메뉴 건너뛰기




Volumn 15, Issue 5, 1999, Pages 385-391

Intracellular regulatory mechanisms in pancreatic acinar cellular function

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINE; BOMBESIN; CALCIUM ION; CHOLECYSTOKININ A RECEPTOR; CHOLECYSTOKININ B RECEPTOR; CHOLECYSTOKININ RECEPTOR; FOCAL ADHESION KINASE; GUANINE NUCLEOTIDE BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; ZYMOGEN GRANULE;

EID: 0032796045     PISSN: 02671379     EISSN: None     Source Type: Journal    
DOI: 10.1097/00001574-199909000-00003     Document Type: Article
Times cited : (5)

References (72)
  • 1
    • 0030747173 scopus 로고    scopus 로고
    • Pancreatic acinar cell intracellular signaling mechanisms
    • 1 Williams JA: Pancreatic acinar cell intracellular signaling mechanisms. Curr Opin Gastroenterol 1997, 13:369-374.
    • (1997) Curr Opin Gastroenterol , vol.13 , pp. 369-374
    • Williams, J.A.1
  • 2
    • 0031665453 scopus 로고    scopus 로고
    • Novel membrane-to-nucleus pathways in the regulation of pancreatic acinar cell function
    • 2 Urrutia R, Miller LJ: Novel membrane-to-nucleus pathways in the regulation of pancreatic acinar cell function. Curr Opin Gastroenterol 1998, 14:369-375.
    • (1998) Curr Opin Gastroenterol , vol.14 , pp. 369-375
    • Urrutia, R.1    Miller, L.J.2
  • 3
    • 0030846864 scopus 로고    scopus 로고
    • Direct identification of a distinct site of interaction between the carboxyl-terminal residue of cholecystokinin and the type A cholecystokinin receptor using photoaffinity labeling
    • 3 Ji Z, Hadac EM, Henne RM, Patel SA, Lybrand TP, Miller LJ: Direct identification of a distinct site of interaction between the carboxyl-terminal residue of cholecystokinin and the type A cholecystokinin receptor using photoaffinity labeling. J Biol Chem 1997, 272:24393-24401.
    • (1997) J Biol Chem , vol.272 , pp. 24393-24401
    • Ji, Z.1    Hadac, E.M.2    Henne, R.M.3    Patel, S.A.4    Lybrand, T.P.5    Miller, L.J.6
  • 4
    • 15644364730 scopus 로고    scopus 로고
    • Identification of two amino acids of the human cholecystokinin-A receptor that interact with the N-terrninal moiety of cholecystokinin
    • 4 Kennedy K, Giigoux V, Escrieut C, Maigret B, Martinez J, Moroder L. et al.: Identification of two amino acids of the human cholecystokinin-A receptor that interact with the N-terrninal moiety of cholecystokinin. J Biol Chem 1997, 272:29920-29926.
    • (1997) J Biol Chem , vol.272 , pp. 29920-29926
    • Kennedy, K.1    Giigoux, V.2    Escrieut, C.3    Maigret, B.4    Martinez, J.5    Moroder, L.6
  • 5
    • 0032557448 scopus 로고    scopus 로고
    • Direct identification of a second distinct site of contact between cholecystokinin and its receptor
    • 5 Hadac EM, Pinon DI, Ji Z, Holicky EL, Henne RM, Lybrand TP, Miller LJ: Direct identification of a second distinct site of contact between cholecystokinin and its receptor. J Biol Chem 1998, 273:12988-12993.
    • (1998) J Biol Chem , vol.273 , pp. 12988-12993
    • Hadac, E.M.1    Pinon, D.I.2    Ji, Z.3    Holicky, E.L.4    Henne, R.M.5    Lybrand, T.P.6    Miller, L.J.7
  • 6
    • 7344250633 scopus 로고    scopus 로고
    • Met-195 of the cholecystokinin-A receptor interacts with the sulfated tyrosine of cholecystokinin and is crucial for receptor transition to high affinity state
    • 6 Giigoux V, Escrieut C, Silvente-Poirot S, Maigret B, Gouilleux L, Fehrentz J-A, et al.: Met-195 of the cholecystokinin-A receptor interacts with the sulfated tyrosine of cholecystokinin and is crucial for receptor transition to high affinity state. J Biol Chem 1998, 273:14380-14386.
