The effects of taurine in the mammalian nervous system are numerous and varied. There has been great difficulty in determining the specific targets of taurine action. The authors present a review of accepted taurine action and highlight recent discoveries regarding taurine and calcium homeostasis in neurons. In general there is a consensus that taurine is a powerful agent in regulating and reducing the intracellular calcium levels in neurons. After prolonged L-glutamate stimulation, neurons lose the ability to effectively regulate intracellular calcium. This condition can lead to acute swelling and lysis of the cell, or culminate in apoptosis. Under these conditions, significant amounts of taurine (mM range) are released from the excited neuron. This extracellular taurine acts to slow the influx of calcium into the cytosol through both transmembrane ion transporters and intracellular storage pools. Two specific targets of taurine action are discussed: Na+-Ca2+ exchangers, and metabotropic receptors mediating phospholipase-C.
This is a preview of subscription content, access via your institution.
Buy single article
Instant access to the full article PDF.
Tax calculation will be finalised during checkout.
Subscribe to journal
Immediate online access to all issues from 2019. Subscription will auto renew annually.
Tax calculation will be finalised during checkout.
Maar, T. E., Lund, T. M., Gegelashvili, G., Hartmann-Petersen, R., Moran, J., Pasantes-Morales, H., Berezin, V., Bock, E., and Schousboe, A. 1998. Effects of taurine depletion on cell migration and NCAM expression in cultures of dissociated mouse cerebellum and N2A cells. Amino Acids. 15(1–2):77–88.
Bruhn, T., Christensen, T., Cobo, M., Damgaard, I., Diemer, N. H., and Schousboe A. 1996. Effects of phenylsuccinate on potassium-stimulated taurine release in cultured neurons and astrocytes and in rat hippocampus in vivo. J. Neurosci. Res. 46(2):198–203.
Jacobsen, J. G. and Smith, L. H. 1968. Biochemistry and physiology of taurine and taurine derivatives. Physiol. Rev. 48:24–511.
Hayes, K. C., Carey, R. E., and Schmidt, S. Y. 1975. Retinal degeneration associated with taurine deficiency in the cat. Science 188:949–951.
Pion, P. D., Kittleson, M. D., Rogers, Q. R., and Morris, J. G. 1987. Myocardial failure in cats associated with low plasma taurine: A reversible cardiomyopathy. Science 237:764–768.
Sturman, J. A. 1993. Taurine in development. Physiol. Rev. 73: 119–147.
Moran, J., Salazar, P., and Pasantes-Morales, H. 1988. Effect of tocopherol and taurine on membrane fluidity of retinal rod outer segments. Experimental Eye Research. 45:769–776.
Lazarewicz, J. W., Noremberg, K., Lehmann, A., and Hamberger, A. 1985. Effects of taurine on calcium binding and accumulation in rabbit hippocampal and cortical synaptosomes. Neurochem. Int. 7:421–428.
Lombardini, J. B. 1985. Effects of taurine on calcium ion uptake and protein phosphorylation in rat retinal membrane preparations. J. Neurochem. 45:268–275.
Solia, J. M., Herranz, A. S., Herreras, O., Lerma, J., and Del Rio, R. M. 1988. Does taurine act as an osmoregulatory substance in the rat brain. Neurosci. Lett. 91:53–58.
Wade, J. V., Olson, J. P., Samson, F. E., Nelson, S. R., and Pazdernik, T. L. 1988. A possible role for taurine in osmoregulation within the brain. J. Neurochem. 51:740–745.
Schaffer, S., Takahashi, K., and Azuma, J. 2000. Role of osmoregulation in the actions of taurine. Amino Acids. 19(3–4):527–546.
Kuriyama, K. 1980. Taurine as a neuromodulator. Fed. Proc. 39:2680–2684.
Okamoto, K., Kimura, H., and Sakai, Y. 1983. Evidence for taurine as an inhibitory neurotransmitter in cerebellar stellate interneurons: Selective antagonism by TAG (6–aminomethyl-3–methyl-4H, 1, 2,4–benzothiadiazine-1,1–dioxide). Brain Res. 265(1):163–168.
Lin, C.-T., Su, Y. Y. T., Song, G.-X., and Wu, J.-Y. 1983. Is taurine a neurotransmitter in rabbit retina? Brain Res. 337:293–298.
Lombardini, J. B., Schaffer, S. W., and Azuma, J. (eds). 1992. Taurine: Nutritional Value and Mechanisms of Action. Adv. Expt. Med. & Biol. 315:1–441.
