This study reveals the expressions of Alzheimer's disease-related amyloid precursor protein, presenilin-1, and a presynaptic marker protein, synaptophysin, in the archi-, paleo- and neocerebellum during the postnatal development of the rat. The Western blot results demonstrate a gradual increase in the soluble amyloid precursor protein level in the archicerebellum during the first 3 weeks, while in the neo- and paleocerebellum the levels reach a plateau as early as the 1st week. Immunohistochemically, the protein is present in the deep part of the external granule cell layer and the internal granule cell layer in the newborn animal, while in 3-week-old animals the staining appears mainly in the perikarya and dendrites of the Purkinje cells. The level of synaptophysin increases progressively from postnatal day 7 up to 3 weeks in the archi- and paleocerebellum, and up to 6 weeks in the neocerebellum. Immunohistochemically, the amyloid precursor protein staining appears first in the inner part of the molecular layer and in the internal granule cell layer. In a 3-week-old animal, synaptophysin staining is present in all areas of the cerebellar molecular layer and in the internal granule cell layer. The presenilin-1 immunohistochemical reaction appeared equally in the archi-, paleo- and neocerebellum. Much of the staining is present in the glial cells and Purkinje cells. Less immunoreactivity is observed in the Golgi cells and granule cells. It is concluded that the postnatal expressions of soluble and membrane-bound amyloid precursor protein, synaptophysin and presenilin-1 are regulated differently during the ontogenetical development of the archi-, paleo- and neocerebellum of rat. Further, the amyloid precursor protein and presenilin-1 may be present in cells which do not degenerate in Alzheimer's disease. Copyright (C) 2000 Elsevier Science Ltd.
- Amyloid precursor protein
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience
- Cell Biology