One of the pathological lesions in Alzheimer's disease (AD) is the amyloid or senile plaque. The plaque core is predominantly made up of amyloid beta peptide (AP), a 42-43 amino acid peptide derived from amyloid precursor protein (APP). APP is a membrane bound glycoprotein which is expressed ubiquit
CLN3 Protein Regulates Lysosomal pH and Alters Intracellular Processing of Alzheimer's Amyloid-β Protein Precursor and Cathepsin D in Human Cells
✍ Scribed by Adam A. Golabek; Elizabeth Kida; Mariusz Walus; Wojciech Kaczmarski; Martin Michalewski; Krystyna E. Wisniewski
- Book ID
- 115639688
- Publisher
- Elsevier Science
- Year
- 2000
- Tongue
- English
- Weight
- 280 KB
- Volume
- 70
- Category
- Article
- ISSN
- 1096-7192
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## Abstract The amyloid precursor protein (APP) is cleaved enzymatically by nonamyloidogenic and amyloidogenic pathways. α‐Secretase (α‐secretase), cleaves APP within the β‐amyloid (Aβ) sequence, resulting in the release of a secreted fragment of APP (αAPPs) and precluding Aβ generation. In this st
Both neural and nonneural human tissues from patients with or without Alzheimer's disease (AD) were surveyed to detect the presence of the P-amyloid protein and its precursors. This was accomplished using polyclonal and monoclonal antibodies to epitopes in the 695 amino acid long p-APP (i.e., P-APPm