Mol. Cells 2007; 23(2): 138~144  
Lactosylceramide α2,3-Sialyltransferase Is Induced Via a PKC/ERK/CREB-dependent Pathway in K562 Human Leukemia Cells
Hee-Jung Choi, Young-Guk Park, Cheorl-Ho Kim
© The Korean Society for Molecular and Cellular Biology. All rights reserved.

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?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?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?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 α2,3-Sialyltransferase, (GM3 Synthase); Human Leukemia K562 Cells;, PKC/ERK/CREB Pathway

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30 September 2021 Volume 44,
Number 9, pp. 627~698
COVER PICTURE Non-mitochondrial localization of the N-terminal-deleted mutant form of ACSL1 in Cos7 cells. Green, ACSL1 mutant; Red, mitotracker; Blue, DAPI (Nan et al., pp. 637-646).

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