메뉴 건너뛰기




Volumn 1404, Issue 3, 1998, Pages 412-426

Are tyrosine phosphorylation of p125(FAK) and paxillin or the small GTP binding protein, Rho, needed for CCK-stimulated pancreatic amylase secretion?

Author keywords

Enzyme secretion; PKC; Rho; Small GTP binding protein; Tyrosine kinase

Indexed keywords

AMYLASE; CHOLECYSTOKININ; CYTOCHALASIN D; FOCAL ADHESION KINASE; GENISTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; PANCREAS ENZYME; PAXILLIN; PROTEIN TYROSINE KINASE INHIBITOR; RHO FACTOR;

EID: 0032537949     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4889(98)00072-X     Document Type: Article
Times cited : (31)

References (48)
  • 1
    • 0000259909 scopus 로고
    • Stimulus-secretion coupling in the pancreatic acinus
    • L.R. Johnson, D.H. Alpers, J. Christensen, E.D. Jacobson, J.H. Walsh (Eds.), Raven Press, New York
    • [1] D.I. Yule, J.A. Williams, Stimulus-secretion coupling in the pancreatic acinus, in: L.R. Johnson, D.H. Alpers, J. Christensen, E.D. Jacobson, J.H. Walsh (Eds.), Physiology of the Gastrointestinal Tract, Vol. 2, 3rd Edn., Raven Press, New York, 1994, pp. 1447-1472.
    • (1994) Physiology of the Gastrointestinal Tract, Vol. 2, 3rd Edn. , vol.2 , pp. 1447-1472
    • Yule, D.I.1    Williams, J.A.2
  • 2
    • 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
    • [2] 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
  • 3
    • 0027995830 scopus 로고
    • Multiple inhibitory effects of genistein on stimulus-secretion coupling in rat pancreatic acini
    • [3] R.D. Duan, A.C.C. wagner, D.I. Yule, J.A. Williams, Multiple inhibitory effects of genistein on stimulus-secretion coupling in rat pancreatic acini, Am. J. Physiol. 266 (1994) G303-G310.
    • (1994) Am. J. Physiol. , vol.266
    • Duan, R.D.1    Wagner, A.C.C.2    Yule, D.I.3    Williams, J.A.4
  • 4
    • 0027265077 scopus 로고
    • A role for cholecystokinin-stimulated protein tyrosine phosphorylation in regulated secretion by the pancreatic acinar cell
    • [4] M.P. Lutz, S.L. Sutor, R.T. Abraham, L.J. Miller, A role for cholecystokinin-stimulated protein tyrosine phosphorylation in regulated secretion by the pancreatic acinar cell, J. Biol. Chem. 268 (1993) 11119-11124.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11119-11124
    • Lutz, M.P.1    Sutor, S.L.2    Abraham, R.T.3    Miller, L.J.4
  • 9
    • 0030020444 scopus 로고    scopus 로고
    • Tyrosine kinases are required for catecholamine secretion and mitogen-activated protein kinase activation in bovine adrenal chromaffin cells
    • [9] M.E. Cox, C.M. Ely, A.D. Catling, M.J. Weber, S.J. Parsons, Tyrosine kinases are required for catecholamine secretion and mitogen-activated protein kinase activation in bovine adrenal chromaffin cells, J. Neurochem. 66 (1996) 1103-1112.
    • (1996) J. Neurochem. , vol.66 , pp. 1103-1112
    • Cox, M.E.1    Ely, C.M.2    Catling, A.D.3    Weber, M.J.4    Parsons, S.J.5
  • 10
    • 0029870190 scopus 로고    scopus 로고
    • Protein tyrosine kinases regulate agonist-stimulated prostacyclin release but not von Willebrand factor secretion from human umbilical vein endothelial cells
    • [10] P.D. Wheeler-Jones, M.J. May, A.J. Morgan, J.D. Pearson, Protein tyrosine kinases regulate agonist-stimulated prostacyclin release but not von Willebrand factor secretion from human umbilical vein endothelial cells, Biochem. J. 315 (1996) 416.
