메뉴 건너뛰기




Volumn 1391, Issue 3, 1998, Pages 337-350

Neuromedin B activates phospholipase D through both PKC-dependent and PKC-independent mechanisms

Author keywords

Calcium; Neuromedin B; Phospholipase C; Phospholipase D; Protein kinase C; Receptor

Indexed keywords

2 [1 (3 DIMETHYLAMINOPROPYL) 3 INDOLYL] 3 (3 INDOLYL)MALEIMIDE; BOMBESIN; CALCIUM ION; NEUROMEDIN B; PHOSPHOLIPASE C; PHOSPHOLIPASE D; PROTEIN KINASE C; RECEPTOR PROTEIN;

EID: 0032557180     PISSN: 00052760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2760(98)00014-9     Document Type: Article
Times cited : (11)

References (59)
  • 2
    • 0002905854 scopus 로고
    • Bombesin-like peptides in health and disease
    • [2] Y. Tache, P. Melchiorri, L. Negri, Bombesin-like peptides in health and disease, Ann. NY Acad. Sci. 547 (1988) 1-541.
    • (1988) Ann. Ny Acad. Sci. , vol.547 , pp. 1-541
    • Tache, Y.1    Melchiorri, P.2    Negri, L.3
  • 3
    • 0001289623 scopus 로고
    • Receptors on pancreatic acinar cells
    • L.R. Johnson, E.D. Jacobsen, J. Christensen, D.H. Alpers, J.H. Walsh (Eds.), Raven Press, New York
    • [3] R.T. Jensen, Receptors on pancreatic acinar cells, in: L.R. Johnson, E.D. Jacobsen, J. Christensen, D.H. Alpers, J.H. Walsh (Eds.), Physiology of the Gastrointestinal Tract, Vol. 2, 3rd edn., Raven Press, New York, 1994, pp. 1377-1446.
    • (1994) Physiology of the Gastrointestinal Tract, Vol. 2, 3rd Edn. , vol.2 , pp. 1377-1446
    • Jensen, R.T.1
  • 4
    • 0028069312 scopus 로고
    • Rapid desensitization and resensitization of bombesin-stimulated phospholipase D activity in Swiss 3T3 cells
    • [4] C.P. Briscoe, R. Plevin, J.O. Wakelam, Rapid desensitization and resensitization of bombesin-stimulated phospholipase D activity in Swiss 3T3 cells, Biochem. J. 298 (1994) 61-67.
    • (1994) Biochem. J. , vol.298 , pp. 61-67
    • Briscoe, C.P.1    Plevin, R.2    Wakelam, J.O.3
  • 5
    • 0025947611 scopus 로고
    • The regulation of phospholipase D activity and its role in sn-1,2-diacylglycerol formation in bombesin-and phorbol 12-myristate 13-acetate-stimulated Swiss 3T3 cells
    • [5] S.J. Cook, C.P. Briscoe, M.J.O. Wakelam, The regulation of phospholipase D activity and its role in sn-1,2-diacylglycerol formation in bombesin-and phorbol 12-myristate 13-acetate-stimulated Swiss 3T3 cells, Biochem. J. 280 (1991) 431-438.
    • (1991) Biochem. J. , vol.280 , pp. 431-438
    • Cook, S.J.1    Briscoe, C.P.2    Wakelam, M.J.O.3
  • 6
    • 0028917266 scopus 로고
    • Heterologous desensitization of bombesin-and vasopressin-stimulated phospholipase D activity in Swiss 3T3 fibroblasts
    • [6] C.P. Briscoe, M.J.O. Wakelam, Heterologous desensitization of bombesin-and vasopressin-stimulated phospholipase D activity in Swiss 3T3 fibroblasts, FEBS Lett. 361 (1995) 162-166.
    • (1995) FEBS Lett. , vol.361 , pp. 162-166
    • Briscoe, C.P.1    Wakelam, M.J.O.2
  • 7
    • 0027396047 scopus 로고
    • Bombesin stimulates distinct time-dependent changes in the sn-1,2-diacylglycerol molecular species profile from Swiss 3T3 fibroblasts as analyzed by 3,5-dinitrobenzoyl derivatization and h.P.L.C. Separation
    • [7] T.R. Pettitt, M.J.O. Wakelam, Bombesin stimulates distinct time-dependent changes in the sn-1,2-diacylglycerol molecular species profile from Swiss 3T3 fibroblasts as analyzed by 3,5-dinitrobenzoyl derivatization and h.p.l.c. separation, Biochem. J. 289 (1993) 487-495.
