Histochemistry and histoenzymology of the hydatid cyst (Echinococcus granulosus Batsch, 1786). II. Scolices and brood capsules.
Scolices and brood capsules of healthy hydatid cysts from lungs of human patients were studied with histochemical and histoenzymatic methods. The subtegumental and flame cells were sepcially rich in glycogen, RNA and some dehydrogenases such as SDH, MDH, NADH-reductase and G-6-PDH. The rostellar zone or invaginated pole, an area of marked contractile movements, showed intense activity in ATP'ase and simple esterase. The so-called excretory pole shows strong activity in simple esterases, lipase, beta-HBH, alpha-GDH and NADPH-reductase. Lipids are also abundant in this zone implying the important role of this metabolic path in the development of the parasite. Intense activity in alkaline phosphatase was observed in cells associated to the calcereous corpuscles. The largest corpuscles were devoid of enzymatic activity. The enzyme could play some role in the calcification of the corpuscles. Wide enzymatic variations are described according to morphology being orthoscolices the most rich in enzyme activity. Accumulations of small cells surrounded by specialized cells on the germinal membrane are interpreted as the origin or "embryo" of brood capsules. Some enzymes detected in the wall of mature brood capsules depicted alternating types of cells. Some of them are positive for ATP'ase that may be related to active transport of substances across the brood capsule wall. The intenst ATP'ase activity at the stalks of scolices may be similarly interpreted. However, a miosine-like activity is a more feasible explanation since this area showed striking contractile movements in vivo.
D000251:Adenosine Triphosphatases / Q000032:analysis; D000429:Alcohol Oxidoreductases / Q000032:analysis; D000469:Alkaline Phosphatase / Q000032:analysis; D000818:Animals; D004446:Echinococcus / Q000032:analysis* / Q000201:enzymology; D004950:Esterases / Q000032:analysis; D006003:Glycogen / Q000032:analysis; D006651:Histocytochemistry; D008049:Lipase / Q000032:analysis; D050356:Lipid Metabolism; D008055:Lipids / Q000032:analysis; D009124:Muscle Proteins; D009247:NADH, NADPH Oxidoreductases / Q000032:analysis; D012313:RNA / Q000032:analysis
D008055:Lipids; D009124:Muscle Proteins; D012313:RNA; D006003:Glycogen; D000429:Alcohol Oxidoreductases; D009247:NADH, NADPH Oxidoreductases; D004950:Esterases; D008049:Lipase; D000469:Alkaline Phosphatase; D000251:Adenosine Triphosphatases