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Articles in PresS, published online ahead of print July 3, 2002
Am J Physiol Gastrointest Liver Physiol, 10.1152/ajpgi.00031.2002
Submitted on January 23, 2002
Accepted on July 2, 2002
1 Surgical Oncology Research Laboratories, Department of Surgery, Massachusetts General Hospital, Boston, MA, USA; Department of Biology, Saint Louis University, St. Louis, MO, USA; Department of Biology, Saint Louis University, St. Louis, MO, USA
2 Department of Biology, Saint Louis University, St. Louis, MO, USA
3 Surgical Oncology Research Laboratories, Department of Surgery, Massachusetts General Hospital, Boston, MA, USA
4 Department of Pediatric Endocrinology, Massachusetts General Hospital, Boston, MA, USA
* To whom correspondence should be addressed. E-mail: bodebp{at}slu.edu.
Human hepatoma cells take up glutamine at rates several-fold 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 ATB - 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 ATB. The 2.9 kb ATB 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 & SN2) were expressed only in well-differentiated hepatomas. ATB mRNA was also expressed in cirrhotic liver, adult and pediatric liver cancer biopsies, but was not detectable in isolated human hepatocytes or fetal liver. While the growth of all hepatomas was glutamine-dependent, competitive inhibition of ATB-mediated glutamine uptake blocked proliferation only in poorly differentiated cells lacking SN1 or SN2 expression and exhibiting low glutamine synthetase mRNA levels.
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