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Volumn 286, Issue 6 49-6, 2004, Pages

Dysregulation of the calpain-calpastatin system plays a role in the development of cerulein-induced acute pancreatitis in the rat

Author keywords

Actin microfilaments; Cytoprotection; Protease activation; Z Val Phe methyl ester

Indexed keywords

AMYLASE; BENZYLOXYCARBONYLVALYLPHENYLALANINE METHYL ESTER; CALCIUM IONOPHORE; CALPAIN; CALPASTATIN; CERULETIDE; CYSTEINE PROTEINASE; PEPTIDE DERIVATIVE; UNCLASSIFIED DRUG; CALCIUM BINDING PROTEIN; DIPEPTIDE; M CALPAIN; M-CALPAIN; MU CALPAIN; MU-CALPAIN; N BENZYLOXYCARBONYL VALYL PHENYLALANINE METHYL ESTER; N-BENZYLOXYCARBONYL-VALYL-PHENYLALANINE METHYL ESTER;

EID: 2642561967     PISSN: 01931857     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpgi.00406.2003     Document Type: Article
Times cited : (19)

References (47)
  • 1
    • 0025974840 scopus 로고
    • Investigation of the role of calpain as a stimulus-response mediator in human platelets using new synthetic inhibitors
    • Anagli J, Hagmann J, and Shaw E. Investigation of the role of calpain as a stimulus-response mediator in human platelets using new synthetic inhibitors. Biochem J 274: 497-502, 1991.
    • (1991) Biochem J , vol.274 , pp. 497-502
    • Anagli, J.1    Hagmann, J.2    Shaw, E.3
  • 4
    • 0029837867 scopus 로고    scopus 로고
    • Impairment of intracellular calcium homeostasis in the exocrine pancreas after caerulein-induced acute pancreatitis in the rat
    • Bragado MJ, San Roman I, Gonzalez A, Garcia LJ, Lopez MA, and Calvo JJ. Impairment of intracellular calcium homeostasis in the exocrine pancreas after caerulein-induced acute pancreatitis in the rat. Clin Sci (Colch) 91: 365-369, 1996.
    • (1996) Clin Sci (Colch) , vol.91 , pp. 365-369
    • Bragado, M.J.1    San Roman, I.2    Gonzalez, A.3    Garcia, L.J.4    Lopez, M.A.5    Calvo, J.J.6
  • 5
    • 0032543442 scopus 로고    scopus 로고
    • Breakthroughs and views. Calpain: A protease in search and function?
    • Carafoli E and Molinari M. Breakthroughs and views. Calpain: a protease in search and function? Biochem Biophys Res Commun 247: 193-203, 1998.
    • (1998) Biochem Biophys Res Commun , vol.247 , pp. 193-203
    • Carafoli, E.1    Molinari, M.2
  • 6
    • 0025831476 scopus 로고
    • Calcium-activated neutral protease (calpain) system: Structure, function, and regulation
    • Croall DE and De Martino GN. Calcium-activated neutral protease (calpain) system: structure, function, and regulation. Physiol Rev 71: 813-847, 1991.
    • (1991) Physiol Rev , vol.71 , pp. 813-847
    • Croall, D.E.1    De Martino, G.N.2
  • 9
    • 0025925367 scopus 로고
    • 2-induced alterations of actin filaments in cultured primary rat proximal tubule epithelial cells labelled with fluorescein phalloidine
    • 2-induced alterations of actin filaments in cultured primary rat proximal tubule epithelial cells labelled with fluorescein phalloidine. Cell Biol Toxicol 7: 263-280, 1991.
    • (1991) Cell Biol Toxicol , vol.7 , pp. 263-280
    • Elliget, K.A.1    Phelps, P.C.2    Trump, B.F.3
  • 11
    • 0003035112 scopus 로고
    • Cerulein-induced pancreatitis
    • edited by Go VLW, DiMagno EP, Gardner JD, Lebenthal E, Reber HA, and Scheele GA: New York: Raven
    • Gorelick FS, Adler G, and Kern HF. Cerulein-induced pancreatitis. In: The Pancreas: Biology, Pathobiology, and Disease, edited by Go VLW, DiMagno EP, Gardner JD, Lebenthal E, Reber HA, and Scheele GA: New York: Raven, 1993, p. 501-526.
    • (1993) The Pancreas: Biology, Pathobiology, and Disease , pp. 501-526
    • Gorelick, F.S.1    Adler, G.2    Kern, H.F.3
  • 13
    • 0030918226 scopus 로고    scopus 로고
    • Distribution of ankyrin isoforms and their proteolysis after ischemia and reperfusion in rat brain
    • Harada K, Fukuda S, Kunimoto M, and Yoshida K. Distribution of ankyrin isoforms and their proteolysis after ischemia and reperfusion in rat brain. J Neurochem 69: 371-376, 1997.
    • (1997) J Neurochem , vol.69 , pp. 371-376
    • Harada, K.1    Fukuda, S.2    Kunimoto, M.3    Yoshida, K.4
  • 15
    • 0031883680 scopus 로고    scopus 로고
    • Comparison of calpains from rabbit, monkey, human and rat
