Abstract
The novel selenium (Se)‐containing strong antioxidant selenoneine, 2‐selenyl‐Nα, Nα, Nα‐trimethyl‐L‐histidine, has recently been discovered to be the predominant form of organic Se in tuna blood (Yamashita & Yamashita, JBC, 285, 18134–18138, 2010). This compound is thought to play a key role in the Se redox antioxidant mechanism in animal cells. Here, we report evidence that the uptake of selenoneine was mediated by organic cations/carnitine transporter‐1 (OCTN1). Although OCTN1 has been known to transport some kinds of organic cations, such as ergothioneine, triethylamine, and carnitine, our data indicate that selenoneine in culture medium is incorporated into human embryonic kidney HEK293 and zebrafish embryo cells by OCTN1. The Km value of selenoneine uptake was determined to be 13.0 μM in HEK293 cells and 9.5 μM in zebrafish erythrocytes, respectively, indicating that selenoneine is the most specific substrate for the OCTN1 in the human and zebrafish cells. When we added selenoneine into culture media of HUVEC and zebrafish embryonic ZE cultured cells, cell growth was promoted and GPx1 gene expression was induced, and cellular ROS level was reduced. Therefore, selenium redox status, mediated by incorporation of selenoenine via OCTN1, might be important in inflammatory and chronic diseases, and methylmercury detoxification caused by Se deficiency and/or oxidative damages.
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