Selenoprotein W: a review

• Published in: Cellular and molecular life sciences : CMLS Vol. 57; no. 13-14; pp. 1846 - 1852
• Main Author: Whanger, P D
• Format: Journal Article
• Language: English
• Published: Switzerland Springer Nature B.V 01.12.2000; Birkhäuser Verlag
• Subjects: Amino Acid Sequence; Amino acids; Animal species; Animals; Antibodies - immunology; Antioxidants; Antioxidants - chemistry; Antioxidants - isolation & purification; Antioxidants - metabolism; Brain; Brain - cytology; Brain - metabolism; Cardiac muscle; Cloning, Molecular; Complementary DNA; Female; Gene Expression Profiling; Glutathione; Homology; Humans; Male; Molecular Sequence Data; Muscles; Nucleotide sequence; Nucleotides; Primates; Proteins - chemistry; Proteins - genetics; Proteins - isolation & purification; Proteins - metabolism; Rodents; Selenium; Selenium - metabolism; Selenium - pharmacology; Selenoprotein W; Selenoproteins; Sex Characteristics; Sheep; Stop codon
• ISSN: 1420-682X; 1420-9071
• DOI: 10.1007/PL00000666

Purification of selenoprotein W (Se-W) from rat and monkey muscles was shown to exist in multiple forms: with or without reduced glutathione and/or a 41-Da moiety (identity still unknown). TGA is located at coding position 13 in Se-W complementary DNA (cDNA) from all five species studied (rats, mice, sheep, human and monkey). TGA is also the stop codon in the rodents and sheep cDNA, but TAA is the stop codon in primates. There is an 80% homology of the nucleotide sequence in the coding region among the five species of animals, and the predicted amino acid sequences are 83% identical (rodents identical and primates identical). Se-W levels are highest in muscle, heart and brain from sheep and primates, but very low in rodent hearts. Studies with tissue cultures of muscle and brain cells indicated that selenium influenced Se-W levels. Although the metabolic function of Se-W is unknown, preliminary data suggest that it has an antioxidant function.