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Volumn 135, Issue 5, 2010, Pages 527-543

Cyclic AMP potentiates Ca2+-dependent exocytosis in pancreatic duct epithelial cells

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; FORSKOLIN; PROTEINASE ACTIVATED RECEPTOR 2; PURINERGIC P2 RECEPTOR; PURINERGIC P2Y2 RECEPTOR;

EID: 77951709772     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.200910355     Document Type: Article
Times cited : (15)

References (54)
  • 1
    • 0032953205 scopus 로고    scopus 로고
    • CFTR channel insertion to the apical surface in rat duodenal villus epithelial cells is upregulated by VIP in vivo
    • Ameen, N.A., B. Martensson, L. Bourguinon, C. Marino. J. Isenberg, and G.E. McLaughlin. 1999. CFTR channel insertion to the apical surface in rat duodenal villus epithelial cells is upregulated by VIP in vivo. J. Cell Sci. 112:887-894.
    • (1999) J. Cell Sci. , vol.112 , pp. 887-894
    • Ameen, N.A.1    Martensson, B.2    Bourguinon, L.3    Marino, C.4    Isenberg, J.5    McLaughlin, G.E.6
  • 2
    • 0029786481 scopus 로고    scopus 로고
    • Mechanisms of desensitization and resensitization of proteinase-activated receptor-2
    • doi:10.1074/jbc.271.36.22003
    • Böhm, S.K., L.M. Khitin, E.F. Grady, G. Aponte, D. G. Payan, and N.W. Bunnett. 1996. Mechanisms of desensitization and resensitization of proteinase-activated receptor-2. J. Biol Chem. 271:22003-22016. doi:10.1074/jbc.271.36.22003
    • (1996) J. Biol Chem. , vol.271 , pp. 22003-22016
    • Böhm, S.K.1    Khitin, L.M.2    Grady, E.F.3    Aponte, G.4    Payan, D.G.5    Bunnett, N.W.6
  • 3
    • 23744437313 scopus 로고    scopus 로고
    • Phosphorylation of synapsin I by cAMP-dependent protein kinase controls synaptic vesicle dynamics in developing neurons
    • DOI 10.1523/JNEUROSCI.1573-05.2005
    • Bonanomi, D., A. Menegon, A. Miccio, G. Ferrari, A. Corradi, H.T. Kao, F. Benfenati, and F. Valtorta. 2005. Phosphorylation of synapsin I by cAMP-dependent protein kinase controls synaptic vesicle dynamics in developing neurons. J. Neurosci. 25:7299-7308. doi: 10.1.523/JNEUROSCI.1573-05.2005 (Pubitemid 41129801)
    • (2005) Journal of Neuroscience , vol.25 , Issue.32 , pp. 7299-7308
    • Bonanomi, D.1    Menegon, A.2    Miccio, A.3    Ferrari, G.4    Corradi, A.5    Kao, H.T.6    Benfenati, F.7    Valtorta, F.8
  • 4
    • 12344311438 scopus 로고    scopus 로고
    • Acute ENaC stimulation by cAMP in a kidney cell line is mediated by exocytic insertion from a recycling channel pool
    • doi:10.1085/jgp.200409124
    • Butterworth, M.B., R.S. Edinger, J.P. Johnson, and R.A. Frizzell. 2005. Acute ENaC stimulation by cAMP in a kidney cell line is mediated by exocytic insertion from a recycling channel pool. J. Gen. Physiol. 125:81-101. doi:10.1085/jgp.200409124
    • (2005) J. Gen. Physiol. , vol.125 , pp. 81-101
    • Butterworth, M.B.1    Edinger, R.S.2    Johnson, J.P.3    Frizzell, R.A.4
  • 6
    • 0035071322 scopus 로고    scopus 로고
    • Phosphoiylation of Snapin by PKA modulates its interaction with the SNARE complex
    • doi: 10.1038/35070000
    • Chheda, M.G., U. Asliery, P. Thakur, J. Rettig, and Z.H. Sheng. 2001. Phosphoiylation of Snapin by PKA modulates its interaction with the SNARE complex. Nat. Cell Biol. 3:331-338. doi: 10.1038/35070000
    • (2001) Nat. Cell Biol. , vol.3 , pp. 331-338
    • Chheda, M.G.1    Asliery, U.2    Thakur, P.3    Rettig, J.4    Sheng, Z.H.5
  • 7
    • 43549083496 scopus 로고    scopus 로고
    • Regulated airway goblet cell mucin secretion
    • doi:10.1146/ arm urev.physiol. 70.113006.100638
    • Davis, C.W., and B.F. Dickey. 2008. Regulated airway goblet cell mucin secretion. Annu. Rev. Physiol. 70:487-512. doi:10.1146/ arm urev.physiol. 70.113006.100638
    • (2008) Annu. Rev. Physiol. , vol.70 , pp. 487-512
    • Davis, C.W.1    Dickey, B.F.2
  • 8
    • 0014154913 scopus 로고
    • Co-operative action a calcium ions in transmitter release at the neuromuscular junction
    • Dodge, F.A. Jr., and R. Rahamimoff. 1967. Co-operative action a calcium ions in transmitter release at the neuromuscular junction. J. Physiol. 193:419-432.