Taber, T. C., Lin, C.-T., Song, G.-X., Thalman, R. H., and Wu, J.-Y. 1986. Taurine in the rat hippocampus-localization and postsynaptic action. Brain Res. 386:113–121.
Cunningham, R. and Miller, R. F. 1976. Taurine: Its selective action on neuronal pathways in the rabbit retina. Brain Res. 117:341–345.
Mandel, P., Pasantes-Morales, H., and Urban, P. F. 1976. Taurine, a putative transmitter in retina. Pages 89–105, in S. L. Bontig (ed.), Transmitters in the Visual Process, Pergamon, Oxford.
Lin, C.-T., Song, G.-X., and Wu, J.-Y. 1985. Ultrastructural demonstration of L-glutamate decarboxylase and cysteinesulfinic acid decarboxylase in rat retina by immunocytochemistry. Brain Res. 331:71–80.
Lin, C.-T., Li, H.-Z., and Wu, J.-Y. 1983. Immunocytochemical localization of L-glutamate decarboxylase, gamma aminobutyric acid transaminase, cysteine-sulfinic acid decarboxylase, aspartate aminotransferase and somatostatin in rat retina. Brain Res. 270:273–283.
Tang, X. W., Deupree, D. L., Sun, Y., and Wu, J.-Y. 1996. Biphasic effect of taurine on excitatory amino acid-induced neurotoxicity. Pages 499–506, in R. J. Huxtable, J. Azuma, M. Nakagawa, K. Kuriyama, and A. Bala, (eds.), Taurine: Basic and Clinical Aspects, Plenum Publishing Co.
El Edrissi, A. and Trenkner, E. 1999. Growth factors and taurine protect against excitotoxicity by stabilizing calcium homeostasis and energy metabolism. J. Neurosci. 19:9459–9468.
Saransari, P. and Oja, S. S. 2000. Taurine and neural cell damage. Amino Acids. 19(3–4):509–526.
Chan-Palay, V., Palay, S. L., Li, C., and Wu, J.-Y. 1982. Sagittal cerebellar micro-bands of taurine neurons: Immunocytochemical demonstration by using antibodies against the taurine synthesizing enzyme cysteinesulfinic acid decarboxylase. Proc. Natl. Acad. Sci. USA 79:4221–4225.
Magnusson, K. R., Madl, J. E., Clements, J. R., Wu, J.-Y., Larson, A. A., and Beitz, A. J. 1988. Co-localization of taurine-and cysteine sulfinic acid decarboxylase-like immunoreactivity in the cerebellum of the rat with the use of a novel monoclonal antibody against taurine. J. Neurosci. 8(12):4551–4564.
Magnusson, K. R., Clements, J. R., Wu, J.-Y., and Beitz, A. J. 1989. Co-localization of taurine-and cysteine sulfinic acid decarboxylase-like immunoreactivity in the hippocampus of the rat. Synapse 4:55–69.
Del Arco, A., Segovia, G., Prieto, L., and Mora, F. 2001. Endogenous glutamate-taurine interaction in striatum and nucleus accumbens of the freely moving rat: studies during the normal process of aging. Mech. Ageing Dev. 122(4):401–414.
Okada, M., Okuma, Y., Osumi, Y., Nishihara, M., Yokotani, K., Ueno, H. 2000. Neurotransmitter contents in the retina of RCS rats. Graefes Arch. Clin. Exp. Ophthalmol. 238(12):998–1001.
Hassel, B., Tauboll, E., and Gjerstad, L. 2001. Chronic lamotrigine treatment increases rat hippocampal GABA shunt activity and elevates cerebral taurine levels. Epilepsy Res. 43(2): 153–163.
Peck, E., Jr. and Awapara, J. 1967. Formation of taurine and isethionic acid in rat brain. Biochim. Biophys. Acta. 141: 499–506.
Sumiz, K. 1962. Oxidation of hypotaurine in rat liver. Biochim. Biophys. Acta. 63:210–212.
Davison, A. N. 1956. Amino acid decarboxylases in rat brain and liver. Biochim. Biophys. Acta. 234:107–108.
Wu, J.-Y. 1982. Purification and characterization of cysteic/cysteinesulfinic acids decarboxylase and L-glutamate decarboxylase in bovine brain. Proc. Natl. Acad. Sci. USA 79:4270–4274.
Blinderman, J. M., Maitre, M., Ossola, L., and Mandel, P. 1978. Purification and some properties of L-glutamate decarboxylase from human brain. Eur. J. Biochem. 86:143–152.
