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LIF, a Novel Myokine, Protects Against Amyloid-Beta-Induced Neurotoxicity via Akt-Mediated Autophagy Signaling in Hippocampal Cells

Authors
Lee, Hye JeongLee, Jung OkLee, Yong WooKim, Shin AeSeo, Il HyeokHan, Jeong AhKang, Min JuKim, Su JinCho, Yun-HoPark, Joong-JeanChoi, Jong-IlPark, Sun HwaKim, Hyeon Soo
Issue Date
6월-2019
Publisher
OXFORD UNIV PRESS
Keywords
LIF; Akt; autophagy; mTOR; myokine; Alzheimer' s disease
Citation
INTERNATIONAL JOURNAL OF NEUROPSYCHOPHARMACOLOGY, v.22, no.6, pp.402 - 414
Indexed
SCIE
SCOPUS
Journal Title
INTERNATIONAL JOURNAL OF NEUROPSYCHOPHARMACOLOGY
Volume
22
Number
6
Start Page
402
End Page
414
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/65347
DOI
10.1093/ijnp/pyz016
ISSN
1461-1457
Abstract
Background: Leukemia inhibitory factor, a novel myokine, is known to be associated with neural function, but the underlying molecular mechanism remains unclear. Methods: HT-22 mouse hippocampal cells, primary hippocampal cells, and Drosophila Alzheimer's disease model were used to determine the effect of leukemia inhibitory factor on neurons. Immunoblot analysis and immunofluorescence method were used to analyze biological mechanism. Results: Leukemia inhibitory factor increased Akt phosphorylation in a phosphoinositide-3-kinase-dependent manner in hippocampal cells. Leukemia inhibitory factor also increased the phosphorylation of the mammalian target of rapamycin and the downstream S6K. Leukemia inhibitory factor stimulated the phosphorylation of signal transducer and activator of transcription via extracellular signal-regulated kinases. Leukemia inhibitory factor increased c-fos expression through both Akt and extracellular signal-regulated kinases. Leukemia inhibitory factor blocked amyloid beta-induced neural viability suppression and inhibited amyloid beta-induced glucose uptake impairment through the block of amyloid beta-mediated insulin receptor downregulation. Leukemia inhibitory factor blocked amyloid beta-mediated induction of the autophagy marker, microtubule-associated protein 1A/1B-light chain 3. Additionally, in primary prepared hippocampal cells, leukemia inhibitory factor stimulated Akt and extracellular signal-regulated kinase, demonstrating that leukemia inhibitory factor has physiological relevance in vivo. Suppression of the autophagy marker, light chain 3II, by leukemia inhibitory factor was observed in a Drosophila model of Alzheimer's disease. Conclusions: These results demonstrate that leukemia inhibitory factor protects against amyloid beta-induced neurotoxicity via Akt/extracellular signal-regulated kinase-mediated c-fos induction, and thus suggest that leukemia inhibitory factor is a potential drug for Alzheimer's disease.
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