    • (1967) J. Physiol. , vol.193 , pp. 419-432
    • Dodge Jr., F.A.1    Rahamimoff, R.2
  • 9
    • 0034697406 scopus 로고    scopus 로고
    • Simulation of regulated exocytosis of amylase from salivary parotid acinar cells by a consecutive reaction model comprising two sequential first-order reactions
    • DOI 10.1006/jtbi.2000.2009
    • Fujita-Yoshigaki, J. 2000. Simulation of regulated exocytosis of amylase from salivary parotid acinar cells by a consecutive reaction model comprising two sequential first-order reactions. J. Theor. Biol. 204:165-177. doi :10.1.006/jtbi. 2000.2009 (Pubitemid 30658683)
    • (2000) Journal of Theoretical Biology , vol.204 , Issue.2 , pp. 165-177
    • Fujita-Yoshigaki, J.1
  • 10
    • 0033551741 scopus 로고    scopus 로고
    • Presence of a complex containing vesicle-associated membrane protein 2 in rat parotid acinar cells and its disassembly upon activation of cAMP-dependent protein kinase
    • Fujita-Yoshigaki, J., Y. Dohke, M. Hara-Yokoyama, S. Furuyama, and H. Sugiya. 1999. Presence of a complex containing vesicleassociated membrane protein 2 in rat parotid acinar cells and its disassembly upon activation of cAMP-dependent. protein kinase. J. Biol. Chem. 274:23642-23646. doi:10.1074/jbc.274.33.23642 (Pubitemid 129529206)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.33 , pp. 23642-23646
    • Fujita-Yoshigaki, J.1    Dohke, Y.2    Hara-Yokoyama, M.3    Furuyama, S.4    Sugiya, H.5
  • 11
    • 0031559931 scopus 로고    scopus 로고
    • SNAP-23 is located in the basolateral plasma membrane of rat. pancreatic acinar cells
    • doi:10.1016/ S0014-5793(97)0l013-2
    • Gaisano, H.Y., L. Sheu, P.P. Wong, A. Hip, and W.S. Trimble. 1997. SNAP-23 is located in the basolateral plasma membrane of rat. pancreatic acinar cells. FEBS Lett. 414:298-302. doi:10.1016/ S0014-5793(97)0l013-2
    • (1997) FEBS Lett. , vol.414 , pp. 298-302
    • Gaisano, H.Y.1    Sheu, L.2    Wong, P.P.3    Hip, A.4    Trimble, W.S.5
  • 12
    • 0030176052 scopus 로고    scopus 로고
    • Protein kinase C. enhances exocytosis from chromaffin cells by increasing the size of the readily releasable pool of secretory granules
    • doi:10.1016/S0896-6273(00)80147-6
    • Gillis, R.D., R. Mossner, and E. Neher. 1996. Protein kinase C. enhances exocytosis from chromaffin cells by increasing the size of the readily releasable pool of secretory granules. Neuron. 16:1209-1220. doi:10.1016/S0896-6273(00)80147-6
    • (1996) Neuron. , vol.16 , pp. 1209-1220
    • Gillis, R.D.1    Mossner, R.2    Neher, E.3
  • 13
    • 0033529593 scopus 로고    scopus 로고
    • Identification of SNAREs involved in regulated exocytosis in the pancreatic acinar cell
    • Hansen, N.J., W. Antonin, and J.M. Edwardson. 1999. Identification of SNAREs involved in regulated exocytosis in the pancreatic acinar cell. J. Biol. Chem. 274:22871-22876. doi:10.1074/ jbc.274.32.22871 (Pubitemid 129529313)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.32 , pp. 22871-22876
    • Hansen, N.J.1    Antonin, W.2    Edwardson, J.M.3
  • 14
    • 0028000081 scopus 로고
