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Volumn 55, Issue 6, 2014, Pages 337-345

Calcium signaling in pancreatic ductal epithelial cells: An old friend and a nasty enemy

Author keywords

Exocrine pancreas; Pancreatic ductal secretion

Indexed keywords

BICARBONATE; CALCIUM ION; ELECTROLYTE; CALCIUM; ADENOSINE TRIPHOSPHATE; NEUROHORMONE;

EID: 84902343209     PISSN: 01434160     EISSN: 15321991     Source Type: Journal    
DOI: 10.1016/j.ceca.2014.02.004     Document Type: Review
Times cited : (52)

References (115)
  • 3
    • 84896730466 scopus 로고    scopus 로고
    • The exocrine pancreas: the acinar-ductal tango in physiology and pathophysiology
    • Hegyi P., Petersen O.H. The exocrine pancreas: the acinar-ductal tango in physiology and pathophysiology. Rev. Physiol. Biochem. Pharmacol. 2013, 165:1-30.
    • (2013) Rev. Physiol. Biochem. Pharmacol. , vol.165 , pp. 1-30
    • Hegyi, P.1    Petersen, O.H.2
  • 4
    • 0016381467 scopus 로고
    • Stereological analysis of the guinea pig pancreas. I. Analytical model and quantitative description of nonstimulated pancreatic exocrine cells
    • Bolender R.P. Stereological analysis of the guinea pig pancreas. I. Analytical model and quantitative description of nonstimulated pancreatic exocrine cells. J. Cell Biol. 1974, 61:269-287.
    • (1974) J. Cell Biol. , vol.61 , pp. 269-287
    • Bolender, R.P.1
  • 6
    • 48249140989 scopus 로고    scopus 로고
    • Effects of bile acids on pancreatic ductal bicarbonate secretion in guinea pig
    • Venglovecz V., Rakonczay Z., Ozsvari B., et al. Effects of bile acids on pancreatic ductal bicarbonate secretion in guinea pig. Gut 2008, 57:1102-1112.
    • (2008) Gut , vol.57 , pp. 1102-1112
    • Venglovecz, V.1    Rakonczay, Z.2    Ozsvari, B.3
  • 7
    • 78651245402 scopus 로고    scopus 로고
    • Non-conjugated chenodeoxycholate induces severe mitochondrial damage and inhibits bicarbonate transport in pancreatic duct cells
    • Maleth J., Venglovecz V., Razga Z., Tiszlavicz L., Rakonczay Z., Hegyi P. Non-conjugated chenodeoxycholate induces severe mitochondrial damage and inhibits bicarbonate transport in pancreatic duct cells. Gut 2011, 60:136-138.
    • (2011) Gut , vol.60 , pp. 136-138
    • Maleth, J.1    Venglovecz, V.2    Razga, Z.3    Tiszlavicz, L.4    Rakonczay, Z.5    Hegyi, P.6
  • 8
    • 77956334526 scopus 로고    scopus 로고
    • Insufficiency of electrolyte and fluid secretion by pancreatic ductal cells leads to increased patient risk for pancreatitis
    • Hegyi P., Rakonczay Z. Insufficiency of electrolyte and fluid secretion by pancreatic ductal cells leads to increased patient risk for pancreatitis. Am. J. Gastroenterol. 2010, 105:2119-2120.
    • (2010) Am. J. Gastroenterol. , vol.105 , pp. 2119-2120
    • Hegyi, P.1    Rakonczay, Z.2
  • 10
    • 0015322031 scopus 로고
    • Effect of acetazolamide on human pancreatic secretion
    • Dyck W.P., Hightower N.C., Janowitz H.D. Effect of acetazolamide on human pancreatic secretion. Gastroenterology 1972, 62:547-552.
    • (1972) Gastroenterology , vol.62 , pp. 547-552
    • Dyck, W.P.1    Hightower, N.C.2    Janowitz, H.D.3
  • 11
    • 0015538840 scopus 로고
    • Influence of amphotericin, amiloride, ionophores, and 2,4-dinitrophenol on the secretion of the isolated cat's pancreas
    • Wizemann V., Schulz I. Influence of amphotericin, amiloride, ionophores, and 2,4-dinitrophenol on the secretion of the isolated cat's pancreas. Pflugers Arch. 1973, 339:317-338.
    • (1973) Pflugers Arch. , vol.339 , pp. 317-338
    • Wizemann, V.1    Schulz, I.2
  • 14
    • 0000903375 scopus 로고    scopus 로고
    • Immuno and functional characterization of CFTR in submandibular and pancreatic acinar and duct cells
    • Zeng W., Lee M.G., Yan M., et al. Immuno and functional characterization of CFTR in submandibular and pancreatic acinar and duct cells. Am. J. Physiol. 1997, 273:C442-C455.
