Cloning and expression of a novel, truncated, progesterone receptor.
Article Details
- CitationCopy to clipboard
Saner KJ, Welter BH, Zhang F, Hansen E, Dupont B, Wei Y, Price TM
Cloning and expression of a novel, truncated, progesterone receptor.
Mol Cell Endocrinol. 2003 Feb 28;200(1-2):155-63.
- PubMed ID
- 12644308 [ View in PubMed]
- 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.