    • 2+
    • Heinemann, C., R.H. Chow, E. Neher, and R.S. Zucker. 1994. Kinetics of the secretory response in bovine chromaffin cells following flash photolysis of caged Ca2+. Biophys. J. 67:2546-2557. doi: 10.1016/S0006-3495(94)80744-1 (Pubitemid 24369679)
    • (1994) Biophysical Journal , vol.67 , Issue.6 , pp. 2546-2557
    • Heinemann, C.1    Chow, R.H.2    Neher, E.3    Zucker, R.S.4
  • 15
    • 0033215525 scopus 로고    scopus 로고
    • Stimulation of" exocytosis without a calcium signal
    • doi: 10.1111/j.1469-7793.1999.00023.x
    • Hille, B., J. Billiard, D.F. Babcock, T. Nguyen, and D.S. Koh. 1999. Stimulation of" exocytosis without a calcium signal. J. Physiol. 520:23-31. doi: 10.1111/j.1469-7793.1999.00023.x
    • (1999) J. Physiol. , vol.520 , pp. 23-31
    • Hille, B.1    Billiard, J.2    Babcock, D.F.3    Nguyen, T.4    Koh, D.S.5
  • 16
    • 85047680153 scopus 로고    scopus 로고
    • 2+/calmodulin and cyclic 3,5′ adenosine monophosphate control movement of secretory granules through protein phosphorylation/ dephosphorylation in the pancreatic beta-cell
    • doi:10.1210/en.187.11.4644
    • 2+/calmodulin and cyclic 3,5′ adenosine monophosphate control movement of secretory granules through protein phosphorylation/dephosphorylation in the pancreatic beta-cell. Endocrinology. 137:4644-4649. doi:10.1210/en.187.11.4644
    • (1996) Endocrinology , vol.137 , pp. 4644-4649
    • Hisatomi, M.1    Hidaka, H.2    Niki, I.3
  • 17
    • 0033366466 scopus 로고    scopus 로고
    • Snapin: A SNAREassociated protein implicated in synaptic transmission
    • doi:10.1038/5673
    • Hardi, J.M., S. Mochida, and Z.H. Sheng. 1999. Snapin: a SNAREassociated protein implicated in synaptic transmission. Nat Neurosci. 2:119-124, doi:10.1038/5673
    • (1999) Nat Neurosci. , vol.2 , pp. 119-124
    • Hardi, J.M.1    Mochida, S.2    Sheng, Z.H.3
  • 19
    • 33748935725 scopus 로고    scopus 로고
    • 2+ increase determines the type of secretory mechanism activated in dog pancreatic duct epithelial cells
    • doi:10.1113/jphysiol.2006.114876
    • 2+ increase determines the type of secretory mechanism activated in dog pancreatic duct epithelial cells. J. Physiol. 576:163-178. doi:10.1113/jphysiol.2006.114876
    • (2006) J. Physiol. , vol.576 , pp. 163-178
    • Jung, S.R.1    Kim, K.2    Hille, B.3    Nguyen, T.D.4    Koh, D.S.5
  • 20
    • 63049101688 scopus 로고    scopus 로고
    • 2+ -dependent formation of F-actin in pancreatic duct epithelial cells
    • doi: 10.1111/j.1600-0854,2009.00884.x
    • 2+ -dependent formation of F-actin in pancreatic duct epithelial cells. Traffix. 10:392-410. doi: 10.1111/j.1600-0854, 2009.00884.x
    • (2009) Traffix , vol.10 , pp. 392-410
    • Jung, S.R.1    Kim, M.H.2    Hille, B.3    Koh, D.S.4
  • 21
    • 6944237411 scopus 로고    scopus 로고
    • Protein kinase A, which regulates intracellular transport, forms complexes with molecular motors on organelles
    • doi:10.1016/j.cub.2004 .10.003
