Jump to ContentJump to Main Navigation
Show Summary Details
More options …

Cellular and Molecular Biology Letters

More options …
Volume 12, Issue 3

Issues

Estrogen regulation and ion dependence of taurine uptake by MCF-7 human breast cancer cells

David Shennan
  • Strathclyde Institute of Pharmacy and Biomedical Sciences, Royal College, University of Strathclyde, 204 George Street, Glasgow, UK, G1 1XW
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Jean Thomson
  • Strathclyde Institute of Pharmacy and Biomedical Sciences, Royal College, University of Strathclyde, 204 George Street, Glasgow, UK, G1 1XW
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2007-03-05 | DOI: https://doi.org/10.2478/s11658-007-0011-4

Abstract

It has been reported that estrogen receptor-positive MCF-7 cells express TauT, a Na+-dependent taurine transporter. However, there is a paucity of information relating to the characteristics of taurine transport in this human breast cancer cell line. Therefore, we have examined the characteristics and regulation of taurine uptake by MCF-7 cells. Taurine uptake by MCF-7 cells showed an absolute dependence upon extracellular Na+. Although taurine uptake was reduced in Cl- free medium a significant portion of taurine uptake persisted in the presence of NO3 -. Taurine uptake by MCF-7 cells was inhibited by extracellular β-alanine but not by L-alanine or L-leucine. 17β-estadiol increased taurine uptake by MCF-7 cells: the Vmax of influx was increased without affecting the Km. The effect of 17β-estradiol on taurine uptake by MCF-7 cells was dependent upon the presence of extracellular Na+. In contrast, 17β-estradiol had no significant effect on the kinetic parameters of taurine uptake by estrogen receptor-negative MDA-MB-231 cells. It appears that estrogen regulates taurine uptake by MCF-7 cells via TauT. In addition, Na+-dependent taurine uptake may not be strictly dependent upon extracellular Cl-.

Keywords: Breast cancer; Taurine uptake; Estrogen

  • [1] Huxtable, R.J. Physiological actions of taurine. Physiol. Rev. 72 (1992) 101–163. Google Scholar

  • [2] Lambert, I.H. Regulation of the cellular content of the organic osmolyte taurine in mammalian cells. Neurochem. Res. 29 (2004) 27–63. http://dx.doi.org/10.1023/B:NERE.0000010433.08577.96CrossrefGoogle Scholar

  • [3] Uchida S., Kwon H.M., Yamauchi A., Preston A.S., Marumo F. and Handler J.S. Molecular cloning of the cDNA for an MDCK cell Na+-and Cl-dependent taurine transporter that is regulated by hypertonicity. Proc. Natl. Acad. Sci. USA 89 (1992) 8230–8234. http://dx.doi.org/10.1073/pnas.89.17.8230CrossrefGoogle Scholar

  • [4] Liu Q., Lopez-Corcuera S., Nelson H., Mandiyan S. and Nelson N. Cloning and expression of a cDNA encoding the transporter of taurine and β-alanine in mouse brain. Proc. Natl. Acad. Sci. USA 89 (1992) 12145–12149. http://dx.doi.org/10.1073/pnas.89.24.12145CrossrefGoogle Scholar

  • [5] Jhiang, S.M., Fithian, L., Smanik, P. McGill, J., Tong, Q. and Mazzaferri E.L. Cloning of the human taurine transporter and characterization of taurine uptake in thyroid cells. FEBS Lett. 318 (1993) 139–144. http://dx.doi.org/10.1016/0014-5793(93)80008-ICrossrefGoogle Scholar

  • [6] Ramamoorthy, S., Leibach, F.H., Mahesh, V.B., Han, H., Yang-Feng T., Blakely, R.D. and Ganapathy V. Functional characterization and chromosomal localization of a cloned taurine transporter from human placenta. Biochem. J. 300 (1994) 893–900. Google Scholar

  • [7] Vinnakota, S., Qian, X., Egal, H., Sarthy, V. and Sarkar H. Molecular characterization and in situ localization of a mouse retinal taurine transporter. J. Neurochem. 69 (1997) 2238–2250. http://dx.doi.org/10.1046/j.1471-4159.1997.69062238.xCrossrefGoogle Scholar

  • [8] Lambert, I.H. Taurine transport in Ehrlich ascites tumour cells, Specificity and chloride dependence. Mol. Physiol. 7 (1985) 323–332. Google Scholar

  • [9] Ballatori, N. and Boyer, N.L. Taurine transport in skate hepatocytes. Am. J. Physiol. 262 (1992) G445–G450. Google Scholar

  • [10] Shennan, D.B. Identification of a high affinity taurine transporter which is not dependent on chloride. Bioscience Rep. 15 (1995) 231–239. http://dx.doi.org/10.1007/BF01540457CrossrefGoogle Scholar

  • [11] Bryson, J.M., Jackson, S.C., Wang, H. and Hurley W.L. Cellular uptake of taurine by lactating porcine mammary tissue. Comp. Biochem. Physiol. Part B 128 (2000) 667–673. http://dx.doi.org/10.1016/S1096-4959(00)00361-4CrossrefGoogle Scholar

