Edema and intrapancreatic trypsinogen activation precede glutathione depletion during caerulein pancreatitis

American Journal of Physiology

Volumn 271, Issue 1 PART 1, 1996, Pages

  Grady, T ^a   Saluja, A ^a   Kaiser, A ^a   Steer, M ^a  

^a BETH ISRAEL DEACONESS MEDICAL CENTER   (United States)

Author keywords

Amylase; Antioxidants; Cathepsin b; Lysosomal hydrolases

Indexed keywords

EID: 33745383777     PISSN: 00029513     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (27)

1. Bialek, R., S. Willemer, R. Arnold, and G. Adler. Evidence of intracellular activation of serine proteases in acute caeruleininduced pancreatitis in rats. Scand. J. Gastroenterol. 26: 190196, 1991.
2. Figarella, C., B. Miszczuk-Jamska, and A. Barret. Possible lysosomal activation of pancreatic zymogens. Biol. Chem. HoppeSeyler 369: 293-298, 1988.
3. Foulis, A. K. Histological evidence of initiating factors in acute necrotizing pancreatitis in man. J. Clin. Pathol. 33: 1123-1131, 1980.
4. Geokas, M. C., and H. Rinderknecht. Free proteolytic enzymes in pancreatic juice of patients with acute pancreatitis. Am. J. Dig. Dis. 19: 591-598, 1974.
5. Greenbaum, L. M., A. Hirshkowitz, and I. Shoichet. The activation of trypsinogen by cathepsin B. J. Biol. Chem. 234: 2885-2890, 1959.
6. Griffith, O. W. Determination of glutathione and glutathione disulfide using glutathione reduction and 2-vinylpyridine. Anal. Biochem. 106: 207-212, 1980.
7. Hirano, T., A. Saluja, P. Ramarao, M. M. Lerch, M. Saluja, and M. L. Steer. Apical secretion of lysosomal enzymes in rabbit pancreas occurs via a secretagogue regulated pathway and is increased after pancreatic duct obstruction. J. Clin. Invest. 87: 865-869, 1991.
8. Kawabata, S., T. Miura, T. Morita, H. Kato, K. Fujikawa, K. Takada, and S. Sakakibara. Highly sensitive peptide-4methylcoumaryl-7-aniide substrates for blood-clotting proteases and trypsin. Eur. J. Biochem. 172: 17-25, 1988.
9. Korsten, M. A., and J. W. Dlugosz. Cathepsin B inhibition in two models of acute pancreatitis. Int. J. Pancreatol. 14: 149-155, 1993.
10. Lampel, M., and H. F. Kern. Acute interstitial pancreatitis in the rat induced by excessive doses of a pancreatic secretagogue. Virchows Arch. Pathol. Anat. Histol. 373: 107-117, 1977.
11. Lerch, M. M., A. K. Saluja, R. Dawra, M. Saluja, and M. L. Steer. The effect of chloroquine administration on two experimental models of acute pancreatitis. Gastroenterology 104: 17681779, 1993.
12. Lüthen, R., C. Niederau, and J. H. Grendell. Intrapancreatic zymogen activation and levels of ATP and glutathione during caerulein pancreatitis in rats. Am. J. Physiol. 268 (Gastrointest. Liver Physiol. 31): G592-G603, 1995.
13. McDonald, J. K., and S. Ellis. On the substrate specificity of cathepsin BI and cathepsin 62 including a new fluorogenic substrate for cathepsin BI. Life. Sei. 17: 1269-1276, 1975.
14. Meister, A. Selective modification of glutathione metabolism. Science Wash. DC 220: 472-477, 1983.
15. Neuschwander-Tetri, B. A., N. M. Barnidge, and C. G. Janney. Caerulein-induced pancreatic cysteine depletion: prevention does not diminish acute pancreatitis in the mouse. Gastroenterology 107: 824-830, 1994.
16. Neuschwander-Tetri, B. A., L. D. Ferrell, R. J. Sukhabote, and J. H. Grendell. Glutathione monoethyl ester ameliorates caerulein-induced pancreatitis in the mouse. J. Clin. Invest. 98, Suppl. 1: 109-161, 1992.
17. Peterson, O. Modified Lowry protein assay. Methods Enzymol. 91: 95-119, 1983.
18. Pierre, K. J., K. K. Tung, and H. Nadj. A new enzymatic kinetic method for determination of amylase (Abstract). Clin. Chem. 22: 1219, 1976.
19. Rao, K. N., J. Tuma, and B. Lombard!. Acute hemorrhagic pancreatic necrosis in mice. Intraparenchymal activation of zymogens and other enzyme changes in pancreas and serum. Gastroenterology 70: 720-726, 1976.
20. Saluja, A. K., S. Hashimoto, M. Saluja, R. E. Powers, J. Meldolesi, and M. L. Steer. Subcellular redistribution of lysosomal enzymes during caerulein-induced pancreatitis. Am. J. Physiol. 253 (Gastrointest. Liver Physiol. 16): G508-G516, 1987.
21. Saluja, A. K., I. Saito, M. Saluja, M. J. Houlihan, R. E. Powers, J. Meldolesi, and M. L. Steer. In vivo rat pancreatic function during supramaximal stimulation with caerulein. Am. J. Physiol. 249 (Gastrointest. Liver Physiol. 12): G702-G710, 1985.
22. Saluja, A. K., M. Saluja, H. Printz, A. Zavertnick, A. Sengupta, and M. L. Steer. Experimental pancreatitis is mediated by low-affinity cholecystokinin receptors that inhibit digestive enzyme secretion. Proc. Natl. Acad. Sei. USA 86: 9871-9896, 1989.
23. Schmidt, J., C. Fernandez-Del Castillo, D. Rattner, K. Lewandrowski, C. Compton, and A. Warshaw. Trypsinogenactivation peptides in experimental rat pancreatitis: prognostic implications and histopathologic correlates. Gastroenterology 103: 1009-1016, 1992.
24. Steer, M. L., and A. K. Saluja. Experimental acute pancreatitis: studies of the early events that lead to cell injury. In: The Pancreas: Biology, Pathophysiology and Disease (2nd ed.), edited by V. L. W. Go, E. P. DiMagno, J. D. Gardner, E. Lebenthal, H. A. Rebar, and G. A. Scheele. New York: Raven, 1993, p. 489-499.
25. Tartakoff, A., and J. E. Jamieson. Fractionation of guinea pig pancreas. Methods Enzymol. 31: 41-59, 1985.
26. Tietze, F. Enzymatic method for quantitative determination of nanogram amounts of total and oxidized glutathione applications to mammal blood and other tissues. Anal. Biochem. 27: 502-522, 1969.
27. Yamaguchi, , H. T., K. Kimura, and H. Nawata. Activation of proteases in caerulein-induced pancreatitis. Pancreas 4: 565571, 1989.