Human gallbladder epithelium: non-specific esterases in cholecystitis.
Esterases active at neutral and acid pH have been demonstrated in human gallbladder epithelium. Reaction to a wide variety of inhibitors and activators suggests that they probably represent the same enzyme with two active sites while a close correlation with acid phosphatase, a known lysosomal enzyme, suggests a lysosomal localization. Esterase activity in the gallbladder mucosa in significantly decreased in chronic cholecystitis. Polyacrylamide gel electrophoresis suggests that cholesterol stones may be associated with a specific type of isoenzyme pattern. Esterase positive cells are present in the inflammatory infiltrate in the lamina propria of the gallbladder in most cases of chronic cholecystitis. Naphthol AS-D chloracetate esterase staining indicates that mast cells form a large part of the infiltrate. Bile acids modulate the enzyme activity in vitro. Although the exact substrate specificity is not known, several possibilities are discussed, implicating esterases in the pathogenesis of chronic cholecystitis.
D000135:Acid Phosphatase / Q000378:metabolism; D043182:Carboxylesterase; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D002764:Cholecystitis / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D004848:Epithelium / Q000201:enzymology; D005260:Female; D005704:Gallbladder / Q000201:enzymology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000378:metabolism
D007527:Isoenzymes; D002265:Carboxylic Ester Hydrolases; D043182:Carboxylesterase; D000135:Acid Phosphatase