Molecular basis for pancreatitis

Current Opinion in Gastroenterology

Volumn 24, Issue 5, 2008, Pages 580-585

  Thrower, Edwin ^a,d   Husain, Sohail ^b   Gorelick, Fred ^a,c,d  

^a Department of Internal Medicine

^b Department of Pediatrics ^*

^c YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d VA CONNECTICUT HEALTHCARE SYSTEM   (United States)

Author keywords

Calcium; Chymotrypsin C; Lipopolysaccharide; Toll like receptor

Indexed keywords

ALCOHOL; BILE ACID; CHYMOTRYPSIN C; ENZYME PRECURSOR; GAMMA INTERFERON; GHRELIN; HEAT SHOCK PROTEIN 70; INTERLEUKIN 1BETA; NEUROKININ 1 RECEPTOR; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PREPROTACHYKININ; PROTEINASE ACTIVATED RECEPTOR 2; SUBSTANCE P; THALIDOMIDE; TOLL LIKE RECEPTOR 4; TRANSMEMBRANE CONDUCTANCE REGULATOR; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; VANILLOID RECEPTOR 1;

ACINAR CELL; ACUTE PANCREATITIS; ALCOHOL ABUSE; ALCOHOL CONSUMPTION; APOPTOSIS; CELL MEMBRANE PERMEABILITY; CHRONIC PANCREATITIS; CYSTIC FIBROSIS; DISEASE PREDISPOSITION; ENDOPLASMIC RETICULUM STRESS; ENZYME ACTIVATION; EXPERIMENTAL MODEL; GENE INACTIVATION; GENE MUTATION; GENETIC POLYMORPHISM; GENETIC PREDISPOSITION; HEMOLYSIS; HYPERTRIGLYCERIDEMIA; INFECTION RISK; INFLAMMATION; INVASIVE PANCREATIC DUCTAL ADENOCARCINOMA; MEMBRANE PERMEABILITY; NONHUMAN; ONCOGENE K RAS; PAIN; PANCREAS CANCER; PANCREATIC INTRAEPITHELIAL NEOPLASIA; REVIEW; STELLATE CELL;

ANIMALS; DISEASE MODELS, ANIMAL; HUMANS; MICE; MOLECULAR BIOLOGY; PANCREATITIS, ACUTE NECROTIZING; PANCREATITIS, ALCOHOLIC; PANCREATITIS, CHRONIC; PROGNOSIS; RISK ASSESSMENT; SENSITIVITY AND SPECIFICITY;

EID: 55549090721     PISSN: 02671379     EISSN: None     Source Type: Journal    
DOI: 10.1097/MOG.0b013e32830b10e6     Document Type: Review

References (44)

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42. Szmola R, Sahin-Toth M. Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: identity with Rinderknecht's enzyme Y. Proc Natl Acad Sci U S A 2007; 104:11227-11232. The degradation of proteases activated within the acinar cell may be an important protective mechanism. This study suggests that chymotrypsin C may have a dual role in pancreatic function. Under the conditions found in the small intestine, it may contribute to trypsin activation. However, within the acinar cell, it may act to degrade trypsin. Clinical studies by Rosendhal et al. [43**] and by Masson et al. [44*] suggest that the latter function is an important protective mechanism.
43. 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. Using genetic analysis, this study demonstrates that mutations in chymotrypsin C may predispose to the development of chronic pancreatitis. The importance of chymotrypsin C as a risk factor may vary among populations. Moreover, in alcoholics, the presence of mutant chymotrypsin C may favor the development of pancreatic rather than liver disease.
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