Wu, J.-Y., Su, Y. Y. T., Brandon, C., Lam, D. M. K., Chen, M. S., and Huang, W. M. 1979. Purification and immunochemical studies of GABA-, acetylcholine-and taurine-synthesizing enzymes from bovine and fish brains. Seventh International Meeting of the ISN, p. 662.
Oertel, W. H., Schmechel, D. E., Weise, V. K., Ransom, D. H., Tappaz, M. L., Krutzsch, H. C., and Kopin, I. J. 1981. Comparison of cysteine sulfinic acid decarboxylase isoenzymes and glutamic acid decarboxylase in rat liver and brain. Neuroscience. 6:2701–2714.
Tappaz, M., Almarghini, K., Legay, F., and Remy, A. 1992. Taurine biosynthesis enzyme cysteine sulfinate decarboxylase (CSD) from brain: the long and tricky trail to identification. Neurochem. Res. 17:849–859.
Almarghini, K., Remy, A., and Tapaz, M. 1991. Immunocytochemistry of the taurine biosynthesis enzyme, cysteine sulfinate decarboxylase in the cerebellum. Evidence for a glial localization. Neuroscience. 43:111–119.
Reymond, I., Almarghini, K., and Tappaz, M. 1996. Immunocytochemical localization of cysteine sulfinate decarboxylase in astrocytes in the cerebellum and hippocampus: a quantitative double immunofluorescence study with glial fibrillary acidic protein and S-100 protein. Neuroscience. 75:619–633.
Almarghini, K., Barbagli, B., and Tappaz, M. 1994. Production and characterization of a new specific antiserum against the taurine putative biosynthetic enzyme cysteine sulfinate decarboxylase. J. Neurochem. 62:1604–1614.
Pasantes-Morales, H., Chatagner, F., and Mandel, P. 1980. Synthesis of taurine in rat liver and brain in vivo. Neurochem. Res. 5:441–451.
Tappaz, M., Bitoun, M., Reymond, I., and Sergeant, A. 1999. Characterization of the cDNA coding for rat brain cysteine sulfinate decarboxylase: brain and liver enzymes are identical proteins encoded by two distinct mRNAs. J. Neurochem. 73:903–912.
Kaisaki, P. J., Jerkins, A. A., Goodspeed, D. C., Steele, R. D., and Kaisakia, P. J. 1995. Cloning and characterization of rat cysteine sulfunic acid decarboxylase. Biochim. Biophys. Acta. 1262:79–82.
Reymond, L., Sergeant, A., and Tappaz, M. 1996. Molecular cloning and sequence analysis of the cDNA encoding rat liver cysteine sulfinate decarboxylase (CSD). Biochim. Biophys. Acta. 1307:152–156.
Erlander, M. G. and Tobin, A. J. 1991. The structure and functional heterogeneity of glutamic acid decarboxylase: A review. Neurochem. Res. 16:215–226.
Nathan, B., Bao, J., Hsu, C.-C., Aguilar, P., Wu, R., Yarom, M., Kuo, C.-Y., and Wu, J.-Y. 1994. A membrane form of brain L-glutamate decarboxylase: identification, isolation and its relation to insulin-dependent diabetes mellitus. Proc. Natl. Acad. Sci. (USA). 91:242–246.
Nathan, B., Hsu, C.-C., Bao, J., Wu, R., and Wu, J.-Y. 1994. Purification and characterization of a novel form of brain L-glutamate decarboxylase-A Ca2+-dependent peripheral membrane protein. J. Biol. Chem. 269:7249–7254.
Nathan, B., Bao, J., Hsu, C. C., Yarom, M., Deupree, D. L., Lee, Y. H., Tang, X. W., Kuo, C. Y., Burghen, G. A., and Wu, J.-Y. 1994. An integral membrane protein form of brain L-glutamate Taurine: Synthesis and Its Role in Calcium Homeostasis 25 decarboxylase-purification and characterization. Brain Res. 642:297–302.
Tang, X. W., Hsu, C.-C., Sun, Y., Wu, E., Yang, C. Y., and Wu, J.-Y. 1997. Protein phosphorylation and taurine biosynthesis in vivo and in vitro. J. Neurosci. 17:6947–6951.
Foos, T. and Wu, J.-Y. 2000. The cloning and characterization of two soluble forms of brain cysteine sulfinic acid decarboxylase. J. Neurochem. 74: supple. S38C.
