Pancreatitis-associated chymotrypsinogen C (CTRC) mutant elicits endoplasmic reticulum stress in pancreatic acinar cells

Gut

Volumn 59, Issue 3, 2010, Pages 365-372

  Szmola, Richárd ^a   Sahin Tóth, Miklós ^a  

^a BOSTON UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; CASPASE 7; CCAAT ENHANCER BINDING PROTEIN; CHYMOTRYPSINOGEN; DEXAMETHASONE; IMMUNOGLOBULIN BINDING FACTOR; MESSENGER RNA; X BOX BINDING PROTEIN 1;

ACINAR CELL; ADENOVIRUS; ANIMAL CELL; ANIMAL EXPERIMENT; APOPTOSIS; ARTICLE; CELL DIFFERENTIATION; CELL ISOLATION; CONTROLLED STUDY; ENDOPLASMIC RETICULUM STRESS; ENZYME ACTIVITY; GENE MUTATION; GENETIC TRANSFECTION; MOUSE; NICK END LABELING; NONHUMAN; PANCREATITIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; RAT; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; RNA BINDING;

ADENOVIRIDAE; ANIMALS; APOPTOSIS; CELLS, CULTURED; CHYMOTRYPSIN; EIF-2 KINASE; ENDOPLASMIC RETICULUM; HUMANS; MICE; NF-KAPPA B; PANCREAS, EXOCRINE; PANCREATITIS, CHRONIC; RATS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; SIGNAL TRANSDUCTION; STRESS, PHYSIOLOGICAL; TRANSFECTION;

EID: 77749318543     PISSN: 00175749     EISSN: 14683288     Source Type: Journal    
DOI: 10.1136/gut.2009.198903     Document Type: Article

References (28)

1. Witt H, Apte MV, Keim V, et al. Chronic pancreatitis: challenges and advances in pathogenesis, genetics, diagnosis, and therapy. Gastroenterology 2007;132:1557e73.
2. Teich N, Rosendahl J, Tóth M, et al. Mutations of human cationic trypsinogen (PRSS1) and chronic pancreatitis. Hum Mutat 2006;27:721e30.
3. Sahin-Tóth M. Biochemical models of hereditary pancreatitis. Endocrinol Metab Clin North Am 2006;35:303e12.
4. Whitcomb DC, Gorry MC, Preston RA, et al. Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene. Nat Genet 1996;14: 141e5.
5. Howes N, Lerch MM, Greenhalf W, et al. Clinical and genetic characteristics of hereditary pancreatitis in Europe. Clin Gastroenterol Hepatol 2004;2: 252e61.
6. Sahin-Tóth M, Tóth M. Gain-of-function mutations associated with hereditary pancreatitis enhance autoactivation of human cationic trypsinogen. Biochem Biophys Res Commun 2000;278:286e9.
7. 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;25:213e16.
8. Pfützer RH, Barmada MM, Brunskill AP, et al. SPINK1/PSTI polymorphisms act as disease modifiers in familial and idiopathic chronic pancreatitis. Gastroenterology 2000;119:615e23.
9. Aoun E, Chang CC, Greer JB, et al. Pathways to injury in chronic pancreatitis: decoding the role of the high-risk SPINK1 N34S haplotype using meta-analysis. PLoS One 2008;3:e2003.
10. Király 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 2007;28:469e76.
11. Király O, Wartmann T, Sahin-Tóth M. Missense mutations in pancreatic secretory trypsin inhibitor (SPINK1) cause intracellular retention and degradation. Gut 2007;56:1433e8.
12. Boulling A, Le Maréchal C, Trouvé P, et al. Functional analysis of pancreatitisassociated missense mutations in the pancreatic secretory trypsin inhibitor (SPINK1) gene. Eur J Hum Genet 2007;15:936e42.
13. Kereszturi E, Király O, Sahin-Tóth M. Minigene analysis of intronic variants in common SPINK1 haplotypes associated with chronic pancreatitis. Gut 2009;58:545e9.
14. Witt H, Sahin-Tóth M, Landt O, et al. A degradation-sensitive anionic trypsinogen (PRSS2) variant protects against chronic pancreatitis. Nat Genet 2006;38: 668e73.
15. Szmola R, Sahin-Tóth M. Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: identity with Rinderknecht's enzyme Y. Proc Natl Acad Sci U S A 2007;104:11227e32.
16. 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;40:78e82.
17. Masson E, Chen JM, Scotet V, et al. Association of rare chymotrypsinogen C (CTRC) gene variations in patients with idiopathic chronic pancreatitis. Hum Genet 2008;123:83e91.
18. Marciniak Ron SJ, Ron D. Endoplasmic reticulum stress signaling in disease. Physiol Rev 2006;86:1133e49.
19. Ron D, Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 2007;8:519e29.
20. Rutkowski DT, Kaufman RJ. That which does not kill me makes me stronger: adapting to chronic ER stress. Trends Biochem Sci 2007;32:469e76.
21. Zhang K, Kaufman RJ. From endoplasmic-reticulum stress to the inflammatory response. Nature 2008;454:455e62.
22. Kubisch CH, Sans MD, Arumugam T, et al. Early activation of endoplasmic reticulum stress is associated with arginine-induced acute pancreatitis. Am J Physiol Gastrointest Liver Physiol 2006;291:G238e45.
23. Kubisch CH, Logsdon CD. Secretagogues differentially activate endoplasmic reticulum stress responses in pancreatic acinar cells. Am J Physiol Gastrointest Liver Physiol 2007;292:G1804e12.
24. Logsdon CD, Moessner J, Williams JA, et al. Glucocorticoids increase amylase mRNA levels, secretory organelles, and secretion in pancreatic acinar AR42J cells. J Cell Biol 1985;100:1200e8.
25. Takemoto H, Yoshimori T, Yamamoto A, et al. Heavy chain binding protein (BiP/ GRP78) and endoplasmin are exported from the endoplasmic reticulum in rat exocrine pancreatic cells, similar to protein disulfide-isomerase. Arch Biochem Biophys 1992;296:129e36.
26. Mareninova OA, Sung KF, Hong P, et al. Cell death in pancreatitis: caspases protect from necrotizing pancreatitis. J Biol Chem 2006;281:3370e81.
27. Kereszturi E, Szmola R, Kukor Z, et al. Hereditary pancreatitis caused by mutationinduced misfolding of human cationic trypsinogen: a novel disease mechanism. Hum Mutat 2009;30:575e82.
28. Schrader H, Menge BA, Schneider S, et al. Reduced pancreatic volume and beta-cell area in patients with chronic pancreatitis. Gastroenterology 2009;136: 513e22.