    • (1996) Biochem. J. , vol.315 , pp. 416
    • Wheeler-Jones, P.D.1    May, M.J.2    Morgan, A.J.3    Pearson, J.D.4
  • 11
    • 0029994505 scopus 로고    scopus 로고
    • Protein tyrosine kinase inhibitors promote amylase secretion and inhibit ornithine decarboxylase induction in sialagogue-stimulated rat parotid explants
    • [11] F. Kinoshita, A. Ueno, Y. Miwa, M. Nishino, H. Inoue, Protein tyrosine kinase inhibitors promote amylase secretion and inhibit ornithine decarboxylase induction in sialagogue-stimulated rat parotid explants, Biochem. Biophys. Res. Commun. 223 (1996) 170-174.
    • (1996) Biochem. Biophys. Res. Commun. , vol.223 , pp. 170-174
    • Kinoshita, F.1    Ueno, A.2    Miwa, Y.3    Nishino, M.4    Inoue, H.5
  • 12
    • 0029028721 scopus 로고
    • The role of phosphotyrosine signaling pathway in parotid gland proliferation and function
    • [12] K.R. Purushotham, M.G. Humphreys-Beher, The role of phosphotyrosine signaling pathway in parotid gland proliferation and function, Crit. Rev. Oral Biol. Med. 6 (1995) 119-131.
    • (1995) Crit. Rev. Oral Biol. Med. , vol.6 , pp. 119-131
    • Purushotham, K.R.1    Humphreys-Beher, M.G.2
  • 14
    • 0030694459 scopus 로고    scopus 로고
    • FAK and paxillin is mediated by phospholipase C-dependent and -independent mechanisms and requires the integrity of the actin cytoskeleton and participation of p21rho
    • FAK and paxillin is mediated by phospholipase C-dependent and -independent mechanisms and requires the integrity of the actin cytoskeleton and participation of p21rho, Biochem. J. 327 (1997) 461-472.
    • (1997) Biochem. J. , vol.327 , pp. 461-472
    • Garcia, L.J.1    Rosado, J.A.2    Gonzalez, A.3    Jensen, R.T.4
  • 15
    • 0029026697 scopus 로고
    • Convergent signalling in the action of integrins, neuropeptides, growth factors and oncogenes
    • [15] E. Rozengurt, Convergent signalling in the action of integrins, neuropeptides, growth factors and oncogenes, Cancer Surv. 24 (1995) 81-96.
    • (1995) Cancer Surv. , vol.24 , pp. 81-96
    • Rozengurt, E.1
  • 16
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • [16] K. Burridge, K. Fath, T. Kelly, G. Nuckolls, C. Turner, Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton, Annu. Rev. Cell Biol. 4 (1988) 487-525.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 19
    • 0025078512 scopus 로고
    • The cellular functions of small GTP-binding proteins
    • [19] A. Hall, The cellular functions of small GTP-binding proteins, Science 249 (1990) 635-640.
    • (1990) Science , vol.249 , pp. 635-640
    • Hall, A.1
  • 21
    • 0020490608 scopus 로고
    • Interaction of COOH-terminal fragments of cholecystokinin with receptors on dispersed acini from guinea pig pancreas
    • [21] R.T. Jensen, G.F. Lemp, J.D. Gardner, Interaction of COOH-terminal fragments of cholecystokinin with receptors on dispersed acini from guinea pig pancreas, J. Biol. Chem. 257 (1982) 5554-5559.
    • (1982) J. Biol. Chem. , vol.257 , pp. 5554-5559
    • Jensen, R.T.1    Lemp, G.F.2    Gardner, J.D.3
  • 22
    • 0018065332 scopus 로고
    • Kinetics of amylase release by dispersed acini prepared from guinea pig pancreas
    • [22] S.R. Peikin, A.J. Rottman, S. Batzri, J.D. Gardner, Kinetics of amylase release by dispersed acini prepared from guinea pig pancreas, Am. J. Physiol. 235 (1978) E743-E749.