    • (1998) J Biol Chem , vol.273 , pp. 14380-14386
    • Giigoux, V.1    Escrieut, C.2    Silvente-Poirot, S.3    Maigret, B.4    Gouilleux, L.5    Fehrentz, J.-A.6
  • 7
    • 0033582530 scopus 로고    scopus 로고
    • Structurally related peptide agonist, parital agonist, and antagonist occupy a similar binding pocket within the cholecystokinin receptor
    • 7 Dong M, Ding X-Q, Pinon DI, Hadac EM, Oda RP, Landers JP, Miller LJ: Structurally related peptide agonist, parital agonist, and antagonist occupy a similar binding pocket within the cholecystokinin receptor. J Biol Chem 1999, 274:4778-4785.
    • (1999) J Biol Chem , vol.274 , pp. 4778-4785
    • Dong, M.1    Ding, X.-Q.2    Pinon, D.I.3    Hadac, E.M.4    Oda, R.P.5    Landers, J.P.6    Miller, L.J.7
  • 8
    • 0031859218 scopus 로고    scopus 로고
    • Identification of a domain in the carboxy terminus of CCK receptor that affects its intracellular trafficking
    • 8 Go WY, Holicky EL, Hadac EM, Rao RV, Miller LJ: Identification of a domain in the carboxy terminus of CCK receptor that affects its intracellular trafficking. Am J Physiol 1998, 275:G56-G62.
    • (1998) Am J Physiol , vol.275
    • Go, W.Y.1    Holicky, E.L.2    Hadac, E.M.3    Rao, R.V.4    Miller, L.J.5
  • 14
    • 0031003586 scopus 로고    scopus 로고
    • First intracellular loop of the human cholecystokinin-A receptor is essential for cyclic AMP signaling in transfected HEK-293 cells
    • 14 Wu V, Yang M, McRoberts JA, Ren J, Seenalu R, Zeng N, et al.: First intracellular loop of the human cholecystokinin-A receptor is essential for cyclic AMP signaling in transfected HEK-293 cells. J Biol Chem 1997, 272:9037-9042
    • (1997) J Biol Chem , vol.272 , pp. 9037-9042
    • Wu, V.1    Yang, M.2    McRoberts, J.A.3    Ren, J.4    Seenalu, R.5    Zeng, N.6
  • 18
    • 0032520663 scopus 로고    scopus 로고
    • Effect of basic fibroblast growth factor on cholecystokinin-induced amylase release and intracellular calcium increase in male rat pancreatic acinar cells
    • 18 Lajas AI, Pozo MJ, Salido GM, Pariente JA: Effect of basic fibroblast growth factor on cholecystokinin-induced amylase release and intracellular calcium increase in male rat pancreatic acinar cells. Biochem Pharmacol 1998, 55:903-908.
    • (1998) Biochem Pharmacol , vol.55 , pp. 903-908
    • Lajas, A.I.1    Pozo, M.J.2    Salido, G.M.3    Pariente, J.A.4
  • 19
    • 0031025091 scopus 로고    scopus 로고
    • 2+ spikes regulating distinct cellular functions in pancreatic acinar cells
    • 2+ spikes regulating distinct cellular functions in pancreatic acinar cells. EMBO J 1997, 16:22242-22251.
    • (1997) EMBO J , vol.16 , pp. 22242-22251
    • Ito, K.1    Miyashita, Y.2    Kasai, H.3
  • 22
    • 0030946534 scopus 로고    scopus 로고
    • Evidence that zymogen granules are not a physiologically relevant calcium pool
    • 22 Yule DI, Ernst SA, Ohnishi H, Wojcikiewicz RJH. Evidence that zymogen granules are not a physiologically relevant calcium pool. J Biol Chem 1997, 272:9093-9098.
    • (1997) J Biol Chem , vol.272 , pp. 9093-9098
    • Yule, D.I.1    Ernst, S.A.2    Ohnishi, H.3    Wojcikiewicz, R.J.H.4
  • 26
    • 0033556106 scopus 로고    scopus 로고
    • Expression and subcellular localization of the ryanodine receptor in rat pancreatic acinar cells
    • 26 Leite MF, Dranoff JA, Gao L, Nathanson MH. Expression and subcellular localization of the ryanodine receptor in rat pancreatic acinar cells. Biochem J 1999, 337:305-309.
