The zona pellucida 'receptors' ZP1, ZP2 and ZP3

Citation
Kd. Hinsch et E. Hinsch, The zona pellucida 'receptors' ZP1, ZP2 and ZP3, ANDROLOGIA, 31(5), 1999, pp. 320-322
Citations number
13
Categorie Soggetti
da verificare
Journal title
ANDROLOGIA
ISSN journal
03034569 → ACNP
Volume
31
Issue
5
Year of publication
1999
Pages
320 - 322
Database
ISI
SICI code
0303-4569(199909)31:5<320:TZP'ZZ>2.0.ZU;2-X
Abstract
The male component that is necessary for successful reproduction depends on a large variety of biological processes working in concert. The sperm-egg interaction occurs through complementary molecules and is an obligatory pro cess for successful fertilization. However, this complex phenomenon and its molecular mechanisms remain to be fully understood. The oocyte is protecte d by the zona pellucida, a network of various proteins which encloses the o ocyte. Depending on the species, the zona pellucida consists of different g lycoproteins that are proposed to function as 'receptors' for spermatozoa. In the mouse, ZP1 is the homodimeric filament crosslinker, held together by intermolecular disulphides. ZP2 is the 'secondary receptor', which is clea ved by egg proteases after egg activation. The mouse ZP3 protein appears to be the 'primary receptor', which is responsible for species-specific bindi ng of spermatozoa to the oocyte and the induction of the acrosome reaction. To localize zona pellucida protein and to evaluate the function of ZP2 and ZP3, polyclonal antisera were raised against synthetic ZP2 or ZP3 peptides which are specific for human or for mouse zona pellucida proteins. It coul d be demonstrated that antisynthetic peptide antisera detected their respec tive zona pellucida proteins in immunoblots, ovary sections and native hemi zonae pellucidae. Functional assays with anti-ZP3 synthetic peptide antibod ies revealed that the antisera did not inhibit sperm-zona pellucida binding , whereas one of the antisera against synthetic ZP2 peptides significantly inhibited binding of spermatozoa to the zona pellucida.