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In: NBER Working Paper No. w31817
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In: Jacobs Levy Equity Management Center for Quantitative Financial Research Paper
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In: The Econometrics Journal, Band 19, Heft 3, S. 261-290
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In: The Wharton School Research Paper
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In: Air quality, atmosphere and health: an international journal, Band 8, Heft 3, S. 243-263
ISSN: 1873-9326
In: Materials and design, Band 97, S. 126-130
ISSN: 1873-4197
In: SNA-D-21-02098
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In: Environmental management: an international journal for decision makers, scientists, and environmental auditors, Band 53, Heft 2, S. 266-273
ISSN: 1432-1009
Cordycepin is a bioactive component of the fungus Cordyceps militaris. Previously, we showed that cordycepin can alleviate hyperlipidemia through enhancing the phosphorylation of AMP-activated protein kinase (AMPK), but the mechanism of this stimulation is unknown. Here, we investigated the potential mechanisms of cordycepin-induced AMPK activation in HepG2 cells. Treatment with cordycepin largely reduced oleic acid (OA)-elicited intracellular lipid accumulation and increased AMPK activity in a dose-dependent manner. Cordycepin-induced AMPK activation was not accompanied by changes in either the intracellular levels of AMP or the AMP/ATP ratio, nor was it influenced by calmodulin-dependent protein kinase kinase (CaMKK) inhibition; however, this activation was significantly suppressed by liver kinase B1 (LKB1) knockdown. Molecular docking, fluorescent and circular dichroism measurements showed that cordycepin interacted with the γ1 subunit of AMPK. Knockdown of AMPKγ1 by siRNA substantially abolished the effects of cordycepin on AMPK activation and lipid regulation. The modulating effects of cordycepin on the mRNA levels of key lipid regulatory genes were also largely reversed when AMPKγ1 expression was inhibited. Together, these data suggest that cordycepin may inhibit intracellular lipid accumulation through activation of AMPK via interaction with the γ1 subunit.
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