Tyrosine phosphorylation is not a relevant mechanism to modulate aquaporin 2 activity in gestational queen endometrium and placenta. Issue 4 (31st January 2020) - Ferré‐Dolcet, Lluis
Abstract: Aquaporins have been shown to be regulated by phosphorylation of serine residues, but the possible role of tyrosine residues phosphorylation has not been evaluated. Changes in the localization of aquaporin 2 (AQP2) in the queen endometrium have been related to serum progesterone levels. The aim of this study was to determine whether these AQP2‐localization changes are mediated by variations in its tyrosine phosphorylation levels. Twelve queens were included in the study and divided into (a) non‐macroscopically pregnant with low levels of progesterone; (b) non‐macroscopically pregnant with high levels of progesterone; (c) 30 days of pregnancy; and (d) 60 days of pregnancy. Samples from endometrium and placental transference zone were obtained, immunoprecipitated and analysed by immunoblotting to determine the abundance of AQP2 and its relative levels of tyrosine phosphorylation. No significant differences in the tyrosine phosphorylation levels of immunoprecipated‐AQP2 were observed between groups. We can thus conclude that changes in the localization of AQP2 in the queen endometrium are not modulated by tyrosine phosphorylation.