    • (1999) Biochem J , vol.337 , pp. 305-309
    • Leite, M.F.1    Dranoff, J.A.2    Gao, L.3    Nathanson, M.H.4
  • 28
    • 0033522228 scopus 로고    scopus 로고
    • 2+-signaling patterns by NAADP in pancreatic acinar cells
    • 2+-signaling patterns by NAADP in pancreatic acinar cells. Nature 1999, 398:74-76.
    • (1999) Nature , vol.398 , pp. 74-76
    • Cancela, J.M.1    Churchill, G.C.2    Galione, A.3
  • 32
  • 33
    • 0032101281 scopus 로고    scopus 로고
    • Enhanced secretion of amylase from exocrine pancreas of connexin32-deficient mice
    • 33 Chanson M, Fanjul M, Bosco D, Nelles E, Suter S, Willecke K, Meda P: Enhanced secretion of amylase from exocrine pancreas of connexin32-deficient mice. J Cell Biol 1998, 141:12267-12275.
    • (1998) J Cell Biol , vol.141 , pp. 12267-12275
    • Chanson, M.1    Fanjul, M.2    Bosco, D.3    Nelles, E.4    Suter, S.5    Willecke, K.6    Meda, P.7
  • 34
    • 0032575666 scopus 로고    scopus 로고
    • Purification and characterization of a novel physiological substrate for calcineurin in mammalian cells
    • 34 Groblewski GE, Yoshida M, Bragado MJ, Ernst SA, Leykam J, Williams JA: Purification and characterization of a novel physiological substrate for calcineurin in mammalian cells. J Biol Chem 1998, 273:22738-22744.
    • (1998) J Biol Chem , vol.273 , pp. 22738-22744
    • Groblewski, G.E.1    Yoshida, M.2    Bragado, M.J.3    Ernst, S.A.4    Leykam, J.5    Williams, J.A.6
  • 35
    • 0032951295 scopus 로고    scopus 로고
    • Immunolocalization of CRHSP28 in exocrine digestive glands and gastrointestinal tissues of the rat
    • 35 Groblewski GE, Yoshida M, Yao H, Williams JA, Ernst SA. Immunolocalization of CRHSP28 in exocrine digestive glands and gastrointestinal tissues of the rat. Am J Physiol 1999, 276:G219-G226.
    • (1999) Am J Physiol , vol.276
    • Groblewski, G.E.1    Yoshida, M.2    Yao, H.3    Williams, J.A.4    Ernst, S.A.5
  • 36
    • 0028385277 scopus 로고
    • Implications of the SNARE hypothesis for intracellular membrane topology and dynamics
    • 36 Rothman JE, Warren G: Implications of the SNARE hypothesis for intracellular membrane topology and dynamics. Curr Biol 1994, 4:220-223.
    • (1994) Curr Biol , vol.4 , pp. 220-223
    • Rothman, J.E.1    Warren, G.2
  • 37
    • 0031559931 scopus 로고    scopus 로고
    • SNAP-23 is located in the basolateral plasma membrane of rat pancreatic acinar cells
    • 37 Gaisano HY, Sheu L, Wong PPC, Klip A, Trimble WS: SNAP-23 is located in the basolateral plasma membrane of rat pancreatic acinar cells. FEBS Lett 1997, 414:298-302.
    • (1997) FEBS Lett , vol.414 , pp. 298-302
    • Gaisano, H.Y.1    Sheu, L.2    Wong, P.P.C.3    Klip, A.4    Trimble, W.S.5
  • 38
    • 0030964221 scopus 로고    scopus 로고
    • q/11 localized on pancreatic zymogen granules is involved in calcium-regulated amylase secretion
    • q/11 localized on pancreatic zymogen granules is involved in calcium-regulated amylase secretion. J Biol Chem 1997, 272:16056-16061.
