Type I deiodinase is the best characterized member of a small family of selenoenzymes catalyzing the bioactivation and disposal of thyroid hormone. This enzyme is an integral membrane protein composed of two 27-kDa subunits that assemble into a functional enzyme after translation using a highly conserved sequence of 16 amino acids in the C-terminal half of the polypeptide, (148)DFLXXYIXEAHXXDGW(163). In this study, we used alanine scanning mutagenesis to identify the key residues in this domain required for holoenzyme assembly.
View Article and Find Full Text PDFBackground: Gestational hypertensive disorders are a leading cause of maternal mortality in the US, accounting for up to 10% of these deaths. During pregnancy, a new rat model (SHHF rat) has been shown to develop spontaneous hypertension with increases of more than 40 mm Hg systolic blood pressure (BP), which resolves after delivery, and which lead us to ask whether the hypertension may be triggered by increased levels of progesterone in these rats.
Methods: To test this hypothesis, groups of SHHF rats were treated with progesterone (PROG), estrogen (EST), or progesterone and estrogen (PROG+EST) that correspond to levels that occur during pregnancy.