Cloning and expression of a novel, truncated, progesterone receptor

Karla J. Saner, Brenda H. Welter, Fan Zhang, Elizabeth Hansen, Barbara Dupont, Yangzhan Wei, Thomas M. Price

Research output: Contribution to journalArticlepeer-review

49 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)155-163
Number of pages9
JournalMolecular and Cellular Endocrinology
Volume200
Issue number1-2
DOIs
StatePublished - Feb 28 2003

Keywords

  • Human aortic endothelial cells
  • Non-genomic
  • Progesterone receptor
  • T47D breast cancer cells
  • T47D-Y breast cancer cells

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Endocrinology

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