scholarly journals Characterization of Nuclear Progesterone Receptor Isoforms in the Term Equine Placenta

2021 ◽  
Vol 8 ◽  
Author(s):  
Ahmed M. Nagy ◽  
Swanand R. Sathe ◽  
Attia H. Atta ◽  
Abdel Mohsen M. Hammam ◽  
Walter H. Hsu

In equine parturition, the role of progestins along with the nuclear progesterone receptor (nPR) signaling pathway in the placenta is not completely clarified. The progestins play an integral role in maintaining myometrial quiescence during the late stage of pregnancy via acting on nPR isoforms (PRA and PRB; PRB is more active than PRA). The current study aimed to determine the PRA and PRB expressions in the term equine placenta at the gene and protein levels. Six term equine placentas were used in this study. Reverse transcription polymerase chain reaction (RT-PCR) was used to quantify the mRNA expression for PRA and PRB. The protein expression was detected using the Western Blot technique. The results revealed that the mRNA and protein expressions for PRA were significantly higher (P < 0.0001) in the term equine placental tissue compared to the mRNA and protein expressions of PRB. These results demonstrated that nPRs are detectable in the term placenta of mares and PRA is the dominant isoform expressed. The present findings raised the possibility that the PRA plays an important role in the parturition process and expulsion of the placenta in mares.

2014 ◽  
Vol 21 (2) ◽  
pp. 155-173 ◽  
Author(s):  
B. Patel ◽  
S. Elguero ◽  
S. Thakore ◽  
W. Dahoud ◽  
M. Bedaiwy ◽  
...  

2011 ◽  
Vol 14 (1) ◽  
pp. 149-158 ◽  
Author(s):  
R. Rękawiecki ◽  
M. Kowalik ◽  
J. Kotwica

Nuclear progesterone receptor isoforms and their functions in the female reproductive tract Progesterone (P4), which is produced by the corpus luteum (CL), creates proper conditions for the embryo implantation, its development, and ensures proper conditions for the duration of pregnancy. Besides the non-genomic activity of P4 on target cells, its main physiological effect is caused through genomic action by the progesterone nuclear receptor (PGR). This nuclear progesterone receptor occurs in two specific isoforms, PGRA and PGRB. PGRA isoform acts as an inhibitor of transcriptional action of PGRB. The inactive receptor is connected with chaperone proteins and attachment of P4 causes disconnection of chaperones and unveiling of DNA binding domain (DBD). After receptor dimerization in the cells' nucleus and interaction with hormone response element (HRE), the receptor coactivators are connected and transcription is initiated. The ratio of these isoforms changes during the estrous cycle and reflects the different levels of P4 effect on the reproductive system. Both isoforms, PGRA and PGRB, also show a different response to the P4 receptor antagonist activity. Connection of the antagonist to PGRA can block PGRB, but acting through the PGRB isoform, P4 receptor antagonist may undergo conversion to a strongly receptor agonist. A third isoform, PGRC, has also been revealed. This isoform is the shortest and does not have transcriptional activity. Alternative splicing and insertion of additional exons may lead to the formation of different PGR isoforms. This paper summarizes the available data on the progesterone receptor isoforms and its regulatory action within the female reproductive system.


2014 ◽  
Vol 102 (3) ◽  
pp. e128
Author(s):  
M. Peavey ◽  
X. Li ◽  
M. Wetendorf ◽  
C. Yallampalli ◽  
J. Lydon ◽  
...  

Steroids ◽  
2013 ◽  
Vol 78 (5) ◽  
pp. 500-507 ◽  
Author(s):  
Valeria Hansberg-Pastor ◽  
Aliesha González-Arenas ◽  
Miguel A. Peña-Ortiz ◽  
Elizabeth García-Gómez ◽  
Mauricio Rodríguez-Dorantes ◽  
...  

Author(s):  
Ignacio Camacho-Arroyo ◽  
Valeria Hansberg-Pastor ◽  
Edith Cabrera-Muñoz ◽  
Olivia Tania Hernández-Hernández ◽  
Aliesha González-Arenas

2009 ◽  
Vol 90 (1) ◽  
pp. 73-81 ◽  
Author(s):  
Christian Guerra-Araiza ◽  
Porfirio Gómora-Arrati ◽  
Marcos García-Juárez ◽  
Alejandra Armengual-Villegas ◽  
Alfredo Miranda-Martínez ◽  
...  

2016 ◽  
Vol 28 (7) ◽  
pp. 907 ◽  
Author(s):  
Robert Rekawiecki ◽  
Magdalena Karolina Kowalik ◽  
Jan Kotwica

The aim of the present study was to examine the effects of luteotropic and luteolytic factors on the mRNA and protein levels of progesterone receptor isoforms A (PGRA) and B (PGRB) in the bovine endometrium. Endometrial slices from Days 6–10 and 17–20 of the oestrous cycle were treated with LH (100 ng mL–1), oestradiol (E2; 1 × 10–8 M), prostaglandin (PG) E2 (1 × 10–6 M) and PGF2α (1 × 10–6 M) and the nitric oxide donor NONOate (1 × 10–4 M); these treatments lasted for 6 h for mRNA expression analysis and 24 h for protein expression analysis. On Days 6–10 of the oestrous cycle PGRAB (PGRAB; the entire PGRA mRNA sequence is common to the PGRB mRNA sequence) mRNA expression in endometrial slices was enhanced by E2 treatment (P < 0.001), whereas PGRB mRNA expression was increased by LH (P < 0.001), E2 (P < 0.05) and NONOate (P < 0.05) treatment. On Days 17–20, PGRAB mRNA expression increased after E2 (P < 0.001) and PGE2 (P < 0.05) treatment; PGRB mRNA expression was increased by PGE2 (P < 0.05) and PGF2α (P < 0.01) treatment, but decreased by LH (P < 0.05). On Days 6–10 protein levels of PGRA were stimulated by E2 (P < 0.01), whereas PGRB protein levels were increased by LH (P < 0.05) and E2 (P < 0.05). On Days 17–20 of the oestrous cycle, PGRA protein levels were enhanced by E2 (P < 0.05) and PGF2α (P < 0.05), whereas PGRB protein levels were stimulated by PGE2 (P < 0.05) and PGF2α (P < 0.001). These data suggest that luteotropic and luteolytic factors affect PGRA and PGRB mRNA and protein levels, and this may regulate the effects of progesterone on endometrial cells.


iScience ◽  
2021 ◽  
pp. 103487
Author(s):  
Rong Li ◽  
Xiaoqiu Wang ◽  
Zhenyao Huang ◽  
Jayani Balaji ◽  
Tae Hoon Kim ◽  
...  

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