    • Kashina, A.S., I.V. Semenova, P.A. Ivanov, E.S. Potekhina, I. Zaliapin, and V.l. Rodionov. 2004. Protein kinase A, which regulates intracellular transport, forms complexes with molecular motors on organelles. Curr. Biol. 14:1877-1881. doi:10.1016/j.cub.2004 .10.003
    • (2004) Curr. Biol. , vol.14 , pp. 1877-1881
    • Kashina, A.S.1    Semenova, I.V.2    Ivanov, P.A.3    Potekhina, E.S.4    Zaliapin, I.5    Rodionov, V.L.6
  • 22
    • 49649092896 scopus 로고    scopus 로고
    • Protease-activated receptor-2increases exocytosis via multiple signal transduction pathways in pancreatic duct epithelial cells
    • doi:10.1074/jbc.M801655200
    • Kim, M.H., B.H. Choi, S.R. Jung, T.J. Semka, S. Kim, K.T. Kim, B. Hille, T.D. Nguyen, and D.S. Koh. 2008. Protease-activated receptor-2increases exocytosis via multiple signal transduction pathways in pancreatic duct epithelial cells. J. Biol Chem, 283:18711-18720. doi:10.1074/jbc.M801655200
    • (2008) J. Biol Chem , vol.283 , pp. 18711-18720
    • Kim, M.H.1    Choi, B.H.2    Jung, S.R.3    Semka, T.J.4    Kim, S.5    Kim, K.T.6    Hille, B.7    Nguyen, T.D.8    Koh, D.S.9
  • 23
    • 36749047893 scopus 로고    scopus 로고
    • Carbon fiber amperometry in the study of ion channels and secretion
    • Koh, D.S. 2006. Carbon fiber amperometry in the study of ion channels and secretion. Methods Mol. Biol 337:139-153.
    • (2006) Methods Mol. Biol , vol.337 , pp. 139-153
    • Koh, D.S.1
  • 25
    • 51149097917 scopus 로고    scopus 로고
    • 2+-evoked transmitter release via acting on both Munc13 and protein kinase C
    • doi:10.1523/JNEUROSCI.055008.2008
    • 2+-evoked transmitter release via acting on both Munc13 and protein kinase C. J. Neurosci. 28:8257-8267. doi:10.1523/JNEUROSCI.055008.2008
    • (2008) J. Neurosci. , vol.28 , pp. 8257-8267
    • Lou, X.1    Korogod, N.2    Brose, N.3    Sclineggenburger, R.4
  • 27
    • 1242306711 scopus 로고    scopus 로고
    • Regulation of releasable vesicle pool sizes by protein kinase a-dependent phosphorylation of SNAP-25
    • DOI 10.1016/S0896-6273(04)00038-8
    • Nagy, G., K. Reim, U. Matti, N. Brose, T. Binz. J. Rettig, E. Neher, and J.B. Sorensen. 2004. Regulation of releasable vesicle pool sizes by protein kinase A-dependent phosphorylation of SNAP-25. Neuron. 41:417-429. doi:10.1016/S0896-6273(04)00038-8 (Pubitemid 38228352)
    • (2004) Neuron , vol.41 , Issue.3 , pp. 417-429
    • Nagy, G.1    Reim, K.2    Matti, U.3    Brose, N.4    Binz, T.5    Rettig, J.6    Neher, E.7    Sorensen, J.B.8
  • 29
    • 0032896792 scopus 로고    scopus 로고
    • Trypsin activates pancreatic duct epithelial cell ion channels through proteinase-activated receptor-2
    • doi:10.1172/JCI2539
    • Nguyen, T.D., M.W. Moody, M. Steinhoff, C. Okolo, D.S. Koh, and N.W. Bunnett. 1999. Trypsin activates pancreatic duct epithelial cell ion channels through proteinase-activated receptor-2. J. Clin. Invest. 103:261-269. doi:10.1172/JCI2539
    • (1999) J. Clin. Invest. , vol.103 , pp. 261-269
    • Nguyen, T.D.1    Moody, M.W.2    Steinhoff, M.3    Okolo, C.4    Koh, D.S.5    Bunnett, N.W.6
  • 31
    • 4444377903 scopus 로고    scopus 로고
