The role of localized cell surface-associated glycoproteins during fertilization in the hydrozoan Aequorea.
Hydrozoan eggs can be fertilized only at the site of polar body formation and first acquire this ability during second polar body formation. The eggs of Aequorea victoria form a discrete Triticum lectin binding moiety in the jelly coat near the first polar body as it is being given off and also a discrete concanavalin A binding moiety associated with the egg surface where the second polar body forms, which disappears immediately after fertilization. The germinal vesicle has an eccentric position in full grown Aequorea oocytes. The region of oocyte surface closest to the germinal vesicle is the site where the polar bodies normally form. When oocytes are centrifuged during oocyte maturation, the meiotic apparatus sometimes shifts to a different position with reference to the egg surface and polar bodies are given off at this new site. There is a corresponding shift in the position of the Triticum and concanavalin A lectin binding moieties, indicating that their formation is associated with local events occurring at the site of polar body formation. Treatment of Aequorea eggs with Triticum or concanavalin A causes a marked reduction in the ability of these eggs to be fertilized, suggesting that sugar-containing moieties, to which the lectins bind, play a role in fertilization. Removal of sugars on these moieties with mannosidase or N-acetylglucosaminidase, or the cleavage of the protein the sugars are attached to with trypsin, results in eggs that do not bind Triticum or concanavalin A and also show a marked reduction in the ability to be fertilized. These experiments suggest that the lectin binding moieties are glycoproteins.
Freeman
G
G
Center for Developmental Biology, Department of Zoology, University of Texas, Austin 78712, USA.
D000818:Animals; D050260:Carbohydrate Metabolism; D002241:Carbohydrates / Q000737:chemistry; D003208:Concanavalin A / Q000378:metabolism; D005260:Female; D005306:Fertilization / Q000502:physiology*; D037102:Lectins / Q000378:metabolism*; D008297:Male; D009865:Oocytes / Q000254:growth & development; D011485:Protein Binding; D037401:Scyphozoa / Q000502:physiology*; D013084:Sperm-Ovum Interactions / Q000502:physiology*; D013499:Surface Properties
D002241:Carbohydrates; D037102:Lectins; D003208:Concanavalin A