    • (1993) Biochem. J. , vol.289 , pp. 487-495
    • Pettitt, T.R.1    Wakelam, M.J.O.2
  • 8
    • 0025356574 scopus 로고
    • The regulation and cellular functions of phosphatidylcholine hydrolysis
    • [8] M.M. Billah, J.C. Anthes, The regulation and cellular functions of phosphatidylcholine hydrolysis, Biochem. J. 269 (1990) 281-291.
    • (1990) Biochem. J. , vol.269 , pp. 281-291
    • Billah, M.M.1    Anthes, J.C.2
  • 9
    • 0026013918 scopus 로고
    • Phospholipase D in cell signalling and its relationship to phospholipase C
    • [9] S.D. Shukla, S.P. Halenda, Phospholipase D in cell signalling and its relationship to phospholipase C, Life Sci. 48 (1991) 851-866.
    • (1991) Life Sci. , vol.48 , pp. 851-866
    • Shukla, S.D.1    Halenda, S.P.2
  • 11
    • 0027142022 scopus 로고
    • ADP-Ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity
    • [11] H.A. Brown, S. Gutowski, C.R. Moomaw, C. Slaughter, P.C. Sternweis, ADP-Ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity, Cell 75 (1993) 1137-1144.
    • (1993) Cell , vol.75 , pp. 1137-1144
    • Brown, H.A.1    Gutowski, S.2    Moomaw, C.R.3    Slaughter, C.4    Sternweis, P.C.5
  • 13
    • 0026703236 scopus 로고
    • Phospholipid base exchange activity in rat liver plasma membranes
    • [13] R.A. Siddiqui, J.H. Exton, Phospholipid base exchange activity in rat liver plasma membranes, J. Biol. Chem. 267 (1992) 5755-5761.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5755-5761
    • Siddiqui, R.A.1    Exton, J.H.2
  • 14
    • 0027986677 scopus 로고
    • Activation of rat brain phospholipase D by ADP-ribosylation factors 1,5, and 6: Separation of ADP-ribosylation factor-dependent and oleate-dependent enzymes
    • [14] D. Massenburg, J.S. Han, M. Liyanage, W.A. Patton, S.G. Rhee, J. Moss, M. Vaughan, Activation of rat brain phospholipase D by ADP-ribosylation factors 1,5, and 6: separation of ADP-ribosylation factor-dependent and oleate-dependent enzymes, Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 11718-11722.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 11718-11722
    • Massenburg, D.1    Han, J.S.2    Liyanage, M.3    Patton, W.A.4    Rhee, S.G.5    Moss, J.6    Vaughan, M.7
  • 15
    • 0029075145 scopus 로고
    • Partial purification and characterization of Arf-sensitive phospholipase D from porcine brain
    • [15] H.A. Brown, S. Gutowski, R.A. Kahn, P.C. Sternweis, Partial purification and characterization of Arf-sensitive phospholipase D from porcine brain, J. Biol. Chem. 270 (1995) 14935-14943.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14935-14943
    • Brown, H.A.1    Gutowski, S.2    Kahn, R.A.3    Sternweis, P.C.4
  • 16
    • 0029020350 scopus 로고
    • Resolved phospholipase D activity is modulated by cytosolic factors other than Arf
    • [16] W.D. Singer, H.A. Brown, G.M. Bokoch, P.C. Sternweis, Resolved phospholipase D activity is modulated by cytosolic factors other than Arf, J. Biol. Chem. 270 (1995) 14944-14950.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14944-14950
    • Singer, W.D.1    Brown, H.A.2    Bokoch, G.M.3    Sternweis, P.C.4
  • 17
    • 0028296793 scopus 로고
    • Phosphatidylcholine breakdown and signal transduction
    • [17] J.H. Exton, Phosphatidylcholine breakdown and signal transduction, Biochim. Biophys. Acta 1212 (1994) 26-42.
