Expression of perivitelline membrane glycoprotein ZP1 in the liver of Japanese quail (Coturnix japonica) after in vivo treatment with diethylstilbestrol
Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University, 836 Ohya, Shizuoka 422-8529, Japan.The Journal of Steroid Biochemistry and Molecular Biology (Impact Factor: 3.63). 02/2003; 84(1):109-16. DOI: 10.1016/S0960-0760(03)00008-6
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.
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- "The CTPs of these proteins, that are missing from assembled VE proteins (Sugiyama et al., 1999), are essentially equivalent to construct ZP3-FLAG-370 (Jovine et al., 2004). Similarly, precursors of avian ZP1 homologues, also secreted by the liver (Sasanami et al., 2003; Bausek et al., 2000), terminate with the EHP. Finally, EHPs were identified in sequences of precursors of other ZP domain proteins, both with and without C-terminal TMDs (Jovine et al., 2004). "
ABSTRACT: For sperm to fertilize eggs, they must bind to and penetrate the zona pellucida (ZP) that surrounds the plasma membrane of all mammalian eggs. The ZP first appears during oocyte growth and increases in thickness as oocytes increase in diameter. The ZP is an extracellular matrix composed of long, crosslinked filaments. In mice, three glycoproteins, called mZP1-3, are synthesised and secreted by growing oocytes and assembled into a thick (-6.5 microm) extracellular coat over a 2-3 week period. Recently, we identified several regions of nascent ZP glycoproteins that affect their secretion and incorporation into the ZP (assembly) by growing oocytes. Among these are the ZP domain, the consensus furin cleavage site (CFCS) and the C-terminal propeptide (CTP) with its transmembrane domain (TMD), external hydrophobic patch (EHP), charged patch (CP), conserved cysteine (Cys) residue, and short cytoplasmic tail (CT). Particularly important is the ZP domain, a approximately 260 amino acid region with 8 conserved Cys residues that is common to a variety of extracellular proteins of diverse functions found in a wide range of multicellular eukaryotes. Our results show that the ZP domain functions as a polymerisation module and that its N-terminal half, including 4 conserved Cys residues, is largely responsible for this role. Additionally, two conserved hydrophobic sequences, one within the ZP domain (internal hydrophobic patch; IHP) and another within the CTP (EHP), apparently regulate polymerisation of nascent ZP glycoproteins. Collectively, our findings suggest a general mechanism for assembly of all ZP domain proteins based on coupling between proteolytic processing and polymerisation.Society of Reproduction and Fertility supplement 02/2007; 63:187-201.
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- "In birds, fertilization occurs within the infundibulum portion of the oviduct, and only the PL encloses the oocyte at the time of fertilization. At least two glycoproteins have been identified as constituents of the avian PL; ZP1 (ZPB1) and ZP3 (ZPC) in Japanese quail (Pan et al. 2001, Sasanami et al. 2003) and ZP1 (ZPB1), ZPB (ZPB2), ZP2 (ZPA), ZP3 (ZPC), and ZPD in chicken (Waclawek et al. 1998, Bausek et al. 2000, Okumura et al. 2004, Smith et al. 2005). We have previously cloned the cDNA encoding ZP3 (GenBank Accession no. "
ABSTRACT: The extracellular matrix surrounding avian oocytes, called the perivitelline membrane (PL), consists of at least two major glycoproteins, ZP3 and ZP1. Our previous study using Japanese quail had demonstrated that the PL obtained from the preovulatory follicles was incubated in vitro with spermatozoa, and perforations were observed. This result indicated that the PL might contain a constituent that possesses activity to initiate the acrosome reaction (AR) in quail. In order to elaborate upon our previous findings, we evaluated the effects of ZP3 and ZP1 on the induction of sperm AR in Japanese quail. Ejaculated sperm were incubated with or without the purified PL glycoprotein, and their acrosome status was determined based on the presence or absence of the acrosome. Treatment of spermatozoa with increasing doses of the purified monomeric ZP1 led to a concentration-dependent stimulation of AR. The purified dimeric ZP1 had similar effect. Moreover, we found that the ZP1-induced AR was significantly blocked by the digestion of the PL protein with PNGaseF. In contrast, the addition of purified ZP3 failed to induce AR at any doses tested. These results indicate that N-linked glycans on ZP1 play an important role in triggering the AR in Japanese quail.Reproduction (Cambridge, England) 02/2007; 133(1):41-9. DOI:10.1530/REP-06-0104 · 3.17 Impact Factor
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ABSTRACT: Avian perivitelline membrane, an investment homologous to the mammalian zona pellucida, is composed of at least two glycoproteins. Our previous studies demonstrated that one of its components, ZPC, which is synthesized in the ovarian granulosa cells, is secreted after carboxy-terminal proteolytic processing, and this event is a prerequisite event for ZPC secretion in quail. In the present study, we examined the role of the cytoplasmic tail, which is successfully removed after proteolytic processing, in membrane transport, proteolytic processing, and the secretion of quail ZPC. In pursuit of this, we produced a truncated ZPC mutant lacking the cytoplasmic tail located in its C-terminus and examined its expression in the mammalian cell line. Western blot analyses demonstrated that the cytoplasmic tail-deficient ZPC was neither secreted nor underwent proteolytic processing in the cells. Immunofluorescence analysis and the acquisition of resistance to endoglycosidase H digestion of the cytoplasmic tail-deficient ZPC demonstrated that the deletion of the cytoplasmic tail interferes with the intracellular trafficking of the protein from the endoplasmic reticulum to the Golgi apparatus. These results indicate that the cytoplasmic tail of quail ZPC might possess the determinant responsible for the efficient transport of the newly synthesized ZPC from the endoplasmic reticulum to the Golgi apparatus.Biology of Reproduction 11/2003; 69(4):1401-7. DOI:10.1095/biolreprod.103.018333 · 3.32 Impact Factor
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