메뉴 건너뛰기




Volumn 22, Issue 1, 2008, Pages 3-15

New advances in pancreatic cell physiology and pathophysiology

Author keywords

acinar cell; apoptosis; Ca2+; cathepsin B; chymotrypsin C; exocytosis; necrosis; protease activation; SPINK1; trypsinogen

Indexed keywords

CALCIUM ION; CATHEPSIN B; CHOLECYSTOKININ; CHYMOTRYPSIN; CHYMOTRYPSIN C; ENZYME PRECURSOR; PROTEINASE; PROTEINASE ACTIVATED RECEPTOR 2; SERINE PROTEINASE INHIBITOR; SERINE PROTEINASE INHIBITOR KAZAL TYPE 1; TRYPSIN; UNCLASSIFIED DRUG;

EID: 38149058901     PISSN: 15216918     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpg.2007.10.017     Document Type: Article
Times cited : (23)

References (60)
  • 1
    • 33846813845 scopus 로고    scopus 로고
    • How does cholecystokinin stimulate exocrine pancreatic secretion? From birds, rodents, to humans
    • Wang B.J., and Cui Z.J. How does cholecystokinin stimulate exocrine pancreatic secretion? From birds, rodents, to humans. Am J Physiol Regul Integr Comp Physiol 292 2 (2007 Feb) R666-R678
    • (2007) Am J Physiol Regul Integr Comp Physiol , vol.292 , Issue.2
    • Wang, B.J.1    Cui, Z.J.2
  • 2
    • 19444363845 scopus 로고    scopus 로고
    • Cholinergic stimulation of amylase secretion from pancreatic acinar cells studied with muscarinic acetylcholine receptor mutant mice
    • Gautam D., Han S.J., Heard T.S., et al. Cholinergic stimulation of amylase secretion from pancreatic acinar cells studied with muscarinic acetylcholine receptor mutant mice. J Pharmacol Exp Therap 313 3 (2005 Jun) 995-1002
    • (2005) J Pharmacol Exp Therap , vol.313 , Issue.3 , pp. 995-1002
    • Gautam, D.1    Han, S.J.2    Heard, T.S.3
  • 3
    • 0020104379 scopus 로고
    • Relationship of cholecystokinin receptor binding to regulation of biological functions in pancreatic acini
    • Sankaran H., Goldfine I.D., Bailey A., et al. Relationship of cholecystokinin receptor binding to regulation of biological functions in pancreatic acini. Am J Physiol 242 3 (1982 Mar) G250-G257
    • (1982) Am J Physiol , vol.242 , Issue.3
    • Sankaran, H.1    Goldfine, I.D.2    Bailey, A.3
  • 4
    • 0034874237 scopus 로고    scopus 로고
    • The cholecystokinin analogues JMV-180 and CCK-8 stimulate phospholipase C through the same binding site of CCK(A) receptor in rat pancreatic acini
    • Sarri E., Ramos B., Salido G.M., et al. The cholecystokinin analogues JMV-180 and CCK-8 stimulate phospholipase C through the same binding site of CCK(A) receptor in rat pancreatic acini. Br J Pharmacol 133 8 (2001 Aug) 1227-1234
    • (2001) Br J Pharmacol , vol.133 , Issue.8 , pp. 1227-1234
    • Sarri, E.1    Ramos, B.2    Salido, G.M.3
  • 5
    • 0035210964 scopus 로고    scopus 로고
    • Human pancreatic acinar cells lack functional responses to cholecystokinin and gastrin
    • Ji B., Bi Y., Simeone D., et al. Human pancreatic acinar cells lack functional responses to cholecystokinin and gastrin. Gastroenterology 121 6 (2001 Dec) 1380-1390
    • (2001) Gastroenterology , vol.121 , Issue.6 , pp. 1380-1390
    • Ji, B.1    Bi, Y.2    Simeone, D.3
  • 6
    • 0036971069 scopus 로고    scopus 로고
    • Human pancreatic acinar cells do not respond to cholecystokinin
    • Ji B., Bi Y., Simeone D., et al. Human pancreatic acinar cells do not respond to cholecystokinin. Pharmacol Toxicol 91 6 (2002 Dec) 327-332
    • (2002) Pharmacol Toxicol , vol.91 , Issue.6 , pp. 327-332
    • Ji, B.1    Bi, Y.2    Simeone, D.3
