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Submitted on April 28, 2005
Accepted on October 19, 2005
Preterm Birth Research Group, Reproductive Sciences, Department of Cancer Studies and Molecular Medicine, University of Leicester, Leicester, Leicestershire, LE2 7LX, UK
* To whom correspondence should be addressed. E-mail: aht3{at}le.ac.uk.
The mechanism that initiates human parturition has been proposed to be ‘functional progesterone withdrawal’ whereby the 116-kDa B-isoform of the progesterone receptor (PR-B) switches in favor of the 94-kDa A-isoform (PR-A) in reproductive tissues. Recently, other PR isoforms, PR-S, PR-C and PR-M generated from the same gene have been identified and partially characterized. Using immunohistochemical, western blotting and RT-PCR techniques, evidence is provided that the major PR isoform present in human term fetal membranes (amnion and chorion) and syncytiotrophoblast of the placenta is neither of the classical nuclear PR-B or PR-A isoforms but is the N terminally truncated 60 kDa PR-C isoform. Evidence is also provided that the PR-C isoform resides in the cytoplasm of the expressing cell types. Data are also presented to show that PR-B PR-A and PR-S isoforms are essentially absent from the amnion and chorion, whereas PR isoforms A, B, C and S are all present in the decidua, with PR-A being the major isoform. The syncytiotrophoblast of the placenta contains the cytoplasmic PR-C isoform, but not PR-A, PR-B or PR-S. The major PR isoform in the amnion, chorion and placenta is PR-C, suggesting that the cytoplasmic PR-C isoform has a specific role in extra-embryonic tissues and may be involved in the regulation of human parturition.
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