Abstract
Progesterone receptor (PGR) for its action required connection of the coregulatory proteins, including coactivators and corepressors. The former group exhibits a histone acetyltransferase (HAT) activity, while the latter cooperates with histone deacetylase (HDAC). Regulations of the coregulators mRNA and protein and HAT and HDAC activity can have an indirect effect on the PGR function and thus progesterone (P4) action on target cells. The highest mRNA expression levels for the coactivators—histone acetyltransferase p300 (P300), cAMP response element-binding protein (CREB), and steroid receptor coactivator-1 (SRC-1)—and nuclear receptor corepressor-2 (NCOR-2) were found in the corpus luteum (CL) on days 6 to 16 of the estrous cycle. The CREB protein level was higher on days 2–10, whereas SRC-1 and NCOR-2 were higher on days 2–5. The activity of HAT and HDAC was higher on days 6–10 of the estrous cycle. All of the coregulators were localized in the nuclei of small and large luteal cells. The mRNA and protein expression levels of the examined coactivators and corepressor changed with the P4 level. Thus, P4 may regulate CL function via the expression of coregulators, which probably affects the activity of the PGR.
Highlights
Progesterone (P4) is a steroid hormone produced by the follicle, corpus luteum (CL), and placenta; it plays a crucial role in regulating the length of the estrous cycle, blastocyst implantation, and the maintenance of pregnancy in many species of mammals, including cows [1]
Positive immunostaining for coactivators P300, cAMP response element-binding protein (CREB), and steroid receptor coactivator-1 (SRC–1) and corepressor nuclear receptor corepressor-2 (NCOR-2) in CL slices on days 6–10 of the estrous cycle was observed in the nuclei of small and large luteal cells
Immunohistochemical analysis shows the localization of proteins for coactivators P300, CREB, and steroid receptor coactivator-1 (SRC-1), and corepressor NCOR-2 in the nuclei of small and large luteal cells in the CL
Summary
Progesterone (P4) is a steroid hormone produced by the follicle, corpus luteum (CL), and placenta; it plays a crucial role in regulating the length of the estrous cycle, blastocyst implantation, and the maintenance of pregnancy in many species of mammals, including cows [1]. The genomic action of P4 is mediated by their specific nuclear receptors (PGRs). These receptors are ligand-regulated transcription factors activated by P4. The cellular response to P4 is mediated by two isoforms of the PGR: isoform A (PGRA) and isoform B (PGRB). Both isoforms are transcribed from the same gene under the influence of two different promoters [2]. They differ in their length—PGRB is longer than
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