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Lactosylceramide α2,3-Sialyltransferase Is Induced Via a PKC/ERK/CREB-dependent Pathway in K562 Human Leukemia Cells  

Choi, Hee-Jung (Molecular and Cellular Glycobiology Unit, Department of Biological Sciences, Sungkyunkwan University)
Park, Young-Guk (Department of Orthodondritics, Kyung-Hee University College of Dental Medicine)
Kim, Cheorl-Ho (Molecular and Cellular Glycobiology Unit, Department of Biological Sciences, Sungkyunkwan University)
Publication Information
Molecules and Cells / v.23, no.2, 2007 , pp. 138-144 More about this Journal
Abstract
Previously we showed that the human GM3 synthase gene was expressed during the induction of megakaryocytic differentiation in human leukemia K562 cells by phorbol 12-myristate 13-acetate (PMA). In this study we found that treatment of PMA-induced K562 cells with $G{\ddot{o}}6976$, a specific inhibitor of PKC, and U0126, an inhibitor of the extracellular signal-regulated kinase (ERK) reduced expression of GM3 synthase, whereas wortmannin, an inhibitor of phosphoinositide 3-kinase (PI3K) did not. Moreover, activation of ERK and cAMP response element binding protein (CREB) was prevented by pretreatment with $G{\ddot{o}}6976$ and U0126. PMA stimulated the promoter activity of the 5'-flanking region from -177 to -83 region of the GM3 synthase gene, and mutation or deletion of a CREB site located around -143 of the promoter reduced PMA-stimulated promoter activity, as did the inhibitors $G{\ddot{o}}6976$ and U0126. Our results demonstrate that induction of GM3 synthase during megakaryocytic differentiation in PMA-stimulated human leukemia K562 cells depends upon the PKC/ERK/CREB pathway.
Keywords
CMP-NeuAc; Lactosylceramide ${\alpha}$2,3-Sialyltransferase (GM3 Synthase); Human Leukemia K562 Cells; PKC/ERK/CREB Pathway;
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