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Am J Physiol Gastrointest Liver Physiol 283: G1062-G1073, 2002. First published July 3, 2002; doi:10.1152/ajpgi.00031.2002
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Vol. 283, Issue 5, G1062-G1073, November 2002

Molecular and functional analysis of glutamine uptake in human hepatoma and liver-derived cells

Barrie P. Bode1,3, Bryan C. Fuchs3, Bryan P. Hurley1, Jennifer L. Conroy1, Julie E. Suetterlin3, Kenneth K. Tanabe1, David B. Rhoads2, Steve F. Abcouwer1, and Wiley W. Souba1

1 Surgical Oncology Research Laboratories, Department of Surgery and 2 Pediatric Endocrinology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts 02114; and 3 Department of Biology, Saint Louis University, St. Louis, Missouri 63103 - 2010

Human hepatoma cells take up glutamine at rates severalfold faster than the system N-mediated transport rates observed in normal human hepatocytes. Amino acid inhibition, kinetic, Northern blotting, RT-PCR, and restriction enzyme analyses collectively identified the transporter responsible in six human hepatoma cell lines as amino acid transporter B0 (ATB0), the human ortholog of rodent ASCT2. The majority of glutamine uptake in liver fibroblasts and an immortalized human liver epithelial cell line (THLE-5B) was also mediated by ATB0. The 2.9-kb ATB0 mRNA was equally expressed in all cell lines, whereas expression of the system A transporters ATA2 and ATA3 was variable. In contrast, the system N isoforms (SN1 and SN2) were expressed only in well-differentiated hepatomas. ATB0 mRNA was also expressed in cirrhotic liver and adult and pediatric liver cancer biopsies but was not detectable in isolated human hepatocytes or fetal liver. Although the growth of all hepatomas was glutamine dependent, competitive inhibition of ATB0-mediated glutamine uptake blocked proliferation only in poorly differentiated cells lacking SN1 or SN2 expression and exhibiting low glutamine synthetase mRNA levels.

amino acid transporter B0; ASCT2; SN1; SN2; hepatocellular carcinoma; transport; system A


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