Mammalian cortical granules: contents, fate, and function.
Recent studies have extended our knowledge regarding the contents of mammalian cortical granules (CG) and their function in postfertilization events. Cytochemical staining has demonstrated the presence of carbohydrates within mammalian CG, and lectin-binding studies have shown that these carbohydrates include alpha-D-mannose, alpha-D-GalNAc, and galactose residues in the hamster, alpha-D-mannose in the mouse and cat, and beta-D-Gal(1,3)-D-GalNAc in the pig. Following fertilization and artificial activation, mannosylated material is released from CG and can be found on the oolemma and within the perivitelline space (PVS) of hamster oocytes. Fertilized or artificially activated rabbit, mouse, and human oocytes also release mannosylated, fucosylated and sialylated, and fucosylated material, respectively, which localizes to the oolemma. These glycosylated materials are probably of CG origin, although they have not been directly localized to the CG in rabbit, mice, and humans. The function(s) of the glycosylated material released from mammalian oocytes is not known, although it may participate in blocking polyspermy at the level of the plasma membrane, PVS, and/or zona pellucida (ZP), or it may facilitate preimplantation embryonic development. Proteinases, including tissue plasminogen activator, are also released from mammalian oocytes following fertilization and artificial activation, suggesting that they are of CG origin. These proteinases modify the ZP such that it is no longer receptive to sperm, and some proteinases have been suggested to bring about ZP hardening (an increased resistance to denaturing agents) by an unknown mechanism. Mouse ZP may also be hardened by an ovoperoxidase (cross-links tyrosine residues) cytochemically identified in mouse CG and CG exudate. The phenomena of ZP hardening in mammalian zygotes is not well understood but is likely to function in blocking polyspermic penetration of the ZP and/or in protecting embryos during preimplantation development. Recently, a 75 kD protein (p75) has been immunocytochemically localized to mouse CG and to the PVS of fertilized oocytes and two-cell embryos. The identity and function of p75 remains to be determined. Heparin binding placental protein may also be a CG component, since it is released from hamster oocytes following fertilization. It has not, however, been directly demonstrated to be a CG component, and its functions in fertilization and/or early embryonic development have yet to be defined.
Hoodbhoy
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T
Department of Biology, University of California, Riverside 92521.
Talbot
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P
D000818:Animals; D003594:Cytoplasmic Granules / Q000502:physiology* / Q000648:ultrastructure; D004527:Egg Proteins / Q000302:isolation & purification / Q000378:metabolism*; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism; D005260:Female; D006031:Glycosylation; D006801:Humans; D037102:Lectins; D008297:Male; D008322:Mammals; D009865:Oocytes / Q000166:cytology / Q000502:physiology*; D010544:Peroxidases / Q000302:isolation & purification / Q000378:metabolism; D013084:Sperm-Ovum Interactions; D015044:Zona Pellucida / Q000502:physiology
D004527:Egg Proteins; D037102:Lectins; D010544:Peroxidases; D010450:Endopeptidases