    • Novel single chain cAMP sensors for receptor-induced signal propagation
    • doi:10.1074/jbc. C400302200
    • Nikolaev, V.O., M. Bünemann, L. Hein, A. Hannawacker, and M.J. Lohse. 2004. Novel single chain cAMP sensors for receptor-induced signal propagation. J. Biol. Chem. 279:37215-37218. doi:10.1074/jbc. C400302200
    • (2004) J. Biol. Chem. , vol.279 , pp. 37215-37218
    • Nikolaev, V.O.1    Bünemann, M.2    Hein, L.3    Hannawacker, A.4    Lohse, M.J.5
  • 32
    • 0031720360 scopus 로고    scopus 로고
    • 2+
    • DOI 10.2337/diabetes.47.11.1699
    • Niwa, T., Y. Matsukawa, T. Senda, Y. Nimura, H. Hidaka, and I. Niki. 1998. Acetylcholine activates intracellular movement of insulin granules in pancreatic beta-cells via inositol triphosphatedependent mobilization of intracellular Ca2+. Diabetes. 47:1699-1706. doi:10.2337/diabetes.47.11.1699 (Pubitemid 28476243)
    • (1998) Diabetes , vol.47 , Issue.11 , pp. 1699-1706
    • Niwa, T.1    Matsukawa, Y.2    Senda, T.3    Nimura, Y.4    Hidaka, H.5    Niki, I.6
  • 34
    • 0034951634 scopus 로고    scopus 로고
    • Imaging transmitter release. II. A practical guide to evanescent-wave imaging
    • Oheim, M. 2001. Imaging transmitter release. II. A practical guide to evanescent-wave imaging. Lasers Med. Sci. 16:159-170. doi:10.1007/PL00011350 (Pubitemid 32606445)
    • (2001) Lasers in Medical Science , vol.16 , Issue.3 , pp. 159-170
    • Oheim, M.1
  • 35
    • 0035185231 scopus 로고    scopus 로고
    • Role of snare proteins in CFTR and ENaC trafficking
    • doi:l0.1007/s004240100647
    • Peters, K.W., J. Qi, J.P. Johnson, S.C. Watkins, and R.A. Frizzell. 2001. Role of snare proteins in CFTR and ENaC trafficking. Pflugers Arch. 443:S65-S69. doi:l0.1007/s004240100647
    • (2001) Pflugers Arch. , vol.443
    • Peters, K.W.1    Qi, J.2    Johnson, J.P.3    Watkins, S.C.4    Frizzell, R.A.5
  • 36
    • 0025997180 scopus 로고
    • Single particle tracking. Analysis of diffusion and flow in two-dimensional systems
    • doi:10.1016/S0006-3495(91) 82125-7
    • Qian, H., M.P. Sheetz, and E.L. Elson. 1991. Single particle tracking. Analysis of diffusion and flow in two-dimensional systems. Biophys. J 60:910-921. doi:10.1016/S0006-3495(91) 82125-7
    • (1991) Biophys. J , vol.60 , pp. 910-921
    • Qian, H.1    Sheetz, M.P.2    Elson, E.L.3
  • 37
    • 0242318330 scopus 로고    scopus 로고
    • Switching between microtubule- and actin-based transport systems in melanophores is controlled by cAMP levels
    • DOI 10.1016/j.cub.2003.10.027
    • Rodionov, V., J. Yi, A. Kashina, A. Oladipo, and S.P. Gross. 2003. Switching between microtubule- and actin-based transport systems in melanophores is controlled by cAMP levels. Curr. Biol. 13:1837-1847. doi: 10.1016/j.cub.2003.10.027 (Pubitemid 37347926)
    • (2003) Current Biology , vol.13 , Issue.21 , pp. 1837-1847
    • Rodionov, V.1    Yi, J.2    Kashina, A.3    Oladipo, A.4    Gross, S.P.5
  • 38
    • 67049156069 scopus 로고    scopus 로고
    • Phosphorylation of myristoylated alanine-rich C. kinase substrate is involved in the cAMP-dependent amylase release in parotid acinar cells
