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Chemical Compound Review

2388-00-3     triethyllead

Synonyms: Hexaethyldilead, EINECS 219-216-3, Hexaethyldiplumbane, Diplumbane, hexaethyl-, Diplumbane, 1,1,1,2,2,2-hexaethyl-
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Disease relevance of triethyllead

 

High impact information on triethyllead

 

Chemical compound and disease context of triethyllead

 

Biological context of triethyllead

  • Surprisingly, in freshly isolated rat liver mitochondria the ATP-synthesizing activity was also inhibited by triethyllead (IC50 16 microM), in spite of a measured high intramitochondrial GSH concentration (up to 10 mM) [10].
  • Triethyllead reduced the rate of dye excretion into the bile without affecting blood pressure, blood or liver sulfhydryl compounds or the volume of bile flow [11].
  • In a previous study we reported that triethyllead (Et3Pb+) inhibits cell proliferation of normal human lymphocytes [12].
  • Triethyllead acetate [1.9 mumol (mg membrane protein)-1] inhibited the reduction by NADH of cytochromes; evidence for more than one site of inhibition in the respiratory chain was obtained [13].
  • In order to determine whether cortical membrane damage was reflected in alteration of a restricted protein population, a series of high-affinity receptor binding sites was determined in cortical membranes derived from treated rats 7 d after the last injection of triethyllead [14].
 

Anatomical context of triethyllead

 

Associations of triethyllead with other chemical compounds

 

Gene context of triethyllead

  • Triethyllead-induced inhibition of proliferation of normal human lymphocytes through decreased expression of the Tac chain of interleukin 2 receptor [18].
  • The data indicate that Pb(NO3)2 is a much more potent inhibitor of delta-aminolevulinic acid dehydratase activity than triethyllead acetate (Ki values of 0.77 microM versus 130.37 microM. respectively) [17].
  • Membrane-bound ATPase activity was strongly inhibited by triethyllead acetate in the absence or presence of Cl-. The concentration of inhibitor giving 50% inhibition [0.02 mumol (mg membrane protein)-1] was about two orders of magnitude lower than that required for 50% inhibition of substrate oxidation rates in membranes [13].
 

Analytical, diagnostic and therapeutic context of triethyllead

References

  1. Induction of chromosomal aberrations in Chinese hamster ovary cells by triethyllead acetate. Blakey, D.H., Bayley, J.M., Douglas, G.R. Mutat. Res. (1992) [Pubmed]
  2. Evidence for a sodium-dependent calcium influx in isolated rat hepatocytes undergoing ATP depletion. Carini, R., Bellomo, G., Dianzani, M.U., Albano, E. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  3. The effect of triethyllead on the motile activity of walker 256 carcinosarcoma cells. Sroka, J., Kamiński, R., Michalik, M., Madeja, Z., Przestalski, S., Korohoda, W. Cell. Mol. Biol. Lett. (2004) [Pubmed]
  4. Excretion of triethyllead, diethyllead and inorganic lead in rabbits after injection of triethyl neopentoxy lead. Arai, F., Yamauchi, H., Chiba, K., Yoshida, K. Industrial health. (1998) [Pubmed]
  5. Chloride-dependent uncoupling of oxidative phosphorylation by triethyllead and triethyltin increases cytosolic free calcium in guinea pig cerebral cortical synaptosomes. Kauppinen, R.A., Komulainen, H., Taipale, H.T. J. Neurochem. (1988) [Pubmed]
  6. Triethyllead inhibits gamma-aminobutyric acid binding to uptake sites in synaptosomal membranes. Seidman, B.C., Olsen, R.W., Verity, M.A. J. Neurochem. (1987) [Pubmed]
  7. Suppressive effect of triethyllead on entry of proteins into the CNS myelin sheath in vitro. Konat, G., Clausen, J. J. Neurochem. (1980) [Pubmed]
  8. Protein composition of forebrain myelin isolated from triethyllead-intoxicated young rats. Konat, G., Clausen, J. J. Neurochem. (1978) [Pubmed]
  9. Neurotoxic effects of combined treatment of 2,5-hexanedione and triethyllead chloride. Lapadula, D.M., Tilson, H.A., Campbell, G., Abou-Donia, M.B. Journal of toxicology and environmental health. (1987) [Pubmed]
  10. Inhibition of cellular activities by triethyllead. Role of glutathione and accumulation of triethyllead in vitro. Münter, K., Athanasiou, M., Stournaras, C. Biochem. Pharmacol. (1989) [Pubmed]
  11. Inhibition of the enzymatic activity of ligandin by organogermanium, organolead or organotin compounds and the biliary excretion of sulfobromophthalein by the rat. Byington, K.H., Hansbrough, E. J. Pharmacol. Exp. Ther. (1979) [Pubmed]
  12. High sensitivity of leukemic peripheral blood lymphocytes to triethyllead action. Stiakaki, E., Stournaras, C., Dimitriou, H., Kalmanti, M. Biochem. Pharmacol. (1997) [Pubmed]
  13. Effects of trialkyllead compounds on growth, respiration and ion transport in Escherichia coli K12. Gibson, J.F., Hadfield, S.G., Hughes, M.N., Poole, R.K. J. Gen. Microbiol. (1980) [Pubmed]
  14. Triethyllead-induced peroxidative damage in various regions of the rat brain. Ali, S.F., Bondy, S.C. Journal of toxicology and environmental health. (1989) [Pubmed]
  15. Reversible neuronal damage in hippocampal pyramidal cells with triethyllead: the role of astrocytes. Nolan, C.C., Brown, A.W. Neuropathol. Appl. Neurobiol. (1989) [Pubmed]
  16. UDPgalactose:ceramide galactosyltransferase and 2',3'-cyclic-nucleotide 3'-phosphodiesterase activities in rat brain after long-term exposure to methylmercury or triethyllead. Grundt, I.K., Neskovic, N.M. Exp. Neurol. (1985) [Pubmed]
  17. A comparison of the effects of inorganic and alkyllead compounds on human erythrocytic delta-aminolevulinic acid dehydratase (ALAD) activity in vitro. Burns, C.B., Godwin, I.R. Journal of applied toxicology : JAT. (1991) [Pubmed]
  18. Triethyllead-induced inhibition of proliferation of normal human lymphocytes through decreased expression of the Tac chain of interleukin 2 receptor. Stournaras, C., Spanakis, E., Perraki, M., Athanasiou, M., Thanos, D., Georgoulias, V. Int. J. Immunopharmacol. (1990) [Pubmed]
  19. Ionic modulation of triethyllead neurotoxicity in cerebellar granule cell culture. Verity, M.A., Sarafian, T.S., Guerra, W., Ettinger, A., Sharp, J. Neurotoxicology (1990) [Pubmed]
  20. Effect of hepatocyte swelling on microtubule stability and tubulin mRNA levels. Häussinger, D., Stoll, B., vom Dahl, S., Theodoropoulos, P.A., Markogiannakis, E., Gravanis, A., Lang, F., Stournaras, C. Biochem. Cell Biol. (1994) [Pubmed]
 
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