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Volumn 276, Issue 4 39-4, 1999, Pages

1,25-Dihydroxyvitamin D3 but not TPA activates PLD in Caco-2 cells via pp60(c-src) and RhoA

Author keywords

Calcitriol; G proteins; Pertussis toxin; Phorbol esters; Signal transduction

Indexed keywords

CALCITRIOL; GUANINE NUCLEOTIDE BINDING PROTEIN; PHORBOL 13 ACETATE 12 MYRISTATE; PHOSPHOLIPASE D; PROTEIN KINASE P60; RHO FACTOR;

EID: 0032957614     PISSN: 01931857     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpgi.1999.276.4.g1005     Document Type: Article
Times cited : (28)

References (51)
  • 2
    • 0027403699 scopus 로고
    • Phospholipase D and cell signaling
    • Billah, M. M. Phospholipase D and cell signaling. Curr. Opin. Immunol. 5: 114-123, 1993.
    • (1993) Curr. Opin. Immunol. , vol.5 , pp. 114-123
    • Billah, M.M.1
  • 5
    • 0028081350 scopus 로고
    • Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins
    • Bokoch, G. M., B. P. Bohl, and T.-H. Chuang. Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins. J. Biol. Chem. 269: 31674-31679, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31674-31679
    • Bokoch, G.M.1    Bohl, B.P.2    Chuang, T.-H.3
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254, 1976.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0030614464 scopus 로고    scopus 로고
    • Neuropeptide Y Y2 receptor and somatostatin sst2 receptor coupling to mobilization of intracellular calcium in SH-SY5Y human
    • Connor, M., A. Yeo, and G. Henderson. Neuropeptide Y Y2 receptor and somatostatin sst2 receptor coupling to mobilization of intracellular calcium in SH-SY5Y human. Br. J. Pharmacol. 120: 455-463, 1997.
    • (1997) Br. J. Pharmacol. , vol.120 , pp. 455-463
    • Connor, M.1    Yeo, A.2    Henderson, G.3
  • 9
    • 0026445085 scopus 로고
    • Phospholipases C and D in mitogenic signal transduction
    • Cook, S. J., and M. J. Wakelam. Phospholipases C and D in mitogenic signal transduction. Rev. Physiol. Biochem. Pharmacol. 119: 13-45, 1992.
    • (1992) Rev. Physiol. Biochem. Pharmacol. , vol.119 , pp. 13-45
    • Cook, S.J.1    Wakelam, M.J.2
  • 10
    • 0029943257 scopus 로고    scopus 로고
    • Activation of phospholipase D by ras proteins is independent of protein kinase C
    • Del Peso, L., R. Hernandez, P. Esteve, and J. C. Lacal. Activation of phospholipase D by ras proteins is independent of protein kinase C. J. Cell. Biochem. 61: 599-608, 1996.
    • (1996) J. Cell. Biochem. , vol.61 , pp. 599-608
    • Del Peso, L.1    Hernandez, R.2    Esteve, P.3    Lacal, J.C.4
  • 11
    • 0029907265 scopus 로고    scopus 로고
    • A role for Pyk2 and Src in linking G protein-coupled receptors with MAP kinase activation
    • Dikic, I., G. Tokiwa, S. Lev, S. A. Courtneidge, and J. Schlessinger. A role for Pyk2 and Src in linking G protein-coupled receptors with MAP kinase activation. Nature 383: 547-550, 1996.