  • 7
    • 27644515221 scopus 로고    scopus 로고
    • Advanced qRT-PCR technology allows detection of the cholecystokinin 1 receptor (CCK1R) expression in human pancreas
    • Galindo J., Jones N., Powell G.L., et al. Advanced qRT-PCR technology allows detection of the cholecystokinin 1 receptor (CCK1R) expression in human pancreas. Pancreas 31 4 (2005 Nov) 325-331
    • (2005) Pancreas , vol.31 , Issue.4 , pp. 325-331
    • Galindo, J.1    Jones, N.2    Powell, G.L.3
  • 8
    • 4444354589 scopus 로고    scopus 로고
    • New insights into neurohormonal regulation of pancreatic secretion
    • Owyang C., and Logsdon C.D. New insights into neurohormonal regulation of pancreatic secretion. Gastroenterology 127 3 (2004 Sep) 957-969
    • (2004) Gastroenterology , vol.127 , Issue.3 , pp. 957-969
    • Owyang, C.1    Logsdon, C.D.2
  • 9
    • 0037019916 scopus 로고    scopus 로고
    • Protease-activated receptor-2 (PAR-2) in the pancreas and parotid gland: immunolocalization and involvement of nitric oxide in the evoked amylase secretion
    • Kawabata A., Kuroda R., Nishida M., et al. Protease-activated receptor-2 (PAR-2) in the pancreas and parotid gland: immunolocalization and involvement of nitric oxide in the evoked amylase secretion. Life Sci 71 20 (2002 Oct 4) 2435-2446
    • (2002) Life Sci , vol.71 , Issue.20 , pp. 2435-2446
    • Kawabata, A.1    Kuroda, R.2    Nishida, M.3
  • 10
    • 0032896792 scopus 로고    scopus 로고
    • Trypsin activates pancreatic duct epithelial cell ion channels through proteinase-activated receptor-2
    • Nguyen T.D., Moody M.W., Steinhoff M., et al. Trypsin activates pancreatic duct epithelial cell ion channels through proteinase-activated receptor-2. J Clin Invest 103 2 (1999 Jan) 261-269
    • (1999) J Clin Invest , vol.103 , Issue.2 , pp. 261-269
    • Nguyen, T.D.1    Moody, M.W.2    Steinhoff, M.3
  • 11
    • 12344258778 scopus 로고    scopus 로고
    • Protection against acute pancreatitis by activation of protease-activated receptor-2
    • Sharma A., Tao X., Gopal A., et al. Protection against acute pancreatitis by activation of protease-activated receptor-2. Am J Physiol 288 2 (2005 Feb) G388-G395
    • (2005) Am J Physiol , vol.288 , Issue.2
    • Sharma, A.1    Tao, X.2    Gopal, A.3
  • 12
    • 34347232392 scopus 로고    scopus 로고
    • Protease-activated receptor-2 protects against pancreatitis by stimulating exocrine secretion
    • Singh V.P., Bhagat L., Navina S., et al. Protease-activated receptor-2 protects against pancreatitis by stimulating exocrine secretion. Gut 56 7 (2007 Jul) 958-964
    • (2007) Gut , vol.56 , Issue.7 , pp. 958-964
    • Singh, V.P.1    Bhagat, L.2    Navina, S.3
  • 13
    • 25444486387 scopus 로고    scopus 로고
    • Calcium dependence of proteinase-activated receptor 2 and cholecystokinin-mediated amylase secretion from pancreatic acini
    • Sharma A., Tao X., Gopal A., et al. Calcium dependence of proteinase-activated receptor 2 and cholecystokinin-mediated amylase secretion from pancreatic acini. Am J Physiol 289 4 (2005 Oct) G686-G695
    • (2005) Am J Physiol , vol.289 , Issue.4
    • Sharma, A.1    Tao, X.2    Gopal, A.3
  • 14
    • 0036878805 scopus 로고    scopus 로고
    • The distribution of the endoplasmic reticulum in living pancreatic acinar cells
    • Gerasimenko O.V., Gerasimenko J.V., Rizzuto R.R., et al. The distribution of the endoplasmic reticulum in living pancreatic acinar cells. Cell Calcium 32 5-6 (2002 Nov-Dec) 261-268
