Serum chitotriosidase activity was determined in different conditions accompanied by macrophage stimulation. Stimulation of macrophages with zymosan, yeast polysaccharide carboxymethylglucan (fraction II), and lysosomotropic preparation Triton WR-1339 1.5-2.0-fold increased enzyme activity. Chitotriosidase activity in intact Wistar rats was similar to that in humans, while in CBA and A/Sn mice this parameter was 5-fold higher. Sharp increase in chitotriosidase activity in the serum from patients with type I Gaucher's disease was probably related to intense secretion of the enzyme by macrophages. Under experimental conditions, stimulation of rat and mouse macrophages (mainly liver cells) caused no increase in chitotriosidase activity typical of patients with Gaucher's disease.
Kinetics of gadolinium accumulation was studied by inductively coupled plasma-emission spectroscopy after intravenous injection of this agent (7.5 mg/kg) to CBA mice. Gadolinium exhibits lysosomotropic properties (long-term selective accumulation in lysosomes in vivo). Gadolinium uptake by hepatic cells attained maximum 1 h after its intravenous injection and remained at this level during the next day. Accumulation of gadolinium in hepatocytic lysosomes disturbed their osmotic properties (as was seen from the increase in free acid phosphatase activity, which persisted for 19 days). Serum activities of beta-D-galactosidase and beta-D-glucuronidase also increased (24-72 h and day 19). Selective depression of liver macrophages (24-48 h) was accompanied by a decrease in serum chitotriosidase activity. We conclude that accumulation of gadolinium in lysosomes of liver macrophages leads to their damage and elimination of a certain population of macrophages (primarily large cells). Changes in activity of serum lysosomal enzymes also reflect repopulation of liver macrophages.
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