Cloning and expression of a novel, truncated, progesterone receptor.

Journal Article (Journal Article)

Progesterone acts via two specific receptors to affect gene transcription in target tissues. Progesterone receptor (PR) B contains 933 amino acids while PR A is a truncated version lacking the initial 164 amino acids. We have cloned a novel, truncated PR from both human adipose and aortic cDNA libraries. This cDNA encodes a predicted protein of 314 amino acids, termed PR-M. Initiation of transcription of PR-M occurs in intron 3, with the initial exon identical to exon 4 of the genomic PRs, except for a novel 16 amino acid amino-terminal sequence, consistent with a signal peptide. The remainder of PR-M is identical to the genomic PR. Transcript for this protein was identified by RT-PCR in human aortic endothelial cells and T47D breast cancer cells. Expression of PR-M in Sf 9 insect cells results in a 38-kDa protein, demonstrated in human aortic endothelial cells and T47D breast cancer cells. The function of PR-M remains to be determined. The presence of a signal peptide and the lack of a DNA binding region suggests a non-genomic action.

Full Text

Duke Authors

Cited Authors

  • Saner, KJ; Welter, BH; Zhang, F; Hansen, E; Dupont, B; Wei, Y; Price, TM

Published Date

  • February 28, 2003

Published In

Volume / Issue

  • 200 / 1-2

Start / End Page

  • 155 - 163

PubMed ID

  • 12644308

International Standard Serial Number (ISSN)

  • 0303-7207

Digital Object Identifier (DOI)

  • 10.1016/s0303-7207(02)00380-5


  • eng

Conference Location

  • Ireland