title: Effects of perturbation of cell polarity on molecular markers of sperm-egg binding sites on mouse eggs.
abstract: The mouse germinal vesicle (GV)-intact oocyte is a symmetric cell, with the GV centrally localized and with components of the plasma membrane and cortex symmetrically distributed around the periphery of the oocyte. During oocyte maturation, two distinct regions of the egg plasma membrane and cortex develop: the amicrovillar region overlying the meiotic spindle and the microvillar region. The development of this polarity is significant, since sperm bind to and fuse with the microvillar region. We are interested in the development of egg polarity and have characterized the localizations of several markers for egg polarity in normal metaphase II eggs and GV-intact oocytes. The asymmetric distributions of these markers (including actin, cortical granules, binding sites for the sperm proteins fertilin alpha and fertilin beta, and two different beta(1) integrin epitopes) develop during oocyte maturation in vitro, and this polarity can be perturbed by treatments that disrupt the actin microfilaments or microtubules. In addition, immunoelectron microscopy reveals that binding sites for recombinant fertilin beta are specifically localized to the microvillar region, suggesting that the binding sites for this sperm ligand are either specifically localized or activated in this region. These results indicate that structural remodeling of the mouse egg plasma membrane is accompanied by molecular remodeling, resulting in the localization or activation of specific molecules in subdomains of the plasma membrane.
authors.affiliation: Division of Reproductive Biology, Department of Biochemistry and Molecular Biology, Johns Hopkins University School of Hygiene and Public Health, Baltimore, Maryland 21205, USA. jpevans@jhsph.edu
authors.forename: J P
authors.initials: JP
authors.lastname: Evans
authors.forename: J A
authors.initials: JA
authors.lastname: Foster
authors.forename: B A
authors.initials: BA
authors.lastname: McAvey
authors.forename: G L
authors.initials: GL
authors.lastname: Gerton
authors.forename: G S
authors.initials: GS
authors.lastname: Kopf
authors.forename: R M
authors.initials: RM
authors.lastname: Schultz
mesh_terms: D051722:ADAM Proteins; D000199:Actins / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D015415:Biomarkers / Q000032:analysis*; D016764:Cell Polarity / Q000502:physiology*; D003078:Colchicine / Q000494:pharmacology; D015638:Cytochalasin D / Q000494:pharmacology; D005260:Female; D000072196:Fertilins; D016023:Integrins / Q000032:analysis; D008297:Male; D008562:Membrane Glycoproteins / Q000378:metabolism; D008666:Metalloendopeptidases / Q000378:metabolism; D051379:Mice; D016253:Microscopy, Immunoelectron; D008871:Microvilli / Q000648:ultrastructure; D019384:Nucleic Acid Synthesis Inhibitors / Q000494:pharmacology; D009865:Oocytes / Q000502:physiology* / Q000648:ultrastructure; D011994:Recombinant Proteins / Q000378:metabolism; D013084:Sperm-Ovum Interactions; D008941:Spindle Apparatus / Q000648:ultrastructure
chemical_list: D000199:Actins; D015415:Biomarkers; D016023:Integrins; D008562:Membrane Glycoproteins; D019384:Nucleic Acid Synthesis Inhibitors; D011994:Recombinant Proteins; D015638:Cytochalasin D; D051722:ADAM Proteins; C000606455:Adam1a protein, mouse; C000606458:Adam2 protein, mouse; D000072196:Fertilins; D008666:Metalloendopeptidases; D003078:Colchicine