    • (2002) Cell Calcium , vol.32 , Issue.5-6 , pp. 261-268
    • Gerasimenko, O.V.1    Gerasimenko, J.V.2    Rizzuto, R.R.3
  • 15
    • 32244432183 scopus 로고    scopus 로고
    • NAADP, cADPR and IP3 all release Ca2+ from the endoplasmic reticulum and an acidic store in the secretory granule area
    • Gerasimenko J.V., Sherwood M., Tepikin A.V., et al. NAADP, cADPR and IP3 all release Ca2+ from the endoplasmic reticulum and an acidic store in the secretory granule area. J Cell Sci 119 Pt 2 (2006 Jan 15) 226-238
    • (2006) J Cell Sci , vol.119 , Issue.PART 2 , pp. 226-238
    • Gerasimenko, J.V.1    Sherwood, M.2    Tepikin, A.V.3
  • 16
    • 12544259102 scopus 로고    scopus 로고
    • The plasma membrane Q-SNARE syntaxin 2 enters the zymogen granule membrane during exocytosis in the pancreatic acinar cell
    • Pickett J.A., Thorn P., and Edwardson J.M. The plasma membrane Q-SNARE syntaxin 2 enters the zymogen granule membrane during exocytosis in the pancreatic acinar cell. J Biol Chem 280 2 (2005 Jan 14) 1506-1511
    • (2005) J Biol Chem , vol.280 , Issue.2 , pp. 1506-1511
    • Pickett, J.A.1    Thorn, P.2    Edwardson, J.M.3
  • 17
    • 4544227227 scopus 로고    scopus 로고
    • A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar cells
    • Wang C.C., Ng C.P., Lu L., et al. A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar cells. Dev Cell 7 3 (2004 Sep) 359-371
    • (2004) Dev Cell , vol.7 , Issue.3 , pp. 359-371
    • Wang, C.C.1    Ng, C.P.2    Lu, L.3
  • 18
    • 14944341050 scopus 로고    scopus 로고
    • Two phases of zymogen granule lifetime in mouse pancreas: ghost granules linger after exocytosis of contents
    • Thorn P., and Parker I. Two phases of zymogen granule lifetime in mouse pancreas: ghost granules linger after exocytosis of contents. J Physiol 563 Pt 2 (2005 Mar 1) 433-442
    • (2005) J Physiol , vol.563 , Issue.PART 2 , pp. 433-442
    • Thorn, P.1    Parker, I.2
  • 19
    • 0028889137 scopus 로고
    • Actin filament disassembly is a sufficient final trigger for exocytosis in nonexcitable cells
    • Muallem S., Kwiatkowska K., Xu X., et al. Actin filament disassembly is a sufficient final trigger for exocytosis in nonexcitable cells. J Cell Biol 128 4 (1995 Feb) 589-598
    • (1995) J Cell Biol , vol.128 , Issue.4 , pp. 589-598
    • Muallem, S.1    Kwiatkowska, K.2    Xu, X.3
  • 20
    • 24044440401 scopus 로고    scopus 로고
    • Rho and Rac promote acinar morphological changes, actin reorganization, and amylase secretion
    • Bi Y., Page S.L., and Williams J.A. Rho and Rac promote acinar morphological changes, actin reorganization, and amylase secretion. Am J Physiol 289 3 (2005 Sep) G561-G570
    • (2005) Am J Physiol , vol.289 , Issue.3
    • Bi, Y.1    Page, S.L.2    Williams, J.A.3
  • 21
    • 21144439797 scopus 로고    scopus 로고
    • A role for Rho and Rac in secretagogue-induced amylase release by pancreatic acini
    • Bi Y., and Williams J.A. A role for Rho and Rac in secretagogue-induced amylase release by pancreatic acini. Am J Physiol Cell Physiol 289 1 (2005 Jul) C22-C32
    • (2005) Am J Physiol Cell Physiol , vol.289 , Issue.1
    • Bi, Y.1    Williams, J.A.2
  • 22
    • 0031789134 scopus 로고    scopus 로고
    • The actin-myosin cytoskeleton mediates reversible agonist-induced membrane blebbing
