βhCG protein expression is upregulated in JEG-3 cells by StarD7 silencing.
Cells were transfected with scrambled or StarD7.1 siRNAs for 6 h and then cultured until 72 hours. A- βhCG and StarD7 protein expression were analyzed by western blot. Protein extracts (100 µg/lane) from StarD7.1 siRNA-transfected (siD7) or scrambled siRNA-transfected (siC) cells were electrophoresed on a 7.5% SDS polyacrylamide gel and transferred to a nitrocellulose filter. Filters were incubated with anti-βhCG (top), anti-StarD7Ct (middle) and with the monoclonal anti-α-tubulin antibodies (bottom). These immunoblots are representative of at least three separate experiments. B- The bar graph represents the densitometric quantification of βhCG protein levels in StarD7 siRNA-transfected JEG-3 cells normalized to α-tubulin of five separate experiments relative to the corresponding normalized protein levels in scrambled siRNA-transfected cells defined as 1 (median and 25th–75th% percentiles). C- hCG secretion from JEG-3 cells after 48 h or 72 h of culture in StarD7.1 siRNA-transfected condition compared to scrambled siRNA-transfected cell culture defined as 1 (n = 5). *p<0.05 compared to scrambled siRNA-transfected cells.