R., Protein kinase C activation inhibits TCR-mediated calcium influx but not inositol trisphosphate production in HPB-ALL T cells, J. Immunol., 154, 1146-1156, 1995.
    • (1995) J. Immunol. , vol.154 , pp. 1146-1156
    • Shivnan, E.1    Alexander, D.R.2
  • 166
    • 0029559820 scopus 로고
    • Protein kinase C modulates cytosolic free calcium by stimulating calcium pump activity in Jurkat cells
    • Balasubramanyam, M. and Gardner, J. P., Protein kinase C modulates cytosolic free calcium by stimulating calcium pump activity in Jurkat cells, Cell. Calcium, 18, 526-541, 1995.
    • (1995) Cell. Calcium , vol.18 , pp. 526-541
    • Balasubramanyam, M.1    Gardner, J.P.2
  • 167
    • 0027497287 scopus 로고
    • Preincubation with anti-CD4 influences activation of human T cells by subsequent co-crosslinking of CD4 with CD3
    • Tsygankov, A. Y., Bröker, B. M., Guse, A. H., Meinke, U., Roth, E., Rossmann, C., and Emmrich, F., Preincubation with anti-CD4 influences activation of human T cells by subsequent co-crosslinking of CD4 with CD3, J. Leukocyte Biol., 54, 430-438, 1993.
    • (1993) J. Leukocyte Biol. , vol.54 , pp. 430-438
    • Tsygankov, A.Y.1    Bröker, B.M.2    Guse, A.H.3    Meinke, U.4    Roth, E.5    Rossmann, C.6    Emmrich, F.7
  • 168
    • 0027422711 scopus 로고
    • Signal transduction in T-lymphocytes and monocytes: Effects of the antiCD4 antibody MAX.16H5
    • Guse, A. H., Tsygankov, A. Y., Broker, B. M., Roth, E., and Emmrich, F., Signal transduction in T-lymphocytes and monocytes: effects of the antiCD4 antibody MAX.16H5, Year Immunol., 7, 175-181, 1993.
    • (1993) Year Immunol. , vol.7 , pp. 175-181
    • Guse, A.H.1    Tsygankov, A.Y.2    Broker, B.M.3    Roth, E.4    Emmrich, F.5
  • 169
    • 0030636724 scopus 로고    scopus 로고
    • CD4 ligands inhibit the formation of multifunctional transduction complexes involved in T cell activation
    • Jabado, N., Pallier, A., LeDeist, F., Bernard, F., Fischer, A., and Hivroz, C., CD4 ligands inhibit the formation of multifunctional transduction complexes involved in T cell activation, J. Immunol., 158, 94-103, 1997.
    • (1997) J. Immunol. , vol.158 , pp. 94-103
    • Jabado, N.1    Pallier, A.2    LeDeist, F.3    Bernard, F.4    Fischer, A.5    Hivroz, C.6
  • 170
    • 0026757719 scopus 로고
    • Complex inositol polyphosphate response induced by co-crosslinking of CD4 and Fcγ receptors in the human monocytoid cell line U937
    • Guse, A. H., Roth, E., Bröker, B. M., and Emmrich, F., Complex inositol polyphosphate response induced by co-crosslinking of CD4 and Fcγ receptors in the human monocytoid cell line U937, J. Immunol., 149, 2452-2458, 1992.
    • (1992) J. Immunol. , vol.149 , pp. 2452-2458
    • Guse, A.H.1    Roth, E.2    Bröker, B.M.3    Emmrich, F.4
  • 173
    • 0030597063 scopus 로고    scopus 로고
    • 2+ in human Jurkat T-cells
    • 2+ in human Jurkat T-cells, FEBS Un., 395, 165-169, 1996.