    • Torgerson R.R., and McNiven M.A. The actin-myosin cytoskeleton mediates reversible agonist-induced membrane blebbing. J Cell Sci 111 Pt 19 (1998 Oct) 2911-2922
    • (1998) J Cell Sci , vol.111 , Issue.PART 19 , pp. 2911-2922
    • Torgerson, R.R.1    McNiven, M.A.2
  • 23
    • 23044493186 scopus 로고    scopus 로고
    • Regulation of zymogen granule exocytosis by Ca2+, cAMP, and PKC in pancreatic acinar cells
    • Lee M., Chung S., Uhm D.Y., et al. Regulation of zymogen granule exocytosis by Ca2+, cAMP, and PKC in pancreatic acinar cells. Biochem Biophys Res Commun 334 4 (2005 Sep 9) 1241-1247
    • (2005) Biochem Biophys Res Commun , vol.334 , Issue.4 , pp. 1241-1247
    • Lee, M.1    Chung, S.2    Uhm, D.Y.3
  • 24
    • 0033887738 scopus 로고    scopus 로고
    • The role of intracellular calcium signaling in premature protease activation and the onset of pancreatitis
    • Kruger B., Albrecht E., and Lerch M.M. The role of intracellular calcium signaling in premature protease activation and the onset of pancreatitis. Am J Pathol 157 1 (2000 Jul) 43-50
    • (2000) Am J Pathol , vol.157 , Issue.1 , pp. 43-50
    • Kruger, B.1    Albrecht, E.2    Lerch, M.M.3
  • 25
    • 0038660678 scopus 로고    scopus 로고
    • Early changes in pancreatic acinar cell calcium signaling after pancreatic duct obstruction
    • Mooren F., Hlouschek V., Finkes T., et al. Early changes in pancreatic acinar cell calcium signaling after pancreatic duct obstruction. J Biol Chem 278 11 (2003 Mar 14) 9361-9369
    • (2003) J Biol Chem , vol.278 , Issue.11 , pp. 9361-9369
    • Mooren, F.1    Hlouschek, V.2    Finkes, T.3
  • 26
    • 0035082040 scopus 로고    scopus 로고
    • Calcium-magnesium interactions in pancreatic acinar cells
    • Mooren F.C., Turi S., Gunzel D., et al. Calcium-magnesium interactions in pancreatic acinar cells. Faseb J 15 3 (2001 Mar) 659-672
    • (2001) Faseb J , vol.15 , Issue.3 , pp. 659-672
    • Mooren, F.C.1    Turi, S.2    Gunzel, D.3
  • 27
    • 26444486943 scopus 로고    scopus 로고
    • The ryanodine receptor mediates early zymogen activation in pancreatitis
    • Husain S.Z., Prasad P., Grant W.M., et al. The ryanodine receptor mediates early zymogen activation in pancreatitis. Proceed Natl Acad Sci U S A 102 40 (2005 Oct 4) 14386-14391
    • (2005) Proceed Natl Acad Sci U S A , vol.102 , Issue.40 , pp. 14386-14391
    • Husain, S.Z.1    Prasad, P.2    Grant, W.M.3
  • 28
    • 12344302086 scopus 로고    scopus 로고
    • Effects of increased intracellular cAMP on carbachol-stimulated zymogen activation, secretion, and injury in the pancreatic acinar cell
    • Chaudhuri A., Kolodecik T.R., and Gorelick F.S. Effects of increased intracellular cAMP on carbachol-stimulated zymogen activation, secretion, and injury in the pancreatic acinar cell. Am J Physiol 288 2 (2005 Feb) G235-G243
    • (2005) Am J Physiol , vol.288 , Issue.2
    • Chaudhuri, A.1    Kolodecik, T.R.2    Gorelick, F.S.3
  • 29
    • 0031867966 scopus 로고    scopus 로고
    • Intra-acinar cell activation of trypsinogen during caerulein-induced pancreatitis in rats
    • Hofbauer B., Saluja A.K., Lerch M.M., et al. Intra-acinar cell activation of trypsinogen during caerulein-induced pancreatitis in rats. Am J Physiol 275 2 Pt 1 (1998 Aug) G352-G362
    • (1998) Am J Physiol , vol.275 , Issue.2 PART 1
    • Hofbauer, B.1    Saluja, A.K.2    Lerch, M.M.3
  • 30
    • 0344589358 scopus 로고    scopus 로고
    • Direct detection of premature protease activation in living pancreatic acinar cells
