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Open AccessArticle

Upregulation of Human ST8Sia VI (α2,8-Sialyltransferase) Gene Expression by Physcion in SK-N-BE(2)-C Human Neuroblastoma Cells

1
Department of Medicinal Biotechnology, College of Health Sciences, Dong-A university, Busan 49315, Korea
2
Department of Horticultural Bioscience, Pusan National University, Miryang 50463, Korea
3
Research Center for Anti-Aging Technology Development, Pusan National University, Busan 46241, Korea
4
Molecular and Cellular Glycobiology Unit, Department of Biological Sciences, SungKyunKwan University, Kyunggi-Do 16419, Korea
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Academic Editor: Li Yang
Int. J. Mol. Sci. 2016, 17(8), 1246; https://doi.org/10.3390/ijms17081246
Received: 3 June 2016 / Revised: 28 June 2016 / Accepted: 25 July 2016 / Published: 2 August 2016
(This article belongs to the Special Issue Glycan–Receptor Interaction)
In this research, we firstly demonstrated that physcion, an anthraquinone derivative, specifically increased the expression of the human α2,8-sialyltransferase (hST8Sia VI) gene in SK-N-BE(2)-C human neuroblastoma cells. To establish the mechanism responsible for the up-regulation of hST8Sia VI gene expression in physcion-treated SK-N-BE(2)-C cells, the putative promoter region of the hST8Sia VI gene was functionally characterized. Promoter analysis with serially truncated fragments of the 5′-flanking region showed that the region between −320 and −240 is crucial for physcion-induced transcription of hST8Sia VI in SK-N-BE(2)-C cells. Putative binding sites for transcription factors Pax-5 and NF-Y are located at this region. The Pax-5 binding site at −262 to −256 was essential for the expression of the hST8Sia VI gene by physcion in SK-N-BE(2)-C cells. Moreover, the transcription of hST8Sia VI induced by physcion in SK-N-BE(2)-C cells was inhibited by extracellular signal-regulated protein kinase (ERK) inhibitor U0126 and p38 mitogen-activated protein kinase (MAPK) inhibitor SB203580, but not c-Jun N-terminal kinase (JNK) inhibitor SP600125. These results suggest that physcion upregulates hST8Sia VI gene expression via ERK and p38 MAPK pathways in SK-N-BE(2)-C cells. View Full-Text
Keywords: physcion; hST8Sia VI; SK-N-BE(2)-C; transcription factor Pax-5; signal pathway physcion; hST8Sia VI; SK-N-BE(2)-C; transcription factor Pax-5; signal pathway
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Yoon, H.-K.; An, H.-K.; Ko, M.J.; Kim, K.-S.; Mun, S.-W.; Kim, D.-H.; Kim, C.M.; Kim, C.-H.; Choi, Y.W.; Lee, Y.-C. Upregulation of Human ST8Sia VI (α2,8-Sialyltransferase) Gene Expression by Physcion in SK-N-BE(2)-C Human Neuroblastoma Cells. Int. J. Mol. Sci. 2016, 17, 1246.

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