Pathogenic cellular role of the p.L104P human cationic trypsinogen variant in chronic pancreatitis

American Journal of Physiology - Gastrointestinal and Liver Physiology

Volumn 310, Issue 7, 2016, Pages G477-G486

  Balázs, Anita ^a,b   Hegyi, Péter ^b,c   Sahin Tóth, Miklós ^a  

^a BOSTON UNIVERSITY   (United States)

^b UNIVERSITY OF SZEGED   (Hungary)

^c UNIVERSITY OF PÉCS   (Hungary)

Author keywords

Autoactivation; Chronic pancreatitis; Endoplasmic reticulum stress; Hereditary pancreatitis; Intracellular aggregation; Misfolding; Trypsinogen activation

Indexed keywords

BENZAMIDINE; BETA CASEIN; CHYMOTRYPSIN; CHYMOTRYPSIN C; MESSENGER RNA; TRYPSIN; TRYPSINOGEN; UNCLASSIFIED DRUG; X BOX BINDING PROTEIN 1; CARRIER PROTEIN; PROTEIN AGGREGATE; PROTEIN BINDING; PRSS1 PROTEIN, HUMAN; SPINK1 PROTEIN, HUMAN;

ARTICLE; BINDING ASSAY; CATALYTIC EFFICIENCY; CELL LYSATE; CELLULAR SECRETION; CHRONIC PANCREATITIS; COMPARATIVE STUDY; CONTROLLED STUDY; ENDOPLASMIC RETICULUM STRESS; ENZYME RELEASE; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; PATHOGENESIS; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN SECRETION; RNA SPLICING; ULTRACENTRIFUGATION; WESTERN BLOTTING; BINDING SITE; CHEMISTRY; ENZYME ACTIVATION; ENZYME SPECIFICITY; ENZYMOLOGY; GENETIC PREDISPOSITION; GENETICS; HEK293 CELL LINE; KINETICS; METABOLISM; MOLECULAR MODEL; MUTATION; PATHOLOGY; PHENOTYPE; PROTEIN CONFORMATION; PROTEIN FOLDING; SECRETION (PROCESS); SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION;

BINDING SITES; CARRIER PROTEINS; CHYMOTRYPSIN; ENDOPLASMIC RETICULUM STRESS; ENZYME ACTIVATION; GENETIC PREDISPOSITION TO DISEASE; HEK293 CELLS; HUMANS; KINETICS; MODELS, MOLECULAR; MUTATION; PANCREATITIS, CHRONIC; PHENOTYPE; PROTEIN AGGREGATES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; SIGNAL TRANSDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; TRANSFECTION; TRYPSIN;

EID: 85011965448     PISSN: 01931857     EISSN: 15221547     Source Type: Journal    
DOI: 10.1152/ajpgi.00444.2015     Document Type: Article

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