    • (1978) Am. J. Physiol. , vol.235
    • Peikin, S.R.1    Rottman, A.J.2    Batzri, S.3    Gardner, J.D.4
  • 24
    • 0030976835 scopus 로고    scopus 로고
    • The gastrin-releasing peptide receptor is differentially coupled to adenylate cyclase and phospholipase C in different tissues
    • [24] L.J. Garcia, T.K. Pradhan, H.C. Weber, T.W. Moody, R.T. Jensen, The gastrin-releasing peptide receptor is differentially coupled to adenylate cyclase and phospholipase C in different tissues, Biochim. Biophys. Acta 1356 (1997) 343-354.
    • (1997) Biochim. Biophys. Acta , vol.1356 , pp. 343-354
    • Garcia, L.J.1    Pradhan, T.K.2    Weber, H.C.3    Moody, T.W.4    Jensen, R.T.5
  • 25
    • 0027280575 scopus 로고
    • ADP-ribosylation of the rhoA gene product by botulinum C3 exoenzyme causes Swiss 3T3 cells to accumulate in the G1 phase of the cell cycle
    • [25] M. Yamamoto, N. Marui, T. Sakai, N. Morii, S. Kozaki, K. Ikai, S. Imamura, S. Narumiya, ADP-ribosylation of the rhoA gene product by botulinum C3 exoenzyme causes Swiss 3T3 cells to accumulate in the G1 phase of the cell cycle, Oncogene 8 (1993) 1449-1455.
    • (1993) Oncogene , vol.8 , pp. 1449-1455
    • Yamamoto, M.1    Marui, N.2    Sakai, T.3    Morii, N.4    Kozaki, S.5    Ikai, K.6    Imamura, S.7    Narumiya, S.8
  • 26
    • 0031423732 scopus 로고    scopus 로고
    • rho and integrity of the acini cytoskeleton
    • rho and integrity of the acini cytoskeleton, Biochemistry 36, (51) (1997) 16328-16337.
    • (1997) Biochemistry , vol.36 , Issue.51 , pp. 16328-16337
    • Tsuda, T.1    Kusui, T.2    Jensen, R.T.3
  • 27
    • 0023110218 scopus 로고
    • Clostridium botulinum type C produces a novel ADP-ribosyltransferase distinct from botulinum C2 toxin
    • [27] K. Aktories, U. Weller, G.S. Chhatwal, Clostridium botulinum type C produces a novel ADP-ribosyltransferase distinct from botulinum C2 toxin, FEBS Lett. 212 (1987) 109-113.
    • (1987) FEBS Lett. , vol.212 , pp. 109-113
    • Aktories, K.1    Weller, U.2    Chhatwal, G.S.3
  • 28
    • 0025934143 scopus 로고
    • Clostridium botulinum C3 ADP-ribosyltransferase gene
    • [28] Y. Nemoto, T. Namba, S. Kozaki, S. Narumiya, Clostridium botulinum C3 ADP-ribosyltransferase gene, J. Biol. Chem. 266 (1991) 19312-19319.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19312-19319
    • Nemoto, Y.1    Namba, T.2    Kozaki, S.3    Narumiya, S.4
  • 29
    • 0024353843 scopus 로고
    • Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase
    • [29] A. Sekine, M. Fujiwara, S. Narumiya, Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase, J. Biol. Chem. 264 (1989) 8602-8605.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8602-8605
    • Sekine, A.1    Fujiwara, M.2    Narumiya, S.3
  • 30
    • 16844366239 scopus 로고    scopus 로고
    • Evidence of Rho-mediated agonist stimulation of phospholipase D in rat1 fibroblasts
    • [30] K.C. Malcolm, C.M. Elliott, J.H. Exton, Evidence of Rho-mediated agonist stimulation of phospholipase D in rat1 fibroblasts, J. Biol. Chem. 271 (1996) 13135-13139.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13135-13139
    • Malcolm, K.C.1    Elliott, C.M.2    Exton, J.H.3
  • 31
    • 0030893929 scopus 로고    scopus 로고
    • Activation and translocation of Rho (and ADP ribosylation factor) by insulin in rat adipocytes
    • [31] P. Karnam, M.L. Standaert, L. Galloway, R.V. Farese, Activation and translocation of Rho (and ADP ribosylation factor) by insulin in rat adipocytes, J. Biol. Chem. 272 (1997) 6136-6140.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6136-6140
    • Karnam, P.1    Standaert, M.L.2    Galloway, L.3    Farese, R.V.4
  • 32
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • [32] J.A. Cooper, Effects of cytochalasin and phalloidin on actin, J. Cell Biol. 105 (1987) 1473-1478.
