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The new transgenic line not only provided a convenient living marker for monitoring female gonad development, but also demonstrated that a single zp3 gene promoter is sufficient for oocyte-specific transcription.
Sperm arylsulfatase A (show ARSA ELISA Kits) binds to mZP2 and mZP3 glycoproteins in a nonenzymatic manner.
Cytoplasmic tails are necessary to prevent intracellular oligomerization while ensuring incorporation of processed ZP2 (show ZP2 ELISA Kits) and ZP3 into the zona pellucida.
The extreme heterogeneity of mature ZP3, with respect to both mol (show DUOXA1 ELISA Kits). wt. and isoelectric point, is partly a consequence of the N-linked oligosaccharides and not the polypeptide chain itself.
stoichiometric disposition of ZP1 (show ZP1 ELISA Kits), ZP2 (show ZP2 ELISA Kits), and ZP3 in the ovarian zona matrix revealed by double and triple immunolocalization studies
Conserved furin (show FURIN ELISA Kits) cleavage site not essential for secretion and integration of ZP3 into the extracellular egg coat of transgenic mice.
Thr (show TRH ELISA Kits) residues can replace the two evolutionarily conserved Ser (show SIGLEC1 ELISA Kits) residues as acceptors for essential O-linked oligosaccharides at the sperm combining-site of ZP3 without affecting the glycoprotein's sperm receptor activity.
intracellular trafficking of ZP3 was observed in growing oocytes. Replacement of the zona domain with EGFP did not prevent secretion of ZP3, suggesting the presence of trafficking signals and a cleavage site in the carboxyl terminus
Le(x) is a ligand for a major class of ZP3 binding sites on mouse sperm
human and mouse ZP3 proteins are quite similar, and alternative explanations of taxon-specific sperm binding warrant exploration
Sperm recognize and bind to a region of ZP3 polypeptide immediately downstream of its ZP domain that is encoded by mZP3 exon-7.
Missense Mutation in ZP3 gene is associated with Empty Follicle Syndrome and Female Infertility.
Mutations in ZP2 (show ZP2 ELISA Kits) and ZP3 have dosage effects which can cause female infertility in humans.
Epididymal CRISP1 (show CRISP1 ELISA Kits) mediates sperm-zona pellucida binding through its interaction with ZP3.
observed sequence variations in exons of ZP3 gene in women with infertility of unknown origin who exhibit abnormal zona pellucida; sperm-ovum interactions appear relatively normal in these patients [CASE REPORTS]
Binding sites for recombinant zona pellucida C (ZPC) glycoprotein are located both at the N- and C-terminus of proacrosin (show ACR ELISA Kits)
Peptides rhuZP3a22 approximately 176 and rhuZP3b177 approximately 348 have a role similar to human ZP3. The mechanism of the response to the peptides involves influx of calcium, the G protein pathway, and a T-type calcium channel.
induces acrosome reactions which are protein kinase-C (show PKC ELISA Kits), protein tyrosine kinase (show EPHA8 ELISA Kits), T-type Ca2 (show CA2 ELISA Kits)+ channels, and extracellular Ca2 (show CA2 ELISA Kits)+ dependent
a significant decrease in acrosomal exocytosis mediated by both recombinant human ZP3 (p<0.005) and ZP4 (show ZP4 ELISA Kits) (p<0.005) was observed in presence of the immune sera
The functional activity of human ZP3 resides in its C-terminal domain.
Polymorphism of Zp2 (show ZP2 ELISA Kits) and the Zp3 did not show any contribution to reproductive isolation between the bovine species.
The expression of zona pellucida glycoprotein 3 and integrin beta-2 (show ITGB2 ELISA Kits) in oocytes after brilliant cresyl blue staining is reported.
The zona pellucida is an extracellular matrix that surrounds the oocyte and early embryo. It is composed primarily of three or four glycoproteins with various functions during fertilization and preimplantation development. The protein encoded by this gene is a structural component of the zona pellucida and functions in primary binding and induction of the sperm acrosome reaction. The nascent protein contains a N-terminal signal peptide sequence, a conserved ZP domain, a C-terminal consensus furin cleavage site, and a transmembrane domain. It is hypothesized that furin cleavage results in release of the mature protein from the plasma membrane for subsequent incorporation into the zona pellucida matrix. However, the requirement for furin cleavage in this process remains controversial based on mouse studies. A variation in the last exon of this gene has previously served as the basis for an additional ZP3 locus\; however, sequence and literature review reveals that there is only one full-length ZP3 locus in the human genome. Another locus encoding a bipartite transcript designated POMZP3 contains a duplication of the last four exons of ZP3, including the above described variation, and maps closely to this gene.
zona pellucida glycoprotein 3.2
, sperm receptor
, zona pellucida glycoprotein ZP3
, zona pellucida protein C
, zona pellucida sperm-binding protein 3
, zona pellucida glycoprotein 3A (sperm receptor)
, zona pellucida glycoprotein 3B
, zona pellucida glycoprotein 3 preproprotein
, zona pellucida glycoprotein ZP3B
, zona pellucida C
, zona pellucida 3 glycoprotein
, zona pellucida glycoprotein C
, zona pellucida 3 glycoprotein (sperm receptor)
, zona pellucida glycoprotein 3-beta
, zona pellucida glycoprotein ZP3-beta
, zona pellucida protein 3-beta
, Sperm receptor
, Zona pellucida protein C
, glycoprotein hZP3
, zona pellucida C protein
, zona pellucida glycoprotein 3 (sperm receptor)
, zona pellucida glycoprotein 3 (sperm receptor)-like