Expression of perivitelline membrane glycoprotein ZP1 in the liver of Japanese quail (Coturnix japonica) after in vivo treatment with diethylstilbestrol.
ABSTRACT Avian perivitelline membrane, an oocyte extracellular matrix homologous to the zona pellucida in mammals or chorion in fish, is composed of at least two glycoproteins. Previous studies have indicated that one of the components, a glycoprotein homologous to mammalian ZPC, is produced in the granulosa cells of the developing follicles of quail ovary on stimulation with testosterone. However, little is known about the molecular biology of the other component of the avian perivitelline membrane, ZP1, and information about gene expression is particularly lacking. We have cloned the ZP1 in Japanese quail and examined its gene expression. A cDNA encoding quail ZP1 was isolated from the livers of mature females using reverse transcription-polymerase chain reaction (RT-PCR) and rapid amplification of cDNA ends. It encoded a 934-amino acid protein that showed greatest homology (87.8% identity) with the chicken ZP1. RT-PCR amplification indicated that the ZP1 mRNA in the liver was restricted to mature laying females. The expression of ZP1 mRNA was stimulated by in vivo treatment with diethylstilbestrol in immature females as well as males. These results suggested that androgens and estrogens coordinately regulate the formation of quail perivitelline membrane proteins. In addition, the use of ZP1 transcriptional induction in males or immature females as a biological marker of environmental estrogens is discussed.
- Journal of Poultry Science - J POULT SCI. 01/2004; 41(4):289-297.
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ABSTRACT: The avian perivitelline layer (PL), a vestment homologous to the zona pellucida (ZP) of mammalian oocytes, is composed of at least three glycoproteins. Our previous studies have demonstrated that the matrix's components, ZP3 and ZPD, are synthesized in ovarian granulosa cells. Another component, ZP1, is synthesized in the liver and is transported to the ovary by blood circulation. In this study, we report the isolation of cDNA encoding quail ZP2 and its expression in the female bird. By RNase protection assay and in situ hybridization, we demonstrate that ZP2 transcripts are restricted to the oocytes of small white follicles (SWF). The expression level of ZP2 decreased dramatically during follicular development, and the highest expression was observed in the SWF. Western blot and immunohistochemical analyses using the specific antibody against ZP2 indicate that the 80 kDa protein is the authentic ZP2, and the immunoreactive ZP2 protein is also present in the oocytes. Moreover, ultrastructural analysis demonstrated that the immunoreactive ZP2 localizes to the zona radiata, the perivitelline space, and the oocyte cytoplasm in the SWF. By means of western blot analysis and immunofluorescence microscopy, we detected a possible interaction of the recombinant ZP2 with ZP3 and that this interaction might lead to the formation of amorphous structure on the cell surface. These results demonstrate for the first time that the avian ZP gene is expressed in the oocyte, and that the ZP2 protein in the oocyte might play a role for the PL formation in the immature follicles of the ovary.Reproduction 10/2009; 139(2):359-71. · 3.56 Impact Factor
Article: Can ovarian follicles fossilize?[Show abstract] [Hide abstract]
ABSTRACT: ARISING FROM X. Zheng et al. 495, 507-511(2013)In a recent report Zheng et al. describe ovarian follicles in three fossil birds from the Early Cretaceous period of China belonging to Jeholornis and two enantiornithine species. Because these were situated in the left half of the body cavity of the fossils, the authors suppose that the right ovary was already reduced in these early birds. Fossilization of ovarian follicles would constitute an extraordinary case of soft tissue preservation, but the morphology of the fossil structures does not agree with the ovulation mode of coelurosaurs. There is a Reply to this Brief Communication Arising by O'Connor, J., Zheng, X. & Zhou, Z. Nature 499, http://dx.doi.org/10.1038/nature12368 (2013).Nature 07/2013; 499(7457):E1. · 38.60 Impact Factor