    • Kruger B., Lerch M.M., and Tessenow W. Direct detection of premature protease activation in living pancreatic acinar cells. Lab Invest J Tech Methods Pathol 78 6 (1998 Jun) 763-764
    • (1998) Lab Invest J Tech Methods Pathol , vol.78 , Issue.6 , pp. 763-764
    • Kruger, B.1    Lerch, M.M.2    Tessenow, W.3
  • 31
    • 0023125973 scopus 로고
    • The cell biology of experimental pancreatitis
    • Steer M.L., and Meldolesi J. The cell biology of experimental pancreatitis. New Engl J Med 316 3 (1987 Jan 15) 144-150
    • (1987) New Engl J Med , vol.316 , Issue.3 , pp. 144-150
    • Steer, M.L.1    Meldolesi, J.2
  • 32
    • 0037077262 scopus 로고    scopus 로고
    • Presence of cathepsin B in the human pancreatic secretory pathway and its role in trypsinogen activation during hereditary pancreatitis
    • Kukor Z., Mayerle J., Kruger B., et al. Presence of cathepsin B in the human pancreatic secretory pathway and its role in trypsinogen activation during hereditary pancreatitis. J Biol Chem 277 24 (2002 Jun 14) 21389-21396
    • (2002) J Biol Chem , vol.277 , Issue.24 , pp. 21389-21396
    • Kukor, Z.1    Mayerle, J.2    Kruger, B.3
  • 33
    • 0033795691 scopus 로고    scopus 로고
    • Role of cathepsin B in intracellular trypsinogen activation and the onset of acute pancreatitis
    • Halangk W., Lerch M.M., Brandt-Nedelev B., et al. Role of cathepsin B in intracellular trypsinogen activation and the onset of acute pancreatitis. J Clin Invest 106 6 (2000 Sep) 773-781
    • (2000) J Clin Invest , vol.106 , Issue.6 , pp. 773-781
    • Halangk, W.1    Lerch, M.M.2    Brandt-Nedelev, B.3
  • 34
    • 33747773624 scopus 로고    scopus 로고
    • Association of cathepsin B gene polymorphisms with tropical calcific pancreatitis
    • Mahurkar S., Idris M.M., Reddy D.N., et al. Association of cathepsin B gene polymorphisms with tropical calcific pancreatitis. Gut 55 9 (2006 Sep) 1270-1275
    • (2006) Gut , vol.55 , Issue.9 , pp. 1270-1275
    • Mahurkar, S.1    Idris, M.M.2    Reddy, D.N.3
  • 35
    • 34548130842 scopus 로고    scopus 로고
    • Cathepsin B gene polymorphism Val26 is not associated with idiopathic chronic pancreatitis in Western patients
    • Weiss F.U., Behn C.O., Simon P., et al. Cathepsin B gene polymorphism Val26 is not associated with idiopathic chronic pancreatitis in Western patients. Gut 56 9 (2007)
    • (2007) Gut , vol.56 , Issue.9
    • Weiss, F.U.1    Behn, C.O.2    Simon, P.3
  • 36
    • 33747766204 scopus 로고    scopus 로고
    • Human pancreatitis and the role of cathepsin B
    • Lerch M.M., and Halangk W. Human pancreatitis and the role of cathepsin B. Gut 55 9 (2006 Sep) 1228-1230
    • (2006) Gut , vol.55 , Issue.9 , pp. 1228-1230
    • Lerch, M.M.1    Halangk, W.2
  • 37
    • 0036857490 scopus 로고    scopus 로고
    • Functional analysis of recombinant pancreatic secretory trypsin inhibitor protein with amino-acid substitution
    • Kuwata K., Hirota M., Shimizu H., et al. Functional analysis of recombinant pancreatic secretory trypsin inhibitor protein with amino-acid substitution. J Gastroenterol 37 11 (2002) 928-934
    • (2002) J Gastroenterol , vol.37 , Issue.11 , pp. 928-934
    • Kuwata, K.1    Hirota, M.2    Shimizu, H.3
  • 38
    • 34248158166 scopus 로고    scopus 로고
    • N34S mutation in the SPINK1 gene is not associated with alternative splicing