    • doi:10.1152/ ajpgi.90536.2008
    • Satoh, K., M. Matsuki-Fukushima, B. Qi, M.Y. Guo, T. Narita, J. Fujita-Yoshigaki, and H. Sugiya. 2009. Phosphorylation of myristoylated alanine-rich C. kinase substrate is involved in the cAMP-dependent amylase release in parotid acinar cells. Am. J. Physiol. Gastrointesl. Liver Physiol. 296:GI382-G1390. doi:10.1152/ ajpgi.90536.2008
    • (2009) Am. J. Physiol. Gastrointesl. Liver Physiol. , vol.296
    • Satoh, K.1    Matsuki-Fukushima, M.2    Qi, B.3    Guo, M.Y.4    Narita, T.5    Fujita-Yoshigaki, J.6    Sugiya, H.7
  • 40
    • 25444520038 scopus 로고    scopus 로고
    • PKA-dependent and PKA-independent pathways for cAMP-regulated exocytosis
    • DOI 10.1152/physrev.00001.2005
    • Seino, S., and T. Shibasaki, 2005. PKA-dependent and PKAindependent pathways for cAMP-regulated exocytosis. Physiol. Rev. 85:1303-1342. doi:10.1152/physrev.00001,2005 (Pubitemid 41362272)
    • (2005) Physiological Reviews , vol.85 , Issue.4 , pp. 1303-1342
    • Seino, S.1    Shibasaki, T.2
  • 41
    • 0024400646 scopus 로고
    • Subunit interactions and physical properties of bovine gallbladder mucin
    • Smith, B.F., J.A. Peetermans, T. Tanaka, and J.T. LaMont. 1989. Subunit interactions and physical properties of bovine gallbladder mucin. Gastroenterology. 97:179-187.
    • (1989) Gastroenterology , vol.97 , pp. 179-187
    • Smith, B.F.1    Peetermans, J.A.2    Tanaka, T.3    Lamont, J.T.4
  • 42
    • 0035980028 scopus 로고    scopus 로고
    • Visualization of ATP release in pancreatic acini in response cholinergic stimulus: Use of fluorescent probes and confocal microscopy
    • DOI 10.1074/jbc.M103313200
    • Sprensen, C.E., and I. Novak. 2001. Visualization of ATP release in pancreatic acini in response to cholinergic stimulus. Use of fluorescent probes and confocal microscopy. J. Biol. Chem. 276:32925-32932. doi:10.1074/jbc. M103313200 (Pubitemid 37384743)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.35 , pp. 32925-32932
    • Sorensen, C.E.1    Novak, I.2
  • 43
    • 0032995380 scopus 로고    scopus 로고
    • Tracking single secretory granules in live chromaffin cells by evanescent-field fluorescence microscopy
    • doi:10.1016/S00063495(99)77382-0
    • Steyer, J.A., and W. Aimers. 1999. Tracking single secretory granules in live chromaffin cells by evanescent-field fluorescence microscopy. Biophys.J. 76:2262-2271, doi:10.1016/S00063495(99)77382-0
    • (1999) Biophys.J. , vol.76 , pp. 2262-2271
    • Steyer, J.A.1    Aimers, W.2
  • 44
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • doi:10.1146/annurev.neuro.26.041002.131412
    • Südhof, TC. 2004. The synaptic vesicle cycle. Annu, Rev. Neurosci. 27:509-547. doi:10.1146/annurev.neuro.26.041002.131412
    • (2004) Annu, Rev. Neurosci. , vol.27 , pp. 509-547
    • Südhof, T.C.1
  • 45
    • 0032499761 scopus 로고    scopus 로고
    • Modulation of an early step in the secretory machinery in hippocampal nerve terminals
    • doi:10.1073/ pnas.95.12.7163