    • (1997) J Biol Chem , vol.272 , pp. 16056-16061
    • Ohnishi, H.1    Ernst, S.A.2    Yule, D.I.3    Baker, C.W.4    Williams, J.A.5
  • 39
    • 0031577346 scopus 로고    scopus 로고
    • Identification of Goα, Gqα, and Gsα immunoreactivity associated with the rat pancreatic zymogen granule membrane
    • 39 Padfield PJ, Panesar N: Identification of Goα, Gqα, and Gsα immunoreactivity associated with the rat pancreatic zymogen granule membrane. Biochem Biophys Res Commun 1997, 237:235-238.
    • (1997) Biochem Biophys Res Commun , vol.237 , pp. 235-238
    • Padfield, P.J.1    Panesar, N.2
  • 41
    • 0032540133 scopus 로고    scopus 로고
    • The two phases of regulated exocytosis in permeabilized pancreatic acini are modulated differently by heterotrimeric G-proteins
    • 41 Padfield PJ, Panesar N: The two phases of regulated exocytosis in permeabilized pancreatic acini are modulated differently by heterotrimeric G-proteins. Biochem Biophys Res Commun 1998, 245:332-336.
    • (1998) Biochem Biophys Res Commun , vol.245 , pp. 332-336
    • Padfield, P.J.1    Panesar, N.2
  • 43
    • 0032167421 scopus 로고    scopus 로고
    • Cysteine string protein [CSP] is an insulin secretory granule-associated protein regulating β-cell exocytosis
    • 43 Brown H, Larsson O, Bränström R, Yang S-N, Leibiger B, Leibiger I, et al.: Cysteine string protein [CSP] is an insulin secretory granule-associated protein regulating β-cell exocytosis. EMBO J 1998, 17:5048-5058.
    • (1998) EMBO J , vol.17 , pp. 5048-5058
    • Brown, H.1    Larsson, O.2    Bränström, R.3    Yang, S.-N.4    Leibiger, B.5    Leibiger, I.6
  • 44
    • 0031928546 scopus 로고    scopus 로고
    • Carboxyl methylation of rab3D is developmentally regulated in the rat pancreas: Correlation with exocrine function
    • 44 Valentijn JA, Jamieson JD: Carboxyl methylation of rab3D is developmentally regulated in the rat pancreas: correlation with exocrine function. Eur J Cell Biol 1998, 76:204-211.
    • (1998) Eur J Cell Biol , vol.76 , pp. 204-211
    • Valentijn, J.A.1    Jamieson, J.D.2
  • 45
    • 0031454368 scopus 로고    scopus 로고
    • Over expression of Rab3D enhances regulated amylase secretion from pancreatic acini of transgenic mice
    • 45 Ohnishi H, Samuelson LC, Yule DI, Ernst SA, Williams JA: Over expression of Rab3D enhances regulated amylase secretion from pancreatic acini of transgenic mice. J Clin Invest 1997, 100:3044-3052.
    • (1997) J Clin Invest , vol.100 , pp. 3044-3052
    • Ohnishi, H.1    Samuelson, L.C.2    Yule, D.I.3    Ernst, S.A.4    Williams, J.A.5
  • 46
    • 0031591692 scopus 로고    scopus 로고
    • Differential expression of Rab3 isoforms during differentiation of pancreatic acinar cell line AR42J
    • 46 Klengel R, Piiper A, Pittelkow S, Zeuzem S: Differential expression of Rab3 isoforms during differentiation of pancreatic acinar cell line AR42J. Biochem Biophys Res Comm 1997, 236:719-722.
    • (1997) Biochem Biophys Res Comm , vol.236 , pp. 719-722
    • Klengel, R.1    Piiper, A.2    Pittelkow, S.3    Zeuzem, S.4
  • 48
    • 0030044189 scopus 로고    scopus 로고
    • Chloride and potassium conductances of mouse pancreatic zymogen granules are inversely regulated by a -80-kDa mdr1a gene product
    • 48 Thévenod F, Hildebrandt J-P, Striessnig J, de Jonge HR, Schulz I: Chloride and potassium conductances of mouse pancreatic zymogen granules are inversely regulated by a -80-kDa mdr1a gene product. J Biol Chem 1996, 271:330-3305.
