Abstract
The purpose of this communication is to elucidate if selenium plays a role in the function of granulocytes and lymphocytes. Thus, the incorpo ration of selenium in proteins from granulocytes and lymphocytes cultured with 1ΜCi/mL radioactive Na2 75SeO3 was studied. The protein peaks containing75Se from two columns of Heparin Sepharose CL-6B and Sephacryl S-200 HR were separated further by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis. The results showed that the incorporation of75Se into granulocytes was about six times higher than that of lymphocytes during a 96-h cultivation, however, the GSH-Px activity in granulocytes did not change significantly. On the other hand, the GSH-Px activity of lymphocytes rose significantly after three days cultivation. These data indicated that the main chemical form of selenium in granulocytes was not GSH-Px. Results from SDS-PAGE revealed a strongly75Se-labeled protein band with subunit molecular weight of 15 kDa in the supernatant of granulocyte homogenate. However, the main chemical forms of selenium in the culture media of granulocytes and lymphocytes were found to be selenoprotein P. The different forms of selenium-containing proteins in the intracellular and extracellular media of granulocytes indicated the different functions of these proteins.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
B. Halliwell and J. M. C. Gutheridge,Free Radicals in Biology and Medicine, 2nd ed., Clarendon, Oxford App. 372–390 (1989).
J. T. Rotruck, A. L. Pope, H. E. Ganther, A. B. Swanson, D. G. Hafeman, and W. G. Hoekstra, Selenium: biochemical role as a component of glutathione proxidase,Science 179, 588–590 (1973).
F. Ursini, M. Maiorino, and C. Gregolin, The selenoenzyme phospholipid hydroperoxide glutathione peroxidase,Biochim. Biophys. Acta 839, 62–70 (1985).
K. Takahashi, N. Avissar, J. Whitin, and H. Cohen, Purification and characterization of human plasma glutathione peroxidase: a selenoglucoprotein distinct from the known cellular enzyme,Arch. Biochem. Biophys. 256, 677–686 (1987).
F. F. Chu, J. H. Doroshow, and R. S. Esworthy, Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI,J. Biol. Chem. 268, 2571–2576 (1993).
D. Behne, A. Kyriakopoulos, H. Meinhold, and J. Kohrle, Identification of type I iodothyronine 5′-deiodinase as a selenoenzyme,Biochem. Biophys. Res. Commun. 173, 1143–1149 (1990).
J. R. Arthur, F. Nicol, and G. J. Beckett, Hepatic iodothyronine 5′-deiodinase. The role of selenium,Biochem. J. 272, 537–540 (1990).
M. J. Berry, L. Banu, and P. R. Larsen, Type I iodothyronine deiodinase is a selenocysteine-containing enzyme,Nature 349, 438–440 (1991).
W. Croteau, S. L. Whittemore, M. J. Schneider, and D. L. St. Germain, Cloning and expression of a cDNA for a mammalian type 3 iodothyronine deiodinase,J. Biol. Chem. 270, 16,569–16,575 (1995).
K. E. Hill, R. S. Lloyd, J. G. Yang, R. Read, and R. F. Burk, The cDNA for rat selenoprotein P contains ten TGA codons in the open reading frame,J. Biol. Chem. 266, 10,050–10,053 (1991).
R. F. Burk and K. E. Hill, Selenoprotein P. A selenium-rich extracellular glycoprotein,J. Nutr. 124, 1891–1897 (1994).
H. S. Chittum, S. Himeno, K. E. Hill, and R. F. Burk, Multiple forms of selenoprotein P in rat plasma,Arch. Biochem. Biophys. 325, 124–128 (1996).
J. T. Deagen, J. A. Butler, B. A. Zachara, and P. D. Whanger, Determination of the distribution of selenium between glutathion peroxidase, selenoprotein P, and albumin in plasma,Anal. Biochem. 208, 176–181 (1993).
B. Akesson, T. Bellew, and R. F. Burk, Purification of selenoprotein P from human plasma,Biochim. Biophys. Acta 1204, 243–249 (1994).
I. Karimpour, M. Cutler, D. Shih, J. Smith, and K. C. Kleene, Sequence of the gene encoding the mitochondrial capsule selenoprotein of mouse sperm: identification of three in-phase TGA selenocysteine codons,DNA Cell Biol. 11, 693–699 (1992).
S. C. Vendeland, M. A. Beilstein, C. L. Chen, O. N. Jensen, E. Barofsky, and P. D. Whanger, Purification and properties of selenoprotein W from rat muscle,J. Biol. Chem. 268, 17,103–17,107 (1993).
M. A. Beilstein, S. C. Vendeland, E. Barofsky, O. N. Jensen, and P. D. Whanger, Selenoprotein Wof rat muscle binds glutathion and an unknown small molecular weight moiety,J. Inorg. Biochem. 61, 117–124 (1996).
M. Kalcklosch, A. Kyriakopoulos, C. Hammel, and D. Behne, A new selenoprotein found in the glandular epithelial cells of the rat prostate,Biochim. Biophys. Res. Commun. 217, 162–170 (1995).
J. Clausen and S. A. Nielsen, Comparison of whole blood selenium values and erythrocyte glutathione peroxidase activities of normal individuals on supplementation with selenate, selenite, L-selenomethionine, and high selenium yeast,Biol. Trace Elem. Res. 15, 125–138 (1988).
B. Åkesson and B. Mårtensson, Heparin interacts with a selenoprotein in human plasma,J. Inorg. Biochem. 33, 257–261 (1988).
G. Riva: Das Serurneiweissbild,Verlag Hans Huber, Bern (1960).
H. E. Ganther and H. S. Hsieh, Mechanism for the conversion of selenite to selenides in mammalian tissues, inTrace Element Metabolism in Animals, W. G. Hoekstra, J. W. Suttie, H. E. Ganther and W. Mertz, eds., Butterworths, London, pp. 339–353 (1974).
J. T. Deagen, M. A. Beilstein, and P. D. Whanger, Chemical forms of selenium in selenium containing proteins from human plasma,J. Inorg. Biochem. 41, 261–268 (1991).
P. A. Southorn and G. Powis, Free radicals in medicine. I. Chemical nature and biologic reactions,Mayo Clin. Proc. 63, 381–389 (1988).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Liu, Q., Lauridsen, E. & Clausen, J. Different selenium-containing proteins in the extracellular and intracellular media of leucocytes cultivated in vitro. Biol Trace Elem Res 61, 237–252 (1998). https://doi.org/10.1007/BF02789085
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF02789085