    • Masamune A., Kume K., Takagi Y., et al. N34S mutation in the SPINK1 gene is not associated with alternative splicing. Pancreas 34 4 (2007 May) 423-428
    • (2007) Pancreas , vol.34 , Issue.4 , pp. 423-428
    • Masamune, A.1    Kume, K.2    Takagi, Y.3
  • 39
    • 23244447063 scopus 로고    scopus 로고
    • Autophagic cell death of pancreatic acinar cells in serine protease inhibitor Kazal type 3-deficient mice
    • Ohmuraya M., Hirota M., Araki M., et al. Autophagic cell death of pancreatic acinar cells in serine protease inhibitor Kazal type 3-deficient mice. Gastroenterology 129 2 (2005 Aug) 696-705
    • (2005) Gastroenterology , vol.129 , Issue.2 , pp. 696-705
    • Ohmuraya, M.1    Hirota, M.2    Araki, M.3
  • 40
    • 33745699252 scopus 로고    scopus 로고
    • Enhanced trypsin activity in pancreatic acinar cells deficient for serine protease inhibitor kazal type 3
    • Ohmuraya M., Hirota M., Araki K., et al. Enhanced trypsin activity in pancreatic acinar cells deficient for serine protease inhibitor kazal type 3. Pancreas 33 1 (2006 Jul) 104-106
    • (2006) Pancreas , vol.33 , Issue.1 , pp. 104-106
    • Ohmuraya, M.1    Hirota, M.2    Araki, K.3
  • 41
    • 34948901262 scopus 로고    scopus 로고
    • Missense mutations in pancreatic secretory trypsin inhibitor (SPINK1) cause intracellular retention and degradation
    • Kiraly O., Wartmann T., and Sahin-Toth M. Missense mutations in pancreatic secretory trypsin inhibitor (SPINK1) cause intracellular retention and degradation. Gut (2007 May 24)
    • (2007) Gut
    • Kiraly, O.1    Wartmann, T.2    Sahin-Toth, M.3
  • 42
    • 34548186235 scopus 로고    scopus 로고
    • Functional analysis of pancreatitis-associated missense mutations in the pancreatic secretory trypsin inhibitor (SPINK1) gene
    • Boulling A., Le Marechal C., Trouve P., et al. Functional analysis of pancreatitis-associated missense mutations in the pancreatic secretory trypsin inhibitor (SPINK1) gene. Eur J Hum Genet 15 9 (2007 Sep) 936-942
    • (2007) Eur J Hum Genet , vol.15 , Issue.9 , pp. 936-942
    • Boulling, A.1    Le Marechal, C.2    Trouve, P.3
  • 43
    • 34247256373 scopus 로고    scopus 로고
    • Signal peptide variants that impair secretion of pancreatic secretory trypsin inhibitor (SPINK1) cause autosomal dominant hereditary pancreatitis
    • Kiraly O., Boulling A., Witt H., et al. Signal peptide variants that impair secretion of pancreatic secretory trypsin inhibitor (SPINK1) cause autosomal dominant hereditary pancreatitis. Hum Mutat 28 5 (2007 May) 469-476
    • (2007) Hum Mutat , vol.28 , Issue.5 , pp. 469-476
    • Kiraly, O.1    Boulling, A.2    Witt, H.3
  • 44
    • 0037387886 scopus 로고    scopus 로고
    • SPINK1 mutations and phenotypic expression in patients with pancreatitis associated with trypsinogen mutations
    • Weiss F.U., Simon P., Witt H., et al. SPINK1 mutations and phenotypic expression in patients with pancreatitis associated with trypsinogen mutations. J Med Genet 40 4 (2003 Apr) e40
    • (2003) J Med Genet , vol.40 , Issue.4
    • Weiss, F.U.1    Simon, P.2    Witt, H.3
  • 45
    • 33845664588 scopus 로고    scopus 로고
    • A mouse model of hereditary pancreatitis generated by transgenic expression of R122H trypsinogen
    • Archer H., Jura N., Keller J., et al. A mouse model of hereditary pancreatitis generated by transgenic expression of R122H trypsinogen. Gastroenterology 131 6 (2006 Dec) 1844-1855
    • (2006) Gastroenterology , vol.131 , Issue.6 , pp. 1844-1855
