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Amino Acids

, Volume 17, Issue 3, pp 301–313 | Cite as

Taurine modulates expression of transporters in rat brain and heart

  • O. Labudova
  • C. Yeghiazarjan
  • H. Höger
  • G. Lubec
Full Papers

Summary

In pro- and eucaryotic life, cellular and subcellular compartments are separated by membranes and the regulated and selective passage of specific molecules across these membranes is a basic and highly conserved principle.

We were interested whether taurine, a naturally occuring amino acid, would be able to induce or suppress expression of transporters with the Rationale that taurine was shown to detoxify a series of endogenous toxins and xenobiotics of various chemically non-related structures.

For this purpose we used a gene hunting technique, subtractive hybridization, subtracting mRNAs of taurine-treated rat brain and heart from untreated controls. Subtracted mRNAs were then converted to cDNAs, amplified, sequenced and identified by gene bank data.

We found five transporter transcripts, the phosphonate transport ATPase PHNC, multidrug transporter homolog MTH104, protein-exportmembrane protein SECD, oligopeptide transporters oppA and oppD, in the brain and two: ABC-transporter BRAF-2 and cation-transport ATPase PACS, in the heart. Homologies of the sequences found were in any case >50% thus permitting the identification of transporters with high probability.

The biological meaning could be that a naturally occuring amino acid, taurine, modulates complex transport systems. The most prominent finding is the upregulation of a multidrug transporter transcript, explaining a mechanism for the nonselective detoxifying action of taurine.

Keywords

Amino acids Taurine Transporter Rat Brain Heart 

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References

  1. Bachmann BJ (1990) Linkage map of Escherichia coli K12. Microbiol Rev 54: 130–197PubMedGoogle Scholar
  2. Chen CM, Ye QZ, Zhu ZM, Wanner BL, Walsh CT (1990) Molecular biology of carbonphosphorus bond cleavage. Cloning and sequencing of the phn genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coli B. J Biol Chem 265: 4461–4471PubMedGoogle Scholar
  3. Gardel C, Johnson K, Jacq A, Beckwith J (1990) The secD locus of E. coli codes for two membrane proteins required for protein export. EMBO J 9: 3209–3216PubMedGoogle Scholar
  4. Germann UA (1993) Molecular analyssis of the multidrug transporter. Cytotechnology 12: 33–62PubMedGoogle Scholar
  5. Gottesmann MM, Hrycyna CA, Schoenlein PV, Germann UA, Pastan I (1995) Genetic analysis of the multidrug transporter. Ann Rev Genet 29: 607–649PubMedGoogle Scholar
  6. Higgins CF (1992) ABC transporters: from microorganisms to man. Annu Rev Cell Biol 8: 67–113PubMedGoogle Scholar
  7. Hoshino T, Kose-Terai-K, Sato K (1992) Solubilization and reconstitution of the Pseudomonas aeruginosa high affinity branched chain amino acid transport system. J Biol Chem 267: 21313–21318PubMedGoogle Scholar
  8. Howard AG, Nickless G (1977) Heavy metal complexation in polluted molluscs. Chem Biol Interact 17: 257–263PubMedGoogle Scholar
  9. Huxtable RJ (1992) Physiological actions of taurine. Physiol Rev 72: 101–163PubMedGoogle Scholar
  10. Kanamaru K, Kashiwagi S, Mizuno T (1994) A copper-transporting P-type ATPase found in the thylakoid membrane of the cyanobacterium Synechococcus species PCC7942. Mol Microbiol 13: 369–377PubMedGoogle Scholar
  11. Koide A, Hoch JA (1994) Identification of a second oligopeptide transport system in bacillus subtilis and determination of its role in sporulation. Mol Microbiol 13: 417–426PubMedGoogle Scholar
  12. Labudova O, Lubec G (1998) cAMP upregulates the transposable element mys-1: a possible link between signaling and mobile DNA. Life Sci 62: 431–437PubMedGoogle Scholar
  13. Lampson WG, Kramer JH, Schaffer SW (1983) Potentiation of the actions of insulin by taurine. Can J Phys Pharmacol 61: 457–463Google Scholar
  14. Lombardini JB (1996) Taurine depletion in the intact animal stimulates in vitro phosphorylation of an approximately 44-kDa protein present in the mitochondrial fraction of the rat heart. J Mol Cell Cardiol 28: 1957–1961PubMedGoogle Scholar
  15. Lubec B, Hoeger H, Kremser K, Amann G, Koller DY, Gialamas J (1996) Decreased tumor incidence and increased survival by one year oral low dose arginine supplementation in the mouse. Life Sci 58: 2317–2325PubMedGoogle Scholar
  16. Metcalf WW, Wanner BL (1991) Involvement of the Escherichia coli phn gene cluster in assimilation of phosphorus in the form of phosphonates, phosphite, Pi esters, and Pi. J Bacteriol 173: 587–600PubMedGoogle Scholar
  17. Neyfakh AA, Bidnenko VE, Chen LB (1991) Efflux-mediated multidrug resistance in bacillus subtilis: similarities and dissimilarities with the mammalian system. Proc Natl Acad Sci (USA) 88: 4781–4785Google Scholar
  18. Pogliano JA, Beckwith J (1994) SecD and SecF facilitate protein export in E. coli. EMBO J 13: 554–561PubMedGoogle Scholar
  19. Richarme G, Caldas TD (1997) Chaperone properties of the bacterial periplasmic substrate — binding proteins. J Biol Chem 272: 15607–15612PubMedGoogle Scholar
  20. Tame JR, Murshudov GN, Dodson EJ, Neil TK, Dodson GG, Higgins CF, Wilkinson AJ (1994) The structural basis of sequence-independent peptide binding bu OppA protein. Science 264: 1578–1581PubMedGoogle Scholar
  21. Tynkkynen S, Buist G, Kunji E, Kok J, Poolman B, Venema G, Haandrikman A (1993) Genetic and biochemical characterization of the oligopeptide transport system of lactococcus lactis. J Bacteriol 175: 7523–7532PubMedGoogle Scholar
  22. Van Veen HW, Venema K, Bolhuis H, Oussenko I, Kok J, Poolman B, Driessen AJ, Konings WN (1996) Multidrug resistance mediated by a bacterial homolog of the human multidrug transporter MDR1. Proc Natl Acad Sci (USA) 93: 10668–10672Google Scholar

Copyright information

© Springer-Verlag 1999

Authors and Affiliations

  • O. Labudova
    • 1
  • C. Yeghiazarjan
    • 2
  • H. Höger
    • 3
  • G. Lubec
    • 1
  1. 1.Department of PediatricsUniversity of ViennaViennaAustria
  2. 2.Department of RadiobiologyUniversity of BonnGermany
  3. 3.Institute for Animal BreedingUniversity of ViennaAustria

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