A novel Aurelia aurita protein mesoglein contains DSL and ZP domains

Matveev, I. V.; Shaposhnikova, T. G.; Podgornaya, O. I.

doi:10.1016/j.gene.2007.04.034

Cited by 19 publications

(26 citation statements)

References 27 publications

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“…5) possesses a 22-aa transmembrane domain (TMD) and a conserved 7-aa external hydrophobic patch (EHP; aa-363 to aa-369). We proposed that the TMD anchors ZP3 in oocyte secretory vesicles and plasma membrane (Qi et al, 2002), and the EHP prevents incorporation of ZP3 into fibrils in oocyte cytoplasm by interacting (Matveev et al, 2007) to human beings (Jovine et al, 2002a(Jovine et al, , 2005, and are often glycosylated, modular structures consisting of multiple types of domains (Jovine et al, 2005). For example, the ZP domain is a feature of all ZP glycoproteins and all egg extracellular coat proteins, from echinoderm to human eggs (Jovine et al, 2005).…”

Section: Characteristics Of Zp3mentioning

confidence: 99%

Mammalian fertilization:the eggs multifunctional zona pellucida

Wassarman

Litscher²

2008

Int. J. Dev. Biol.

117

103

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The zona pellucida (ZP) is a specialized extracellular coat that surrounds the plasma membrane of mammalian eggs. Its presence is essential for successful completion of oogenesis, fertilization and preimplantation development. The ZP is composed of only a few glycoproteins which are organized into long crosslinked fibrils that constitute the extracellular coat. A hallmark of ZP glycoproteins is the presence of a ZP domain, a region of polypeptide responsible for polymerization of the glycoproteins into a network of interconnected fibrils. The mouse egg ZP consists of only three glycoproteins, called ZP1, ZP2, and ZP3, that are synthesized and secreted exclusively by growing oocytes. One of the glycoproteins, ZP3, serves as both a binding partner for sperm and inducer of sperm exocytosis, the acrosome reaction. Female mice lacking ZP3 fail to assemble a ZP around growing oocytes and are completely infertile. Sperm bind to the carboxyterminal region of ZP3 polypeptide encoded by ZP3 exon-7 and binding is sufficient to induce sperm to complete the acrosome reaction. Whether sperm recognize and bind to ZP3 polypeptide, oligosaccharide, or both remains an unresolved issue. Purified ZP3 self-assembles into long homomeric fibrils under non-denaturing conditions. Apparently, sperm added to ZP3 bind to the fibrils and are prevented from binding to ovulated eggs in vitro. These, as well as other aspects of ZP structure and function are addressed in this article.

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Section: Characteristics Of Zp3mentioning

confidence: 99%

Mammalian fertilization:the eggs multifunctional zona pellucida

Wassarman

Litscher²

2008

Int. J. Dev. Biol.

117

103

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“…A protein with a similar M r was observed in the Hydra ECM, but it did not react with any AB against known vertebrate ECM proteins, and no suggestion was made about its nature [7]. We supposed that p47 of A.aurita mesoglea could be an unknown protein and we made an attempt to clone its gene [8]. The merged sequences acquired by 3′ and 5′ RACE produced mRNA sequence 1421 bp long.…”

Section: Introductionmentioning

confidence: 99%

Aurelia aurita (Cnidaria) Oocytes' Contact Plate Structure and Development

2012

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One of the A. aurita medusa main mesoglea polypeptides, mesoglein, has been described previously. Mesoglein belongs to ZP-domain protein family and therefore we focused on A.aurita oogenesis. Antibodies against mesoglein (AB RA47) stain the plate in the place where germinal epithelium contacts oocyte on the paraffin sections. According to its position, we named the structure found the “contact plate”. Our main instrument was AB against mesoglein. ZP-domain occupies about half of the whole amino acid sequence of the mesoglein. Immunoblot after SDS-PAGE and AU-PAGE reveals two charged and high Mr bands among the female gonad germinal epithelium polypeptides. One of the gonads' polypeptides Mr corresponds to that of mesogleal cells, the other ones' Mr is higher. The morphological description of contact plate formation is the subject of the current work. Two types of AB RA47 positive granules were observed during progressive oogenesis stages. Granules form the contact plate in mature oocyte. Contact plate of A.aurita oocyte marks its animal pole and resembles Zona Pellucida by the following features: (1) it attracts spermatozoids; (2) the material of the contact plate is synthesized by oocyte and stored in granules; (3) these granules and the contact plate itself contain ZP domain protein(s); (4) contact plate is an extracellular structure made up of fiber bundles similar to those of conventional Zona Pellucida.

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“…The RA47 serum was obtained against mesoglein (Shaposhnikova et al, 2005), in the amino acid sequence of which a ZP domain was found, compris ing more than half of the protein (Matveev et al, 2007). It is quite probable that the serum contains a large number of antibodies specifically against the ZP domain.…”

Section: Discussionmentioning

confidence: 99%

“…One of them is a protein with a molecular weight of 47 kDa, mesoglein (Matveev et al, 2007). Isolated antibodies to mesoglein (RA47) allowed determining its localization: in specific granules of mesogleal cells and in the composition of "elastic" fibers of the extracellular mesogleal matrix in mature medusae (Shaposhnikova et al, 2005).…”

Section: Introductionmentioning

confidence: 99%