    • (1996) J Biol Chem , vol.271 , pp. 330-3305
    • Thévenod, F.1    Hildebrandt, J.-P.2    Striessnig, J.3    De Jonge, H.R.4    Schulz, I.5
  • 49
    • 0031031403 scopus 로고    scopus 로고
    • Surface dynamics in living acinar cells imaged by atomic force microscopy: Identification of plasma membrane structures involved in exocytosis
    • 49 Schneider SW, Sritharan KG, Geibel JP, Oberleithner H, Jena BP: Surface dynamics in living acinar cells imaged by atomic force microscopy: identification of plasma membrane structures involved in exocytosis. Proc Natl Acad Sci U S A 1997, 94:316-321.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 316-321
    • Schneider, S.W.1    Sritharan, K.G.2    Geibel, J.P.3    Oberleithner, H.4    Jena, B.P.5
  • 50
    • 0031717851 scopus 로고    scopus 로고
    • Optical measurement of stimulusevoked membrane dynamics in single pancreatic acinar cells
    • 50 Giovannucci DR, Yule DI, Stuenkel EL: Optical measurement of stimulusevoked membrane dynamics in single pancreatic acinar cells. Am J Physiol 1998, 275:C732-C739.
    • (1998) Am J Physiol , vol.275
    • Giovannucci, D.R.1    Yule, D.I.2    Stuenkel, E.L.3
  • 51
    • 0030871052 scopus 로고    scopus 로고
    • 2+ to prime amylase secretion from permeabilized rat pancreatic acini
    • 2+ to prime amylase secretion from permeabilized rat pancreatic acini. Am J Physiol 1997, 73:G655-G660.
    • (1997) Am J Physiol , vol.73
    • Padfield, P.J.1    Panesar, N.2
  • 52
    • 0032519773 scopus 로고    scopus 로고
    • 2+-dependent amylase secretion from permeabilized pancreatic acini by blocking the MgATP-dependent priming of exocytosis
    • 2+-dependent amylase secretion from permeabilized pancreatic acini by blocking the MgATP-dependent priming of exocytosis. Biochem J 1998, 330:329-334.
    • (1998) Biochem J , vol.330 , pp. 329-334
    • Padfield, P.J.1    Panesar, N.2
  • 54
    • 0031026978 scopus 로고    scopus 로고
    • Rab4 associates with the actin terminal web in developing rat pancreatic acinar cells
    • 54 Valentijn JA, LaCivita DQ, Gumkowski FD, Jamieson JD: Rab4 associates with the actin terminal web in developing rat pancreatic acinar cells. Eur J Cell Biol 1997, 72:1-8.
    • (1997) Eur J Cell Biol , vol.72 , pp. 1-8
    • Valentijn, J.A.1    LaCivita, D.Q.2    Gumkowski, F.D.3    Jamieson, J.D.4
  • 55
    • 0031789134 scopus 로고    scopus 로고
    • The actin-myosin cytoskeleton mediates reversible agonist-induced membrane blebbing
    • 55 Torgerson RR, McNiven MA: The actin-myosin cytoskeleton mediates reversible agonist-induced membrane blebbing. J Cell Sci 1998, 111:2911-2922.
    • (1998) J Cell Sci , vol.111 , pp. 2911-2922
    • Torgerson, R.R.1    McNiven, M.A.2
  • 56
    • 0030720786 scopus 로고    scopus 로고
    • Cholecystokinin and EGF activate a MAPK cascade by different mechanisms in rat pancreatic acinar cells
    • 56 Dabrowski A, Groblewski GE, Schäfer C, Guan K-L, Williams JA: Cholecystokinin and EGF activate a MAPK cascade by different mechanisms in rat pancreatic acinar cells. Am J Physiol 1997, 273:C1472-C1479.
    • (1997) Am J Physiol , vol.273
    • Dabrowski, A.1    Groblewski, G.E.2    Schäfer, C.3    Guan, K.-L.4    Williams, J.A.5
  • 57
    • 0030750222 scopus 로고    scopus 로고
    • 2+ and protein kinase C-dependent mechanisms involved in gastrin-induced Shc/Grb2 complex formation and P44-mitogen-activated protein kinase activation
    • 2+ and protein kinase C-dependent mechanisms involved in gastrin-induced Shc/Grb2 complex formation and P44-mitogen-activated protein kinase activation. Biochem J 1997, 325:383-389.
