WC studied the expression of the human cellular glutathionc peroxidase (GPx) gene, from which a key enzyme containing sclenocysteine (Sty) at the active site is produced. Expression of some human GPx gene mutants in COS-7 cells revealed that the 5' untranslated region (utr) was necessary for expression of the GPx gene, since mutant genes having 10 base pairs (bps) at the S'utr (the complete had 311 bps) expressed GPx at very low levels. The genes with 31 I or 405 bps at the S'utr wcrc better expressed than those having 257 bps. The GPx gene having 133 bps at the 3'utr (80 bps shorter than the entire length) was highly expressed. This deletion did not influence expression. We constructed some mutants in which 3 bases were altered at the upstream region of the Sty UGA codon i. *. the frame ,of the GPx Ben.+ by site-directed mutagenesis. GPx expression decreased but the expression was restored. Therefore, the upstream region of the in-frame Sty codon was nL?t essential in the Sty decoding mechanisms. Finally, the S'utr was essential for the expression of GPx gene. However, the deletion of a part of the 3'utr and the siw-directed mutation upstream of the Sty codon did not show drastic effects on the expression.