    • (1996) Nature , vol.383 , pp. 547-550
    • Dikic, I.1    Tokiwa, G.2    Lev, S.3    Courtneidge, S.A.4    Schlessinger, J.5
  • 13
    • 0030948743 scopus 로고    scopus 로고
    • New developments in phospholipase D
    • Exton, J. H. New developments in phospholipase D. J. Biol. Chem. 272: 15579-15582, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15579-15582
    • Exton, J.H.1
  • 14
    • 0021895138 scopus 로고
    • 2+ indicators with greatly improved fluorescence properties
    • 2+ indicators with greatly improved fluorescence properties. J. Biol. Chem. 260: 3440-3450, 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 16
    • 0008855384 scopus 로고    scopus 로고
    • Characterization of two alternately spliced forms of phospholipase D1. Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-α
    • Hammond, S. M., J. M. Jenco, S. Nakashima, K. Cadwallader, Q. Gu, S. Cook, Y. Nozawa, G. D. Prestwich, M. A. Frohman, and A. J. Morris. Characterization of two alternately spliced forms of phospholipase D1. Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-α. J. Biol. Chem. 272: 3860-3868, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3860-3868
    • Hammond, S.M.1    Jenco, J.M.2    Nakashima, S.3    Cadwallader, K.4    Gu, Q.5    Cook, S.6    Nozawa, Y.7    Prestwich, G.D.8    Frohman, M.A.9    Morris, A.J.10
  • 17
    • 0024391004 scopus 로고
    • Regulation of protein kinase C by nerve growth factor, epidermal growth factor and phorbol esters in PC12 pheochromocytoma cells
    • Heasley, L. E., and G. L. Johnson. Regulation of protein kinase C by nerve growth factor, epidermal growth factor and phorbol esters in PC12 pheochromocytoma cells. J. Biol. Chem. 264: 8646-8652, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8646-8652
    • Heasley, L.E.1    Johnson, G.L.2
  • 18
    • 0031019308 scopus 로고    scopus 로고
    • Role of Rho family proteins in phospholipase D activation by growth factors
    • Hess, J. A., A. H. Ross, R. G. Qiu, M. Symons, and J. H. Exton. Role of Rho family proteins in phospholipase D activation by growth factors. J. Biol. Chem. 272: 1615-1620, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1615-1620
    • Hess, J.A.1    Ross, A.H.2    Qiu, R.G.3    Symons, M.4    Exton, J.H.5
  • 19
    • 0029155727 scopus 로고
    • ADP-ribosylation factor translocation correlates with potentiation of GTPγS-stimulated phospholipase D activity in membrane fractions of HL-60 cells
    • Houle, M. G., R. A. Kahn, P. H. Naccache, and S. Bourgoin. ADP-ribosylation factor translocation correlates with potentiation of GTPγS-stimulated phospholipase D activity in membrane fractions of HL-60 cells. J. Biol. Chem. 270: 22795-22800, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22795-22800
    • Houle, M.G.1    Kahn, R.A.2    Naccache, P.H.3    Bourgoin, S.4
  • 20
    • 0031028641 scopus 로고    scopus 로고
    • 2+-dependent protein tyrosine phosphorylation in carbachol-induced phospholipase D activation in rat pheochromocytoma PC12 cells
    • 2+-dependent protein tyrosine phosphorylation in carbachol-induced phospholipase D activation in rat pheochromocytoma PC12 cells. J. Neurochem. 68: 419-425, 1997.
    • (1997) J. Neurochem. , vol.68 , pp. 419-425
    • Ito, Y.1    Nakashima, S.2    Kanoh, H.3    Nozawa, Y.4
  • 21
    • 0028921344 scopus 로고
    • Ras mediates the activation of phospholipase D by v-Src
    • Jiang, H., Z. Lu, J.-Q. Luo, A. Wolfman, and D. A. Foster. Ras mediates the activation of phospholipase D by v-Src. J. Biol. Chem. 270: 6006-6009, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6006-6009
    • Jiang, H.1    Lu, Z.2    Luo, J.-Q.3    Wolfman, A.4    Foster, D.A.5
  • 22
    • 0028818914 scopus 로고
    • Involvement of Ral GTPase in v-Src-induced phospholipase D activation
    • Jiang, H., J. Q. Luo, T. Urano, P. Frankel, Z. Lu, D. A. Foster, and L. A. Feig. Involvement of Ral GTPase in v-Src-induced phospholipase D activation. Nature 378: 409-412, 1995.
    • (1995) Nature , vol.378 , pp. 409-412
    • Jiang, H.1    Luo, J.Q.2    Urano, T.3    Frankel, P.4    Lu, Z.5    Foster, D.A.6    Feig, L.A.7
  • 23
    • 0030610466 scopus 로고    scopus 로고
    • 2D-adrenergic receptor coupling to phospholipase D in a PC12 cell lysate
    • 2D-adrenergic receptor coupling to phospholipase D in a PC12 cell lysate. J. Biol. Chem. 272: 14556-14561, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14556-14561
    • Jinsi-Parimoo, A.1    Deth, R.C.2
  • 24
    • 0028138774 scopus 로고
    • Activation of human monocytes via a non-neurokinin substance P receptor that is coupled to Gi protein, calcium, phospholipase D, MAP kinase, and IL-6 production
    • Kavelaars, A., D. Broeke, F. Jeurissen, J. Kardux, A. Meijer, R. Franklin, E. W. Gelfand, and C. J. Heijnen. Activation of human monocytes via a non-neurokinin substance P receptor that is coupled to Gi protein, calcium, phospholipase D, MAP kinase, and IL-6 production. J. Immunol. 153: 3691-3699, 1994.