    • (1997) Am. J. Physiol. , vol.273
    • Zeng, W.1    Lee, M.G.2    Yan, M.3
  • 15
    • 0035282581 scopus 로고    scopus 로고
    • Aberrant CFTR-dependent HCO3- transport in mutations associated with cystic fibrosis
    • Choi J.Y., Muallem D., Kiselyov K., Lee M.G., Thomas P.J., Muallem S. Aberrant CFTR-dependent HCO3- transport in mutations associated with cystic fibrosis. Nature 2001, 410:94-97.
    • (2001) Nature , vol.410 , pp. 94-97
    • Choi, J.Y.1    Muallem, D.2    Kiselyov, K.3    Lee, M.G.4    Thomas, P.J.5    Muallem, S.6
  • 16
    • 77955480968 scopus 로고    scopus 로고
    • i and its role in pancreatic bicarbonate secretion
    • i and its role in pancreatic bicarbonate secretion. Gastroenterology 2010, 139:620-631.
    • (2010) Gastroenterology , vol.139 , pp. 620-631
    • Park, H.W.1    Nam, J.H.2    Kim, J.Y.3
  • 17
    • 61749090806 scopus 로고    scopus 로고
    • - secretion by stimulating the transporters pNBC1 and CFTR in the murine pancreatic duct
    • - secretion by stimulating the transporters pNBC1 and CFTR in the murine pancreatic duct. J. Clin. Invest. 2009, 119:193-202.
    • (2009) J. Clin. Invest. , vol.119 , pp. 193-202
    • Yang, D.1    Shcheynikov, N.2    Zeng, W.3
  • 18
    • 84879492181 scopus 로고    scopus 로고
    • 2+ and cAMP signaling pathways during epithelial transport in mice
    • 2+ and cAMP signaling pathways during epithelial transport in mice. Gastroenterology 2013, 145:232-241.
    • (2013) Gastroenterology , vol.145 , pp. 232-241
    • Park, S.1    Shcheynikov, N.2    Hong, J.H.3
  • 19
    • 84902323307 scopus 로고    scopus 로고
    • Mechanism and synergism in epithelial fluid and electrolyte secretion
    • Epub ahead of print
    • Hong J.H., Park S., Shcheynikov N., Muallem S. Mechanism and synergism in epithelial fluid and electrolyte secretion. Pflugers Arch. 2013, Epub ahead of print.
    • (2013) Pflugers Arch.
    • Hong, J.H.1    Park, S.2    Shcheynikov, N.3    Muallem, S.4
  • 20
    • 84867169446 scopus 로고    scopus 로고
    • The WNK/SPAK and IRBIT/PP1 pathways in epithelial fluid and electrolyte transport
    • Park S., Hong J.H., Ohana E., Muallem S. The WNK/SPAK and IRBIT/PP1 pathways in epithelial fluid and electrolyte transport. Physiology (Bethesda) 2012, 27:291-299.
    • (2012) Physiology (Bethesda) , vol.27 , pp. 291-299
    • Park, S.1    Hong, J.H.2    Ohana, E.3    Muallem, S.4
  • 21
    • 0028047688 scopus 로고
    • CFTR and calcium-activated chloride currents in pancreatic duct cells of a transgenic CF mouse
    • Gray M.A., Winpenny J.P., Porteous D.J., Dorin J.R., Argent B.E. CFTR and calcium-activated chloride currents in pancreatic duct cells of a transgenic CF mouse. Am. J. Physiol. 1994, 266:C213-C221.
    • (1994) Am. J. Physiol. , vol.266
    • Gray, M.A.1    Winpenny, J.P.2    Porteous, D.J.3    Dorin, J.R.4    Argent, B.E.5
  • 22
    • 75849162765 scopus 로고    scopus 로고
    • Studies on expression and function of the TMEM16A calcium-activated chloride channel
    • Huang F., Rock J.R., Harfe B.D., et al. Studies on expression and function of the TMEM16A calcium-activated chloride channel. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:21413-21418.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 21413-21418
    • Huang, F.1    Rock, J.R.2    Harfe, B.D.3
  • 23
    • 0038460939 scopus 로고    scopus 로고
    • Distribution of aquaporin water channels AQP1 and AQP5 in the ductal system of the human pancreas
    • Burghardt B., Elkaer M.L., Kwon T.H., et al. Distribution of aquaporin water channels AQP1 and AQP5 in the ductal system of the human pancreas. Gut 2003, 52:1008-1016.
    • (2003) Gut , vol.52 , pp. 1008-1016
    • Burghardt, B.1    Elkaer, M.L.2    Kwon, T.H.3
  • 24
    • 0027239721 scopus 로고
    • Muscarinic receptors in isolated guinea pig pancreatic ducts
    • Hootman S.R., Zukerman J., Kovalcik S.A. Muscarinic receptors in isolated guinea pig pancreatic ducts. Biochem. Pharmacol. 1993, 46:291-296.
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 291-296
    • Hootman, S.R.1    Zukerman, J.2    Kovalcik, S.A.3
  • 25
    • 48449099104 scopus 로고    scopus 로고
    • Purinergic receptors in the endocrine and exocrine pancreas
    • Novak I. Purinergic receptors in the endocrine and exocrine pancreas. Purinergic Signal. 2008, 4:237-253.
