Human progesterone A-receptors can be synthesized intracellularly and are biologically functional.
In order to investigate the origin and functional independence of the human progesterone receptor A binding protein, we have expressed a truncated human progesterone receptor cDNA in both gene transfer and in vitro translation assays. Proteins identical in size and antigenicity to the A-receptors found naturally in human progesterone target cells are synthesized from this cDNA that lacks the putative B receptor initiator methionine codon of the complete cDNA. The functional independence of A-receptors is suggested by their ability to bind hormone and to stimulate transcription from the progestin responsive mouse mammary tumor virus promoter.
Krett
N L
NL
Department of Medicine, University of Colorado Health Sciences Center, Denver 80262.
Wei
L L
LL
Francis
M D
MD
Nordeen
S K
SK
Gordon
D F
DF
Wood
W M
WM
Horwitz
K B
KB
D015153:Blotting, Western; D003001:Cloning, Molecular; D003593:Cytoplasm / Q000378:metabolism; D004247:DNA / Q000235:genetics; D005786:Gene Expression Regulation; D006801:Humans; D011233:Precipitin Tests; D011397:Promegestone / Q000378:metabolism; D011980:Receptors, Progesterone / Q000096:biosynthesis / Q000235:genetics / Q000502:physiology*; D014162:Transfection
D011980:Receptors, Progesterone; D004247:DNA; D011397:Promegestone