l-Cysteine influx and efflux: A possible role for red blood cells in regulation of redox status of the plasma

References

• Griffith OW. Biologic and pharmacologic regulation of mammalian glutathione synthesis. Free Radic Biol Med 1992; 27: 922–935
   Google Scholar
• Gille G, Sigler K. Oxidative stress and living cells. Folia Microbiol 1995; 40(2)131–152
   PubMedGoogle Scholar
• Clemens MR, Waller HD. Lipid peroxidation in erythrocytes. Chem Phys Lipids 1987; 45: 251–268
   PubMed Web of Science ®Google Scholar
• Eckert KG, Eyer P. Formation and transport of xenobiotic glutathione-S-conjugates in red cells. Biochem Pharmacol 1986; 35: 325–329
   PubMed Web of Science ®Google Scholar
• Awasthi YC, Garg HS, Dao DD, Partridge CA, Srivastava SK. Enzymatic conjugation of erythrocyte glutathione with 1-chloro-2,4-dinitrobenzene: The fate of glutathione conjugate in erythrocytes and the effect of glutathione depletion on hemoglobin. Blood 1981; 58: 733–738
   PubMed Web of Science ®Google Scholar
• Ansari GAS, Singh SV, Gan JC, Awasthi YC. Human erythrocyte glutathione S-transferase: A possible marker of chemical exposure. Toxicol Lett 1987; 37: 57–62
   PubMedGoogle Scholar
• Strange RC, Jones PW, Fryer AA. Glutathione S-transferase: Genetics and role in toxicology. Toxicol Lett 2000; 112: 357–363
   PubMed Web of Science ®Google Scholar
• Olive C, Board P. Glutathione S-conjugate transport by cultured human cells. Biochim Biophys Acta 1994; 1224: 264–268
   PubMedGoogle Scholar
• Matsuda Y, Epstein LF, Gatmaitan Z, Arias IM. The role of thiols in ATP-dependent transport of S-(2,4-dinitrophenyl) glutathione by rat liver plasma membrane vesicles. Biochim Biophys Acta 1996; 1279: 35–42
   PubMedGoogle Scholar
• Keppler D. Export pumps for glutathione S-conjugates. Free Radic Biol Med 1999; 27: 985–991
   PubMed Web of Science ®Google Scholar
• LaBelle EF, Singh SV, Srivastava SK, Awasthi YC. Dinitrophenyl glutathione efflux from human erythrocytes is primary active ATP-dependent transport. Biochem J 1986; 238: 443–449
   PubMed Web of Science ®Google Scholar
• Lunn G, Dale GL, Beutler E. Transport accounts for glutathione turnover in human erythrocytes. Blood 1979; 54: 238–244
   PubMed Web of Science ®Google Scholar
• Lu SC, Sun WM, Yi J, Ookhtens M, Sze G, Kaplowitz N. Role of two recently cloned rat liver GSH transporters in the ubiquitous transport of GSH in mammalian cells. J Clin Invest 1996; 97: 1488–1496
   PubMedGoogle Scholar
• Young JD, Wolowyk MW, Jones SM, Ellory JC. Red-cell amino acid transport. Evidence for the presence of system ASC in mature human red blood cells. Biochem J 1983; 216(2)349–357
   PubMedGoogle Scholar
• Awasthi YC, Mısra G, Rassın DK, Srivastava SK. Detoxification of xenobiotics by glutathione S-transferase in erythrocytes: The transport of the conjugate of glutathione and 1-chloro-2,4-dinitrobenzene. Br J Haematol 1983; 55: 419–425
   PubMed Web of Science ®Google Scholar
• Sedlak J, Lindsay RH. Determination of sulfhydriyl groups in biological samples. Anal Biochem 1963; 25: 192–205
   Google Scholar
• Palacin M, Estevez R, Bertran J, Zorzano A. Molecular biology of mammalian plasma membrane amino acid transporters. Physiol Rev 1988; 78: 969–1054
   Google Scholar
• Rosenberg R. Na-independent and Na-dependent transport of neutral amino acids in the human red blood cells. Acta Physiol Scand 1982; 116(4)321–330
   PubMedGoogle Scholar
• Yidiz D, Bagdadioglu T. l-Cysteine uptake is stimulated by 1-chloro-2,4-dinitrobenzene in vitro in human erythrocytes. Toxicol Mech Method 2004; 14: 241–245
   PubMedGoogle Scholar
• Suliman ME, Barany P, Filho JCD, Qureshi AR, Stenvinkel P, Heimburger O, Anderstam B, Lindholm B, Bergstrom J. Influence of nutritional status on plasma and erythrocyte sulphur amino acids, sulph-hydryls, and inorganic sulphate in end-stage renal disease. Nephrol Dial Transplant 2002; 17: 1050–1056
   PubMedGoogle Scholar
• Wang FX, Cynader MX. Pyruvate released by astrocytes protects neurons from copper-catalyzed cysteine neurotoxicity. J Neurosci 2001; 21(10)3322–3331
   PubMed Web of Science ®Google Scholar
• Pittman MS, Corker H, Wu G, Binet MB, Moir AJ, Poole RK. Cysteine is exported from the Escherichia coli cytoplasm by CydDC, an ATP-binding cassette-type transporter required for cytochrome assembly. J Biol Chem 2002; 277(51)49841–49849
   PubMedGoogle Scholar
• Sagne C, Agulhon C, Ravassard P, Darmon M, Hamon M, Mestikwy SE, Gasnier B, Giros B. Identification and characterization of lysosomal transporter for small neutral amino acids. PNAS 2001; 98(13)7206–7211
   PubMedGoogle Scholar
• Berk L, Matsudaira Z, Darnell B. Molecular cell biology. W. H. Freeman and Company, New York 2000; 597–604
   Google Scholar
• Badaloo A, Reid M, Forrester T, Heird WC, Jahoor F. Cysteine supplementation improves the erythrocyte glutathione synthesis rate in children with severe edematous malnutrition. Am J Clin Nutr 2002; 76(3)646–652
   PubMedGoogle Scholar
• Sen CK, Packer L. Thiol homeostasis and supplements in physical exercise. Am J Clin Nutr 2000; 72(2)653S–669S
   PubMed Web of Science ®Google Scholar
• Lomaestro BM, Malone M. Glutathione in health and disease: Pharmacotherapeuticissu. Ann Pharmacother 1995; 29: 1263–1273
   PubMedGoogle Scholar
• Andersson A, Lindgren A, Arnadottir M, Prytz H, Hulfberg B. Thiols as a measure of plasma redox status in healthy subjects and in patients with renal or liver failure. Clin Chem 1999; 45: 1084–1087
   PubMed Web of Science ®Google Scholar