On the Mediation of Inflammatory Reaction in the Human Gallbladder Epithelium

Abstract

Sjödahl, R. & Tagesson, C. On the mediation of inflammatory reaction in the human gallblader epitheiium. Scand. J. Gastroent. 1976, 11, 321-328.

Human gallbladder epithelium was homogenized with a view to maintaining the integrity of subcellular components. In such homogenates. N-acetyl-β-glucosaminidase. β-glucuronidase, β-galactosidase, β-glucosidase, β-fucosidase, β-xylosidase, and acid phosphatase were demonstrated together with phospholipase activity. All the enzymes exhibited structure-linked latency. After discarding cellular debris from the homogenate, remaining subcellular organelles were analytically separated by density gradient centrifugation. After 100,000 g for 1 hour, particles containing acid glycosidases were recovered at a sucrose density of 1.18–1.19, whereas the mitochondrial marker enzyme succinate-reductase accumulated at a density of 1.16. The bulk of sedimentable phospholipase activity was recovered with particles sedimenting at 1.18–1.19. The results are interpreted as indicating that phospholipase is present in lysosomes of the human gallbladder epithelium. Release of acid hydrolases, particularly phospholipase A, from the gallbladder epithelium is discussed as mediation of an inflammatory reaction in the gallbladder, i.e. cholecystitis.

Keywords::

• Acute cholecystitis
• gallbladder epithelium
• lysolecithin
• lysosomal enzymes
• phospholipase A