    • Archer, H.1    Jura, N.2    Keller, J.3
  • 46
    • 33751233226 scopus 로고    scopus 로고
    • Characterisation of a transgenic mouse expressing R122H human cationic trypsinogen
    • Selig L., Sack U., Gaiser S., et al. Characterisation of a transgenic mouse expressing R122H human cationic trypsinogen. BMC Gastroenterol 6 (2006) 30
    • (2006) BMC Gastroenterol , vol.6 , pp. 30
    • Selig, L.1    Sack, U.2    Gaiser, S.3
  • 47
    • 18544365392 scopus 로고    scopus 로고
    • Hereditary pancreatitis caused by a novel PRSS1 mutation (Arg-122 → Cys) that alters autoactivation and autodegradation of cationic trypsinogen
    • Simon P., Weiss F.U., Sahin-Toth M., et al. Hereditary pancreatitis caused by a novel PRSS1 mutation (Arg-122 → Cys) that alters autoactivation and autodegradation of cationic trypsinogen. J Biol Chem 277 7 (2002 Feb 15) 5404-5410
    • (2002) J Biol Chem , vol.277 , Issue.7 , pp. 5404-5410
    • Simon, P.1    Weiss, F.U.2    Sahin-Toth, M.3
  • 48
    • 9144233558 scopus 로고    scopus 로고
    • Interaction between trypsinogen isoforms in genetically determined pancreatitis: mutation E79K in cationic trypsin (PRSS1) causes increased transactivation of anionic trypsinogen (PRSS2)
    • Teich N., Le Marechal C., Kukor Z., et al. Interaction between trypsinogen isoforms in genetically determined pancreatitis: mutation E79K in cationic trypsin (PRSS1) causes increased transactivation of anionic trypsinogen (PRSS2). Hum Mutat 23 1 (2004 Jan) 22-31
    • (2004) Hum Mutat , vol.23 , Issue.1 , pp. 22-31
    • Teich, N.1    Le Marechal, C.2    Kukor, Z.3
  • 49
    • 0036085976 scopus 로고    scopus 로고
    • Trypsin activity is not involved in premature, intrapancreatic trypsinogen activation
    • Halangk W., Kruger B., Ruthenburger M., et al. Trypsin activity is not involved in premature, intrapancreatic trypsinogen activation. Am J Physiol 282 2 (2002 Feb) G367-G374
    • (2002) Am J Physiol , vol.282 , Issue.2
    • Halangk, W.1    Kruger, B.2    Ruthenburger, M.3
  • 50
    • 0023879411 scopus 로고
    • A possible zymogen self-destruct mechanism preventing pancreatic autodigestion
    • Rinderknecht H., Adham N.F., Renner I.G., et al. A possible zymogen self-destruct mechanism preventing pancreatic autodigestion. Int J Pancreatol 3 1 (1988 Jan-Feb) 33-44
    • (1988) Int J Pancreatol , vol.3 , Issue.1 , pp. 33-44
    • Rinderknecht, H.1    Adham, N.F.2    Renner, I.G.3
  • 51
    • 10144246566 scopus 로고    scopus 로고
    • Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene
    • Whitcomb D.C., Gorry M.C., Preston R.A., et al. Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene. Nat Genet 14 2 (1996 Oct) 141-145
    • (1996) Nat Genet , vol.14 , Issue.2 , pp. 141-145
    • Whitcomb, D.C.1    Gorry, M.C.2    Preston, R.A.3
  • 52
    • 0038029879 scopus 로고    scopus 로고
    • Human anionic trypsinogen: properties of autocatalytic activation and degradation and implications in pancreatic diseases
    • Kukor Z., Toth M., and Sahin-Toth M. Human anionic trypsinogen: properties of autocatalytic activation and degradation and implications in pancreatic diseases. Eur J Biochem/FEBS 270 9 (2003 May) 2047-2058
    • (2003) Eur J Biochem/FEBS , vol.270 , Issue.9 , pp. 2047-2058
    • Kukor, Z.1    Toth, M.2    Sahin-Toth, M.3
  • 53
    • 0034687560 scopus 로고    scopus 로고
    • Gain-of-function mutations associated with hereditary pancreatitis enhance autoactivation of human cationic trypsinogen