    • (2008) Purinergic Signal. , vol.4 , pp. 237-253
    • Novak, I.1
  • 26
    • 84862076637 scopus 로고    scopus 로고
    • Purinergic signalling in the pancreas in health and disease
    • Burnstock G., Novak I. Purinergic signalling in the pancreas in health and disease. J. Endocrinol. 2012, 213:123-141.
    • (2012) J. Endocrinol. , vol.213 , pp. 123-141
    • Burnstock, G.1    Novak, I.2
  • 28
    • 48549100809 scopus 로고    scopus 로고
    • 2+ signaling and enzyme secretion by cholecystokinin in human pancreatic acinar cells
    • 2+ signaling and enzyme secretion by cholecystokinin in human pancreatic acinar cells. Gastroenterology 2008, 135:632-641.
    • (2008) Gastroenterology , vol.135 , pp. 632-641
    • Murphy, J.A.1    Criddle, D.N.2    Sherwood, M.3
  • 29
    • 0020581625 scopus 로고
    • Potentiation effect of cholecystokinin-octapeptide on pancreatic bicarbonate secretion stimulated by a physiologic dose of secretin in humans
    • You C.H., Rominger J.M., Chey W.Y. Potentiation effect of cholecystokinin-octapeptide on pancreatic bicarbonate secretion stimulated by a physiologic dose of secretin in humans. Gastroenterology 1983, 85:40-45.
    • (1983) Gastroenterology , vol.85 , pp. 40-45
    • You, C.H.1    Rominger, J.M.2    Chey, W.Y.3
  • 30
    • 0023038362 scopus 로고
    • Morphological, biochemical and secretory studies on rat pancreatic ducts maintained in tissue culture
    • Argent B.E., Arkle S., Cullen M.J., Green R. Morphological, biochemical and secretory studies on rat pancreatic ducts maintained in tissue culture. Q. J. Exp. Physiol. 1986, 71:633-648.
    • (1986) Q. J. Exp. Physiol. , vol.71 , pp. 633-648
    • Argent, B.E.1    Arkle, S.2    Cullen, M.J.3    Green, R.4
  • 31
    • 0024409931 scopus 로고
    • Patterns of pancreatic secretion in the anaesthetised guinea pig following stimulation with secretin, cholecystokinin octapeptide, or bombesin
    • Padfield P.J., Garner A., Case R.M. Patterns of pancreatic secretion in the anaesthetised guinea pig following stimulation with secretin, cholecystokinin octapeptide, or bombesin. Pancreas 1989, 4:204-209.
    • (1989) Pancreas , vol.4 , pp. 204-209
    • Padfield, P.J.1    Garner, A.2    Case, R.M.3
  • 32
    • 0023007412 scopus 로고
    • Isolation of ducts from the pancreas of copper-deficient rats
    • Arkle S., Lee C.M., Cullen M.J., Argent B.E. Isolation of ducts from the pancreas of copper-deficient rats. Q. J. Exp. Physiol. 1986, 71:249-265.
    • (1986) Q. J. Exp. Physiol. , vol.71 , pp. 249-265
    • Arkle, S.1    Lee, C.M.2    Cullen, M.J.3    Argent, B.E.4
  • 33
    • 84881022178 scopus 로고    scopus 로고
    • Adenylyl cyclase 6 mediates the action of cyclic AMP-dependent secretagogues in mouse pancreatic exocrine cells via protein kinase A pathway activation
    • Sabbatini M.E., D'Alecy L., Lentz S.I., Tang T., Williams J.A. Adenylyl cyclase 6 mediates the action of cyclic AMP-dependent secretagogues in mouse pancreatic exocrine cells via protein kinase A pathway activation. J. Physiol. 2013, 591:3693-3707.
    • (2013) J. Physiol. , vol.591 , pp. 3693-3707
    • Sabbatini, M.E.1    D'Alecy, L.2    Lentz, S.I.3    Tang, T.4    Williams, J.A.5
  • 34
    • 0034787415 scopus 로고    scopus 로고
    • Pancreatic acinar cell dysfunction in CFTR(-/-) mice is associated with impairments in luminal pH and endocytosis
    • Freedman S.D., Kern H.F., Scheele G.A. Pancreatic acinar cell dysfunction in CFTR(-/-) mice is associated with impairments in luminal pH and endocytosis. Gastroenterology 2001, 121:950-957.
    • (2001) Gastroenterology , vol.121 , pp. 950-957
    • Freedman, S.D.1    Kern, H.F.2    Scheele, G.A.3
  • 35
    • 0035114296 scopus 로고    scopus 로고
    • Guanylin in the human pancreas: a novel luminocrine regulatory pathway of electrolyte secretion via cGMP and CFTR in the ductal system
    • Kulaksiz H., Schmid A., Honscheid M., Eissele R., Klempnauer J., Cetin Y. Guanylin in the human pancreas: a novel luminocrine regulatory pathway of electrolyte secretion via cGMP and CFTR in the ductal system. Histochem. Cell Biol. 2001, 115:131-145.