    • Kawashima S, Akanuma H, and Asaoka K. Comparison of calpains from rabbit, monkey, human and rat. Biol Chem 379: 201-204, 1998.
    • (1998) Biol Chem , vol.379 , pp. 201-204
    • Kawashima, S.1    Akanuma, H.2    Asaoka, K.3
  • 16
    • 0030847177 scopus 로고    scopus 로고
    • Calpain is a mediator of preservation-reperfusion injury in rat liver transplantation
    • Kohli V, Gao W, Camargo CA, and Clavien PA. Calpain is a mediator of preservation-reperfusion injury in rat liver transplantation. Proc Natl Acad Sci USA 94: 9354-9359, 1997.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9354-9359
    • Kohli, V.1    Gao, W.2    Camargo, C.A.3    Clavien, P.A.4
  • 17
    • 0032898002 scopus 로고    scopus 로고
    • Calpain mediates ischemic injury of the liver through modulation of apoptosis and necrosis
    • Kohli V, Madden JF, Bentley RC, and Clavien PA. Calpain mediates ischemic injury of the liver through modulation of apoptosis and necrosis. Gastroenterology 116: 168-178, 1999.
    • (1999) Gastroenterology , vol.116 , pp. 168-178
    • Kohli, V.1    Madden, J.F.2    Bentley, R.C.3    Clavien, P.A.4
  • 18
    • 0017324230 scopus 로고
    • Acute interstitial pancreatitis in the rat induced by excessive doses of a pancreatic secretagogue
    • Lampel M and Kern HF. Acute interstitial pancreatitis in the rat induced by excessive doses of a pancreatic secretagogue. Virchows Arch 373: 97-117, 1977.
    • (1977) Virchows Arch , vol.373 , pp. 97-117
    • Lampel, M.1    Kern, H.F.2
  • 19
    • 0026515545 scopus 로고
    • Multiple forms of rat calpastatin cDNA in the coding region of functionally unknown amino-terminal domain
    • Lee WJ, Hatanaka M, and Maki M. Multiple forms of rat calpastatin cDNA in the coding region of functionally unknown amino-terminal domain. Biochem Biophys Acta 1129: 251-253, 1992.
    • (1992) Biochem Biophys Acta , vol.1129 , pp. 251-253
    • Lee, W.J.1    Hatanaka, M.2    Maki, M.3
  • 22
    • 0026600301 scopus 로고
    • The calpain-calpastatin system in mammalian cells: Properties and possible functions
    • Melloni E, Salamino F, and Sparatore B. The calpain-calpastatin system in mammalian cells: properties and possible functions. Biochimie 74: 217-223, 1992.
    • (1992) Biochimie , vol.74 , pp. 217-223
    • Melloni, E.1    Salamino, F.2    Sparatore, B.3
  • 24
    • 0026079729 scopus 로고
    • Binding of calpain fragments to calpastatin
    • Nishimura T and Goll DE. Binding of calpain fragments to calpastatin. J Biol Chem 266: 11842-11850, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 11842-11850
    • Nishimura, T.1    Goll, D.E.2
  • 25
    • 0031059566 scopus 로고    scopus 로고
    • Distribution of a synthetic protease inhibitor in rat pancreatic acini after supramaximal secretagogue stimulation
    • Otani T, Atomi Y, Kuroda A, Muto T, Tamura M, Fukuda S, Akao S, and Gorelick FS. Distribution of a synthetic protease inhibitor in rat pancreatic acini after supramaximal secretagogue stimulation. Pancreas 14: 142-149, 1997.
    • (1997) Pancreas , vol.14 , pp. 142-149
    • Otani, T.1    Atomi, Y.2    Kuroda, A.3    Muto, T.4    Tamura, M.5    Fukuda, S.6    Akao, S.7    Gorelick, F.S.8
  • 26
    • 0033962648 scopus 로고    scopus 로고
    • Calpain I induced alterations in the cytoskeletal structure and impaired mechanical properties of single myocytes of rat heart
    • Papp Z, van der Velden J, and Stienen GJ. Calpain I induced alterations in the cytoskeletal structure and impaired mechanical properties of single myocytes of rat heart. Cardiovasc Res 45: 981-993, 2000.
    • (2000) Cardiovasc Res , vol.45 , pp. 981-993
    • Papp, Z.1    Van Der Velden, J.2    Stienen, G.J.3
  • 27
    • 0041018181 scopus 로고    scopus 로고
    • Cleavage of the calpain inhibitor, calpastatin, during apoptosis
    • Pörn-Ares MI, Samali A, and Orrenius S. Cleavage of the calpain inhibitor, calpastatin, during apoptosis. Cell Death Differ 12: 1028-1033, 1998.
    • (1998) Cell Death Differ , vol.12 , pp. 1028-1033
    • Pörn-Ares, M.I.1    Samali, A.2    Orrenius, S.3
  • 28
    • 0037155557 scopus 로고    scopus 로고
