![]() R., Pfleger, C., Altmuller, J., Herebian, D., Beyer, M., Zollner, H. N., Gorg, B., Friedburg, C., Qvartskhava, N., Budde, B. Mapping of the taurine transporter gene to mouse chromosome 6 and to the short arm of human chromosome 3. W., Azuma, J.Ĭardiac and skeletal muscle abnormality in taurine transporter-knockout mice. Ito, T., Oishi, S., Takai, M., Kimura, Y., Uozumi, Y., Fujio, Y., Schaffer, S. Taurine treatment of retinal degeneration and cardiomyopathy in a consanguineous family with SLC6A6 taurine transporter deficiency. J., Malcles, A., Kecik, M., Rivolta, C., and 11 others. A., Azam, M., Kern, I., Iwaszkiewicz, J., Farooq, O., Pournaras, C. Cultured human cell lines derived from placenta, intestine, cervix (HeLa), and retinal pigment epithelium, which are known to possess Na(+)- and Cl(-)-coupled taurine transport activity, also contained the 6.9-kb transcript.Īnsar, M., Ranza, E., Shetty M., Paracha, S. Northern blot analysis demonstrated that the principal transcript, 6.9 kb in size, is expressed abundantly in placenta and skeletal muscle, at intermediate levels in heart, brain, lung, kidney, and pancreas, and at low levels in liver. The nucleotide sequence of the coding region predicted a 620-amino acid protein with a calculated molecular mass of 69,853. The clone included a coding region of 1,863 bp (including the termination codon). (1994) isolated a cDNA clone highly related to the rat brain taurine transporter. Furthermore, the Northern hybridizations indicated that the taurine transporter is present also in ileal mucosa, brain, liver, and heart.įrom a human placenta cDNA library, Ramamoorthy et al. Northern hybridization indicated that the quantity of mRNA for the taurine transporter in MDCK cells is regulated by hypertonicity. The sequence of the cDNA indicated that the taurine transporter has considerable amino acid sequence similarity to previously cloned Na(+)- and Cl(-)-dependent transporters. (1992) cloned the cDNA for the taurine transporter in MDCK cells. Taurine transport in these cells is dependent on sodium and chloride ions and is localized primarily in the basolateral plasma membrane (summary by Uchida et al., 1992). When MDCK cells cultured in isotonic medium are switched to hypertonic medium, their content of taurine doubles through the taking up of taurine from the medium. Indeed, taurine functions as an osmolyte in Madin-Darby canine kidney (MDCK) cells. The taurine content of the renal medulla of rats infused with 5% NaCl is higher than that in controls, suggesting that taurine behaves as an osmolyte in the renal medulla. Its hypertonicity when the kidney is excreting a concentrated urine is fundamental to water conservation. The renal medulla is normally the only tissue in mammals that undergoes wide shifts in tonicity. The cells of most organisms respond to hypertonicity by the intracellular accumulation of high concentrations of small organic solutes (osmolytes) that, in contrast to high concentrations of electrolytes, do not perturb the function of macromolecules. It is involved in a number of important physiologic processes, including bile acid conjugation in hepatocytes, modulation of calcium flux and neural excitability, osmoregulation, detoxification, and membrane stabilization. Taurine (2-aminoethanesulfonic acid) is a major intracellular amino acid in mammals.
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