    • (1994) J. Immunol. , vol.153 , pp. 3691-3699
    • Kavelaars, A.1    Broeke, D.2    Jeurissen, F.3    Kardux, J.4    Meijer, A.5    Franklin, R.6    Gelfand, E.W.7    Heijnen, C.J.8
  • 27
    • 0029978898 scopus 로고    scopus 로고
    • Regulation of phospholipase D by protein kinase C
    • Kiss, Z. Regulation of phospholipase D by protein kinase C. Chem. Phys. Lipids 80: 81-102, 1996.
    • (1996) Chem. Phys. Lipids , vol.80 , pp. 81-102
    • Kiss, Z.1
  • 28
    • 0030013233 scopus 로고    scopus 로고
    • Evidence that phospholipase D mediates ADP ribosylation factor-dependent formation of Golgi coated vesicles
    • Ktistakis, N. T., H. A. Brown, M. G. Waters, P. C. Sternweis, and M. G. Roth. Evidence that phospholipase D mediates ADP ribosylation factor-dependent formation of Golgi coated vesicles. J. Cell Biol. 134: 295-306, 1996.
    • (1996) J. Cell Biol. , vol.134 , pp. 295-306
    • Ktistakis, N.T.1    Brown, H.A.2    Waters, M.G.3    Sternweis, P.C.4    Roth, M.G.5
  • 29
    • 0029929668 scopus 로고    scopus 로고
    • Phospholipase D is activated by G protein and not by calcium ions in vascular smooth muscle
    • Heart Circ. Physiol. 39
    • LaBelle, E. F., R. M. Fulbright, R. J. Barsotti, H. Gu, and E. Polyak. Phospholipase D is activated by G protein and not by calcium ions in vascular smooth muscle. Am. J. Physiol. 270 (Heart Circ. Physiol. 39): H1031-H1037, 1996.
    • (1996) Am. J. Physiol. , vol.270
    • LaBelle, E.F.1    Fulbright, R.M.2    Barsotti, R.J.3    Gu, H.4    Polyak, E.5
  • 30
    • 0030978912 scopus 로고    scopus 로고
    • Phospholipase C and membrane action of calcitriol and estradiol
    • Le Mellay, V., B. Grosse, and M. Lieberherr. Phospholipase C and membrane action of calcitriol and estradiol. J. Biol. Chem. 272: 11902-11907, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11902-11907
    • Le Mellay, V.1    Grosse, B.2    Lieberherr, M.3
  • 31
    • 0030614911 scopus 로고    scopus 로고
    • Gβγ subunits mediate Src-dependent phosphorylation of the epidermal growth factor receptor. A scaffold for G protein-coupled receptor-mediated Ras activation
    • Luttrell, L. M., G. J. Della Rocca, T. van Biesen, D. K. Luttrell, and R. J. Lefkowitz. Gβγ subunits mediate Src-dependent phosphorylation of the epidermal growth factor receptor. A scaffold for G protein-coupled receptor-mediated Ras activation. J. Biol. Chem. 272: 4637-4644, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4637-4644
    • Luttrell, L.M.1    Della Rocca, G.J.2    Van Biesen, T.3    Luttrell, D.K.4    Lefkowitz, R.J.5
  • 32
    • 0026787683 scopus 로고
    • α2-C10 adrenergic receptors expressed in rat 1 fibroblasts can regulate both adenylylcyclase and phospholipase D-mediated hydrolysis of phosphatidylcholine by interacting with pertussis toxin-sensitive guanine nucleotide-binding proteins
    • MacNulty, E. E., S. J. McClue, I. C. Carr, T. Jess, M. J. Wakelam, and G. Milligan. α2-C10 adrenergic receptors expressed in rat 1 fibroblasts can regulate both adenylylcyclase and phospholipase D-mediated hydrolysis of phosphatidylcholine by interacting with pertussis toxin-sensitive guanine nucleotide-binding proteins. J. Biol. Chem. 267: 2149-2156, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2149-2156
    • MacNulty, E.E.1    McClue, S.J.2    Carr, I.C.3    Jess, T.4    Wakelam, M.J.5    Milligan, G.6
  • 33
    • 16844366239 scopus 로고    scopus 로고
