Mammalian selenium-containing proteins can be divided into three groups: pr
oteins containing nonspecifically incorporated selenium, specific selenium-
binding proteins, and specific selenocysteine-containing selenoproteins. Se
lenoproteins with known functions identified so far include five glutathion
e peroxidases, two deiodinases, several thioredoxin reductases, and selenop
hosphate synthetase 2. Alternative splicing leads to a greater variety of s
elenoproteins, as was shown in the cases of a specific sperm nuclei glutath
ione peroxidase and some thioredoxin reductases. Selenoprotein P, selenopro
tein W, a 15-kDa selenoprotein, an 18-kDa selenoprotein, and several seleno
proteins identified in silico from nucleotide sequence databases were found
to contain selenocysteine but their functions are not known. Gel electroph
oretic separation of tissue samples from rats labeled in vivo with Se-75 sh
owed the existence of further selenium-containing proteins.