    • (1996) FEBS Un. , vol.395 , pp. 165-169
    • Dong, S.1    Hughes, R.C.2
  • 174
    • 0029096916 scopus 로고
    • Activation of dual T cell signaling pathways by the chemokine RANTES
    • Bacon, K. B., Premack, B. A., Gardner, P., and Schall, T. J., Activation of dual T cell signaling pathways by the chemokine RANTES, Science, 269,1727-1730, 1995.
    • (1995) Science , vol.269 , pp. 1727-1730
    • Bacon, K.B.1    Premack, B.A.2    Gardner, P.3    Schall, T.J.4
  • 175
    • 0029126042 scopus 로고
    • RANTES-activated human T-lymphocytes. A role for phosphoinositide 3-kinase
    • Turner, L., Ward, S. G., and Westwick, J., RANTES-activated human T-lymphocytes. A role for phosphoinositide 3-kinase, J. Immunol., 155, 2437-2444, 1995.
    • (1995) J. Immunol. , vol.155 , pp. 2437-2444
    • Turner, L.1    Ward, S.G.2    Westwick, J.3
  • 176
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation and signalling in cell adhesion
    • Hynes, R. O., Integrins: versatility, modulation and signalling in cell adhesion, Cell, 69, 11-25, 1992.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 177
    • 0019865674 scopus 로고
    • Response of basal epithelial cell surface and skeleton to solubilized extracellular matrix molecules
    • Sugrue, S. P. and Hay, E. D., Response of basal epithelial cell surface and skeleton to solubilized extracellular matrix molecules, J Cell Biol., 91, 45-54, 1981.
    • (1981) J Cell Biol. , vol.91 , pp. 45-54
    • Sugrue, S.P.1    Hay, E.D.2
  • 178
    • 0343237235 scopus 로고
    • The heparin binding domain of laminin is responsible for its effects on neurite outgrowth and neuronal survival
    • Edgar, D., Timpl, R., and Thoenen, H., The heparin binding domain of laminin is responsible for its effects on neurite outgrowth and neuronal survival. EMBO J., 3, 1463-1468, 1984.
    • (1984) EMBO J. , vol.3 , pp. 1463-1468
    • Edgar, D.1    Timpl, R.2    Thoenen, H.3
  • 179
    • 0002429706 scopus 로고
    • Cell-matrix interaction in the embryo: Cell shape, cell surface, cell skeleton, and their role in differentiation
    • Trelstad, R. L., Ed., Alan Liss, Inc., New York
    • Hay, E. D., Cell-matrix interaction in the embryo: cell shape, cell surface, cell skeleton, and their role in differentiation, in The Role of the Extracellular Matrix in Development, Trelstad, R. L., Ed., Alan Liss, Inc., New York, 1984, 1-31.
    • (1984) The Role of the Extracellular Matrix in Development , pp. 1-31
    • Hay, E.D.1
  • 180
    • 0023664920 scopus 로고
    • The cellular interactions of laminin fragments. Cell adhesion correlates with two fragment-specific high affinity binding sites
    • Aumailley, M., Nurcombe, V., Edgar, D., Paulsson, M., and Timpl, R., The cellular interactions of laminin fragments. Cell adhesion correlates with two fragment-specific high affinity binding sites, J. Biol. Chem., 262, 11532-11538, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11532-11538
    • Aumailley, M.1    Nurcombe, V.2    Edgar, D.3    Paulsson, M.4    Timpl, R.5
  • 181
    • 0023376198 scopus 로고
    • Two distinct cell-binding domains in laminin can independentley promote non-neuronal cell adhesion and spreading
    • Goodman, S. L., Deutzmann, R., and von der Mark, K., Two distinct cell-binding domains in laminin can independentley promote non-neuronal cell adhesion and spreading, J. Cell. Biol., 105, 589-594, 1987.
    • (1987) J. Cell. Biol. , vol.105 , pp. 589-594
    • Goodman, S.L.1    Deutzmann, R.2    Von der Mark, K.3
  • 182
    • 0023375129 scopus 로고
    • Epithelial-mesenchymal interactions in the developing kidney lead to expression of tenascin in the mesenchyme
    • Aufderheide, E., Chiquet-Ehrismann, R., and Ekblom, P., Epithelial-mesenchymal interactions in the developing kidney lead to expression of tenascin in the mesenchyme, J. Cell. Biol., 105, 599-608, 1987.