    • (1987) J. Cell Biol. , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 33
    • 0028071784 scopus 로고
    • FAK and paxillin are substrates for bradykinin-stimulated tyrosine phosphorylation in Swiss 3T3 cells
    • FAK and paxillin are substrates for bradykinin-stimulated tyrosine phosphorylation in Swiss 3T3 cells, J. Biol. Chem. 269 (1994) 24328-24334.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24328-24334
    • Leeb-Lundberg, L.M.F.1    Song, X.H.2    Mathis, S.A.3
  • 34
    • 0027370725 scopus 로고
    • Bombesin, vasopressin and endothelin rapidly stimulate tyrosine phosphorylation of the focal adhesion-associated protein paxillin in Swiss 3T3 cells
    • [34] I. Zachary, J. Sinnett-Smith, C.E. Turner, E. Rozengurt, Bombesin, vasopressin and endothelin rapidly stimulate tyrosine phosphorylation of the focal adhesion-associated protein paxillin in Swiss 3T3 cells, J. Biol. Chem. 268 (1993) 27060-27065.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27060-27065
    • Zachary, I.1    Sinnett-Smith, J.2    Turner, C.E.3    Rozengurt, E.4
  • 36
    • 0029793537 scopus 로고    scopus 로고
    • Glucose-induced tyrosine phosphorylation of p125 in beta cells and pancreatic islets
    • [36] R.J. Konrad, R.M. Dean, R.A. Young, P.C. Billings, B.A. Wolf, Glucose-induced tyrosine phosphorylation of p125 in beta cells and pancreatic islets, J. Biol. Chem. 271 (1996) 24179-24186.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24179-24186
    • Konrad, R.J.1    Dean, R.M.2    Young, R.A.3    Billings, P.C.4    Wolf, B.A.5
  • 38
    • 0020066102 scopus 로고
    • Effects of high concentrations of secretagogues on the morphology and secretory activity of the pancreas: A role for microfilaments
    • [38] D.B. Burnham, J.A. Williams, Effects of high concentrations of secretagogues on the morphology and secretory activity of the pancreas: a role for microfilaments, Cell Tissue Res. 222 (1982) 201-212.
    • (1982) Cell Tissue Res. , vol.222 , pp. 201-212
    • Burnham, D.B.1    Williams, J.A.2
  • 39
    • 0017653255 scopus 로고
    • Biochemical reactions involved in pancreatic enzyme secretion. 4. Effects of cytochalasin B on functions of the endocrine pancreas
    • [39] J. Morisset, A.R. Beaudoin, Biochemical reactions involved in pancreatic enzyme secretion. 4. Effects of cytochalasin B on functions of the endocrine pancreas, Can. J. Physiol. Pharmacol. 55 (1977) 644-651.
    • (1977) Can. J. Physiol. Pharmacol. , vol.55 , pp. 644-651
    • Morisset, J.1    Beaudoin, A.R.2
  • 40
    • 0028889137 scopus 로고
    • Actin filament disassembly is a sufficient final trigger for exocytosis in nonexcitable cells
    • [40] S. Muallem, K. Kwiatkowska, X. Xu, H.L. Yin, Actin filament disassembly is a sufficient final trigger for exocytosis in nonexcitable cells, J. Cell Biol. 128 (1995) 589-598.
