Background Recently, we demonstrated that AQP1 and AQP5 in the porcine

Background Recently, we demonstrated that AQP1 and AQP5 in the porcine uterus are regulated by steroid hormones (P4, E2), arachidonic acid (AA), forskolin (FSK) and cAMP during the estrous cycle. increased the expression of AQP1/AQP5 mRNAs and BMS-265246 proteins in the myometrium during mid-luteal BMS-265246 phase. Moreover, a stimulatory effect of forskolin and cAMP on the expression of AQP1/AQP5 mRNAs and proteins in the endometrium and myometrium dominated during luteolysis, but during the mid-luteal phase their influence on the expression of these AQPs was differentiated depending on the type of tissue and the incubation duration. Conclusions These results seem to indicate that uterine tissues; endometrium and myometrium, exhibit their own AQP expression profiles in response to examined factors. Moreover, the responses of AQP1/AQP5 at mRNA and protein levels to the studied factors in the endometrium and myometrium are more pronounced during luteolysis. This suggests that the above effects of the studied factors are connected with morphological and physiological changes taking place in the pig uterus during the estrous cycle. studies, Franczak and Kotwica [4], and Wojciechowicz et al. [5] reported that both porcine endometrium and myometrium are steroidogenic tissues producing progesterone, estrogens and androgens. Other reports indicate that porcine endometrium [6C8] as well as myometrium [9, 10] also produce PGE2 and PGF2alpha. As a result of ovarian steroid action, the uterine glands expand and the secretory activity increases, becoming the highest at the end of the secretory phase, while during luteolysis, under the influence of oxytocin (OT), uterine fluids and unnecessary cell debris are excreted [11, 12]. Aquaporins (AQPs) are BMS-265246 ubiquitous membrane proteins which provide a molecular basis for transmembrane water transport [13]. AQPs are constitutively expressed in the cell membranes, to where they may be trafficked from intracellular vesicles upon appropriate stimulation [14]. So far, at least nine AQP isoforms (including AQP1 and AQP5) have been confirmed in the female reproductive system of humans, rats, mice and pigs Tpo [15]. BMS-265246 AQP1 is found in many secretory and osmotically-active tissues [16], and is expressed in vascular endothelial cells throughout the body [17, 18]. AQP5 is mainly located in the apical plasma membranes of various secretory glands [19]. Studies with animal models and humans have shown that sufficient expression and proper subcellular targeting of AQP5 channels are necessary to support physiological BMS-265246 functions [20C22]. The transport and homeostasis of water in the endometrium is crucial for maintaining proper reproductive processes. Previous reports have demonstrated that the vasculature and epithelium of the uterus have high expression of AQPs [23C25] and that uterine fluid homeostasis is effectively regulated by steroid hormones [26]. Our previous research indicated that AQP1, 5 and 9 are expressed in the porcine uterus, [27, 28], oviduct [29], ovary [30] and peri-ovarian vascular complex [31]. We also observed that these AQPs are differently localized and expressed in these structures during the estrous cycle and early pregnancy. Very recently, we described the response of AQPs (AQP1 and AQP5) to treatments with steroids, OT, arachidonic acid (AA), forskolin (FSK) and cAMP in the uterine explants from cyclic gilts during the mid-luteal phase (Days 10C12) and luteolysis (Days 14C16) [32]. However, to date, the potential of the porcine uterine tissues, endometrium and myometrium to express AQPs has not been studied separately. Therefore, the objectives of the study were: 1/ to describe endometrial and myometrial basal expression of AQP1/AQP5 mRNAs and proteins during Days 10C12 (the mid-luteal phase) and Days 14C16 (luteolysis) of the estrous cycle; 2/ to evaluate whether the steroid hormones (P4 and E2), OT, AA (substrate for prostaglandin synthesis), FSK (adenylate cyclase activator) and cAMP (cyclic adenosine monophosphate; second messenger) may regulate the endometrial and myometrial AQP1 and AQP5 expression at the mRNA and protein levels during these periods. It is assumed that the obtained results will provide useful information on the regulatory mechanism concerning the examined aquaporins in the porcine endometrium and myometrium. Methods Animals and sample collection All experiments were performed in accordance with the.

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