KMID : 0624620160490080437
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BMB Reports 2016 Volume.49 No. 8 p.437 ~ p.442
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Critical role of protein L-isoaspartyl methyltransferase in basic fibroblast growth factor-mediated neuronal cell differentiation
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Dung To Thi Mai
Yi Young-Su Heo Ji-Eun Yang Woo-Seok Kim Ji-Hye Kim Han-Gyung Park Jae-Gwang Yoo Byong-Chul Cho Jae-Youl Hong Sung-Youl
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Abstract
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We aimed to study the role of protein L-isoaspartyl methyltransferase (PIMT) in neuronal differentiation using basic fibroblast growth factor (bFGF)-induced neuronal differentiation, characterized by cell-body shrinkage, long neurite outgrowth, and expression of neuronal differentiation markers light and medium neurofilaments (NF). The bFGF-mediated neuronal differentiation of PC12 cells was induced through activation of mitogen-activated protein kinase (MAPK) signaling molecules [MAPK kinase 1/2 (MEK1/2), extracellular signal-regulated kinase 1/2 (ERK1/2), and p90RSK], and phosphatidylinositide 3-kinase (PI3K)/Akt signaling molecules PI3Kp110¥â, PI3Kp110¥ã, Akt, and mTOR. Inhibitors (adenosine dialdehyde and S-adenosylhomocysteine) of protein methylation suppressed bFGF-mediated neuronal differentiation of PC12 cells. PIMTeficiency caused by PIMT-specific siRNA inhibited neuronal differentiation of PC12 cells by suppressing phosphorylation of MEK1/2 and ERK1/2 in the MAPK signaling pathway and Akt and mTOR in the PI3K/Akt signaling pathway. Therefore, these results suggested that PIMT was critical for bFGF-mediated neuronal differentiation of PC12 cells and regulated the MAPK and Akt signaling pathways.
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KEYWORD
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Akt, Basic fibroblast growth factor, Mitogen-activated protein kinase, Neuronal differentiation, Phosphatidylinositide 3-kinase, Protein L-isoaspartyl methyltransferase
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