University of Leicester
Browse

The progesterone receptor in human term amniochorion and placenta is isoform C.

Download (428.33 kB)
journal contribution
posted on 2009-12-08, 16:04 authored by Anthony H. Taylor, Penny C. McParland, David J. Taylor, Stephen C. Bell
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 extraembryonic tissues and may be involved in the regulation of human parturition.

History

Citation

Endocrinology, 2006, 147 (2), pp.687-693

Version

  • VoR (Version of Record)

Published in

Endocrinology

Publisher

The Endocrine Society

issn

0013-7227

eissn

1945-7170

Copyright date

2005

Available date

2009-12-08

Publisher version

http://endo.endojournals.org/content/147/2/687

Language

en

Usage metrics

    University of Leicester Publications

    Categories

    No categories selected

    Keywords

    Exports

    RefWorks
    BibTeX
    Ref. manager
    Endnote
    DataCite
    NLM
    DC