    • (1987) J. Cell. Biol. , vol.105 , pp. 599-608
    • Aufderheide, E.1    Chiquet-Ehrismann, R.2    Ekblom, P.3
  • 183
    • 0023875632 scopus 로고
    • Laminin alters cellshape and stimulates motility and proliferation of murine skeletal myoblasts
    • Öcalan, M., Goodman, S. L., Kuhl, U., Hauschka, S. D. and von der Mark, K., Laminin alters cellshape and stimulates motility and proliferation of murine skeletal myoblasts, Develop. Biol., 125, 158-167, 1988.
    • (1988) Develop. Biol. , vol.125 , pp. 158-167
    • Öcalan, M.1    Goodman, S.L.2    Kuhl, U.3    Hauschka, S.D.4    Von der Mark, K.5
  • 184
    • 0024504538 scopus 로고
    • Domains of laminin with growth-factor activity
    • Panayotou, R., End, P., Aumailley, M., Timpl, R., and Engel, J., Domains of laminin with growth-factor activity, Cell, 56, 93-99, 1989.
    • (1989) Cell , vol.56 , pp. 93-99
    • Panayotou, R.1    End, P.2    Aumailley, M.3    Timpl, R.4    Engel, J.5
  • 185
    • 0011247587 scopus 로고
    • Structure and assembly of basement membrane and related extracellular matrix proteins
    • Steiner, M. and Richardson, P. D., Eds., CRC Press, Boca Raton
    • Beck, S. and Gruber, M., Structure and assembly of basement membrane and related extracellular matrix proteins, in Cell Adhesion, Steiner, M. and Richardson, P. D., Eds., CRC Press, Boca Raton, 1995, 219-251.
    • (1995) Cell Adhesion , pp. 219-251
    • Beck, S.1    Gruber, M.2
  • 186
    • 0025831155 scopus 로고
    • Structure and biological role of vitronectin, Annnu
    • Preissner, K. T., Structure and biological role of vitronectin, Annnu. Rev. Cell Biol., 7, 275-310, 1991.
    • (1991) Rev. Cell Biol. , vol.7 , pp. 275-310
    • Preissner, K.T.1
  • 187
    • 0021933434 scopus 로고
    • Monocytes and macrophages synthesize and secrete thrombospondin
    • Jaffe, E. A., Ruggiero, J. T., and Falcone, D. J., Monocytes and macrophages synthesize and secrete thrombospondin, Blood, 65, 79-84, 1985.
    • (1985) Blood , vol.65 , pp. 79-84
    • Jaffe, E.A.1    Ruggiero, J.T.2    Falcone, D.J.3
  • 188
    • 0020394721 scopus 로고
    • Thrombospondin: Synthesis and secretion by cells in culture
    • Raugi, G. J., Mumby, S. M., Abbott Brown, D., and Bornstein, P., Thrombospondin: synthesis and secretion by cells in culture, J. Cell Biol., 95, 351-354, 1982.
    • (1982) J. Cell Biol. , vol.95 , pp. 351-354
    • Raugi, G.J.1    Mumby, S.M.2    Abbott Brown, D.3    Bornstein, P.4
  • 189
    • 0024447313 scopus 로고
    • Thrombospondin and fibronectin are synthesized by neutrophils in human inflammatory joint disease and in rabbit model of in vivo neutrophil activation
    • Kreis, C., La Fleur, M., Menard, C., Paquin, R., and Beautieu, A. D., Thrombospondin and fibronectin are synthesized by neutrophils in human inflammatory joint disease and in rabbit model of in vivo neutrophil activation, J. Immunol., 143, 1961-1968, 1989.
