Molecular basis of fertilization in the mouse

David J. Miller, Barry D. Shur

Research output: Contribution to journalArticlepeer-review

Abstract

Recent studies of mouse fertilization have identified two complementary gamete receptors that mediate sperm-egg binding. Sperm surface β1,4-galactosyltransferase (GalTase) binds to specific oligosaccharides of the egg coat (zona pellucida) glycoprotein ZP3. Evidence suggests that these same molecules may stimulate the acrosome reaction in sperm. After the acrosome reaction, it is thought that sperm remain adherent to the zona by binding another glycoprotein, ZP2. The acrosome-reacted sperm releases hydrolytic enzymes, including acrosin and N-acetylglucosaminidase, enabling it to penetrate the zona pellucida. After the penetrating sperm binds to the egg membrane and activates development, N-acetylglucosaminidase is exocytosed from egg cortical granules and, as part of the zona block to polyspermy, globally removes the sperm GalTase binding site from ZP3 oligosaccharides.

Original languageEnglish (US)
Pages (from-to)255-264
Number of pages10
JournalSeminars in Developmental Biology
Volume5
Issue number4
DOIs
StatePublished - Aug 1994

Keywords

  • sperm/egg/β1,4-galactosyltransferase/ZP3/N-acetylglucosaminidase

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