Spermine oxidase promotes bile canalicular lumen formation through acrolein production

Scientific Reports
Takeshi UemuraHiroshi Ikegaya

Abstract

Spermine oxidase (SMOX) catalyzes oxidation of spermine to generate spermidine, hydrogen peroxide (H2O2) and 3-aminopropanal, which is spontaneously converted to acrolein. SMOX is induced by a variety of stimuli including bacterial infection, polyamine analogues and acetaldehyde exposure. However, the physiological functions of SMOX are not yet fully understood. We investigated the physiological role of SMOX in liver cells using human hepatocellular carcinoma cell line HepG2. SMOX localized to the bile canalicular lumen, as determined by F-actin staining. Knockdown of SMOX reduced the formation of bile canalicular lumen. We also found that phospho-Akt (phosphorylated protein kinase B) was localized to canalicular lumen. Treatment with Akt inhibitor significantly reduced the formation of bile canalicular lumen. Acrolein scavenger also inhibited the formation of bile canalicular lumen. PTEN, phosphatase and tensin homolog and an inhibitor of Akt, was alkylated in a SMOX-dependent manner. Our results suggest that SMOX plays a central role in the formation of bile canalicular lumen in liver cells by activating Akt pathway through acrolein production.

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Citations

Feb 15, 2018·Medical Sciences : Open Access Journal·Manuela CervelliPaolo Mariottini
Jun 5, 2019·Journal of Enzyme Inhibition and Medicinal Chemistry·Lidan SunChunyu Cao
Jun 3, 2021·Medical Sciences : Open Access Journal·Shima Nakanishi, John L Cleveland

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Methods Mentioned

BETA
transfection
PCR
protein assay

Software Mentioned

GraphPad
GraphPad Prism

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