    • (1994) Biochim. Biophys. Acta , vol.1212 , pp. 26-42
    • Exton, J.H.1
  • 18
    • 0026445085 scopus 로고
    • Phospholipases C and D in mitogenic signal transduction
    • [18] S.J. Cook, M.J.O. Wakelam, Phospholipases C and D in mitogenic signal transduction, Rev. Physiol. Biochem. Pharmacol. 119 (1992) 14-38.
    • (1992) Rev. Physiol. Biochem. Pharmacol. , vol.119 , pp. 14-38
    • Cook, S.J.1    Wakelam, M.J.O.2
  • 20
    • 0028082428 scopus 로고
    • Basic FGF activates phospholipase D in endothelial cells in the absence of inositol-lipid hydrolysis
    • [20] A. Ahmed, R. Plevin, M.A. Shoaibi, S.A. Fountain, R.A. Ferriani, S.K. Smith, Basic FGF activates phospholipase D in endothelial cells in the absence of inositol-lipid hydrolysis, Am. J. Physiol. 266 (1994) C206-C212.
    • (1994) Am. J. Physiol. , vol.266
    • Ahmed, A.1    Plevin, R.2    Shoaibi, M.A.3    Fountain, S.A.4    Ferriani, R.A.5    Smith, S.K.6
  • 21
    • 0026734616 scopus 로고
    • Epidermal growth factor increases sn-1,2-diacylglycerol levels and activates phospholipase D-catalyzed phosphatidycholine breakdown in Swiss 3T3 cells in the absence of inositol-lipid hydrolysis
    • [21] S.J. Cook, M.J.O. Wakelam, Epidermal growth factor increases sn-1,2-diacylglycerol levels and activates phospholipase D-catalyzed phosphatidycholine breakdown in Swiss 3T3 cells in the absence of inositol-lipid hydrolysis, Biochem. J. 285 (1992) 247-253.
    • (1992) Biochem. J. , vol.285 , pp. 247-253
    • Cook, S.J.1    Wakelam, M.J.O.2
  • 22
    • 0027337101 scopus 로고
    • Distinct mechanisms of phospholipase D activation and attenuation utilized by different mitogens in NIH-3T3 fibroblasts
    • [22] P. Ben-Av, Y. Eli, U.S. Schmidt, K.E. Tobias, M. Liscovitch, Distinct mechanisms of phospholipase D activation and attenuation utilized by different mitogens in NIH-3T3 fibroblasts, Eur. J. Biochem. 215 (1993) 455-463.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 455-463
    • Ben-Av, P.1    Eli, Y.2    Schmidt, U.S.3    Tobias, K.E.4    Liscovitch, M.5
  • 24
    • 0030070494 scopus 로고    scopus 로고
    • Phospholipase D activation by P2Z-purinoceptor agonists in human lymphocytes is dependent on bivalent cation influx
    • [24] C.E. Gargett, E.J. Cornish, J.S. Wiley, Phospholipase D activation by P2Z-purinoceptor agonists in human lymphocytes is dependent on bivalent cation influx, Biochem. J. 313 (1996) 529-535.
    • (1996) Biochem. J. , vol.313 , pp. 529-535
    • Gargett, C.E.1    Cornish, E.J.2    Wiley, J.S.3
  • 25
    • 0023229006 scopus 로고
    • Phosphatidylethanol formation via transphosphatidylation by rat brain synaptosomal phospholipase D
    • [25] M. Kobayashi, J.N. Kanfer, Phosphatidylethanol formation via transphosphatidylation by rat brain synaptosomal phospholipase D, J. Neurochem. 48 (1987) 1597-1603.
    • (1987) J. Neurochem. , vol.48 , pp. 1597-1603
    • Kobayashi, M.1    Kanfer, J.N.2
  • 27
    • 0027082327 scopus 로고
    • Neuromedin B receptors retain functional expression when transfected into BALB 3T3 fibroblasts: Analysis of binding, kinetics, stoichiometry, modulation by guanine nucleotide binding proteins, signal transduction and comparison with natively expressed receptors
    • [27] R.V. Benya, E. Wada, J.F. Battey, Z. Fahti, L.H. Wang, S.A. Mantey, D.H. Coy, R.T. Jensen, Neuromedin B receptors retain functional expression when transfected into BALB 3T3 fibroblasts: analysis of binding, kinetics, stoichiometry, modulation by guanine nucleotide binding proteins, signal transduction and comparison with natively expressed receptors, Mol. Pharmacol. 42 (6) (1992) 1058-1068.
