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Recent Developments in Trace Element Metabolism and Function: Newer Roles of Selenium in Nutrition^1,2,

Division of Gastroenterology, Department of Medicine and Center in Molecular Toxicology, Vanderbilt University School of Medicine, Nashville, TN 37232

Until recently, studies of the function of selenium focused on the selenoenzyme, glutathione peroxidase. However, the recognition that several metabolic effects of selenium are not associated with glutathione peroxidase has forced a re-evaluation of the function of this enzyme and the element. Hepatic glutathione peroxidase contains a significant percentage of the regulated selenium in the rat and is more sensitive to selenium deficiency than other selenoproteins. Thus, in addition to its enzymatic activity, it might have a storage function for the element. Another selenoprotein, designated selenoprotein P, has been found in rat plasma and has been quantitated. Its function is not yet known, but it has been postulated to be a transport protein for selenium and a defense against oxidant stress. Understanding the nutritional effects of selenium will require better characterization of glutathione peroxidase, selenoprotein P and other selenoproteins.

KEY WORDS: • selenium • rat • selenoproteins • glutathione peroxidase

¹ Presented as part of the 29th Annual Ruminant Nutrition Conference: Recent Developments in Trace Element Metabolism and Function, given at the 72nd Annual Meeting of the Federation of American Societies for Experimental Biology, Las Vegas, NV, May 1–5, 1988 and supported by grants from American Cyanamid Company; Cargill, Nutrena Feed Division; Carl S. Akey, Inc.; Hoffmann-LaRoche Inc.; Lilly Research Laboratories; Monsanto Co.; Pitman-Moore, Inc.; Schering Animal Health; and Zinpro Corp.

² The author's research was supported by National Institutes of Health Grants ES 02497 and HL 36371.

Manuscript received 28 October 1988. Revision accepted 24 January 1989.