    • (1989) J. Immunol. , vol.143 , pp. 1961-1968
    • Kreis, C.1    La Fleur, M.2    Menard, C.3    Paquin, R.4    Beautieu, A.D.5
  • 190
    • 0025823515 scopus 로고
    • Extracellular proteins that modulate cell-matrix interactions
    • Sage, E. H. and Bornstein, P., Extracellular proteins that modulate cell-matrix interactions, J. Biol. Chem., 266, 14831-14834, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14831-14834
    • Sage, E.H.1    Bornstein, P.2
  • 192
    • 0028179351 scopus 로고
    • v Integrins mediate the rise in intracellular calcium in endothelial cells on fibronectin even though they play a minor role in adhesion
    • v Integrins mediate the rise in intracellular calcium in endothelial cells on fibronectin even though they play a minor role in adhesion. J. Biol. Chem., 269, 11133-11137, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11133-11137
    • Schwartz, M.A.1    Denninghoff, K.2
  • 195
    • 0025065013 scopus 로고
    • Serotonin-activated signal transduction via serotonin receptors on Jurkat cells
    • Aune, T. M., Kelley, K. A., Ranges, G. E., and Bombara, M. P., Serotonin-activated signal transduction via serotonin receptors on Jurkat cells, J. Immunol., 145, 1826-1831, 1990.
    • (1990) J. Immunol. , vol.145 , pp. 1826-1831
    • Aune, T.M.1    Kelley, K.A.2    Ranges, G.E.3    Bombara, M.P.4
  • 196
    • 0027457818 scopus 로고
    • 2+ in Jurkat, a human leukemic helper T lymphocyte line
    • 2+ in Jurkat, a human leukemic helper T lymphocyte line, Mol. Pharmacol., 43, 356-364, 1993.
    • (1993) Mol. Pharmacol. , vol.43 , pp. 356-364
    • Kaneda, T.1    Kitamura, Y.2    Nomura, Y.3
  • 199
    • 0022212592 scopus 로고
    • Exogenous ATP enhances calcium influx in intact thymocytes
    • Lin, J., Krishnaraj, R., and Kemp, R. G., Exogenous ATP enhances calcium influx in intact thymocytes, J. Immunol., 135, 3403-3410, 1985.
    • (1985) J. Immunol. , vol.135 , pp. 3403-3410
    • Lin, J.1    Krishnaraj, R.2    Kemp, R.G.3
  • 200
    • 0025915013 scopus 로고
    • Stimulation of DNA synthesis in Jukrat cells by synergistic action between adenine and guanine nucleotides
    • Tokumitsu, Y., Yanagawa, Y., and Nomura, Y., Stimulation of DNA synthesis in Jukrat cells by synergistic action between adenine and guanine nucleotides, FEBS Lett., 288, 81-85, 1991.
    • (1991) FEBS Lett. , vol.288 , pp. 81-85
    • Tokumitsu, Y.1    Yanagawa, Y.2    Nomura, Y.3
  • 203
    • 0025831191 scopus 로고
    • A phosphatidic acid-sensitive intracellular pool of calcium is released by anti-CD3 in Jurkat T cells
    • Breittmayer, J.-P., Aussel, C., Farahifar, D., Cousin, J.-L., and Fehlmann, M., A phosphatidic acid-sensitive intracellular pool of calcium is released by anti-CD3 in Jurkat T cells, Immunology, 73, 134-139, 1991.
    • (1991) Immunology , vol.73 , pp. 134-139
    • Breittmayer, J.-P.1    Aussel, C.2    Farahifar, D.3    Cousin, J.-L.4    Fehlmann, M.5
  • 204
    • 0029043134 scopus 로고
    • Effect of lysophospholipids on signaling in the human Jurkat T cell line
    • Xu, Y., Casey, G., and Mills, G. B., Effect of lysophospholipids on signaling in the human Jurkat T cell line, J. Cell Physiol., 163, 441-450, 1995.