    • (2001) Histochem. Cell Biol. , vol.115 , pp. 131-145
    • Kulaksiz, H.1    Schmid, A.2    Honscheid, M.3    Eissele, R.4    Klempnauer, J.5    Cetin, Y.6
  • 36
    • 0036839540 scopus 로고    scopus 로고
    • Extracellular calcium sensing receptor in human pancreatic cells
    • Racz G.Z., Kittel A., Riccardi D., Case R.M., Elliott A.C., Varga G. Extracellular calcium sensing receptor in human pancreatic cells. Gut 2002, 51:705-711.
    • (2002) Gut , vol.51 , pp. 705-711
    • Racz, G.Z.1    Kittel, A.2    Riccardi, D.3    Case, R.M.4    Elliott, A.C.5    Varga, G.6
  • 37
    • 0042242920 scopus 로고    scopus 로고
    • P inhibits bicarbonate secretion from guinea pig pancreatic ducts by modulating an anion exchanger
    • Hegyi P., Gray M.A., Argent B.E., Substance P inhibits bicarbonate secretion from guinea pig pancreatic ducts by modulating an anion exchanger. Am. J. Physiol. Cell Physiol. 2003, 285:C268-C276.
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285
    • Hegyi, P.1    Gray, M.A.2    Argent, B.E.3
  • 38
    • 0034794969 scopus 로고    scopus 로고
    • 5-Hydroxytryptamine strongly inhibits fluid secretion in guinea pig pancreatic duct cells
    • Suzuki A., Naruse S., Kitagawa M., et al. 5-Hydroxytryptamine strongly inhibits fluid secretion in guinea pig pancreatic duct cells. J. Clin. Invest. 2001, 108:749-756.
    • (2001) J. Clin. Invest. , vol.108 , pp. 749-756
    • Suzuki, A.1    Naruse, S.2    Kitagawa, M.3
  • 39
    • 0034685801 scopus 로고    scopus 로고
    • The role of the pleckstrin homology domain in membrane targeting and activation of phospholipase Cbeta(1)
    • Razzini G., Brancaccio A., Lemmon M.A., Guarnieri S., Falasca M. The role of the pleckstrin homology domain in membrane targeting and activation of phospholipase Cbeta(1). J. Biol. Chem. 2000, 275:14873-14881.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14873-14881
    • Razzini, G.1    Brancaccio, A.2    Lemmon, M.A.3    Guarnieri, S.4    Falasca, M.5
  • 40
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • Berridge M.J. Inositol trisphosphate and calcium signalling. Nature 1993, 361:315-325.
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 42
    • 25844462280 scopus 로고    scopus 로고
    • IP3 receptor types 2 and 3 mediate exocrine secretion underlying energy metabolism
    • Futatsugi A., Nakamura T., Yamada M.K., et al. IP3 receptor types 2 and 3 mediate exocrine secretion underlying energy metabolism. Science 2005, 309:2232-2234.
    • (2005) Science , vol.309 , pp. 2232-2234
    • Futatsugi, A.1    Nakamura, T.2    Yamada, M.K.3
  • 43
    • 79955999336 scopus 로고    scopus 로고
    • IP3 receptors and Orai channels in pancreatic acinar cells: co-localisation and its consequences
    • Lur G., Sherwood M.W., Ebisui E., et al. IP3 receptors and Orai channels in pancreatic acinar cells: co-localisation and its consequences. Biochem. J. 2011, 436:231-239.
    • (2011) Biochem. J. , vol.436 , pp. 231-239
    • Lur, G.1    Sherwood, M.W.2    Ebisui, E.3
  • 44
    • 0037518204 scopus 로고    scopus 로고
    • IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding protein, is released from the IP3 receptor upon IP3 binding to the receptor
    • Ando H., Mizutani A., Matsu-ura T., Mikoshiba K. IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding protein, is released from the IP3 receptor upon IP3 binding to the receptor. J. Biol. Chem. 2003, 278:10602-106012.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10602-106012
    • Ando, H.1    Mizutani, A.2    Matsu-ura, T.3    Mikoshiba, K.4
  • 45
    • 79952205039 scopus 로고    scopus 로고
    • IRBIT governs epithelial secretion in mice by antagonizing the WNK/SPAK kinase pathway
    • Yang D., Li Q., So I., et al. IRBIT governs epithelial secretion in mice by antagonizing the WNK/SPAK kinase pathway. J. Clin. Invest. 2011, 121:956-965.
    • (2011) J. Clin. Invest. , vol.121 , pp. 956-965
    • Yang, D.1    Li, Q.2    So, I.3
  • 48
    • 39549112572 scopus 로고    scopus 로고
    • Polarized calcium signaling in exocrine gland cells
    • Petersen O.H., Tepikin A.V. Polarized calcium signaling in exocrine gland cells. Annu. Rev. Physiol. 2008, 70:273-299.