    • (1997) Biochem J , vol.325 , pp. 383-389
    • Daulhac, L.1    Kowalski-Chauvel, A.2    Pradayrol, L.3    Vaysse, N.4    Seva, C.5
  • 58
    • 0032911205 scopus 로고    scopus 로고
    • Adenovirus-mediated gene transfer of RasN17 inhibits specific CCK actions on pancreatic acinar cells
    • 58 Nicke B, Tsend M-J, Fenrich MC, Logsdon CD: Adenovirus-mediated gene transfer of RasN17 inhibits specific CCK actions on pancreatic acinar cells. Am J Physiol 1999, 276:G499-G506. A dominant negative Ras introduced by an adenoviral vector inhibited DNA synthesis and JNK activation but did not affect activation of ERKs. These results are consistent with Ras-independent activation of the MAPK cascade, but alternative actions of Ras are important for mitogenesis.
    • (1999) Am J Physiol , vol.276
    • Nicke, B.1    Tsend, M.-J.2    Fenrich, M.C.3    Logsdon, C.D.4
  • 59
    • 0032508660 scopus 로고    scopus 로고
    • A role for the p38 mitogen-activated protein kinase/Hsp27 pathway in cholecystokinin-induced changes in the actin cytoskelelon in rat pancreatic acini
    • 59 Schäfer C, Ross SE, Bragado MJ, Groblewski GE, Ernst SA, Williams JA: A role for the p38 mitogen-activated protein kinase/Hsp27 pathway in cholecystokinin-induced changes in the actin cytoskelelon in rat pancreatic acini. J Biol Chem 1998, 273:24173-24180. This study showed that CCK and other G-protein-coupled secretagogues activated p38 MAPK and thereby increased phosphorylation of small heat-shock protein hsp27. These effects are necessary but not sufficient for induction of disruption of the actin cytoskeleton in response to high concentrations of CCK.
    • (1998) J Biol Chem , vol.273 , pp. 24173-24180
    • Schäfer, C.1    Ross, S.E.2    Bragado, M.J.3    Groblewski, G.E.4    Ernst, S.A.5    Williams, J.A.6
  • 60
    • 0032893960 scopus 로고    scopus 로고
    • P38 MAP kinase is expressed in the pancreas and is immediately activated following cerulein hyperstimulation
    • 60 Wagner ACC, Metzzler W, Höfken T, Weber H, Göke B: P38 MAP kinase is expressed in the pancreas and is immediately activated following cerulein hyperstimulation. Digestion 1999, 60:41-47.
    • (1999) Digestion , vol.60 , pp. 41-47
    • Wagner, A.C.C.1    Metzzler, W.2    Höfken, T.3    Weber, H.4    Göke, B.5
  • 61
    • 0030666262 scopus 로고    scopus 로고
    • Molecular mechanisms for the control of translation by insulin
    • 61 Proud CG, Denton RM: Molecular mechanisms for the control of translation by insulin. Biochem J 1997, 328:329-341.
    • (1997) Biochem J , vol.328 , pp. 329-341
    • Proud, C.G.1    Denton, R.M.2
  • 64
    • 0031708618 scopus 로고    scopus 로고
    • Regulation of protein synthesis by cholecystokinin in rat pancreatic acini involves PHAS-1 and the p70 S6 kinase pathway
    • 64 Bragado MJ, Groblewski GE, Williams JA: Regulation of protein synthesis by cholecystokinin in rat pancreatic acini involves PHAS-1 and the p70 S6 kinase pathway. Gastroenterology 1998, 115:733-742. In this study, CCK was shown to enhance the phosphorylation of pHAS-1, an elF4E-binding protein leading to release of elF4E, which is a rate-limiting factor for translation. Blocking of these events and phosphorylation of p70 S6 kinase with rapamycin and wortmannin were shown to inhibit acinar cell protein synthesis by both CCK and insulin.
    • (1998) Gastroenterology , vol.115 , pp. 733-742
    • Bragado, M.J.1    Groblewski, G.E.2    Williams, J.A.3
  • 65
    • 0032580332 scopus 로고    scopus 로고
    • Gastrin induces phosphorylation of elF4E binding protein 1 and translation initiation of ornithine decarboxylase mRNA
    • 65 Pyronnet S, Gingras A-C, Bouisson M, Kowalski-Chauvel A, Seva C, Vaysse N, et al.: Gastrin induces phosphorylation of elF4E binding protein 1 and translation initiation of ornithine decarboxylase mRNA. Oncogene 1998, 16:2219-2227.
