acid-phosphatase and Trypanosomiasis

Histochemical variations in tissues from rats inoculated with Trypanosoma lewisi and Trypanosoma rhodesiense were investigated. During peak parasitemia, the liver of rats inoculated with T lewisi showed increased glycogen distribution. However, glycogen depletion was noted in the liver and spleen of animals inoculated with living cells of T rhodesiense. Depletion was very apparent from day 4 to day 10. Throughout the period of observation, only a small amount of lipid infiltration occurred in tissues from animals inoculated with both organisms. Protein tests revealed a normal distribution of protein in tissues. Sections of the liver from rats inoculated with T lewisi showed strong alkaline phosphatase activity on days 7, 10, and 13. Alkaline phosphatase activity for T rhodesiense-infected animals was positive for days 4, 7, and 10. Strong positive reactions for acid phosphatase were observed on days 10 and 13 for some tissues (liver, spleen, and kidney) from rats inoculated with T lewisi. On days 4, 7, and 10, intense staining reactions also were observed for livers and spleens of animals inoculated with T rhodesiense. Regardless of tissues observed, histochemical variations were not observed in animals inoculated with the derivatives (ie, metabolic products and homogenates) of T lewisi and T rhodesiense.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Female; Glycogen; Histocytochemistry; Lipid Metabolism; Lipids; Rats; Rats, Inbred Strains; Tissue Distribution; Trypanosoma brucei brucei; Trypanosoma lewisi; Trypanosomiasis

MACROPHAGE ACTIVITY WAS STUDIED IN RATS INFECTED WITH TRYPANOSOMA LEWISI IN THREE PROTOCOL GROUPS: one group was fed complete diet, a second group was given a vitamin B(12)-deficient diet, and a third group was fed a pair-fed control (calorically restricted) diet. Throughout the observational period, in animals fed complete and pairfed diets, marked increases in acid phosphatase levels in peritoneal macrophages were directly related to the degree of parasitemia. Acid phosphatase levels in rats deprived of vitamin B(12) were approximately one third that of animals with an adequate supply of the vitamin. Irrespective of the diets, the infection with T lewisi also elicited increased macrophage phagocytosis of polystyrene latex particles and macrophage spreading. Both of these activities occurred at a much slower rate in the vitamin B(12)-deficient animals.

Topics: Acid Phosphatase; Animals; Female; Macrophages; Phagocytosis; Rats; Rats, Inbred Strains; Trypanosoma lewisi; Trypanosomiasis; Vitamin B 12 Deficiency

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alcohol Oxidoreductases; Animals; Cell Fractionation; Centrifugation, Isopycnic; Eukaryota; Glycerolphosphate Dehydrogenase; Glycerophosphates; Glycolysis; Isocitrate Dehydrogenase; Malate Dehydrogenase; Microbodies; Mitochondria; Organoids; Protein Binding; Superoxide Dismutase; Trypanosoma brucei brucei; Trypanosomiasis

We have screened the bloodstream form of Trypanosoma brucei for the presence of enzymes that could serve as markers for the microbodies and the highly repressed mitochondrion of this organism. None of seven known microbody enzymes were detected at all, but glycerol-3-phosphate oxidase, ATPase, isocitrate dehydrogenase, acid phosphatase and part of the hyperoxide dismutase and malate dehydrogenase activities were found to be particle-bound after fractionation of homogenates by differential centrifugation. Part of the ATPase activity was sensitive to oligomycin, an inhibitor of oxidative phosphorylation. This oligomycin-sensitive activity can serve as a specific marker for the mitochondria. More than 80% of the NAD+-linked glycerol-3-phosphate dehydrogenase in T. brucei was found to be particulate and latent. The enzyme could be activated by Triton X-100, by the combined action of sonication and salt, but not by salt alone, and partially by freezing and thawing. We conclude that the NAD+-linked glycerol-3-phosphate dehydrogenase is located inside an organelle.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alcohol Oxidoreductases; Animals; Cell Fractionation; Cell Nucleus; Enzyme Activation; Glycerolphosphate Dehydrogenase; Glycerophosphates; Isocitrate Dehydrogenase; Malate Dehydrogenase; Microbodies; Microsomes; Mitochondria; NAD; Protein Binding; Superoxide Dismutase; Trypanosoma brucei brucei; Trypanosomiasis

Topics: Acid Phosphatase; Animals; Arteriosclerosis; Cholesterol; Daunorubicin; DNA; Ethidium; Heart; Humans; Hydrolases; Lysosomes; Mice; Muscles; Neoplasms; Parasitic Diseases; Pinocytosis; Rabbits; Subcellular Fractions; Trypanosoma cruzi; Trypanosomiasis

Topics: Acid Phosphatase; Africa; Africa, Eastern; Africa, Western; Histocytochemistry; Humans; Trypanosoma; Trypanosomiasis; Trypanosomiasis, African; Virulence