| Abstract: | Selenium is a biologically active trace elements, which is part of several proteins, and thus linked with the activity of many organs, tissues and systems of organism. There are 25 mammalian selenoproteins at present, one of which is SelV (Selenoprotein V). Since this protein has thioredoxin-like folding and a conserved motif (CXXU, where C is cysteine, U-selenocysteine) in its catalytic center, it belongs to the family of redox proteins, whose members are involved in redox reactions. In this paper, we show that the redox protein SelV can interact with O-linked N-acetylglucosamine transferase (OGT) and proteins belonging to the family of ASB: Asb-17, and Asb-9. The specificity of interactions SelV with OGT and Asb-9, but not with Asb-17 is confirmed by coimmunopretsipitation. In addition, expression of SelV mRNA in the later stages spermatogenesis, as well as in puberty and reproductive periods of rats is shown. |