    • (1995) J. Cell Physiol. , vol.163 , pp. 441-450
    • Xu, Y.1    Casey, G.2    Mills, G.B.3
  • 205
    • 0027959081 scopus 로고
    • 2+ signals elicited by CD3 monoclonal antibody, thapsigargin, or ionomycin in the Jurkat T cell line
    • 2+ signals elicited by CD3 monoclonal antibody, thapsigargin, or ionomycin in the Jurkat T cell line, J. Biol. Chem., 269, 5054-5058, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5054-5058
    • Breittmayer1    Bernard, A.2    Aussei, C.3
  • 209
    • 0028278702 scopus 로고
    • M1cell surface gangliosides in the human Jurkat T cell line
    • M1cell surface gangliosides in the human Jurkat T cell line, J. immunol., 152, 3271-3281, 1994.
    • (1994) J. Immunol. , vol.152 , pp. 3271-3281
    • Gouy, H.1    Deterre, P.2    Debre, P.3    Bismuth, G.4
  • 210
    • 0027178088 scopus 로고
    • 7,-12-Dimethyl- Benz[a]anthracene activates protein-tyrosine kinases Fyn and Lck in the HPB-ALL human T-cell line and increases tyrosine phosphorylation of phospholipase C-γ 1, formation of inosiol 1,4,5-trisphosphate, and mobilization of intracellular calcium
    • Archuleta, M. M., Schieven, G. L., Ledbetter, J. A., Deanin, G. G., and Burchiel, S. W., 7,-12-Dimethyl- benz[a]anthracene activates protein-tyrosine kinases Fyn and Lck in the HPB-ALL human T-cell line and increases tyrosine phosphorylation of phospholipase C-γ 1, formation of inosiol 1,4,5-trisphosphate, and mobilization of intracellular calcium, Proc, Natl. Acad. Sci. U.S.A., 90, 6105-6109, 1993.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 6105-6109
    • Archuleta, M.M.1    Schieven, G.L.2    Ledbetter, J.A.3    Deanin, G.G.4    Burchiel, S.W.5
  • 211
    • 0027283617 scopus 로고
    • Intracellular calcium oscillations induced in a T-cell line by a weak 50 Hz magnetic field
    • Lindström, E., Lindström, P., Berglund, A., Hansson Mild, K., and Lundgren, E., Intracellular calcium oscillations induced in a T-cell line by a weak 50 Hz magnetic field, J. Cell Physiol., 156, 395-398, 1993.
    • (1993) J. Cell Physiol. , vol.156 , pp. 395-398
    • Lindström, E.1    Lindström, P.2    Berglund, A.3    Hansson Mild, K.4    Lundgren, E.5
  • 212
    • 0028893427 scopus 로고
    • Low-frequency MFs increased inositol 1,4,5-trisphosphate levels in the Jurkat cell line
    • Korzh-Sleptsova, I. L., Lindström, E., Mild, K. H., Berglund, A., and Lundgren, E., Low-frequency MFs increased inositol 1,4,5-trisphosphate levels in the Jurkat cell line, FEBS Lett., 359, 151-154, 1995.
    • (1995) FEBS Lett. , vol.359 , pp. 151-154
    • Korzh-Sleptsova, I.L.1    Lindström, E.2    Mild, K.H.3    Berglund, A.4    Lundgren, E.5
  • 213
    • 0029150708 scopus 로고
    • CD45 phosphatase in Jurkat cells is necessary for response to applied ELF magnetic fields
    • Lindström, E., Berglund, A., Hansson Mild, K., Lindström, P., and Lundgren, E., CD45 phosphatase in Jurkat cells is necessary for response to applied ELF magnetic fields, FEBS Lett., 370,118-122,1995.
    • (1995) FEBS Lett. , vol.370 , pp. 118-122
    • Lindström, E.1    Berglund, A.2    Hansson Mild, K.3    Lindström, P.4    Lundgren, E.5


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