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Reelin is a secreted glycoprotein that plays essential roles in the brain. Reelin is specifically cleaved at two distinct sites, called N-t and C-t, with the former being the major one. N-t cleavage can occur both in the extracellular space and in the endosomes, although the physiological importance of endosomal N-t cleavage has not been investigated. In(More)
  • M Koie
  • 1977
The cercaria of Cryptocotyle lingua has simple pointed spines all over the body. Four pointed modified spines occur dorsally in the mouth, and similar spines surround the openings of the penetration glands. The modified spines are shed shortly after penetration and encystment in the fish host. Less than a week after encystment, cytoplasmic folds develop all(More)
The egg of Fasciola hepatica has a smooth surface with a slightly elevated circle marking the fracture of the operculum. The operculum and the aperture have crenated edges. The epithelial cells of the miracidium are covered with long cilia. When miracidia are vibrated in an ultrasonic cleaner the cilia of the epithelial cells of the four posteroir tiers are(More)
Reelin is a glycoprotein essential for brain development and functions. Reelin is subject to specific proteolysis at two distinct (N-t and C-t) sites, and these cleavages significantly diminish Reelin activity. The decrease of Reelin activity is detrimental for brain function, but the protease that catalyzes specific cleavage of Reelin remains elusive. Here(More)
Whole miracidia of Schistosoma mansoni, miracidia vibrated in an ultrasonic cleaner, and the miracidium-sporocyst transition were studied in the stereoscan electron microscope. After vibrating, the cilia broke off near the bases and the epidermal cells, intercellular ridge and sensory structures were revealed. The apical papilla had a folded surface with(More)
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