    • (1998) Oncogene , vol.16 , pp. 2219-2227
    • Pyronnet, S.1    Gingras, A.-C.2    Bouisson, M.3    Kowalski-Chauvel, A.4    Seva, C.5    Vaysse, N.6
  • 67
    • 0030864755 scopus 로고    scopus 로고
    • CCK causes rapid tyrosine phosphorylation of p125FAK focal adhesion kinase and paxillin in rat pancreatic acini
    • 67 Garcia U, Rosado JA, Tsuda T, Jensen RT: CCK causes rapid tyrosine phosphorylation of p125FAK focal adhesion kinase and paxillin in rat pancreatic acini. Biochim Biophys Acta 1997, 1358:189-199.
    • (1997) Biochim Biophys Acta , vol.1358 , pp. 189-199
    • Garcia, U.1    Rosado, J.A.2    Tsuda, T.3    Jensen, R.T.4
  • 68
    • 0030694459 scopus 로고    scopus 로고
    • Cholecystokinin-stimulated tyrosine phosphorylation of p125FAK and paxillin is mediated by phospholipase C-dependent and -independent mechanisms and requires the integrity of the actin cytoskeleton and participation of p21rho
    • 68 Garcia LJ, Rosado JA, González A, Jensen RT: Cholecystokinin-stimulated tyrosine phosphorylation of p125FAK 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 1997, 327:461-472.
    • (1997) Biochem J , vol.327 , pp. 461-472
    • Garcia, L.J.1    Rosado, J.A.2    González, A.3    Jensen, R.T.4
  • 69
    • 0032537949 scopus 로고    scopus 로고
    • Are tyrosine phosphorylation of p125FAK and paxillin or the small GTP binding protein, Rho, needed for CCK-stimulated pancreatic amylase secretion?
    • 69 Rosado JA, Salido GM, Jensen RT, Garcia LJ: Are tyrosine phosphorylation of p125FAK and paxillin or the small GTP binding protein, Rho, needed for CCK-stimulated pancreatic amylase secretion? Biochim Biophys Acta 1998, 1404:412-426.
    • (1998) Biochim Biophys Acta , vol.1404 , pp. 412-426
    • Rosado, J.A.1    Salido, G.M.2    Jensen, R.T.3    Garcia, L.J.4
  • 70
    • 0033035609 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton by p125 focal adhesion kinase in rat pancreatic acinar cells
    • 70 Kiehne K, Herzig KH, Fölsch UR: Regulation of the actin cytoskeleton by p125 focal adhesion kinase in rat pancreatic acinar cells. Digestion 1999, 60:153-160.
    • (1999) Digestion , vol.60 , pp. 153-160
    • Kiehne, K.1    Herzig, K.H.2    Fölsch, U.R.3
  • 71
    • 0032568815 scopus 로고    scopus 로고
    • Pervanadate stimulates amytase release and protein tyrosine phosphorylation of paxillin and p125FAK in differentiated AR4-2J pancreatic acinar cells
    • 71 Feick P, Gilhaus S, Schulz I: Pervanadate stimulates amytase release and protein tyrosine phosphorylation of paxillin and p125FAK in differentiated AR4-2J pancreatic acinar cells. J Biol Chem 1998, 273:16366-16373.
    • (1998) J Biol Chem , vol.273 , pp. 16366-16373
    • Feick, P.1    Gilhaus, S.2    Schulz, I.3
  • 72
    • 0345593673 scopus 로고    scopus 로고
    • Cholecystokinin-induced redistribution of paxillin in rat pancreatic acinar cells
    • 72 Leser J, Lührs H, Beil MF, Adler G, Lutz MP: Cholecystokinin-induced redistribution of paxillin in rat pancreatic acinar cells. Biochem Biophys Res Commun 1999, 254:400-405.
    • (1999) Biochem Biophys Res Commun , vol.254 , pp. 400-405
    • Leser, J.1    Lührs, H.2    Beil, M.F.3    Adler, G.4    Lutz, M.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.