    • Evidence for Rho-mediated agonist stimulation of phospholipase D in rat1 fibroblasts. Effects of Clostridium botulinum C3 exoenzyme
    • Malcolm, K. C., C. M. Elliott, and J. H. Exton. Evidence for Rho-mediated agonist stimulation of phospholipase D in rat1 fibroblasts. Effects of Clostridium botulinum C3 exoenzyme. J. Biol. Chem. 271: 13135-13139, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13135-13139
    • Malcolm, K.C.1    Elliott, C.M.2    Exton, J.H.3
  • 34
    • 0030037396 scopus 로고    scopus 로고
    • Activation of phospholipase D and phosphatidylinositol 4-phosphate 5-kinase in HL60 membranes is mediated by endogenous Arf but not Rho
    • Martin, A., F. D. Brown, M. N. Hodgkin, A. J. Bradwell, S. J. Cook, M. Hart, and M. J. O. Wakelam. Activation of phospholipase D and phosphatidylinositol 4-phosphate 5-kinase in HL60 membranes is mediated by endogenous Arf but not Rho. J. Biol. Chem. 271: 17397-17403, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17397-17403
    • Martin, A.1    Brown, F.D.2    Hodgkin, M.N.3    Bradwell, A.J.4    Cook, S.J.5    Hart, M.6    Wakelam, M.J.O.7
  • 37
    • 0030592239 scopus 로고    scopus 로고
    • 3 stimulation of phospholipases C and D in muscle cells involves extracellular calcium and a pertussis-sensitive G protein
    • 3 stimulation of phospholipases C and D in muscle cells involves extracellular calcium and a pertussis-sensitive G protein. Mol. Cell. Endocrinol. 122: 207-211, 1996.
    • (1996) Mol. Cell. Endocrinol. , vol.122 , pp. 207-211
    • Morelli, S.1    Boland, R.2    De Boland, A.R.3
  • 38
    • 0028843905 scopus 로고
    • Mechanism of interaction of protein kinase C with phorbol esters
    • Mosior, M., and A. C. Newton. Mechanism of interaction of protein kinase C with phorbol esters. J. Biol. Chem. 270: 25526-25533, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25526-25533
    • Mosior, M.1    Newton, A.C.2
  • 39
    • 0027272575 scopus 로고
    • Phopholipase C and phospholipase D are activated independently of each other in chemotactic peptide-stimulated human neutrophils
    • Mullmann, T. J., B. Cheewatrakoolpong, J. C. Anthes, M. I. Siegel, R. W. Egan, and M. M. Billah. Phopholipase C and phospholipase D are activated independently of each other in chemotactic peptide-stimulated human neutrophils. J. Leukoc. Biol. 53: 630-635, 1993.
    • (1993) J. Leukoc. Biol. , vol.53 , pp. 630-635
    • Mullmann, T.J.1    Cheewatrakoolpong, B.2    Anthes, J.C.3    Siegel, M.I.4    Egan, R.W.5    Billah, M.M.6
  • 40
    • 0030044056 scopus 로고    scopus 로고
    • Regulation of membrane-bound phospholipase D by protein kinase C in HL60 cells. Synergistic action of small GTP-binding protein RhoA
    • Ohguchi, K., Y. Banno, S. Nakashima, and Y. Nozawa. Regulation of membrane-bound phospholipase D by protein kinase C in HL60 cells. Synergistic action of small GTP-binding protein RhoA. J. Biol. Chem. 271: 4366-4372, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4366-4372
    • Ohguchi, K.1    Banno, Y.2    Nakashima, S.3    Nozawa, Y.4
  • 43
    • 0028000140 scopus 로고
    • Serum alleviates the requirement of the granulocyte-macrophage colony-stimulating factor (GM-CSF)-induced Ras activation for proliferation of BaF3 cells
    • Sakamaki, K., and S. Yonehara. Serum alleviates the requirement of the granulocyte-macrophage colony-stimulating factor (GM-CSF)-induced Ras activation for proliferation of BaF3 cells. FEBS Lett. 353: 133-137, 1994.