    • (2008) Annu. Rev. Physiol. , vol.70 , pp. 273-299
    • Petersen, O.H.1    Tepikin, A.V.2
  • 49
    • 0018238365 scopus 로고
    • Stimulus-permeability coupling: role of calcium in the receptor regulation of membrane permeability
    • Putney J.W. Stimulus-permeability coupling: role of calcium in the receptor regulation of membrane permeability. Pharmacol. Rev. 1978, 30:209-245.
    • (1978) Pharmacol. Rev. , vol.30 , pp. 209-245
    • Putney, J.W.1
  • 50
    • 0026594980 scopus 로고
    • Depletion of intracellular calcium stores activates a calcium current in mast cells
    • Hoth M., Penner R. Depletion of intracellular calcium stores activates a calcium current in mast cells. Nature 1992, 355:353-356.
    • (1992) Nature , vol.355 , pp. 353-356
    • Hoth, M.1    Penner, R.2
  • 52
    • 33646576875 scopus 로고    scopus 로고
    • A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function
    • Feske S., Gwack Y., Prakriya M., et al. A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function. Nature 2006, 441:179-185.
    • (2006) Nature , vol.441 , pp. 179-185
    • Feske, S.1    Gwack, Y.2    Prakriya, M.3
  • 54
    • 77952668956 scopus 로고    scopus 로고
    • An endoplasmic reticulum/plasma membrane junction: STIM1/Orai1/TRPCs
    • Lee K.P., Yuan J.P., Hong J.H., So I., Worley P.F., Muallem S. An endoplasmic reticulum/plasma membrane junction: STIM1/Orai1/TRPCs. FEBS Lett. 2010, 584:2022-2027.
    • (2010) FEBS Lett. , vol.584 , pp. 2022-2027
    • Lee, K.P.1    Yuan, J.P.2    Hong, J.H.3    So, I.4    Worley, P.F.5    Muallem, S.6
  • 56
    • 34447097610 scopus 로고    scopus 로고
    • STIM1 heteromultimerizes TRPC channels to determine their function as store-operated channels
    • Yuan J.P., Zeng W., Huang G.N., Worley P.F., Muallem S. STIM1 heteromultimerizes TRPC channels to determine their function as store-operated channels. Nat. Cell Biol. 2007, 9:636-645.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 636-645
    • Yuan, J.P.1    Zeng, W.2    Huang, G.N.3    Worley, P.F.4    Muallem, S.5
  • 57
    • 78651094967 scopus 로고    scopus 로고
    • Polarized but differential localization and recruitment of STIM1, Orai1 and TRPC channels in secretory cells
    • Hong J.H., Li Q., Kim M.S., et al. Polarized but differential localization and recruitment of STIM1, Orai1 and TRPC channels in secretory cells. Traffic 2011, 12:232-245.
    • (2011) Traffic , vol.12 , pp. 232-245
    • Hong, J.H.1    Li, Q.2    Kim, M.S.3
  • 58
    • 70349786480 scopus 로고    scopus 로고
    • Ribosome-free terminals of rough ER allow formation of STIM1 puncta and segregation of STIM1 from IP3 receptors
    • Lur G., Haynes L.P., Prior I.A., et al. Ribosome-free terminals of rough ER allow formation of STIM1 puncta and segregation of STIM1 from IP3 receptors. Curr. Biol. 2009, 19:1648-1653.
    • (2009) Curr. Biol. , vol.19 , pp. 1648-1653
    • Lur, G.1    Haynes, L.P.2    Prior, I.A.3
  • 59
    • 84871280934 scopus 로고    scopus 로고
    • Polarization of calcium signaling and fluid secretion in salivary gland cells
    • Ambudkar I.S. Polarization of calcium signaling and fluid secretion in salivary gland cells. Curr. Med. Chem. 2012, 19:5774-5781.
    • (2012) Curr. Med. Chem. , vol.19 , pp. 5774-5781
    • Ambudkar, I.S.1
  • 62
    • 0033521586 scopus 로고    scopus 로고
    • Quasi-synaptic calcium signal transmission between endoplasmic reticulum and mitochondria
    • Csordas G., Thomas A.P., Hajnoczky G. Quasi-synaptic calcium signal transmission between endoplasmic reticulum and mitochondria. EMBO J. 1999, 18:96-108.
    • (1999) EMBO J. , vol.18 , pp. 96-108
    • Csordas, G.1    Thomas, A.P.2    Hajnoczky, G.3
  • 64
    • 1642540210 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter is a highly selective ion channel
    • Kirichok Y., Krapivinsky G., Clapham D.E. The mitochondrial calcium uniporter is a highly selective ion channel. Nature 2004, 427:360-364.
    • (2004) Nature , vol.427 , pp. 360-364
    • Kirichok, Y.1    Krapivinsky, G.2    Clapham, D.E.3
  • 65
    • 80051936634 scopus 로고    scopus 로고
    • A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter
    • De Stefani D., Raffaello A., Teardo E., Szabo I., Rizzuto R. A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter. Nature 2011, 476:336-340.