    • (1992) Mol. Pharmacol. , vol.42 , Issue.6 , pp. 1058-1068
    • Benya, R.V.1    Wada, E.2    Battey, J.F.3    Fahti, Z.4    Wang, L.H.5    Mantey, S.A.6    Coy, D.H.7    Jensen, R.T.8
  • 29
    • 0020595443 scopus 로고
    • Changes in the levels of inositol phosphates after agonist-dependent hydrolysis of membrane phosphoinositides
    • [29] M.J. Berridge, R.M. Dawson, C.P. Downes, J.P. Heslop, R.F. Irvine, Changes in the levels of inositol phosphates after agonist-dependent hydrolysis of membrane phosphoinositides, Biochem. J. 212 (1983) 473-482.
    • (1983) Biochem. J. , vol.212 , pp. 473-482
    • Berridge, M.J.1    Dawson, R.M.2    Downes, C.P.3    Heslop, J.P.4    Irvine, R.F.5
  • 31
    • 0021895138 scopus 로고
    • 2+ indicators with greatly improved fluorescence properties
    • 2+ indicators with greatly improved fluorescence properties, J. Biol. Chem. 260 (1985) 3440-3450.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 32
    • 0030867843 scopus 로고    scopus 로고
    • Discovery of a high affinity radioligand for the human orphan receptor, BRS-3, which demonstrates it has a unique pharmacology compared to other mammalian bombesin receptors
    • [32] S.A. Mantey, H.C. Weber, E. Sainz, M. Akeson, R.R. Ryan, T.K. Pradhan, R.P. Searles, E.R. Spindel, J.F. Battey, D.H. Coy, R.T. Jensen, Discovery of a high affinity radioligand for the human orphan receptor, BRS-3, which demonstrates it has a unique pharmacology compared to other mammalian bombesin receptors, J. Biol. Chem. 272 (1997) 26062-26071.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26062-26071
    • Mantey, S.A.1    Weber, H.C.2    Sainz, E.3    Akeson, M.4    Ryan, R.R.5    Pradhan, T.K.6    Searles, R.P.7    Spindel, E.R.8    Battey, J.F.9    Coy, D.H.10    Jensen, R.T.11
  • 33
    • 0027963251 scopus 로고
    • Gastrin-releasing peptide receptor-induced internalization, down-regulation, desensitization and growth: Possible role of cAMP
    • [33] R.V. Benya, Z. Fathi, T. Pradhan, J.F. Battey, T. Kusui, R.T. Jensen, Gastrin-releasing peptide receptor-induced internalization, down-regulation, desensitization and growth: possible role of cAMP, Mol. Pharmacol. 46 (1994) 235-245.
    • (1994) Mol. Pharmacol. , vol.46 , pp. 235-245
    • Benya, R.V.1    Fathi, Z.2    Pradhan, T.3    Battey, J.F.4    Kusui, T.5    Jensen, R.T.6
  • 34
    • 0023106038 scopus 로고
    • Formation of phosphatidylethanol in rat brain by phospholipase D
    • [34] L. Gustavsson, C. Alling, Formation of phosphatidylethanol in rat brain by phospholipase D, Biochem. Biophys. Res. Commun. 142 (1987) 958-963.
    • (1987) Biochem. Biophys. Res. Commun. , vol.142 , pp. 958-963
    • Gustavsson, L.1    Alling, C.2
  • 35
    • 0028800366 scopus 로고
    • Mitogenic signaling by transfected neuromedin B receptors in Rat-1 cells
    • [35] E.B. Lach, S. Broad, E. Rozengurt, Mitogenic signaling by transfected neuromedin B receptors in Rat-1 cells, Cell Growth Differ. 6 (1995) 1427-1435.
    • (1995) Cell Growth Differ. , vol.6 , pp. 1427-1435
    • Lach, E.B.1    Broad, S.2    Rozengurt, E.3
  • 36
    • 0029155830 scopus 로고
    • Neuromedin B stimulates arachidonic acid release, c-fos gene expression, and the growth of C6 glioma cells
    • [36] T.W. Moody, M. Fagarasan, F. Zia, Neuromedin B stimulates arachidonic acid release, c-fos gene expression, and the growth of C6 glioma cells, Peptides 16 (1995) 1133-1140.