Ramamoorthy, S., Del-Monte, M. A., Leibach, F. H., and Ganapathy, V. 1994. Molecular identity and calmodulin-mediated regulation of the taurine transporter in a human retinal pigment epithelial cell line. Curr. Eye Res. 13:523–529.
Uchida, S., Kwon, H. M., Yamauchi, A., Preston, A. S., Marumo, F., and Handler, J. S. 1992. The molecular cloning of the cDNA for an MDCK cell Na(1)-and Cl(2)-dependent taurine transporter that is regulated by hypertonicity. Proc. Natl. Acad. Sci. USA 89:8230–8234.
Jessen, H. 1994. Taurine and beta-alanine transport in an established human kidney cell line derived from the proximal tubule. Biochim. Biophys. Acta. 1194:44–52.
Chung, S. J., Ramanathan, V., Giacomini, K. M., and Brett, C. M. 1994. Characterization of a sodium-dependent taurine transporter in rabbit choroid plexus. Biochim. Biophys. Acta. 1193:10–16.
Ramamoorthy, S., Leibach, F. H., Mahesh, V. B., Han, H., Yang-Feng, T. Blakely, R. D., and Ganapathy, V. 1994. Functional characterization and chromosomal localization of a cloned taurine transporter from human placenta. Biochem. J. 300:893–900.
Jhiang, S. M., Fithian, L., Smanik, P., McGill, J., Tang, W., and Mazzaferri, E. L. 1993. Cloning of the human taurine transporter and characterization of taurine uptake in thyroid cells. FEBS Lett. 318:139–44.
Brandsch, M., Miyamoto, Y., Ganapathy, V., and Leibach, F. H. 1993. Regulation of taurine transport in human colon carcinoma cell lines (HT-29 and Caco-2) by protein kinase C. Am. J. Physiol. 264:G939–G946.
Liu, Q. R., Lopez-Corcuera, B., Nelson, H., Mandiyan, S., and Nelson, N. 1992. Cloning and expression of a cDNA encoding the transporter of taurine and beta-alanine in mouse brain. Proc. Natl. Acad. Sci. USA 89:12145–12149.
Smith, K. E., Borden, L. A., Wang, C. H., Hartig, R. R. Branchek, T. A., and Weinshank, R. L. 1992. Cloning and expressing of a high affinity taurine transporter from rat brain. Mol. Pharmacol. 42:563–569.
Bitoun, M. and Tappaz, M. 2000. Taurine down-regulates basal and osmolarity-induced gene expression of its transporter, but not the gene expression of its biosynthetic enzymes, in astrocyte primary cultures. J. Neurochem. 3:919–924.
Beetsch, J. W. and Olson, J. E. 1998. Taurine synthesis and cysteine metabolism in cultured rat astrocytes: effects of hyperosmotic exposure. Am J. Physiol. 274(4 Pt 1):C866–874.
Bitoun, M. and Tappaz, M. 2000. Gene expression of the transporters and biosynthetic enzymes of the osmolytes in astrocyte primary cultures exposed to hyperosmotic conditions. Glia 32(2):165–176.
Bitoun, M. and Tappaz, M. 2000. Taurine down-regulates basal and osmolarity-induced gene expression of its transporter, but not the gene expression of its biosynthetic enzymes, in astrocyte primary cultures. J. Neurochem. 75(3):919–924.
Bitoun, M. and Tappaz, M. 2000. Gene expression of taurine transporter and taurine biosynthetic enzymes in brain of rats with acute or chronic hyperosmotic plasma: a comparative study with gene expression of myo-inositol transporter, betaine transporter and sorbitol biosynthetic enzyme. Brain Res. Mol. Brain Res. 77(1):10–18.
Jerkins, A. A. and Steele, R. D. 1992. Quantification of cysteine sulfinic acid decarboxylase in male and female rats: effect of adrenalectomy and methionine. Arch. Biochim. Biophys. 294:534–538.
Jerkins, A. A. and Steele, R. D. 1991. Dietary sulfur amino acid modulation of cysteine sulfinic acid decarboxylase. Am. J. Physiol. 261:551–555.
Bella, D. L., Hahn, C., and Stipanuk, M. H. 1999. Effects of nonsulfur and sulfur amino acids on the regulation of hepatic enzymes of cysteine metabolism. Am. J. Physiol. 277(1 Pt 1):E144–153.
Jerkins, A. A. and Steele, R. D. 1991. Cysteine sulfinic acid decarboxylase activity in response to thyroid hormone administration in rats. Arch. Biochem. Biophys. 286:428–432.