    • Trudeau, L.E., Y. Fang, and P.G. Haydon. 1998. Modulation of an early step in the secretory machinery in hippocampal nerve terminals. Proc. Natl. Acad. Sci. USA. 95:7163-7168. doi:10.1073/ pnas.95.12.7163
    • (1998) Proc. Natl. Acad. Sci. USA. , vol.95 , pp. 7163-7168
    • Trudeau, L.E.1    Fang, Y.2    Haydon, P.G.3
  • 46
    • 0030614827 scopus 로고    scopus 로고
    • 2+ release from internal stores controls exocytosis in pituitary gonadotrophs
    • doi:10.1016/S08966273(01)80051-9
    • 2+ release from internal stores controls exocytosis in pituitary gonadotrophs. Neuron. 18:121-132. doi:10.1016/S08966273(01)80051-9
    • (1997) Neuron. , vol.18 , pp. 121-132
    • Tse, F.W.1    Tse, A.2    Hille, B.3    Horstmann, H.4    Aimers, W.5
  • 47
    • 0346732321 scopus 로고    scopus 로고
    • 5′-AMP-activated protein kinase controls insulin-containing secretory vesicle dynamics
    • doi: 10 .1074/jbc.M307800200
    • Tsuboi, T., G. da Silva Xavier, I. Ledere, and G.A. Rutter. 2003. 5′-AMP-activated protein kinase controls insulin-containing secretory vesicle dynamics. J Biol. Cliem. 278:52042-52051, doi: 10 .1074/jbc.M307800200
    • (2003) J Biol. Cliem. , vol.278 , pp. 52042-52051
    • Tsuboi, T.1    Da Silva Xavier, G.2    Ledere, I.3    Rutter, G.A.4
  • 50
    • 10344221040 scopus 로고    scopus 로고
    • 2+-sensitive pool of granules is regulated by glucose and protein kinases in insulinsecreting INS-I cells
    • doi: 10.1085/ jgp. 200409081
    • 2+-sensitive pool of granules is regulated by glucose and protein kinases in insulinsecreting INS-I cells. J. Gen. Physiol 124:641-651, doi: 10.1085/ jgp. 200409081
    • (2004) J. Gen. Physiol , vol.124 , pp. 641-651
    • Yang, Y.1    Gillis, K.D.2
  • 51
    • 15244353284 scopus 로고    scopus 로고
    • 2+ cooperativity in pituitary gonadotropes
    • doi:10.1085/jgp.200409230
    • 2+ cooperativity in pituitary gonadotropes. J. Gen, Physiol. 125:327-334. doi:10.1085/jgp.200409230
    • (2005) J. Gen, Physiol. , vol.125 , pp. 327-334
    • Yang, H.1    Liu, H.2    Hu, Z.3    Zhu, H.4    Xu, T.5
  • 53
    • 0033980372 scopus 로고    scopus 로고
    • Growth and function of isolated canine pancreatic ductal cells
    • DOI 10.1097/00006676-200001000-00010
    • Zhang, M., R.L. Schleicher, AS. Fink, P. Gunter-Smith, C. Savard, T. Nguyen, and S.P. Lee. 2000. Growth and function of isolated canine pancreatic ductal cells. Pancreas. 20:67-76. doi:10.1097/ 00006676-200001000-200100010 (Pubitemid 30022646)
    • (2000) Pancreas , vol.20 , Issue.1 , pp. 67-76
    • Zhang, M.1    Schleicher, R.L.2    Fink, A.S.3    Gunter-Smith, P.4    Savard, C.5    Nguyen, T.6    Lee, S.P.7
  • 54
    • 0037168549 scopus 로고    scopus 로고
    • Sensitization of regulated exocytosis by protein kinase C
    • doi:10.1073/pnas.232588899
    • Zhu, H., B. Hille, and T. Xu. 2002. Sensitization of regulated exocytosis by protein kinase C. Proc. Natl. Acad. Sci. USA. 99:17055-17059. doi:10.1073/pnas.232588899
    • (2002) Proc. Natl. Acad. Sci. USA. , vol.99 , pp. 17055-17059
    • Zhu, H.1    Hille, B.2    Xu, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.