Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2018 May 14;7(5):66.
doi: 10.3390/antiox7050066.

Selenium-Dependent Antioxidant Enzymes: Actions and Properties of Selenoproteins

Evangelos Zoidis  1 , Isidoros Seremelis  2 , Nikolaos Kontopoulos  3 , Georgios P Danezis  4
Affiliations
Review

Selenium-Dependent Antioxidant Enzymes: Actions and Properties of Selenoproteins

Evangelos Zoidis et al. Antioxidants (Basel). .

Abstract

Unlike other essential trace elements that interact with proteins in the form of cofactors, selenium (Se) becomes co-translationally incorporated into the polypeptide chain as part of 21st naturally occurring amino acid, selenocysteine (Sec), encoded by the UGA codon. Any protein that includes Sec in its polypeptide chain is defined as selenoprotein. Members of the selenoproteins family exert various functions and their synthesis depends on specific cofactors and on dietary Se. The Se intake in productive animals such as chickens affect nutrient utilization, production performances, antioxidative status and responses of the immune system. Although several functions of selenoproteins are unknown, many disorders are related to alterations in selenoprotein expression or activity. Selenium insufficiency and polymorphisms or mutations in selenoproteins' genes and synthesis cofactors are involved in the pathophysiology of many diseases, including cardiovascular disorders, immune dysfunctions, cancer, muscle and bone disorders, endocrine functions and neurological disorders. Finally, heavy metal poisoning decreases mRNA levels of selenoproteins and increases mRNA levels of inflammatory factors, underlying the antagonistic effect of Se. This review is an update on Se dependent antioxidant enzymes, presenting the current state of the art and is focusing on results obtained mainly in chicken.

Keywords: antioxidant system; reactive oxygen species (ROS); selenium; selenocysteine; selenomethionine; selenoproteins.

PubMed Disclaimer

Conflict of interest statement

The authors declare no conflict of interest.

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Mariotti M., Santesmasses D., Guigó R. Evolution of Selenophosphate Synthetase. Springer; New York, NY, USA: 2016.
    1. Hatfield D.L., Marla J.B., Vadim N., Gladyshev V.N. Selenium: Its Molecular Biology and Role in Human Health. Springer Science & Business Media; Berlin, Germany: 2011.
    1. Mariotti M. Short Views on Insect Genomics and Proteomics. Springer; New York, NY, USA: 2016. Selenocysteine Extinctions in Insects.
    1. Mariotti M., Lobanov A.V., Manta B., Santesmasses D., Bofill A., Guigó R., Gabaldón T., Gladyshev V.N. Lokiarchaeota marks the transition between the archaeal and eukaryotic selenocysteine encoding systems. Mol. Biol. Evol. 2016;33:2441–2453. doi: 10.1093/molbev/msw122. - DOI - PMC - PubMed
    1. Sarangi K.G., White L., Castellano S. Genetic Adaptation and Selenium Uptake in Vertebrates. Wiley; Chichester, UK: 2017.

LinkOut - more resources

-