![rayman weeber rayman weeber](https://cache.legacy.net/legacy/images/cobrands/DemocratAndChronicle/photos/RDC093142-1_20170317.jpg)
SELENOP possesses two different functions: Se transport activity to supply Se to cells and GPX-like activity to reduce phospholipid hydroperoxide ( 8, 9). Most selenoproteins have a Sec residue, while SELENOP has 10, making it multifunctional ( 6, 7). Twenty-five genes encoding human Sec-containing proteins, i.e., selenoproteins, have been discovered, which play significant roles in several physiological processes such as antioxidant defense and metabolism five types of glutathione (GSH) peroxidases (GPXs) play significant roles in the removal of several hydroperoxides, three types of thioredoxin reductases (TRXRs) in redox regulation, three types of iodothyronine deiodinases in the regulation of thyroid hormones, and selenophosphate synthetase 2 (SEPHS2) in Sec synthesis ( 4, 5). SELENOP contains the essential trace element Se in the form of selenocysteine (Sec), which is an analog of cysteine that contains Se instead of sulfur ( 2ā 4). The āPā in SELENOP denotes its presence in plasma.
![rayman weeber rayman weeber](https://i.ytimg.com/vi/u9nGVyGnTwA/hqdefault.jpg)
SELENOP is mainly synthesized in the liver and secreted to the plasma after cleavage of the signal peptide. Selenoprotein P (encoded as SELENOP) was first described in 1973, and its character was reported as the major selenium (Se)-containing protein in plasma ( 1, 2).