Abstract
Chemerin, belonging to the adipokine family, exhibits pleiotropic activity. We hypothesised that the adipokine could be involved in the regulation of steroidogenesis in the porcine endometrium. Thus, the aim of this study was to determine the effect of chemerin on the key steroidogenic enzyme proteins’ abundance (Western blot), as well as on P4 and E2 secretion (radioimmunoassay) by the porcine endometrium during early pregnancy and the mid-luteal phase of the oestrous cycle. Moreover, we investigated the hormone impact on Erk and Akt signalling pathway activation (Western blot). Chemerin stimulated E2 production on days 10 to 11 of pregnancy. On days 10 to 11 and 15 to 16 of gestation, and on days 10 to 11 of the cycle, chemerin enhanced the expression of StAR and all steroidogenic enzyme proteins. On days 12 to 13 of pregnancy, chemerin decreased StAR and most of the steroidogenic enzyme proteins’ abundance, whereas the P450C17 abundance was increased. On days 27 to 28 of pregnancy, chemerin increased StAR and P450C17 protein contents and decreased 3βHSD protein amounts. It was noted that the adipokine inhibited Erk1/2 and stimulated Akt phosphorylation. The obtained results indicate that chemerin affected P4 and E2 synthesis through the Erk1/2 and Akt signalling pathways.
Highlights
Chemerin was first described as retinoic acid responder protein 2 (RARRES2) or tazarotene-induced gene 2 protein (TIG2) [1]
On days 12 to 13 of gestation and 10 to 11 of the oestrous cycle, chemerin at the dose of 100 ng/mL reduced the release of P4
On days 15 to 28 of pregnancy and during the mid-luteal phase of the cycle, chemerin did not affect the secretion of E2 (p < 0.05; Figure 1b)
Summary
Chemerin was first described as retinoic acid responder protein 2 (RARRES2) or tazarotene-induced gene 2 protein (TIG2) [1]. Chemerin belongs to the group of adipokines, hormones produced mainly in the adipose tissue, and cytokines, a large group of proteins secreted by specific cells of the immune system [2]. The hormone is produced as a 163-amino-acid protein (prochemerin) and is non-active before the cleavage of the Cterminus [2]. Expression of RARRES2, the gene encoding chemerin, has been noted in various tissues of humans, rodents, bovine, poultry, and pigs [3,4,5,6,7]. The highest expression of the adipokine was noted in the white adipose tissue, liver, and placenta. In the case of porcine tissues, in our previous studies, we have indicated chemerin gene and protein expression in the elements of the female hypothalamic–pituitary–gonadal (HPG) axis [4,5,6], as well as in the uterus [7]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
