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Gallbladder epithelial acid hydrolases in human cholecystitis.

E Kouroumalis, D Hopwood, P E Ross

The Journal of Pathology

|February 1, 1983

Summary

Lysosomal enzymes beta-glucuronidase and acid phosphatase were studied in cholecystitis patients. Elevated beta-glucuronidase in acalculous cholecystitis suggests a role in gallstone formation.

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Area of Science:

Biochemistry
Gastroenterology
Cell Biology

Background:

Cholecystitis involves inflammation of the gallbladder.
Gallstones (cholelithiasis) are a common complication.
Lysosomal enzymes may play a role in gallstone pathogenesis.

Purpose of the Study:

To investigate the activity of lysosomal enzymes beta-glucuronidase and acid phosphatase in patients with cholecystitis.
To explore the relationship between enzyme activity and different types of gallstones or cholecystitis.
To elucidate the cellular localization and secretion pathways of these enzymes.

Main Methods:

Enzyme activity assays for beta-glucuronidase and acid phosphatase in patient samples.
Histochemical staining for light and electron microscopy.

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Analysis of enzyme distribution in relation to gallstone type and gallbladder tissue.

Main Results:

Acid phosphatase activity was lower in cholesterol stones compared to pigment stones.
Beta-glucuronidase activity was highest in acalculous cholecystitis.
Histochemistry confirmed lysosomal localization and presence in macrophages; electron microscopy showed activity in lysosomes and mucous droplets.

Conclusions:

Beta-glucuronidase may be secreted into bile, potentially contributing to gallstone nidus formation.
Acid phosphatase is secreted with mucus from the gallbladder epithelium into bile.
These findings highlight the role of lysosomal hydrolases in cholecystitis and gallstone disease.