Browsing by Subject "Acid phosphatase"

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    In vitro effects of hormones and autacoids on the activity of acid phosphatase in the lysates of endotoxin-activated rat peritoneal and bronchoalveolar macrophages
    (Murcia : F. Hernández, 2003) Kondomerkos, D.J.; Kalamidas, Stefanos; Kotoulas, Othon B.
    Peritoneal and bronchoalveolar macrophages activated in vitro by endotoxin, exhibit alterations in the acid phosphatase activity of cell lysates when certain hormones or autacoids are present in the culture medium. They also show morphological changes concerning general appearance and acid phosphatase cytochemistry. Certain agents known to increase the intracellular levels of cyclic AMP, such as dopamine and prostaglandin E2, decreased this enzyme activity in the lysates of peritoneal macrophages. Adrenalin had no effect on this activity at 14 hours, but was found to increase the activity in the culture medium at the initial hours of incubation. Glucagon decreased whereas insulin increased acid phosphatase activity in bronchoalveolar macrophages. Serotonin or histamine, known to activate phospholipase C, increased this activity in peritoneal or bronchoalveolar macrophages. The results of this study, taken together with previously published data (Kondomerkos et al., 2003), suggest that hormones and autacoids may control certain parameters of macrophage activation including acid phosphatase activity.
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    Ultrastructural localisation of acid phosphatase in intestinal eosinophilic granule cells (EGC) of rainbow trout
    (Murcia : F. Hernández, 1992) Powell, Mark D.; Briand, Heather A.; Wright, Glenda M.; Burka, John F.
    Enzyme cytochemistry was used to investigate possible lysosome involvement in capsaicin induced degranulation of the eosinophilic granule cell (EGC) of the rainbow trout intestine. Three adult rainbow trout (Oncorhynchus mykiss) were injected intra 'k eritoneally with capsaicin in a saline vehicle (0.5 pg.g- body weight). Following a 2 hour period of incubation, the fish were killed, and a mid portion of the intestine was dissected and fixed in cold glutaraldehyde buffered with sodium cacodylate. Vibratome sections were incubated in either reaction medium containing B-glycerophosphate and cerium chloride in acetate buffer or substrate (Bglycerophosphate) deficient control medium. Sections were then refixed in osmium tetroxide and processed for electron microscopy. Acid phosphatase was found to be localised within lysosomes. The enzyme was not found in the large cytoplasmic granules under normal or capsaicin-stimulated conditions. EGCs which had migrated to the lamina propria in response to the capsaicin stimulation had a distinct multivesicular granule morphology. These multivesicular granules did not contain acid phosphatase suggesting that this form of EGC degranulation is not a lysosomally mediated event.