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• W459647400 abstract "Alzheimer’s disease (AD) is characterized by loss of higher brain functions and appearance of specific pathological lesions such as neurofibrillary tangles, s-amyloid plaques and neuronal degeneration. As s-amyloid generation and accumulation occur very early in the disease process the fate and role of its precursor proteins (s-APPs) is important for understanding AD pathogenesis. The primary structure of s-APP resembles glycosylated cell surface proteins (Kang et al., 1987) and they can be proteolyzed in two different ways giving rise either to extracellular secreted C-terminal truncated molecules or to the s-amyloid peptide (Haass and Selkoe, 1993). Different length isoforms of s-APP are derived from alternative NA splicing (s-APP695, s-APP751, s-APP770) all of which may be N-and O-glycosylated (Weidemann et al., 1989). The s-APP gene products are expressed in different tissues and show highest abundance in neurons in the brain (Shivers et al., 1988). Co-localization of B-APP with synaptophysin was found at synaptic sites (Schubert et al., 1991) and s-APP levels, in particular s-APP695, increase transiently during synaptogenesis in rats (Loftier and Huber, 1992). The potential roles of s-APPs in higher brain function were explored by intracerebroventricular injection of anti-s-APP antibodies in rats followed by behavioural analysis(Huber et al., 1993) and by comparison of s-APP levels in brains of rats with different “cognitive” capabilities." @default.
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• W459647400 date "1997-01-01" @default.
• W459647400 modified "2023-09-23" @default.
• W459647400 title "ß-Amyloid Precursor Protein — Role in Cognitive Brain Function?" @default.
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• W459647400 doi "https://doi.org/10.1007/978-1-4612-4116-4_14" @default.
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