    • (1995) Peptides , vol.16 , pp. 1133-1140
    • Moody, T.W.1    Fagarasan, M.2    Zia, F.3
  • 37
    • 0031423732 scopus 로고    scopus 로고
    • rho and integrity of the actin cytoskeleton
    • rho and integrity of the actin cytoskeleton, Biochemistry 36 (1997) 16328-16337.
    • (1997) Biochemistry , vol.36 , pp. 16328-16337
    • Tsuda, T.1    Kusui, T.2    Jensen, R.T.3
  • 38
    • 0027457992 scopus 로고
    • Pigment dispersion in frog melanophores can be induced by a phorbol ester or stimulation of a recombinant receptor that activates phospholipase C
    • [38] G.F. Graminski, C.K. Jayawickreme, M.N. Potenza, M.R. Lerner, Pigment dispersion in frog melanophores can be induced by a phorbol ester or stimulation of a recombinant receptor that activates phospholipase C, J. Biol. Chem. 268 (1993) 5957-5964.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5957-5964
    • Graminski, G.F.1    Jayawickreme, C.K.2    Potenza, M.N.3    Lerner, M.R.4
  • 39
    • 0024207852 scopus 로고
    • Bombesin enhancement of cAMP accumulation in Swiss 3T3 cells: Evidence of a dual mechanism of action
    • [39] J.B.A. Millar, E. Rozengurt, Bombesin enhancement of cAMP accumulation in Swiss 3T3 cells: evidence of a dual mechanism of action, J. Cell. Physiol. 137 (1988) 214-222.
    • (1988) J. Cell. Physiol. , vol.137 , pp. 214-222
    • Millar, J.B.A.1    Rozengurt, E.2
  • 45
    • 0029012939 scopus 로고
    • Porcine m2 muscarinic acetylcholine receptor-effector coupling in Chinese hamster ovary cells
    • [45] W.K. Vogel, V.A. Mosser, D.A. bulseco, M.I. Schimerlik, Porcine m2 muscarinic acetylcholine receptor-effector coupling in Chinese hamster ovary cells, J. Biol. Chem. 270 (1995) 15485-15493.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15485-15493
    • Vogel, W.K.1    Mosser, V.A.2    Bulseco, D.A.3    Schimerlik, M.I.4
  • 46
    • 0030957917 scopus 로고    scopus 로고
    • Effect of gastrin-releasing peptide receptor number on receptor affinity, coupling, degradation and receptor modulation
    • [46] T. Tsuda, T. Kusui, W. Hou, R.V. Benya, M.A. Akeson, G.S. Kroog, J.F. Battey, R.T. Jensen, Effect of gastrin-releasing peptide receptor number on receptor affinity, coupling, degradation and receptor modulation, Mol. Pharmacol. 51 (1997) 721-732.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 721-732
    • Tsuda, T.1    Kusui, T.2    Hou, W.3    Benya, R.V.4    Akeson, M.A.5    Kroog, G.S.6    Battey, J.F.7    Jensen, R.T.8
  • 49
    • 0028125178 scopus 로고
    • Analysis of delta-opioid receptor activities stably expressed in CHO cell lines: Function of receptor density?
    • [49] P.Y. Law, T.M. McGinn, M.J. Wick, L.J. Erikson, C. Evans, H.H. Loh, Analysis of delta-opioid receptor activities stably expressed in CHO cell lines: function of receptor density?, J. Pharmacol. Exp. Ther. 271 (1994) 1686-1694.
    • (1994) J. Pharmacol. Exp. Ther. , vol.271 , pp. 1686-1694
    • Law, P.Y.1    McGinn, T.M.2    Wick, M.J.3    Erikson, L.J.4    Evans, C.5    Loh, H.H.6
  • 50
    • 0029121436 scopus 로고
    • Rapid and persistent desensitization of m3 muscarinic acetylcholine receptor-stimulated phospholipase D
    • [50] M. Schmidt, B. Fasselt, U. Rumenapp, C. Bienek, T. Wieland, C.J. van Koppen, K.H. Jakobs, Rapid and persistent desensitization of m3 muscarinic acetylcholine receptor-stimulated phospholipase D, J. Biol. Chem. 34 (1995) 19949-19956.