  • [12] Han, X. Patters, A.B. and Chesney R.W. Transactivation of TauT by p53 in MCF-7 cells: the role of estrogen receptors. Adv. Exp. Med. Biol. 526 (2003) 139–147. Google Scholar

  • [13] Pine, M., Kim, U. and Ip C. Free amino acid pools of rodent mammary tumors. J. Natl. Can. Inst. 69 (1982) 729–735. Google Scholar

  • [14] Beckonert, O., Monnerjahn, J., Bonk, U. and Leibfritz D. Visualizing metabolic changes in breast-cancer tissue using 1H-NMR spectroscopy and self-organizing maps. NMR Biomed. 16 (2003) 1–11. http://dx.doi.org/10.1002/nbm.797CrossrefGoogle Scholar

  • [15] Moreno, A., Rey, M., Montane, J.M., Alonso, J. and Arus C. 1H NMR spectroscopy of colon tumours and normal mucosal biopsies; elevated taurine levels and reduced polyethyleneglycol absorption in tumors may have diagnostic significance. NMR Biomed. 6 (1993) 111–118. http://dx.doi.org/10.1002/nbm.1940060202CrossrefGoogle Scholar

  • [16] Palacin, M., Estevez, R., Bertran, J. and Zorzano A. Molecular biology of mammalian plasma membrane amino acid transporters. Physiol. Rev. 78 (1998) 969–1054. Google Scholar

  • [17] Bhat, H.K. and Vadgama J.V. Role of estrogen receptor in the regulation of estrogen induced amino acid transport of system A in breast cancer and other receptor positive tumor cells. Int. J. Mol. Med. 9 (2002) 271–279. Google Scholar

  • [18] Shennan, D.B., Thomson, J., Gow, I.F., Travers, M.T. and Barber M.C. L-Leucine transport in human breast cancer cells (MCF-7 and MBA-MB-231): kinetics, regulation by estrogen and molecular identity of the transporter. Biochim. Biophys. Acta 1664 (2004) 206–216. http://dx.doi.org/10.1016/j.bbamem.2004.05.008CrossrefGoogle Scholar

  • [19] Storey, B.T., Fugere, C., Lesieur-Brooks, A., Vaslet, C. and Thompson N.L. Adenoviral modulation of the tumor-associated system L amino acid transporter, LAT1, alters amino acid transport, cell growth and 4F2/CD98 expression with cell-type specific effects in cultured hepatic cells. Int. J. Cancer 117 (2005) 387–397. http://dx.doi.org/10.1002/ijc.21169Google Scholar

  • [20] Haussinger, D. The role of cellular hydration in the regulation of cell function. Biochem. J. 313 (1996) 697–710. Google Scholar

  • [21] Grant, A.C., Gow, I.F., Zammit, V.A. and Shennan D.B., Regulation of protein synthesis in lactating rat mammary tissue by cell volume. Biochim. Biophys. Acta 1475 (2000) 39–46. Google Scholar

  • [22] Lang, F., Busch, G.L., Ritter, M., Volkl, H., Waldegger, S., Gulbins, E. and Haussinger D. Functional significance of cell volume regulatory mechanisms. Physiol. Rev. 78 (1998) 247–306. Google Scholar

  • [23] Shennan, D.B., Thomson, J. and Gow, I.F. Osmoregulation of Taurine efflux from cultured human breast cancer cells: comparison with volume-activated Cl-efflux and regulation by extracellular ATP. Cell. Physiol. Biochem. 18 (2006) 113–122. http://dx.doi.org/10.1159/000095178CrossrefGoogle Scholar

  • [24] Tchoumkeu, G.C. and Rebel, G. Characterization of taurine transport in human glioma GL15 cell line: regulation by protein kinase C. Neuropharmacology 35 (1996) 37–44. http://dx.doi.org/10.1016/0028-3908(95)00139-5CrossrefGoogle Scholar

About the article

Published Online: 2007-03-05

Published in Print: 2007-09-01


Citation Information: Cellular and Molecular Biology Letters, Volume 12, Issue 3, Pages 396–406, ISSN (Online) 1689-1392, DOI: https://doi.org/10.2478/s11658-007-0011-4.

Export Citation

© 2007 University of Wrocław, Poland. This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License. BY-NC-ND 3.0

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

[1]
Mengnan Zeng, Meng Li, Miao Li, Beibei Zhang, Benke Li, Li Zhang, Weisheng Feng, and Xiaoke Zheng
Molecules, 2018, Volume 23, Number 9, Page 2293
[2]
Raeesa Gupte, Sarah Christian, Paul Keselman, Joshua Habiger, William M. Brooks, and Janna L. Harris
Brain Imaging and Behavior, 2018
[3]
João M.N. Duarte, Kim Q. Do, and Rolf Gruetter
Neurobiology of Aging, 2014, Volume 35, Number 7, Page 1660

Comments (0)

Please log in or register to comment.
Log in