On the Mediation of Inflammatory Reaction in the Human Gallbladder Epithelium

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Abstract
Human gallbladder epithelium was homogenized with a view to maintaining the integrity of subcellular components. In such homogenates, N-acetyl-.beta.-glucosaminidase, .beta.-glucuronidase, .beta.-galactosidase, .beta.-glucosidase, .beta.-fucosidase, .beta.-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 h particles containing acid glycosidases were recovered at a sucrose density of 1.18-1.19; 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. Phospholipase is probably present in lysosomes of the human gallbladder epithelium. Release of acid hydrolases, particularly phospholipase A, from the gallbladder epithelium is discussed as mediation of a inflammatory reaction in the gallbladder, i.e., cholecystitis.