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Selenium-Dependent Antioxidant Enzymes: Actions and Properties of Selenoproteins.

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.

Authors+Show Affiliations

Department of Nutritional Physiology and Feeding, Faculty of Animal Science and Aquaculture, Agricultural University of Athens, 75 Iera Odos, 11855 Athens, Greece. ezoidis@aua.gr.Chemistry Laboratory, Department of Food Science and Human Nutrition, Agricultural University of Athens, 75 Iera Odos, 11855 Athens, Greece. iseremelis@gmail.com.Chemistry Laboratory, Department of Food Science and Human Nutrition, Agricultural University of Athens, 75 Iera Odos, 11855 Athens, Greece. stud315044@aua.gr.Chemistry Laboratory, Department of Food Science and Human Nutrition, Agricultural University of Athens, 75 Iera Odos, 11855 Athens, Greece. gdanezis@aua.gr.

Pub Type(s)

Journal Article
Review

Language

eng

PubMed ID

29758013

Citation

Zoidis, Evangelos, et al. "Selenium-Dependent Antioxidant Enzymes: Actions and Properties of Selenoproteins." Antioxidants (Basel, Switzerland), vol. 7, no. 5, 2018.
Zoidis E, Seremelis I, Kontopoulos N, et al. Selenium-Dependent Antioxidant Enzymes: Actions and Properties of Selenoproteins. Antioxidants (Basel). 2018;7(5).
Zoidis, E., Seremelis, I., Kontopoulos, N., & Danezis, G. P. (2018). Selenium-Dependent Antioxidant Enzymes: Actions and Properties of Selenoproteins. Antioxidants (Basel, Switzerland), 7(5), doi:10.3390/antiox7050066.
Zoidis E, et al. Selenium-Dependent Antioxidant Enzymes: Actions and Properties of Selenoproteins. Antioxidants (Basel). 2018 May 14;7(5) PubMed PMID: 29758013.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Selenium-Dependent Antioxidant Enzymes: Actions and Properties of Selenoproteins. AU - Zoidis,Evangelos, AU - Seremelis,Isidoros, AU - Kontopoulos,Nikolaos, AU - Danezis,Georgios P, Y1 - 2018/05/14/ PY - 2018/03/23/received PY - 2018/05/07/revised PY - 2018/05/09/accepted PY - 2018/5/15/entrez PY - 2018/5/15/pubmed PY - 2018/5/15/medline KW - antioxidant system KW - reactive oxygen species (ROS) KW - selenium KW - selenocysteine KW - selenomethionine KW - selenoproteins JF - Antioxidants (Basel, Switzerland) JO - Antioxidants (Basel) VL - 7 IS - 5 N2 - 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. SN - 2076-3921 UR - https://www.unboundmedicine.com/medline/citation/29758013/Selenium_Dependent_Antioxidant_Enzymes:_Actions_and_Properties_of_Selenoproteins_ L2 - http://www.mdpi.com/resolver?pii=antiox7050066 DB - PRIME DP - Unbound Medicine ER -