    • (1995) J. Cell Biol. , vol.128 , pp. 589-598
    • Muallem, S.1    Kwiatkowska, K.2    Xu, X.3    Yin, H.L.4
  • 42
    • 0029737549 scopus 로고    scopus 로고
    • Rab3D localizes to zymogen granules in rat pancreatic acini and other exocrine glands
    • [42] H. Ohnishi, S.A. Ernst, N. Wys, M. McNiven, J.A. Williams, Rab3D localizes to zymogen granules in rat pancreatic acini and other exocrine glands, Am. J. Physiol. 271 (1996) G531-G538.
    • (1996) Am. J. Physiol. , vol.271
    • Ohnishi, H.1    Ernst, S.A.2    Wys, N.3    McNiven, M.4    Williams, J.A.5
  • 44
    • 0028086795 scopus 로고
    • Effect of a Rab3A effector domain-related peptide, CCK, and EGF in permeabilized pancreatic acini
    • [44] S. Zeuzem, D. Stryjek-Kaminska, W.F. Caspary, J. Stein, A. Piiper, Effect of a Rab3A effector domain-related peptide, CCK, and EGF in permeabilized pancreatic acini, Am. J. Physiol. 267 (1994) G350-G356.
    • (1994) Am. J. Physiol. , vol.267
    • Zeuzem, S.1    Stryjek-Kaminska, D.2    Caspary, W.F.3    Stein, J.4    Piiper, A.5
  • 45
    • 0029139385 scopus 로고
    • The small GTPases Rac and Rho as regulators of secretion in mast cells
    • [45] L.S. Price, J.C. Norman, A.J. Ridley, A. Koffer, The small GTPases Rac and Rho as regulators of secretion in mast cells, Curr. Biol. 5 (1995) 68-73.
    • (1995) Curr. Biol. , vol.5 , pp. 68-73
    • Price, L.S.1    Norman, J.C.2    Ridley, A.J.3    Koffer, A.4
  • 46
    • 0029809141 scopus 로고    scopus 로고
    • The small GTP-binding proteins, Rac and Rho, regulate cytoskeletal organization and exocytosis in mast cells by parallel pathways
    • [46] J.C. Norman, L.S. Price, A.J. Ridley, A. Koffer, The small GTP-binding proteins, Rac and Rho, regulate cytoskeletal organization and exocytosis in mast cells by parallel pathways, Mol. Biol. Cell 7 (1996) 1429-1442.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1429-1442
    • Norman, J.C.1    Price, L.S.2    Ridley, A.J.3    Koffer, A.4
  • 47
    • 0029803812 scopus 로고    scopus 로고
    • Rho guanine nucleotide dissociation inhibitor protein (RhoGDI) inhibits exocytosis in mast cells
    • [47] P. Mariot, A.J. O'Sullivan, A.M. Brown, P.E.R. Tatham, Rho guanine nucleotide dissociation inhibitor protein (RhoGDI) inhibits exocytosis in mast cells, EMBO J. 15 (1996) 6476-6482.
    • (1996) EMBO J. , vol.15 , pp. 6476-6482
    • Mariot, P.1    O'Sullivan, A.J.2    Brown, A.M.3    Tatham, P.E.R.4
  • 48
    • 0029611728 scopus 로고
    • Regulation of exocytosis by the small GTP-binding protein Rho in rat basophilic leukemia (RBL-2H3) cells
    • [48] S.G. Yonei, K. Oishi, M.K. Uchida, Regulation of exocytosis by the small GTP-binding protein Rho in rat basophilic leukemia (RBL-2H3) cells, Gen. Pharmacol. 26 (1995) 1583-1589.
    • (1995) Gen. Pharmacol. , vol.26 , pp. 1583-1589
    • Yonei, S.G.1    Oishi, K.2    Uchida, M.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.