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 language | English (US) |
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Pages (from-to) | 155-163 |
Number of pages | 9 |
Journal | Molecular and Cellular Endocrinology |
Volume | 200 |
Issue number | 1-2 |
DOIs | |
State | Published - 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