title: Transcription-dependent and transcription-independent functions of the classical progesterone receptor in Xenopus ovaries.
abstract: Two forms of the classical progesterone receptors (PR), XPR-1 and XPR-2, have been cloned in Xenopus laevis. Their relative roles in mediating progesterone action in the ovaries are not clear. Using antibodies generated against the cloned XPR-2, we demonstrated here that the somatic follicle cells expressed an 80-kDa PR protein, termed XPR-1. Treatment of follicle cells with progesterone resulted in disappearance of this protein, consistent with proteosome-mediated XPR-1 protein degradation. A smaller (approximately 70 kDa) PR protein, termed XPR-2, was expressed in the oocytes, but not in follicle cells. XPR-2 underwent progesterone-induced phosphorylation but not protein degradation. Treating isolated ovarian fragments with progesterone caused oocyte maturation and the release of the mature oocytes from the ovarian tissues ("ovulation"). Inhibition of transcription, with actinomycin D, did not interfere with progesterone-induced oocyte maturation but blocked "ovulation" so that mature oocytes were trapped in the follicles. These results suggest that the dual functions of progesterone, transcription-dependent follicle rupture and transcription-independent oocyte maturation, are mediated by the two forms of PR proteins differentially expressed in the follicle cells and the oocytes, respectively.
authors.affiliation: Ottawa Health Research Institute, Ottawa Hospital Civic Campus, 1053 Carling Avenue, Ottawa, Ontario, Canada K1Y 4E9.
authors.forename: Xun Shawn
authors.initials: XS
authors.lastname: Liu
authors.forename: Chunqi
authors.initials: C
authors.lastname: Ma
authors.forename: Al-Walid
authors.initials: AW
authors.lastname: Hamam
authors.forename: X Johné
authors.initials: XJ
authors.lastname: Liu
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D005260:Female; D018507:Gene Expression Regulation, Developmental; D008969:Molecular Sequence Data; D009024:Morphogenesis; D009865:Oocytes / Q000502:physiology; D006080:Ovarian Follicle / Q000196:embryology / Q000502:physiology; D010053:Ovary / Q000196:embryology* / Q000502:physiology; D011980:Receptors, Progesterone / Q000737:chemistry / Q000235:genetics*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014158:Transcription, Genetic; D029867:Xenopus Proteins / Q000737:chemistry / Q000235:genetics*
chemical_list: D011980:Receptors, Progesterone; C419774:XPR-1 protein, Xenopus; D029867:Xenopus Proteins; C503420:pr2 protein, Xenopus