Release of Excess Amyloid β Protein from a Mutant Amyloid β Protein Precursor
Copyright policy )Release of Excess Amyloid β Protein from a Mutant Amyloid β Protein Precursor
The 4-kilodalton amyloid βprotein (Aβ), which forms fibrillar deposits in Alzheimer's disease (AD), is derived from a large protein referred to as the amyloid β protein precursor (βAPP). Human neuroblastoma (M17) cells transfected with constructs expressing wild-type βAPP or a mutant, βAPP ΔNL , recently linked to familial AD were compared. After continuous metabolic labeling for 8 hours, cells expressing β APP ΔNL had five times more of an Aβ-bearing, carboxyl terminal, βAPP derivative than cells expressing wild-type βAPP and they released six times more Aβ into the medium. Thus this mutant βAPP may cause AD because its processing is altered in a way that releases increased amounts of Aβ.
- Case Western Reserve University United States
Amyloid beta-Peptides, Base Sequence, Molecular Sequence Data, Transfection, Polymerase Chain Reaction, Amyloid beta-Protein Precursor, Neuroblastoma, Oligodeoxyribonucleotides, Alzheimer Disease, Mutagenesis, Site-Directed, Tumor Cells, Cultured, Humans, Amino Acid Sequence, Cloning, Molecular
Amyloid beta-Peptides, Base Sequence, Molecular Sequence Data, Transfection, Polymerase Chain Reaction, Amyloid beta-Protein Precursor, Neuroblastoma, Oligodeoxyribonucleotides, Alzheimer Disease, Mutagenesis, Site-Directed, Tumor Cells, Cultured, Humans, Amino Acid Sequence, Cloning, Molecular
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