Release of lysosomal enzymes in Candida albicans phagocytosis by rat peritoneal macrophages.
The present paper reports the in vitro release of lysosomal enzymes in the supernatant of cultures of rat peritoneal macrophages, with the addition of Candida albicans cells. Macrophages were taken from the rat peritoneal cavity 72 hr after non-specific activation with Brain-Heart-Infusion (B.H.I.) broth containing 10% proteose-peptone No. 3. They were then cultured in Parker medium No. 199 (TC 199). After 24 hr a suspension of Candida albicans cells, in a determined concentration, was added to the peritoneal macrophage cultures. At that time, and during pre-determined periods, the following enzymes in the culture supernatants were studied using colorimetric methods: beta-glucuronidase, beta-galactosidase and acid phosphatase. It is concluded that, under identical conditions, the release of beta-galactosidase and acid phosphatase is higher than for beta-glucuronidase. The release rate of all three enzymes is the highest at a 6 hr incubation period, after which, a gradual decrease leads to the rate down to 50% at 24 hr.
D000135:Acid Phosphatase / Q000378:metabolism; D000818:Animals; D002176:Candida albicans; D005966:Glucuronidase / Q000378:metabolism; D008247:Lysosomes / Q000201:enzymology*; D008264:Macrophages / Q000201:enzymology / Q000378:metabolism*; D010587:Phagocytosis; D051381:Rats; D001616:beta-Galactosidase / Q000378:metabolism
D000135:Acid Phosphatase; D001616:beta-Galactosidase; D005966:Glucuronidase