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Title: Modulation of succinate transport in Hep G2 cell line by PKC
Authors: Piyarat Srisawang
Atip Chatsudthipong
Varanuj Chatsudthipong
Mahidol University
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Jun-2007
Citation: Biochimica et Biophysica Acta - Biomembranes. Vol.1768, No.6 (2007), 1378-1388
Abstract: The cellular uptake of the tricarboxylic acid cycle (TCA) intermediates is very important for cellular metabolism. However, the transport pathways for these intermediates in liver cells are not well characterized. We have examined the transport of succinate and citrate in the human hepatoma cell line Hep G2 and found that it exhibited a higher rate of succinate compared to citrate transport, which was sodium dependent. Comparison of the transport properties of Hep G2 to that of human retinal pigment epithelial (HRPE) cells transfected with human sodium dicarboxylate transporters, hNaDC-1, hNaDC-3, and hNaCT indicated that Hep G2 cells express a combination of hNaDC-3 and hNaCT. Short period activation of protein kinase C (PKC) by phorbol 12-myristate, 13-acetate (PMA) and α-adrenergic receptor agonist, phenylephrine (PE), downregulated sodium-dependent succinate transport presumably via hNaDC-3. The inhibition by PMA was partially prevented by cytochalasin D, suggesting that PKC reduces the hNaDC-3 activity, at least in part, by increased endocytosis. In contrast, activation of PKA by both forskolin and epidermal growth factor (EGF) had no effect on succinate transport. Our results suggest that Hep G2 cells provide a useful model for studies of di- and tricarboxylate regulation of human liver. © 2007 Elsevier B.V. All rights reserved.
ISSN: 00052736
Appears in Collections:Scopus 2006-2010

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