Abstract
Purified rat hemoglobin catalyzes the oxidative degradation of iodothyronines to form iodide and an iodine-containing intermediate that reacts with protein. Hemoglobin also catalyzes peroxidation of linoleic acid. These observations are consistent with the reported intrinsic peroxidase activity of hemoglobin and other heme-proteins. However, incubations containing both linoleic acid and an iodothyronine produced a surprising result: deiodination was stimulated rather than competitively inhibited. In contrast, linoleic-acid peroxidation was inhibited by iodothyronines. Thus, low levels of iodothyronines (2.6×10−7M) are effective inhibitors of linoleic-acid peroxidation. Thyroxine and reverse T3 were found to be more effective in this antioxidant activity than vitamin E, glutathione, ascorbic acid and DTT. Since linoleic-acid peroxidation proceeds by a propagating free-radical mechanism, we have concluded that iodothyronines can effectively terminate the free-radical chain reaction to become oxidatively deiodinated. Consistent with this antioxidant mechanism, reverse T3 is effective in preserving red cell membranes as measured by the inhibition of erythrocyte hemolysis.
Similar content being viewed by others
References
Tseng, Y.L., and Latham, K.R. (1981) Abstract, 63rd Annual Meeting of the Endocrine Society.
Misra, H.P., and Fridovich, I. (1972) J. Biol. Chem. 247, 6960–6062.
Tappel, A.L. (1961) in Autoxidation and Antioxidants (Lundberg, W.O., ed.) Vol. 1, pp. 325–366, Interscience, New York.
Mengel, C.E. (1972) Ann. N.Y. Acad. Sci. 203, 163–171.
Wright, W.D. (1963) Nature 198, 1239–1244.
Bradford, M.M. (1976) Anal. Biochem. 72, 248–254.
Worthington Enzyme Manual (1972) pp. 25–26, Worthington Biochem. Corp., Freehold, NJ.
Salvati, S.M., Ambrogloni, M.T., and Tentori, L. (1969) Ital. J. Biochem. 18, 1–18.
Green, W.L. (1972) J. Chromatogr. 72, 83–91.
Svedberg, T., and Fahraeus, R. (1926) J. Am. Chem. Soc., 48, 430–438.
Marcial, R.M.B., Ozwa, Y., and Chopra, I.H. (1979) Endocrinology 104, 365–371.
Visser, T.J., van der Dors-Tobe, I., Docter, R., and Hennemann, G. (1976) Biochem. J. 157, 479–482.
Leonard, J.L., and Rosenberg, I.N. (1978) Endocrinology 103, 274–280.
Kessler, G. and Pileggi, V. (1968) J. Clin. Chem. 14, 811–815.
Smallridge, R.C., Burman, K.D., Ward, K.E., Wartofsky, L., Dimond, R.C., Wright, F.D., and Latham, K.R. (1981) Endocrinology 108, 2336–2345.
Lissitzky, P.S., and Bouchildoux, S. (1957) Bull. Soc. Chim. Biol. 39, 133–143.
Balsam, A., Sexton, F., Borges, M., and Ingbar, S.H. (1983) J. Clin. Invest. 72, 1234–1245.
Matsuura, T., Nagamachi, T., Nishinaga, H.K., and Cahnmann, H.J. (1969) J. Org. Chem. 34, 2554–2558.
Plaskett, L.G. (1961) Biochem. J. 78, 652–657.
Grimes, A.J. (1980) in Human Red Cell Metabolism, pp. 14–15, Blackwell Scientific Publications, Oxford, England.
Tappel, A.L. (1973) Fed. Proc. 32, 1870–1874.
Ames, B.N., Cathcart, R., Schwiers, E., and Hochstein, P. (1981) Proc. Natl. Acad. Sci. USA 78, 6858–6862.
Wynn, J. (1968) Arch. Biochem. Biophys. 126, 880–891.
Rose, S., and György, P. (1952) Am. J. Physiol. 168, 414–420.
McCay, P.B., Poyer, J.L., Pfeifer, P.M., May, H.E., and Gilliam, J.M., (1971) Lipids 6, 297–306.
Oppenheimer, J.H., Schartz, H.L., and Surks, M.I. (1972) J. Clin. Invest. 51, 2493–2497.
Hoch, F.L., Subramanian, C., Phopeshwarker, G.A., and Mead, J.E. (1981) Lipids 16, 328–335.
de Gomez Dumm, I.N.T., de Alaniz, M.J.T., and Brenner, R.R. (1977) Adv. Exp. Med. Biol. 83, 609–616.
Horton, L., Coburn, R.J., England, J.M., and Himsworth, R.L. (1976) Q. J. Med. (NS) 45, 101–124.
Harman, D. (1972) Am. J. Clin. Nutr. 25, 839–843.
György, P., Cogan, G., and Rose, C. (1952) Proc. Soc. Exp. Biol. Med. 81, 536–538.
Wright, S.W. (1951), Paediatrics 7, 386–393.
Burman, K.D., Read, J., Dimond, R.C., Strum, O., Wright, F.D., Patow, W., Earll, J.M., and Wartofsky, L. (1976) J. Clin. Endocrinol. Metab. 43, 1351–1359.
Roti, E., Braverman, L.E., Fang, S.L., Alex, S., and Emerson, C.H. (1982) Endocrinology 111, 959–963.
Banovac, K., Bzik, L., Tislaric, T., and Sekso, M. (1980) Hormone Res. 12, 253–259.
Burman, K.D. (1978) Metabolism 27, 615–630.
Chopra, I.J., Sack, J., and Fisher, D.A. (1975) J. Clin. Invest. 55, 1137–1144.
Nakano, M., Tsutsumi, Y., and Ushijima, Y. (1971) Biochim. Biophys. Acta 252, 335–347.
Latham, K.R., MacLeod, K.M., Papavasiliou, S.S., Martial, J.A., Seeburg, P.H., Goodman, H.M., and Baxter, J.D. (1978) in Receptors and Hormone Action (O'Malley, B.W., and Birnbaumer, L., eds.) Vol. 3, pp. 76–100, Academic Press, New York.
Author information
Authors and Affiliations
Additional information
The opinions or assertions contained here are the authors' and are not to be construed as official or as reflecting the views of the Department of Defense or the Uniformed Services University of the Health Sciences. The experiments reported here were conducted according to the principles in the “Guide for the Care and Use of Laboratory Animals,” Institute of Laboratory Animal Resources, National Research Council DHEW Pub. No. (NIH) 74-23.
Supported by NIH Postdoctoral fellowship No. 5F32-AM-0610502.
About this article
Cite this article
Tseng, YC.L., Latham, K.R. Iodothyronines: Oxidative deiodination by hemoglobin and inhibition of lipid peroxidation. Lipids 19, 96–102 (1984). https://doi.org/10.1007/BF02534498
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF02534498