    • (2011) Nature , vol.476 , pp. 336-340
    • De Stefani, D.1    Raffaello, A.2    Teardo, E.3    Szabo, I.4    Rizzuto, R.5
  • 66
    • 84891393224 scopus 로고    scopus 로고
    • The physiological role of mitochondrial calcium revealed by mice lacking the mitochondrial calcium uniporter
    • Pan X., Liu J., Nguyen T., et al. The physiological role of mitochondrial calcium revealed by mice lacking the mitochondrial calcium uniporter. Nat. Cell Biol. 2013, 15:1464-1472.
    • (2013) Nat. Cell Biol. , vol.15 , pp. 1464-1472
    • Pan, X.1    Liu, J.2    Nguyen, T.3
  • 71
    • 0025319665 scopus 로고
    • Role of calcium ions in regulation of mammalian intramitochondrial metabolism
    • McCormack J.G., Halestrap A.P., Denton R.M. Role of calcium ions in regulation of mammalian intramitochondrial metabolism. Physiol. Rev. 1990, 70:391-425.
    • (1990) Physiol. Rev. , vol.70 , pp. 391-425
    • McCormack, J.G.1    Halestrap, A.P.2    Denton, R.M.3
  • 72
    • 0029143569 scopus 로고
    • Decoding of cytosolic calcium oscillations in the mitochondria
    • Hajnoczky G., Robb-Gaspers L.D., Seitz M.B., Thomas A.P. Decoding of cytosolic calcium oscillations in the mitochondria. Cell 1995, 82:415-424.
    • (1995) Cell , vol.82 , pp. 415-424
    • Hajnoczky, G.1    Robb-Gaspers, L.D.2    Seitz, M.B.3    Thomas, A.P.4
  • 73
    • 3042637611 scopus 로고    scopus 로고
    • Effects of secretagogues and bile acids on mitochondrial membrane potential of pancreatic acinar cells: comparison of different modes of evaluating DeltaPsim
    • Voronina S.G., Barrow S.L., Gerasimenko O.V., Petersen O.H., Tepikin A.V. Effects of secretagogues and bile acids on mitochondrial membrane potential of pancreatic acinar cells: comparison of different modes of evaluating DeltaPsim. J. Biol. Chem. 2004, 279:27327-27338.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27327-27338
    • Voronina, S.G.1    Barrow, S.L.2    Gerasimenko, O.V.3    Petersen, O.H.4    Tepikin, A.V.5
  • 74
    • 77951695106 scopus 로고    scopus 로고
    • Dynamic changes in cytosolic and mitochondrial ATP levels in pancreatic acinar cells
    • Voronina S.G., Barrow S.L., Simpson A.W., et al. Dynamic changes in cytosolic and mitochondrial ATP levels in pancreatic acinar cells. Gastroenterology 2010, 138:1976-1987.
    • (2010) Gastroenterology , vol.138 , pp. 1976-1987
    • Voronina, S.G.1    Barrow, S.L.2    Simpson, A.W.3
  • 75
    • 23844483240 scopus 로고    scopus 로고
    • Phosphorylation of CFTR by PKA promotes binding of the regulatory domain
    • Chappe V., Irvine T., Liao J., Evagelidis A., Hanrahan J.W. Phosphorylation of CFTR by PKA promotes binding of the regulatory domain. EMBO J. 2005, 24:2730-2740.
    • (2005) EMBO J. , vol.24 , pp. 2730-2740
    • Chappe, V.1    Irvine, T.2    Liao, J.3    Evagelidis, A.4    Hanrahan, J.W.5
  • 77
    • 84874710058 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator (ABCC7) structure
    • Hunt J.F., Wang C., Ford R.C. Cystic fibrosis transmembrane conductance regulator (ABCC7) structure. Cold Spring Harb. Perspect. Med. 2013, 3:a009514.
    • (2013) Cold Spring Harb. Perspect. Med. , vol.3
    • Hunt, J.F.1    Wang, C.2    Ford, R.C.3
  • 78
    • 2342449944 scopus 로고    scopus 로고
    • Gating of CFTR by the STAS domain of SLC26 transporters
    • Ko S.B., Zeng W., Dorwart M.R., et al. Gating of CFTR by the STAS domain of SLC26 transporters. Nat. Cell Biol. 2004, 6:343-350.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 343-350
    • Ko, S.B.1    Zeng, W.2    Dorwart, M.R.3
  • 80
    • 0029066116 scopus 로고
    • CaMKII regulates the frequency-response function of hippocampal synapses for the production of both LTD and LTP
    • Mayford M., Wang J., Kandel E.R., O'Dell T.J. CaMKII regulates the frequency-response function of hippocampal synapses for the production of both LTD and LTP. Cell 1995, 81:891-904.
    • (1995) Cell , vol.81 , pp. 891-904
    • Mayford, M.1    Wang, J.2    Kandel, E.R.3    O'Dell, T.J.4
  • 81
    • 0030463470 scopus 로고    scopus 로고
    • 2+- and stimulus duration-dependent switch for hippocampal gene expression
    • 2+- and stimulus duration-dependent switch for hippocampal gene expression. Cell 1996, 87:1203-1214.