    • (1994) FEBS Lett. , vol.353 , pp. 133-137
    • Sakamaki, K.1    Yonehara, S.2
  • 44
    • 0028872684 scopus 로고
    • Determination of absolute amounts of GDP and GTP bound to Ras in mammalian cells: Comparison of parental and Ras-overproducing NIH 3T3 fibroblasts
    • Scheele, J. S., J. M. Rhee, and G. R. Boss. Determination of absolute amounts of GDP and GTP bound to Ras in mammalian cells: comparison of parental and Ras-overproducing NIH 3T3 fibroblasts. Proc. Natl. Acad. Sci. USA 92: 1097-1100, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1097-1100
    • Scheele, J.S.1    Rhee, J.M.2    Boss, G.R.3
  • 45
    • 0029671455 scopus 로고    scopus 로고
    • Regulation of phospholipase D by protein kinase C is synergistic with ADP-ribosylation factor and independent of protein kinase activity
    • Singer, W. D., H. A. Brown, X. Jiang, and P. C. Sternweis. Regulation of phospholipase D by protein kinase C is synergistic with ADP-ribosylation factor and independent of protein kinase activity. J. Biol. Chem. 271: 4504-4510, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4504-4510
    • Singer, W.D.1    Brown, H.A.2    Jiang, X.3    Sternweis, P.C.4
  • 46
    • 0028169506 scopus 로고
    • Epidermal growth factor induces the production of biologically distinguishable diglyceride species from phosphatidylinositol and phosphatidylcholine via the independent activation of type C and type D phospholipases
    • Song, J., Y. W. Jiang, and D. A. Foster. Epidermal growth factor induces the production of biologically distinguishable diglyceride species from phosphatidylinositol and phosphatidylcholine via the independent activation of type C and type D phospholipases. Cell Growth Differ. 5: 79-85, 1994.
    • (1994) Cell Growth Differ. , vol.5 , pp. 79-85
    • Song, J.1    Jiang, Y.W.2    Foster, D.A.3
  • 47
    • 0025610723 scopus 로고
    • Activation of protein kinase C is not required for exocytosis from bovine adrenal chromaffin cells
    • Terbush, D. R., and R. W. Holz. Activation of protein kinase C is not required for exocytosis from bovine adrenal chromaffin cells. J. Biol. Chem. 265: 21179-21184, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21179-21184
    • Terbush, D.R.1    Holz, R.W.2
  • 48
    • 0029809315 scopus 로고    scopus 로고
    • What's new in ras genes? Physiological role of ras genes in signal transduction and significance of ras gene activation in tumorigenesis
    • Waldmann, V., and H. M. Rabes. What's new in ras genes? Physiological role of ras genes in signal transduction and significance of ras gene activation in tumorigenesis. Pathol. Res. Pract. 192: 883-891, 1996.
    • (1996) Pathol. Res. Pract. , vol.192 , pp. 883-891
    • Waldmann, V.1    Rabes, H.M.2
  • 49
    • 0026808823 scopus 로고
    • + exchange by stimulating membrane phosphoinositide turnover and increasing cytosolic calcium in CaCo-2 cells
    • + exchange by stimulating membrane phosphoinositide turnover and increasing cytosolic calcium in CaCo-2 cells. Endocrinology 131: 1125-1133, 1992.
    • (1992) Endocrinology , vol.131 , pp. 1125-1133
    • Wali, R.K.1    Baum, C.L.2    Bolt, M.J.G.3    Brasitus, T.A.4    Sitrin, M.D.5
  • 50
    • 0025323383 scopus 로고
    • 3 stimulates membrane phosphoinositide turnover, activates protein kinase C, and increases cytosolic calcium in rat colonic epithelium
    • 3 stimulates membrane phosphoinositide turnover, activates protein kinase C, and increases cytosolic calcium in rat colonic epithelium. J. Clin. Invest. 85: 1296-1303, 1990.
    • (1990) J. Clin. Invest. , vol.85 , pp. 1296-1303
    • Wali, R.K.1    Baum, C.L.2    Sitrin, M.D.3    Brasitus, T.A.4


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