    • (1995) J. Biol. Chem. , vol.34 , pp. 19949-19956
    • Schmidt, M.1    Fasselt, B.2    Rumenapp, U.3    Bienek, C.4    Wieland, T.5    Van Koppen, C.J.6    Jakobs, K.H.7
  • 51
    • 0026485367 scopus 로고
    • Stimulation of phosphatidylcholine breakdown by thrombin and carbachol but not by tyrosine kinase receptor ligands in cells transfected with M1 muscarinic receptors
    • [51] F.R. McKenzie, K. Seuwen, J. Pouyssegur, Stimulation of phosphatidylcholine breakdown by thrombin and carbachol but not by tyrosine kinase receptor ligands in cells transfected with M1 muscarinic receptors, J. Biol. Chem. 32 (1992) 22759-22769.
    • (1992) J. Biol. Chem. , vol.32 , pp. 22759-22769
    • McKenzie, F.R.1    Seuwen, K.2    Pouyssegur, J.3
  • 52
    • 0026299048 scopus 로고
    • 2+ inhibits guanine nucleotide-activated phospholipase D in neural-derived NG108-15 cells
    • 2+ inhibits guanine nucleotide-activated phospholipase D in neural-derived NG108-15 cells, Cell Regul. 2 (1991) 1011-1019.
    • (1991) Cell Regul. , vol.2 , pp. 1011-1019
    • Liscovitch, M.1    Eli, Y.2
  • 53
    • 0028171403 scopus 로고
    • Activation of phospholipase C-gamma is necessary for stimulation of phospholipase D by platelet-derived growth factor
    • [53] E.J. Yeo, A. Kazlauskas, J.H. Exton, Activation of phospholipase C-gamma is necessary for stimulation of phospholipase D by platelet-derived growth factor, J. Biol. Chem. 269 (1994) 27823-27826.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27823-27826
    • Yeo, E.J.1    Kazlauskas, A.2    Exton, J.H.3
  • 54
    • 0027749388 scopus 로고
    • Calponin: Thin filament-linked regulation of smooth muscle contraction
    • [54] S.J. Winder, M.P. Walsh, Calponin: thin filament-linked regulation of smooth muscle contraction, Cell Signalling 5 (1993) 677-686.
    • (1993) Cell Signalling , vol.5 , pp. 677-686
    • Winder, S.J.1    Walsh, M.P.2
  • 55
    • 0028104901 scopus 로고
    • Regulation of vascular smooth muscle tone
    • [55] M.P. Walsh, Regulation of vascular smooth muscle tone, Can. J. Physiol. Pharmacol. 72 (1994) 919-936.
    • (1994) Can. J. Physiol. Pharmacol. , vol.72 , pp. 919-936
    • Walsh, M.P.1
  • 58
    • 0001030641 scopus 로고
    • Stimulus-secretion coupling in pancreatic acinar cells
    • V.L.W. Go, E.P. DiMagno, J.D. Gardner, E. Lebenthal, H.A. Reber, G.A. Scheele (Eds.), Raven Press, New York
    • [58] J.A. Williams, D.I. Yule, Stimulus-secretion coupling in pancreatic acinar cells, in: V.L.W. Go, E.P. DiMagno, J.D. Gardner, E. Lebenthal, H.A. Reber, G.A. Scheele (Eds.), Pancreas: Biology, Pathobiology, and Disease, 2nd edn., Raven Press, New York, 1993, pp. 167-189.
    • (1993) Pancreas: Biology, Pathobiology, and Disease, 2nd Edn. , pp. 167-189
    • Williams, J.A.1    Yule, D.I.2
  • 59
    • 0029079448 scopus 로고
    • Role of calcium and protein kinase C in the activation of phospholipase D by angiotensin II in vascular smooth muscle cells
    • [59] E.J. Freeman, G.M. Chisolm, E.A. Tallant, Role of calcium and protein kinase C in the activation of phospholipase D by angiotensin II in vascular smooth muscle cells, Arch. Biochem. Biophys. 319 (1995) 84-92.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 84-92
    • Freeman, E.J.1    Chisolm, G.M.2    Tallant, E.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.