Abnormal and deficient processing of β-amyloid precursor protein in familial Alzheimer's disease lymphoblastoid cells
1991; Elsevier BV; Volume: 175; Issue: 2 Linguagem: Inglês
10.1016/0006-291x(91)91572-t
ISSN1090-2104
AutoresAkira Matsumoto, Yoshisada Fujiwara,
Tópico(s)Prion Diseases and Protein Misfolding
ResumoWestern blot analysis showed abnormal processing of β-amyloid precursor protein (APP) in lymphoblastoid cell lines (LCLs) of familial Alzheimer's disease (FAD). Antibody raised against central APP751 revealed that media of early and late-onset FAD LCLs had highly increased amounts of a 120 kD long-lived, SDS-stable, heat-labile complex of the Kunitz protease inhibitor domain of secreted APP and a ∼70 kD FAD-specific, yet unidentified serine protease. Antibody against the βA4-cytoplasmic domain showed a slower APP processing and increased amounts of 16 kD C-terminal preamyloid in lysates of early and late-onset FAD LCLs, first indicating a deficient intra-βA4 proteolysis in FAD as a possible cause of abundant amyloid deposits in AD brain.
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