Bella, D. L., Hirschberger, L. L., Hosokawa, Y., and Stipanuk, M. H. 1999. Mechanisms involved in the regulation of key enzymes of cysteine metabolism in rat liver in vivo. Am. J. Physiol. 276(2 Pt 1):E326:335.
Jerkins, A. A., Jones, D. D., and Kohlhepp, E. A. 1998. Cysteine sulfinic acid decarboxylase mRNA abundance decreases in rats fed a high-protein diet. J. Nutr. 128(11):1890–1895.
Trenkner, E., Gargano, A., Scala, P., and Sturman, J. 1992. Taurine synthesis in cat and mouse in vivo and in vitro. Adv. Expt. Med. Biol. 315:7–14.
Bao, J., Cheung, W. Y., and Wu, J.-Y. 1995. Brain L-glutamate decarboxylase: Inhibition by phosphorylation and activation by dephosphorylation. J. Biol. Chem. 270:6464–6467.
Hsu, C.-C., Thomas, C., Chen, W., Davis, K. M., Foos, T., Chen, J. L., Wu, E., Floor, E., Schloss, J. V., and Wu, J.-Y. 1999. Role of synaptic vesicle proton gradient and protein phosphorylation on ATP-mediated activation of membrane associated brain glutamate decarboxylase. J. Biol. Chem. 274:24366–24371.
Hsu, C.-C., Davis, K. M., Jin, H., Foos, T., Floor, E., Chen, W., Tyburski, J. B., Yang, C.-Y., Schloss, J. V., and Wu, J.-Y. 2000. Association of L-glutamate decarboxylase to the 70–KDA heat shock protein as a potential anchoring mechanism to synaptic vesicles. J. Biol. Chem. 275:20822–20828.
Morales-Mulia, S., Morales-Mulia, S., Cardin V., Torres-Marquez M. E., Crevenna A., and Pasantes-Morales H. 2001. Influence of protein kinases on the osmosensitive release of taurine from cerebellar granule neurons. Neurochem. Int. 38(2):153–161.
Chen, W. Q., Jin, H., Nguyen, M., Carr, J., Lee, Y. J., Hsu, C. C., Faiman, M. D., Schloss, J. V., and Wu, J.-Y. Role of taurine in regulation of intracellular calcium level and neuroprotective function in cultured neurons. J. Neurosci. Res. (In Press).
Chen, W. Q., Jin, H., Nguyen, M., Carr, J., Lee, Y. J., Foos, T., Hsu, C. C., Davis, K. M., Schloss, J. V., and Wu, J.-Y. The neuroprotective role of taurine in cultured neurons. Chang-Hua Med. Journal (In Press).
Wu, J.-Y., Chen, W. Q., Tang, X. W., Jin, H., Foos, T., Schloss, J. V., Davis, K. M., Faiman, M. D., and Hsu, C.-C. 2000. Mode of action of taurine and regulation dynamics of its synthesis in the CNS. Pages 35–44, in Della-Corte, L. and Huxtable, R. J. (eds.), Taurine and Excitable Tissues, Vol. 4, Plenum Press.
Takuma, K., Matsuda, T., Hashimoto, H., Asano, S., and Baba, A., 1994. Cultured rat astrocytes possess Na+ - Ca2+ exchanger. Glia 12:336–342.
Hill, D. R., Bowery, N. G., and Hudson, A. L. 1984. Inhibition of GABAB receptor binding by guanyl nucleotides. J. Neurochem. 42:652–657.
Wu, J.-Y., Jin, H., Schloss, J. V., Faiman, M. D., Ningaraj, S. N., Foos, T., and Chen, W. 2001. Neurotoxic effect of acamprosate, n-acetyl-homotaurine, in cultured neurons. J. Biomed. Sci. 8(1):96–103.
Foos, T. and Wu J.-Y. Unpublished data.
Lee, Y.-H., Deupree, D. L., Chen, S. C., Kao, L. S., and Wu, J.-Y. 1994. Role of Ca2+ in AMPA mediated poly phosphoinositides turnover in primary neuronal cultures. J. Neurochem. 62:2325–2332.
About this article
Cite this article
Foos, T.M., Wu, JY. The Role of Taurine in the Central Nervous System and the Modulation of Intracellular Calcium Homeostasis. Neurochem Res 27, 21–26 (2002). https://doi.org/10.1023/A:1014890219513
- cysteinesulfinic acid decarboxylase
- calcium homeostasis
- taurine receptors