The DOI matches its Crossref record; 74 of the 74 references it cites were found in a registry or an index.
Profile of a mammalian sperm receptor1,2
Abstract
Complementary molecules on the surface of eggs and sperm are responsible for species-specific interactions between gametes during fertilization in both plants and animals. In this essay, several aspects of current research on the mouse egg receptor for sperm, a zona pellucida glycoprotein called ZP3, are addressed. These include the structure, synthesis, and functions of the sperm receptor during oogenesis and fertilization in mice. Several conclusions are drawn from available information. These include (/) ZP3 is a member of a unique class of glycoproteins found exclusively in the extracellular coat (zona pellucida) of mammalian eggs. (If) ZP3 gene expression is an example of oocyte-specific and, therefore, sex-specific gene expression during mammalian development. (Ill) ZP3 is a structural glycoprotein Involved in assembly of the egg extracellular coat during mammalian oogenesis. (ZV) ZP3 is a sperm receptor involved in carbohydrate-mediated gamete recognition and adhesion during mammalian fertilization. (V) ZP3 is an inducer of sperm exocytosis (acrosome reaction) during mammalian fertilization. (Vf) ZP3 participates in the secondary block to polyspermy following fertilization in mammals. (VII) The extracellular coat of other mammalian eggs contains a glycoprotein that is functionally analogous to mouse ZP3. The unique nature, highly restricted expression, and multiple roles of ZP3 during mammalian development make this glycoprotein a particularly attractive subject for investigation at both the cellular and molecular levels.
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Metadata
- Authors
- Wassarman, P. M.
- Venue
- Development
- Publisher
- The Company of Biologists
- Published
- 1990-01-01
- Volume
- 108
- Issue
- 1
- Pages
- 1-17
- ISSN
- 0950-1991 (ISSN-L)
- 1477-9129
- OpenAlex
- W1771107213
- Cited by
- 362
- References
- 74
- FWCI
- 39.16
- Type
- journal article
- Language
- en
- Open access
- closed
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