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Soluble Neuregulin-1 from Microglia Enhances Amyloid Beta-induced Neuronal Death

Authors
Liew HyunjeongKim Yun-MiChoi Hee SoonJang Ah RamChurchill DavidLee Sang HyungSuh Yoo-Hun
Issue Date
Jan-2016
Publisher
BENTHAM SCIENCE PUBL
Keywords
Amyloid beta peptide; ER stress; ErbB4; microglial cells; neuregulin-1; neuronal cell death
Citation
CNS & NEUROLOGICAL DISORDERS-DRUG TARGETS, v.15, no.8, pp.918 - 926
Journal Title
CNS & NEUROLOGICAL DISORDERS-DRUG TARGETS
Volume
15
Number
8
Start Page
918
End Page
926
URI
http://scholarworks.bwise.kr/kbri/handle/2023.sw.kbri/951
DOI
10.2174/1871527315666160815160505
ISSN
1871-5273
Abstract
Neuregulin-1 (NRG-1) is a ligand of the epidermal growth factor receptor (erbB), and its interaction involves activation of the glutamatergic N-methyl-D-aspartate receptor, which increases the expression of the beta 2 subunit of the gamma-aminobutyric acid receptor and subunits of the nicotinic acetylcholine receptor. In the dentate gyrus of 14-month-old Tg2576 mice, NRG-1 was strongly expressed compared with age-matched controls. The supernatant of oligomeric amyloid beta peptide (A beta(42))-treated glial cells enhanced the A beta(42)-induced cytotoxic effects, but the expression of Fas ligand and tumor necrosis factor-related apoptosis-inducing ligand in microglial cells was not changed upon cytotoxic treatment. This suggests that the oligomeric form of A beta(42) toxicity is not related to apoptosis, which is mediated by cell-to-cell interaction. During the 24-h incubation, the secretion of the soluble form of NRG-1 was increased, but interleukin 6 secretion was not changed. Further, soluble NRG-1 increased A beta(42)-induced toxicity. In conclusion, soluble NRG-1 significantly enhanced oligomeric A beta(42)-induced toxicity through the activation of endoplasmic reticulum stress by the increase of a phospho-translation initiation factor 2 alpha (p-eIF2 alpha).
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