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Sperm Binding and Fertilization Envelope Formation in a Cell Surface Complex Isolated from Sea Urchin Eggs

Overview
Journal J Cell Biol
Specialty Cell Biology
Date 1979 Apr 1
PMID 479292
Citations 9
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Abstract

An isolated surface complex consisting of the vitelline layer, plasma membrane, and attached secretory vesicles has been examined for its ability to bind sperm and to form the fertilization envelope. Isolated surface complexes (or intact eggs) fixed in glutaraldehyde and then washed in artificial sea water are capable of binding sperm in a species-specific manner. Sperm which bind to the isolated surface complex exhibit the acrosomal process only when they are associated with the exterior surface (vitelline layer) of the complex. Upon resuspension of the unfixed surface complex in artificial sea water, a limiting envelope is formed which, based on examination of thin sections and negatively stained surface preparations, is structurally similar to the fertilization envelope formed by the fertilized egg. These results suggest that the isolated egg surface complex retains the sperm receptor, as well as integrated functions for the secretion of components involved in assembly of the fertilization envelope.

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References
1.
Endo Y . Changes in the cortical layer of sea urchin eggs at fertilization as studied with the electron microscope. I. Clypeaster japonicus. Exp Cell Res. 1961; 25:383-97. DOI: 10.1016/0014-4827(61)90288-9. View

2.
Glabe C, Vacquier V . Isolation and characterization of the vitelline layer of sea urchin eggs. J Cell Biol. 1977; 75(2 Pt 1):410-21. PMC: 2109943. DOI: 10.1083/jcb.75.2.410. View

3.
Decker G, Joseph D, Lennarz W . A study of factors involved in induction of the acrosomal reaction in sperm of the sea urchin, Arbacia punctulata. Dev Biol. 1976; 53(1):115-25. DOI: 10.1016/0012-1606(76)90213-x. View

4.
Foerder C, SHAPIRO B . Release of ovoperoxidase from sea urchin eggs hardens the fertilization membrane with tyrosine crosslinks. Proc Natl Acad Sci U S A. 1977; 74(10):4214-8. PMC: 431909. DOI: 10.1073/pnas.74.10.4214. View

5.
Detering N, Decker G, Schmell E, Lennarz W . Isolation and characterization of plasma membrane-associated cortical granules from sea urchin eggs. J Cell Biol. 1977; 75(3):899-914. PMC: 2111596. DOI: 10.1083/jcb.75.3.899. View