    • Sahin-Toth M., and Toth M. Gain-of-function mutations associated with hereditary pancreatitis enhance autoactivation of human cationic trypsinogen. Biochem Biophys Res Commun 278 2 (2000 Nov 19) 286-289
    • (2000) Biochem Biophys Res Commun , vol.278 , Issue.2 , pp. 286-289
    • Sahin-Toth, M.1    Toth, M.2
  • 54
    • 34547437254 scopus 로고    scopus 로고
    • Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: identity with Rinderknecht's enzyme Y
    • Szmola R., and Sahin-Toth M. Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: identity with Rinderknecht's enzyme Y. Proceed Natl Acad Sci U S A 104 27 (2007 Jul 3) 11227-11232
    • (2007) Proceed Natl Acad Sci U S A , vol.104 , Issue.27 , pp. 11227-11232
    • Szmola, R.1    Sahin-Toth, M.2
  • 55
    • 34248363193 scopus 로고    scopus 로고
    • Activation of trypsinogen in large endocytic vacuoles of pancreatic acinar cells
    • Sherwood M.W., Prior I.A., Voronina S.G., et al. Activation of trypsinogen in large endocytic vacuoles of pancreatic acinar cells. Proc Natl Acad Sci U S A 104 13 (2007 Mar 27) 5674-5679
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.13 , pp. 5674-5679
    • Sherwood, M.W.1    Prior, I.A.2    Voronina, S.G.3
  • 56
    • 33645640921 scopus 로고    scopus 로고
    • Cell death in pancreatitis: caspases protect from necrotizing pancreatitis
    • Mareninova O.A., Sung K.F., Hong P., et al. Cell death in pancreatitis: caspases protect from necrotizing pancreatitis. J Biol Chem 281 6 (2006 Feb 10) 3370-3381
    • (2006) J Biol Chem , vol.281 , Issue.6 , pp. 3370-3381
    • Mareninova, O.A.1    Sung, K.F.2    Hong, P.3
  • 57
    • 33646830314 scopus 로고    scopus 로고
    • Ethanol feeding alters death signaling in the pancreas
    • Wang Y.L., Hu R., Lugea A., et al. Ethanol feeding alters death signaling in the pancreas. Pancreas 32 4 (2006 May) 351-359
    • (2006) Pancreas , vol.32 , Issue.4 , pp. 351-359
    • Wang, Y.L.1    Hu, R.2    Lugea, A.3
  • 58
    • 0032546484 scopus 로고    scopus 로고
    • Induction of apoptosis in pancreatic acinar cells reduces the severity of acute pancreatitis
    • Bhatia M., Wallig M.A., Hofbauer B., et al. Induction of apoptosis in pancreatic acinar cells reduces the severity of acute pancreatitis. Biochem Biophys Res Commun 246 2 (1998 May 19) 476-483
    • (1998) Biochem Biophys Res Commun , vol.246 , Issue.2 , pp. 476-483
    • Bhatia, M.1    Wallig, M.A.2    Hofbauer, B.3
  • 59
    • 33745798205 scopus 로고    scopus 로고
    • Crambene induces pancreatic acinar cell apoptosis via the activation of mitochondrial pathway
    • Cao Y., Adhikari S., Ang A.D., et al. Crambene induces pancreatic acinar cell apoptosis via the activation of mitochondrial pathway. Am J Physiol 291 1 (2006 Jul) G95-G101
    • (2006) Am J Physiol , vol.291 , Issue.1
    • Cao, Y.1    Adhikari, S.2    Ang, A.D.3
  • 60
    • 34250833401 scopus 로고    scopus 로고
    • Induction of apoptosis by crambene protects mice against acute pancreatitis via anti-inflammatory pathways
    • Cao Y., Adhikari S., Clement M.V., et al. Induction of apoptosis by crambene protects mice against acute pancreatitis via anti-inflammatory pathways. Am J Pathol 170 5 (2007 May) 1521-1534
    • (2007) Am J Pathol , vol.170 , Issue.5 , pp. 1521-1534
    • Cao, Y.1    Adhikari, S.2    Clement, M.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.