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Related Experiment Videos

Human gallbladder epithelium: non-specific esterases in cholecystitis.

E Kouroumalis, D Hopwood, P E Ross

    The Journal of Pathology
    |February 1, 1984
    PubMed
    Summary

    Esterase activity in human gallbladder mucosa is reduced in chronic cholecystitis and may be linked to cholesterol gallstone formation. Bile acids influence this enzyme, suggesting a role in gallbladder disease pathogenesis.

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    Area of Science:

    • Biochemistry
    • Gastroenterology
    • Pathology

    Background:

    • Esterases are enzymes found in human gallbladder epithelium.
    • These enzymes exhibit activity at neutral and acidic pH.
    • Their properties suggest a lysosomal localization, similar to acid phosphatase.

    Purpose of the Study:

    • To investigate the role of esterases in chronic cholecystitis and cholesterol gallstone formation.
    • To explore the relationship between esterase activity, isoenzyme patterns, and gallbladder disease.
    • To understand the influence of bile acids on gallbladder esterase activity.

    Main Methods:

    • Enzyme activity assays with various inhibitors and activators.
    • Polyacrylamide gel electrophoresis for isoenzyme pattern analysis.

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  • Histochemical staining (Naphthol AS-D chloracetate esterase) to identify specific cell types.

    • Main Results:

    • Esterase activity is significantly decreased in gallbladder mucosa affected by chronic cholecystitis.
    • Specific isoenzyme patterns may be associated with cholesterol gallstones.
    • Esterase-positive cells, including mast cells, are prevalent in the inflammatory infiltrate of chronic cholecystitis.
    • Bile acids were found to modulate enzyme activity in vitro.

    Conclusions:

    • Reduced esterase activity and altered isoenzyme patterns are linked to chronic cholecystitis and cholesterol gallstones.
    • Mast cells contribute to the inflammatory infiltrate in chronic cholecystitis.
    • Esterases may play a role in the pathogenesis of chronic cholecystitis, with bile acids influencing their activity.