The Guinea pig pancreas secretes a single trypsinogen isoform, which is defective in autoactivation

Pancreas

Volumn 37, Issue 2, 2008, Pages 182-188

  Ózsvári, Béla ^a,b   Hegyi, Péter ^b   Sahin Tóth, Miklós ^a,c  

^a BOSTON UNIVERSITY   (United States)

^b UNIVERSITY OF SZEGED   (Hungary)

^c BOSTON UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

Autoactivation; Cathepsin B; Ecotin; Enteropeptidase; Trypsinogen isoforms; Zymogen activation

Indexed keywords

ALANINE; CATHEPSIN B; COMPLEMENTARY DNA; ENTEROPEPTIDASE; ISOENZYME; RNA; SERINE; TRYPSIN; TRYPSINOGEN; MESSENGER RNA;

AFFINITY CHROMATOGRAPHY; AMINO TERMINAL SEQUENCE; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME PURIFICATION; ENZYME RELEASE; GUINEA PIG; HUMAN; ION EXCHANGE CHROMATOGRAPHY; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PANCREAS; PRIORITY JOURNAL; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; TISSUE HOMOGENATE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL; ENZYMOLOGY; GENETICS; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; MOLECULAR GENETICS; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BASE SEQUENCE; CLONING, MOLECULAR; DNA, COMPLEMENTARY; ENZYME ACTIVATION; GUINEA PIGS; ISOENZYMES; KINETICS; MOLECULAR SEQUENCE DATA; PANCREAS; RNA, MESSENGER; SEQUENCE HOMOLOGY, AMINO ACID; SEQUENCE HOMOLOGY, NUCLEIC ACID; TRYPSIN; TRYPSINOGEN;

EID: 55949131560     PISSN: 08853177     EISSN: None     Source Type: Journal    
DOI: 10.1097/MPA.0b013e3181663066     Document Type: Article

References (36)