    • (1996) Cell , vol.87 , pp. 1203-1214
    • Bito, H.1    Deisseroth, K.2    Tsien, R.W.3
  • 82
    • 0033551228 scopus 로고    scopus 로고
    • Hormone-induced secretory and nuclear translocation of calmodulin: oscillations of calmodulin concentration with the nucleus as an integrator
    • Craske M., Takeo T., Gerasimenko O., et al. Hormone-induced secretory and nuclear translocation of calmodulin: oscillations of calmodulin concentration with the nucleus as an integrator. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:4426-4431.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 4426-4431
    • Craske, M.1    Takeo, T.2    Gerasimenko, O.3
  • 84
    • 84893141356 scopus 로고    scopus 로고
    • Activation of the Ano1 (TMEM16A) chloride channel by calcium is not mediated by calmodulin
    • Yu K., Zhu J., Qu Z., Cui Y.Y., Hartzell H.C. Activation of the Ano1 (TMEM16A) chloride channel by calcium is not mediated by calmodulin. J. Gen. Physiol. 2014, 143:253-267.
    • (2014) J. Gen. Physiol. , vol.143 , pp. 253-267
    • Yu, K.1    Zhu, J.2    Qu, Z.3    Cui, Y.Y.4    Hartzell, H.C.5
  • 89
    • 0030973579 scopus 로고    scopus 로고
    • Transcription factors of the NFAT family: regulation and function
    • Rao A., Luo C., Hogan P.G. Transcription factors of the NFAT family: regulation and function. Annu. Rev. Immunol. 1997, 15:707-747.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 707-747
    • Rao, A.1    Luo, C.2    Hogan, P.G.3
  • 90
    • 0036554826 scopus 로고    scopus 로고
    • Bile acids induce calcium signals in mouse pancreatic acinar cells: implications for bile-induced pancreatic pathology
    • Voronina S., Longbottom R., Sutton R., Petersen O.H., Tepikin A. Bile acids induce calcium signals in mouse pancreatic acinar cells: implications for bile-induced pancreatic pathology. J. Physiol. 2002, 540:49-55.
    • (2002) J. Physiol. , vol.540 , pp. 49-55
    • Voronina, S.1    Longbottom, R.2    Sutton, R.3    Petersen, O.H.4    Tepikin, A.5
  • 91
    • 33644872533 scopus 로고    scopus 로고
    • Fatty acid ethyl esters cause pancreatic calcium toxicity via inositol trisphosphate receptors and loss of ATP synthesis
    • Criddle D.N., Murphy J., Fistetto G., et al. Fatty acid ethyl esters cause pancreatic calcium toxicity via inositol trisphosphate receptors and loss of ATP synthesis. Gastroenterology 2006, 130:781-793.
    • (2006) Gastroenterology , vol.130 , pp. 781-793
    • Criddle, D.N.1    Murphy, J.2    Fistetto, G.3
  • 92
    • 84876787550 scopus 로고    scopus 로고
    • The epidemiology of pancreatitis and pancreatic cancer
    • Yadav D., Lowenfels A.B. The epidemiology of pancreatitis and pancreatic cancer. Gastroenterology 2013, 144:1252-1261.
    • (2013) Gastroenterology , vol.144 , pp. 1252-1261
    • Yadav, D.1    Lowenfels, A.B.2
  • 93
    • 33845994072 scopus 로고    scopus 로고
    • 2+ release from both the endoplasmic reticulum and acidic intracellular calcium stores through activation of inositol trisphosphate receptors and ryanodine receptors
    • 2+ release from both the endoplasmic reticulum and acidic intracellular calcium stores through activation of inositol trisphosphate receptors and ryanodine receptors. J. Biol. Chem. 2006, 281:40154-40163.
    • (2006) J. Biol. Chem. , vol.281 , pp. 40154-40163
    • Gerasimenko, J.V.1    Flowerdew, S.E.2    Voronina, S.G.3
  • 94
    • 12444272245 scopus 로고    scopus 로고
    • Ethanol induces fluid hypersecretion from guinea-pig pancreatic duct cells
    • Yamamoto A., Ishiguro H., Ko S.B., et al. Ethanol induces fluid hypersecretion from guinea-pig pancreatic duct cells. J. Physiol. 2003, 551:917-926.
    • (2003) J. Physiol. , vol.551 , pp. 917-926
    • Yamamoto, A.1    Ishiguro, H.2    Ko, S.B.3
  • 95
    • 84895186916 scopus 로고    scopus 로고
    • Non-oxidative ethanol metabolites induce intracellular ATP depletion and inhibit pancreatic ductal bicarbonate secretion in human pancreatic ductal epithelial cell line
    • S460-S
    • Hegyi P., Venglovecz R.Z., Wittmann V., Maleth T.J. Non-oxidative ethanol metabolites induce intracellular ATP depletion and inhibit pancreatic ductal bicarbonate secretion in human pancreatic ductal epithelial cell line. Gastroenterology 2012, 142. S460-S.
