JBiSE  Vol.3 No.1 , January 2010
Aquaporin 1-expressing MCF-7 mammary carcinoma cells show enhanced migration in vitro
Abstract: Recent studies have demonstrated that aquaporin (AQP) expression facilitates cell migration and promotes angiogenesis and neutrophil motility. Migration of tumor cells is a crucial step in tumor invasion and metastasis. Here we investigated the expression of AQP in MCF-7 human mammary carcinoma cells and characterized its function in cell migration. Reverse Transcription–Polymerase Chain Reaction, Immunoblot and Immunofluorescence analysis demonstrated two populations of MCF-7 cell clones with low (AQP1L) and high (AQP1H) AQP1 expression and the AQP1 protein expression patterns in the plasma membrane of MCF-7 cells. MCF-7 cell clones (AQP1L and AQP1H) with low and about two-fold higher osmotic water permeability were identified by functional assays with corresponding low and high AQP1 expression. Cell migration rate was remarkably higher in AQP1H cells as compared to AQP1L cells, assessed by wound healing and transwell migration assays. Adenoviral-mediated mRNA and protein expression of AQP1 in AQP1L cells increased their water permeability and migration rate to the level similar to AQP1H cells. The results provided direct evidence that aquaporin-mediated plasma membrane water permeability played an important role in mammary carcinoma cell migration and may be associated with mammary carcinoma invasion and metastasis.
Cite this paper: nullJiang, Y. and Jiang, Z. (2010) Aquaporin 1-expressing MCF-7 mammary carcinoma cells show enhanced migration in vitro. Journal of Biomedical Science and Engineering, 3, 95-100. doi: 10.4236/jbise.2010.31014.

[1]   Preston, G.M., Carroll, T.P., Guggino, W.B. and Agre P. (1992) Appearance of water channels in Xenopus oocytes expressing red cell CHIP 28 protein. Science, 256, 385-387.

[2]   Agre P. (2006) The aquaporin water channels. Proc Am Thorac Soc, 3, 5–13.

[3]   Takata, K., Matsuzaki, T. and Tajika, Y. (2004) Aquaporins: water channel proteins of the cell membrane. Prog Histochem Cytochem, 39, 1-83.

[4]   Agre, P., King, L.S., Yasui, M., Guggino, W.B. and Ottersen, O.P. (2002) Aquaporin water channels–from atomic structure to clinical medicine. J Physiol, 542, 3-16.

[5]   Verkman, A.S. (2002) Physiological importance of aquaporin water channels. Ann Med, 34, 192-200.

[6]   Verkman, A.S. (2005) More than just water channels: unexpected cellular roles of aquaporins. J Cell Sci, 118, 3225-3232.

[7]   Saadoun, S., Papadopoulos, M.C., Chikuma, M.H. and Verkman, A.S. (2005) Impairment of angiogenesis and cell migration by targeted aquaporin-1 gene disruption Nature, 434, 786-792.

[8]   Chikuma, M.H. and Verkman, A.S. (2006) Aquaporin-1 facilitates epithelial cell migration in kidney proximal tubule. J Am Soc Nephrol, 17, 39-45.

[9]   Saadoun, S., Papadopoulos, M.C., Watanabe ,H., Yan, D. and Manley G.T. (2005) Involvement of aquaporin-4 in astroglial cell migration and glial scar formation. J Cell Sci, 118, 5691-5698.

[10]   Loitto, V.M., Forslund, T., Sundqvist, T., Magnusson, K. E. and Gustafsson, M. (2002) Neutrophil leukocyte motility requires directed water influx, J Leukoc Biol, 71, 212-222.

[11]   Loitto, V.M. and Magnusson, K.E. (2004) Hg2+ and small-sized polyethylene glycols have inverse effects on membrane permeability, while both impair neutrophil cell motility. Biochem Biophys Res Commun, 316, 370- 378.

[12]   Bogenrieder, T. and Herlyn, M. (2003) Axis of evil: molecular mechanisms of cancer metastasis. Oncogene, 22, 6524-6536.

[13]   Harlozinska, A. (2005) Progress in molecular mecha- nisms of tumor metastasis and angiogenesis. Anticancer Res, 25, 3327–3333.

[14]   Yang, J.H., Shi, Y.F., Cheng, Q. and Deng, L. (2006) Expression and localization of aquaporin-5 in the epithelial ovarian tumors. Gynecol Oncol, 100, 294-299.

[15]   Mazal, P.R., Susani, M., Wrba, F. and Haitel, A. (2005) Diagnostic significance of aquaporin-1 in liver tumors. Hum Pathol, 36, 1226-1231.

[16]   Warth, A., Mittelbronn, M. and Wolburg, H. (2005) Redistribution of the water channel protein aquaporin-4 and the K+ channel protein Kir4.1 differs in low-and high-grade human brain tumors. Acta Neuropathol, 109, 418-426.

[17]   Solenov, E., Watanabe, H., Manley, G.T. and Verkman, A. S. (2004) Sevenfold-reduced osmotic water permeability in primary astrocyte cultures from AQP-4-deficient mice, measured by a fluorescence quenching method. Am J Physiol Cell Physiol, 286, 426-432.

[18]   Ransom, C.B., O'Neal, J.T. and Sontheimer, H. (2001) Volume-activated chloride currents contribute to the resting conductance and invasive migration of human glioma cells. J Neurosci, 21, 7674-7683.

[19]   Soroceanu, L., Manning, T.J. and Sontheimer, H. (1999) Modulation of glioma cell migration and invasion using Cl- and K+ ion channel blockers. J Neurosci, 19, 5942-5954.