Biosynthesis and expression of zona pellucida glycoproteins in mammals.

نویسندگان

  • F Sinowatz
  • S Kölle
  • E Töpfer-Petersen
چکیده

The zona pellucida (ZP) is an extracellular matrix surrounding the oocyte and the early embryo that exerts several important functions during fertilization and early embryonic development. The ZP of most mammalian species is composed of three glycoproteins (ZPA, ZPB, ZPC), products of the gene families ZPA, ZPB and ZPC that have been found to be highly homologous within mammalian species. Most data on the structure and function of the ZP are obtained from studies in mouse. New data from pig and other domestic animals, however, indicate that the mouse model does not hold for all other species. Whereas in the mouse ZPB is the primary sperm receptor, in the pig ZPA has been shown to possess receptor activity. Contrary to the mouse, where the growing oocyte is the only source of zona glycoproteins, in domestic animals these proteins are expressed in both the oocyte and granulosa cells in a stage-specific pattern and may play also a role in granulosa cell differentiation. In several mammalian species, the epithelial secretory cells of the oviduct synthesize and secrete specific glycoproteins (oviductins) that become closely associated with the ZP of the ovulated oocyte. Once bound to the ZP, oviductin molecules could act as a protective layer around the oocyte and early embryo by virtue of their densely glycosylated mucin-type domains.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Assembly of the inner perivitelline layer, a homolog of the mammalian zona pellucida: an immunohistochemical and ultrastructural study.

The avian inner perivitelline layer (IPVL), a homologous structure to the mammalian zona pellucida, is deposited between the granulosa cells and the oocyte cell membrane during folliculogenesis. The glycoprotein meshwork of the IPVL forms a 3-dimensional matrix and possesses important functions in the fertilization process: it contributes to the binding of avian spermatozoa to the oocyte and in...

متن کامل

Structural changes of the zona pellucida during fertilization and embryo development.

The zona pellucida (ZP) is a unique extracellular coat surrounding the maturing oocyte, during ovulation, fertilization, and early embryo development. It is formed by three/four glycoproteins. Ultrastructural data obtained with transmission (TEM) and scanning electron microscopy (SEM) were compared with molecular data on the glycoproteins network from ovulation to blastocyst formation. Molecula...

متن کامل

Interaction of zona pellucida glycoproteins, sulphated carbohydrates and synthetic polymers with proacrosin, the putative egg-binding protein from mammalian spermatozoa.

Fertilization in mammals is a unique cell-cell recognition event that involves specific receptors on the surface of each gamete. Previous work has shown that proacrosin, a protein found within the acrosome of mammalian spermatozoa, binds non-enzymatically to zona pellucida glycoproteins (ZPGPs) that surround the egg and that this binding can be inhibited by sulphated polysaccharides such as fuc...

متن کامل

Localization and synthesis of zona pellucida proteins in the marmoset monkey (Callithrix jacchus) ovary.

In most species, the zona pellucida (ZP), an extracellular matrix surrounding the mammalian oocyte, is composed of three glycoproteins: ZPA, ZPB and ZPC. Based mainly on results with mice, the site of zona pellucida biosynthesis has been suggested to be exclusively in the oocyte cytoplasm. However, evidence is accumulating that among various species cumulus/granulosa cells may be involved. Beca...

متن کامل

Characterization of human zona pellucida glycoproteins.

The human egg may only be fertilized by one spermatozoon to prevent polyploidy. In most mammals, the primary block to polyspermy occurs at the zona pellucida (ZP). Little is known of the human ZP and the changes occurring following fertilization to prevent polyploidy. Using antibodies directed against synthetic peptides predicted from the human ZP2 and ZP3 cDNA, we identified ZP3 as a 53-60 kDa...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Cells, tissues, organs

دوره 168 1-2  شماره 

صفحات  -

تاریخ انتشار 2001