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.
Highlights
Selenium (Se) is an essential trace element which is co-translationally incorporated into the polypeptide chain as part of the amino acid selenocysteine (Sec)
The results showed that reduced expression of GPX4, GPX2, GPX1, DIO1–2, TXNRD2–3, selenoprotein U, selenoprotein I, Sepx1, selenoprotein O, selenoprotein M, selenoprotein K, selenoprotein W, selenoprotein 15, Sepn1, selenoprotein T, and selenoprotein S in the meniscus cartilage, triggered by Pb exposure, might be alleviated by Se
Selenoproteins need for their synthesis several cofactors and depend mainly on Se intake through the diet
Summary
Selenium (Se) is an essential trace element which is co-translationally incorporated into the polypeptide chain as part of the amino acid selenocysteine (Sec). Selenoproteins have pivotal significance for optimal human and animal health mainly due to their antioxidant activity [8]. They have anti-inflammatory, chemo preventive and antiviral properties and are related with the improvement of immune responses [9,10]. The health-related properties of selenoproteins include among others protection against cancer [11,12], proper thyroid function [13]. According to the Office of Dietary Supplements (ODS) of the National Institutes of Health (NIH, Bethesda, MD, USA), Recommended Daily Allowance (RDA) of Se is 55 μg/day for men of 31–50 years old up to 70 μg/day for women on lactation. Se-enriched eggs can be obtained in more than 25 countries worldwide [36,38]
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