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P4–040: Amyloid–beta 1–42 induces cytoplasmic vacuolization and Apo J /clusterin expression in human astrocytes
Author(s) -
Nuutinen Tapio,
Huuskonen Jari,
Miettinen Riitta,
Suuronen Tiina,
Salminen Antero
Publication year - 2006
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2006.05.1778
Subject(s) - vacuolization , clusterin , astrocyte , amyloid beta , endoplasmic reticulum , vacuole , beta (programming language) , microbiology and biotechnology , biology , human brain , cytoplasm , neuroglia , chemistry , biochemistry , peptide , central nervous system , endocrinology , neuroscience , apoptosis , computer science , programming language
mutation was demonstrated by surface plasmon resonance. Furthermore, co-incubation of HspB8 with D-A 1-40 resulted in complete inhibition of D-A 1-40-mediated death of cerebrovascular cells, likely mediated by a reduction both in -sheet formation of D-A 1-40 and its accumulation at the cell surface. In contrast, however, with A 1-42, HspB8 neither affected -sheet formation nor A -mediated cell death. Conclusions: HspB8 might play an important role in regulating A aggregation and, therefore, the development of classic SPs in AD and CAA in HCHWA-D.