    • (2012) Gastroenterology , vol.142
    • Hegyi, P.1    Venglovecz, R.Z.2    Wittmann, V.3    Maleth, T.J.4
  • 100
    • 67349117275 scopus 로고    scopus 로고
    • What is the mitochondrial permeability transition pore?
    • Halestrap A.P. What is the mitochondrial permeability transition pore?. J. Mol. Cell. Cardiol. 2009, 46:821-831.
    • (2009) J. Mol. Cell. Cardiol. , vol.46 , pp. 821-831
    • Halestrap, A.P.1
  • 101
    • 84872006971 scopus 로고    scopus 로고
    • Where killers meet-permeabilization of the outer mitochondrial membrane during apoptosis
    • Bender T., Martinou J.C. Where killers meet-permeabilization of the outer mitochondrial membrane during apoptosis. Cold Spring Harb. Perspect. Biol. 2013, 5:a011106.
    • (2013) Cold Spring Harb. Perspect. Biol. , vol.5
    • Bender, T.1    Martinou, J.C.2
  • 102
    • 68649090703 scopus 로고    scopus 로고
    • The role of the mitochondrial permeability transition pore in heart disease
    • Halestrap A.P., Pasdois P. The role of the mitochondrial permeability transition pore in heart disease. Biochim. Biophys. Acta 2009, 1787:1402-1415.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1402-1415
    • Halestrap, A.P.1    Pasdois, P.2
  • 103
    • 68649127352 scopus 로고    scopus 로고
    • Mitochondrial calcium in health and disease
    • Halestrap A.P. Mitochondrial calcium in health and disease. Biochim. Biophys. Acta 2009, 1787:1289-1290.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1289-1290
    • Halestrap, A.P.1
  • 104
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer G., Galluzzi L., Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol. Rev. 2007, 87:99-163.
    • (2007) Physiol. Rev. , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 105
    • 33645994183 scopus 로고    scopus 로고
    • Calcium, mitochondria and reperfusion injury: a pore way to die
    • Halestrap A.P. Calcium, mitochondria and reperfusion injury: a pore way to die. Biochem. Soc. Trans. 2006, 34:232-237.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 232-237
    • Halestrap, A.P.1
  • 108
    • 84894617428 scopus 로고    scopus 로고
    • Ethanol and its non-oxidative metabolites profoundly inhibit CFTR function in pancreatic epithelial cells which is prevented by ATP supplementation
    • Epub ahead of print
    • Judak L., Hegyi P., Rakonczay Z., Maleth J., Gray M.A., Venglovecz V. Ethanol and its non-oxidative metabolites profoundly inhibit CFTR function in pancreatic epithelial cells which is prevented by ATP supplementation. Pflugers Arch. 2013, Epub ahead of print.
    • (2013) Pflugers Arch.
    • Judak, L.1    Hegyi, P.2    Rakonczay, Z.3    Maleth, J.4    Gray, M.A.5    Venglovecz, V.6
  • 109
    • 84893856723 scopus 로고    scopus 로고
    • The interactive roles of zinc and calcium in mitochondrial dysfunction and neurodegeneration
    • Pivovarova N.B., Stanika R.I., Kazanina G., Villanueva I., Andrews S.B. The interactive roles of zinc and calcium in mitochondrial dysfunction and neurodegeneration. J. Neurochem. 2013, 128:592-602.
    • (2013) J. Neurochem. , vol.128 , pp. 592-602
    • Pivovarova, N.B.1    Stanika, R.I.2    Kazanina, G.3    Villanueva, I.4    Andrews, S.B.5
  • 110
    • 77951251848 scopus 로고    scopus 로고
    • Calcium signaling and amyloid toxicity in Alzheimer disease
    • Demuro A., Parker I., Stutzmann G.E. Calcium signaling and amyloid toxicity in Alzheimer disease. J. Biol. Chem. 2010, 285:12463-12468.
    • (2010) J. Biol. Chem. , vol.285 , pp. 12463-12468
    • Demuro, A.1    Parker, I.2    Stutzmann, G.E.3
  • 111
    • 84877575360 scopus 로고    scopus 로고
    • Type 2 ryanodine receptor: a novel therapeutic target in myocardial ischemia/reperfusion
    • Fauconnier J., Roberge S., Saint N., Lacampagne A. Type 2 ryanodine receptor: a novel therapeutic target in myocardial ischemia/reperfusion. Pharmacol. Ther. 2013, 138:323-332.
    • (2013) Pharmacol. Ther. , vol.138 , pp. 323-332
    • Fauconnier, J.1    Roberge, S.2    Saint, N.3    Lacampagne, A.4
  • 114
    • 70349435370 scopus 로고    scopus 로고
    • 2+ influx and the severity of acute pancreatitis
    • 2+ influx and the severity of acute pancreatitis. Gastroenterology 2009, 137:1509-1517.
    • (2009) Gastroenterology , vol.137 , pp. 1509-1517
    • Kim, M.S.1    Hong, J.H.2    Li, Q.3


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