    • Calpain activation and α-spectrin cleavage in rat brain by ethanol
    • Rajgopal Y and Vemuri MC. Calpain activation and α-spectrin cleavage in rat brain by ethanol. Neurosci Lett 321: 187-191, 2002.
    • (2002) Neurosci Lett , vol.321 , pp. 187-191
    • Rajgopal, Y.1    Vemuri, M.C.2
  • 29
    • 0034595540 scopus 로고    scopus 로고
    • Mu-calpain activation, DNA fragmentation, and synergistic effects of caspase and calpain inhibitors in promoting hippocampal neurons from ischemic damage
    • Rami A, Agarwal R, Botez G, and Winckler J. Mu-calpain activation, DNA fragmentation, and synergistic effects of caspase and calpain inhibitors in promoting hippocampal neurons from ischemic damage. Brain Res 866: 299-312, 2000.
    • (2000) Brain Res , vol.866 , pp. 299-312
    • Rami, A.1    Agarwal, R.2    Botez, G.3    Winckler, J.4
  • 30
  • 31
    • 0037989744 scopus 로고    scopus 로고
    • Calpain in the pathophysiology of spinal cord injury: Neuroprotection with calpain inhibitors
    • Ray SK, Hogan EL, and Banik NL. Calpain in the pathophysiology of spinal cord injury: neuroprotection with calpain inhibitors. Brain Res Rev 42: 169-185, 2003.
    • (2003) Brain Res Rev , vol.42 , pp. 169-185
    • Ray, S.K.1    Hogan, E.L.2    Banik, N.L.3
  • 33
    • 0028088153 scopus 로고
    • Calpain: New perspectives in molecular diversity and physiological-pathological involvement
    • Saido TC, Sorimachi H, and Suzuki K. Calpain: new perspectives in molecular diversity and physiological-pathological involvement. FASEB J 8: 814-822, 1994.
    • (1994) FASEB J , vol.8 , pp. 814-822
    • Saido, T.C.1    Sorimachi, H.2    Suzuki, K.3
  • 35
    • 0033826589 scopus 로고    scopus 로고
    • Downregulation of the calpain inhibitor protein calpastatin by caspases during renal ischemia-reperfusion
    • Shi Y, Melnikow VY, Schrier RW, and Edelstein CL. Downregulation of the calpain inhibitor protein calpastatin by caspases during renal ischemia-reperfusion. Am J Physiol Renal Physiol 279: F509-F517, 2000.
    • (2000) Am J Physiol Renal Physiol , vol.279
    • Shi, Y.1    Melnikow, V.Y.2    Schrier, R.W.3    Edelstein, C.L.4
  • 37
    • 0029360698 scopus 로고
    • Calpain. Novel family members, activation, and physiological function
    • Suzuki K, Sorimachi H, Yoshizawa T, Kinbara K, and Ishiura S. Calpain. Novel family members, activation, and physiological function. Biol Chem 376: 523-529, 1995.
    • (1995) Biol Chem , vol.376 , pp. 523-529
    • Suzuki, K.1    Sorimachi, H.2    Yoshizawa, T.3    Kinbara, K.4    Ishiura, S.5
  • 39
    • 0031969695 scopus 로고    scopus 로고
    • Calpain inhibitors but not caspase inhibitors, prevent actin proteolysis and DNA fragmentation during apoptosis
    • Villa PG, Henzel WJ, Sensenbrenner M, Henderson CE, and Pettmann B. Calpain inhibitors but not caspase inhibitors, prevent actin proteolysis and DNA fragmentation during apoptosis. J Cell Sci 111: 713-722, 1998.
    • (1998) J Cell Sci , vol.111 , pp. 713-722
    • Villa, P.G.1    Henzel, W.J.2    Sensenbrenner, M.3    Henderson, C.E.4    Pettmann, B.5
  • 40
    • 0033956278 scopus 로고    scopus 로고
    • Calpain and caspase: Can you tell the difference?
    • Wang KKW. Calpain and caspase: can you tell the difference? Trends Neurosci 23: 20-26, 2000.
    • (2000) Trends Neurosci , vol.23 , pp. 20-26
    • Wang, K.K.W.1
  • 42
    • 0030035935 scopus 로고    scopus 로고
    • Progressive disruption of acinar cell signaling is an early feature of cerulein-induced pancreatitis in mice
    • Ward JB, Sutton R, Jenkins SA, and Petersen OH. Progressive disruption of acinar cell signaling is an early feature of cerulein-induced pancreatitis in mice. Gastroenterology 111: 481-491, 1996.
    • (1996) Gastroenterology , vol.111 , pp. 481-491
    • Ward, J.B.1    Sutton, R.2    Jenkins, S.A.3    Petersen, O.H.4
  • 46
    • 0034739734 scopus 로고    scopus 로고
    • Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates
    • Yamashima T. Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates. Prog Neurobiol 62: 273-295, 2000.
    • (2000) Prog Neurobiol , vol.62 , pp. 273-295
    • Yamashima, T.1


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