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- W1994434045 abstract "Immunoglobulin-binding protein (BiP), also known as the 78-kDa glucose-regulated protein 78 (GRP78), is an abundant endoplasmic reticulum (ER) chaperone that is rapidly induced by ER stress.Recently, studies have demonstrated Bip increased in the cortex and hippocampus of patients with Alzhemer's Disease (AD). A mutation of Sil1, an important co-chaperon of Bip, causes ataxia and neurodegeneration. We constructed the plasmids of Bip and Sil1 and transfected them into HEK293/tau or N2a cells. Tau hyperphosphorylation and glycogen synthase kinase-3β (GSK-3β) activation were detected by by Western blotting. The association with tau, Bip and GSK-3β was analysised by immunoprecipitation. Bip was found increased while Sil1 was reduced in the brains of Tg2576 mice compared to the age-matched control mice. We constructed Bip-EGFP plasmid and transfected it into HEK293/tau or N2a cells and found that overexpression of Bip induced tau hyperphosphorylation via activating GSK-3β, and increased association with tau and GSK-3β. Transfection of Sil1 plasmid could inverse the above. Increasing of Bip in AD brain and ER stress may be an important upstream factor of tau hyperphosphorylation." @default.
- W1994434045 created "2016-06-24" @default.
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- W1994434045 date "2014-07-01" @default.
- W1994434045 modified "2023-09-27" @default.
- W1994434045 title "P3-054: OVEREXPRESSION OF BIP-INDUCED TAU HYPERPHOSPHORYLATION AND REVERSED BY SIL1" @default.
- W1994434045 doi "https://doi.org/10.1016/j.jalz.2014.05.1142" @default.
- W1994434045 hasPublicationYear "2014" @default.
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