Expression and transcriptional activity of progesterone receptor A and progesterone receptor B in mammalian cells.
Progesterone is an essential regulator of normal female reproductive function. Its effects are mediated by two nuclear progesterone receptor (PR) proteins, PRA and PRB, which are identical except for an additional 164 amino acids at the N-terminal end of PRB. Transcriptional analyses of the two receptor forms have assigned strikingly distinct functional signatures to the two PRs, despite their apparent physical similarity. The basis of these differences is yet to be fully understood. Furthermore, these differences are strongly influenced by the cell type and the promoter used. We review the mammalian transcriptional studies of PRA and PRB, and compare them with what is known about their expression and function in target tissues.
Graham
J Dinny
JD
Westmead Institute for Cancer Research, University of Sydney Westmead Hospital, New South Wales, Australia. Dinny_Graham@wmi.usyd.edu.au
Clarke
Christine L
CL
D014408:Biomarkers, Tumor / Q000378:metabolism; D001943:Breast Neoplasms / Q000235:genetics* / Q000378:metabolism; D002471:Cell Transformation, Neoplastic / Q000235:genetics / Q000378:metabolism; D005260:Female; D006801:Humans; D011980:Receptors, Progesterone / Q000235:genetics* / Q000378:metabolism; D015398:Signal Transduction; D014158:Transcription, Genetic; D015533:Transcriptional Activation
D014408:Biomarkers, Tumor; D011980:Receptors, Progesterone; C101118:progesterone receptor A; C097314:progesterone receptor B