1. Scheele GA, Palade GE. Studies on the guinea pig pancreas. Parallel discharge of exocrine enzyme activities. J Biol Chem. 1975;250: 2660-2670.
2. Tartakoff AM, Jamieson JD, Scheele GA, et al. Studies on the pancreas of the guinea pig. Parallel processing and discharge of exocrine proteins. J Biol Chem. 1975;250:2671-2677.
3. Case RM, Argent BE. Pancreatic duct secretion: control and mechanisms of transport. In: Go VLW, DiMagno EP, et al, eds. The Pancreas: Biology, Pathobiology, and Disease. New York: Raven Press; 1993:301-350.
4. Hegyi P, Rakonczay Z Jr. The inhibitory pathways of pancreatic ductal bicarbonate secretion. Int J Biochem Cell Biol. 2007;39:25-30.
5. Tartakoff A, Greene LJ, Palade GE. Studies on the guinea pig pancreas. Fractionation and partial characterization of exocrine proteins. J Biol Chem. 1974;249:7420-7431.
6. Scheele GA. Two-dimensional gel analysis of soluble proteins. Characterization of guinea pig exocrine pancreatic proteins. J Biol Chem. 1975;250:5375-5385.
7. Lampel M, Kern HF. Acute interstitial pancreatitis in the rat induced by excessive doses of a pancreatic secretagogue. Virchows Arch A Pathol Anat Histol. 1977;373:97-117.
8. Mizunuma T, Kawamura S, Kishino Y. Effects of injecting excess arginine on rat pancreas. J Nutr. 1984;114:467-471.
9. Hegyi P, Rakonczay Z Jr, Sari R, et al. L-arginine-induced experimental pancreatitis. World J Gastroenterol. 2004;15:2003-2009.
10. Dawra R, Sharif R, Phillips P, et al. Development of a new mouse model of acute pancreatitis induced by administration of L-arginine. Am J Physiol Gastrointest Liver Physiol. 2007;292:G1009-G1018.
11. Aho HJ, Koskensalo SM, Nevalainen TJ. Experimental pancreatitis in the rat. Sodium taurocholate-induced acute haemorrhagic pancreatitis. Scand J Gastroenterol. 1980;15:411-416.
12. Laukkarinen JM, Van Acker GJ, Weiss ER, et al. A mouse model of acute biliary pancreatitis induced by retrograde pancreatic duct infusion of Na-taurocholate. Gut. 2007;56:1590-1598.
13. Harell D, Orda R, Wiznitzer T, et al. Proteolytic proenzymes in the pancreas in the course of experimental bile-induced pancreatitis in the guinea pig. Digestion. 1978;18:394-401.
14. Frick TW, Hailemariam S, Heitz PU, et al. Acute hypercalcemia induces acinar cell necrosis and intraductal protein precipitation in the pancreas of cats and guinea pigs. Gastroenterology. 1990;98:1675-1681.
15. Chen JM, Férec C. Trypsinogen genes: evolution. In: Cooper DN, ed. Nature Encyclopedia of the Human Genome. London: Macmillan; 2003:645-650.
16. Whitcomb DC, Gorry MC, Preston RA, et al. Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene. Nat Genet. 1996;14:141-145.
17. Teich N, Rosendahl J, Tóth M, et al. Mutations of human cationic trypsinogen (PRSS1) and chronic pancreatitis. Hum Mutat. 2006;27: 721-730.
18. Witt H, Sahin-Tóth M, Landt O, et al. A degradation-sensitive anionic trypsinogen (PRSS2) variant protects against chronic pancreatitis. Nat Genet. 2006;38:668-673.
19. Witt H, Luck W, Hennies HC, et al. Mutations in the gene encoding the serine protease inhibitor, Kazal type 1 are associated with chronic pancreatitis. Nat Genet. 2000;25:213-216.
20. Rosendahl J, Witt H, Szmola R, et al. Chymotrypsin C (CTRC) variants that diminish activity or secretion are associated with chronic pancreatitis. Nat Genet. 2008;40:78-82.
21. Sahin-Tóth M. Human cationic trypsinogen. Role of Asn-21 in zymogen activation and implications in hereditary pancreatitis. J Biol Chem. 2000;275:22750-22755.
22. Sahin-Tóth M, Tóth M. Gain-of-function mutations associated with hereditary pancreatitis enhance autoactivation of human cationic trypsinogen. Biochem Biophys Res Commun. 2000;278:286-289.
23. Szilágyi L, Kénesi E, Katona G, et al. Comparative in vitro studies on native and recombinant human cationic trypsins. Cathepsin B is a possible pathological activator of trypsinogen in pancreatitis. J Biol Chem. 2001;276:24574-24580.
24. Kukor Z, Tóth M, Sahin-Tóth M. Human anionic trypsinogen. Properties of autocatalytic activation and degradation and implications in pancreatic diseases. Eur J Biochem. 2003;270:2047-2058.
25. 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. 2002;277:21389-212396.
26. Lengyel Z, Pál G, Sahin-Tóth M. Affinity purification of recombinant trypsinogen using immobilized ecotin. Protein Expr Purif. 1998;12: 291-294.
27. Teich N, Le Maréchal 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. 2004;23:22-31.
28. Várallyay E, Pál G, Patthy A, et al. Two mutations in rat trypsin confer resistance against autolysis. Biochem Biophys Res Commun. 1998;243: 56-60.
29. 117 is the reactive site of an inhibitory surface loop that controls spontaneous zymogen activation. J Biol Chem. 2002;277:6111-6117.
30. Mallory PA, Travis J. Human pancreatic enzymes. Characterization of anionic human trypsin. Biochemistry. 1973;12:2847-2851.
31. Colomb E, Guy O, Deprez P, et al. The two human trypsinogens: catalytic properties of the corresponding trypsins. Biochim Biophys Acta. 1978;525:186-193.
32. Hood L, Rowen L, Koop BF. Human and mouse T-cell receptor loci: genomics, evolution, diversity, and serendipity. Ann N Y Acad Sci. 1995;758:390-412.
33. Wang K, Gan L, Lee I, et al. Isolation and characterization of the chicken trypsinogen gene family. Biochem J. 1995;307:471-479.
34. Rowen L, Koop BF, Hood L. The complete 685-kilobase DNA sequence of the human beta T cell receptor locus. Science. 1996;272:1755-1762.
35. Glusman G, Rowen L, Lee I, et al. Comparative genomics of the human and mouse T cell receptor loci. Immunity. 2001;15:337-349.
36. Roach JC, Wang K, Gan L, et al. The molecular evolution of the vertebrate trypsinogens. J Mol Evol. 1997;45:640-652.