Expression and processing of fluorescent fusion proteins of amyloid precursor protein (APP)

• Published in: Biochimica et biophysica acta Vol. 1833; no. 6; pp. 1562 - 1571
• Main Authors: Coughlan, Kathleen, Huang, Xiangping, He, Xiangyuan, Chung, Charlotte H.Y., Li, Guangpu, Tang, Jordan
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.06.2013
• Subjects: Amyloid beta-Protein Precursor - metabolism; Amyloid precursor protein; Amyloid-beta; Amyloidosis - metabolism; Amyloidosis - pathology; Animals; Beta-secretase; Blotting, Western; Cell Survival; Cells, Cultured; Fluorescence; Gamma-secretase; Green fluorescence protein; Green Fluorescent Proteins - metabolism; Luminescent Proteins - metabolism; Mice; Neurons - cytology; Neurons - metabolism; Peptide Fragments - metabolism; Protein Processing, Post-Translational; Protein Transport; Recombinant Fusion Proteins - metabolism; Red Fluorescent Protein; Subcellular Fractions; Gamma-secretase; APP106; Green fluorescence protein; sGappβ; sGappα; RappG; sRapp; sGapp; Beta-secretase; GappR; Amyloid precursor protein; Amyloid-beta

Processing of β-amyloid precursor protein (APP) by β- and γ-secretases in neurons produces amyloid-β (Aβ), whose excess accumulation leads to Alzheimer's disease (AD). Knowledge on subcellular trafficking pathways of APP and its fragments is important for the understanding of AD pathogenesis. W...