Identification of the sea urchin egg receptor for sperm using an antiserum raised against a fragment of its extracellular domain.

Foltz, Kathy R.; Lennarz, William J.

doi:10.1083/jcb.116.3.647

Cited by 52 publications

(12 citation statements)

References 46 publications

(73 reference statements)

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“…Egg envelope products released in the water after egg deposition have been shown to interact with homologous spermatozoa and trigger certain cell activities. These activities include activation of oriented sperm motility and an increase in sperm respiration rate and have been reported in invertebrates (Kopf et al, 1979;Ward et al, 19851, and in vertebrates (Cherr and Clark, 1985;Diaz-Fontdevila et al, 1991;Foltz and Lennarz, 1992). In ascidians, egg envelope products bind homologous spermatozoa and have been biochemically characterized as glycoproteins (Litscher and Honegger, 1991).…”

Section: Introductionmentioning

confidence: 93%

Characterization of the main egg envelope proteins of the sea bass Dicentrarchus labrax L. (teleostea, serranidae)

Scapigliati

Carcupino

Taddei

et al. 1994

Molecular Reproduction Devel

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Fish eggs are surrounded by a resistant acellular coat commonly called the chorion or zona radiata. This study characterizes the eggshell proteinaceous content of unfertilized eggs of the sea bass Dicentrarchus labrax, with a view to the preparation of immunogens. Solubilization of the purified eggshells was achieved in 8 M urea followed by one- and two-dimensional gel electrophoresis. Glycoproteins were detected using concanavalin-A in one and two-dimensional gels, and the principal glycoproteins had a molecular weight of 47 kDa and 170 kDa. Partial purification of a few polypeptides in the 45 kDa to 55 kDa range was achieved by gel filtration chromatography. Although whole eggshells were relatively insoluble even in 8 M urea, partial purification of these polypeptides enable them to dissolve completely in solutions at low ionic strength.

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Section: Introductionmentioning

confidence: 93%

Characterization of the main egg envelope proteins of the sea bass Dicentrarchus labrax L. (teleostea, serranidae)

Scapigliati

Carcupino

Taddei

et al. 1994

Molecular Reproduction Devel

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“…In sea urchin eggs, a sperm receptor protein was identified as a 350 x 103 Mr membrane glycoprotein [6] that-together with bindin, a complementary molecule on the sperm [7]-is responsible for binding of the gametes. Though purified bindin does not activate eggs [8], Fab fragments generated from the polyclonal antiserum against the purified 70-kDa fragment of the receptor induce a small amount of activation, suggesting that the receptor might have a linkage to a signal transduction system [9].…”

Section: Introductionmentioning

confidence: 99%

Activation of Porcine Oocytes Via an Exogenously Introduced Rat Muscarinic M1 Receptor1

Macháty

Mayes

Kovács

et al. 1997

Biology of Reproduction

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Thirty hours after the beginning of in vitro maturation, porcine oocytes were microinjected with mRNA coding for the rat muscarinic M1 receptor. They were then incubated for 15 h to allow sufficient time for completing maturation, translation of the mRNA, and insertion of the receptor into the plasma membrane. They were then treated with acetylcholine, the receptor's agonist, and its effect on inducing various activation-related changes was examined. Acetylcholine treatment triggered the release of Ca2+ from internal stores that could be blocked by atropine, the receptor's antagonist. The Ca2+ release was probably mediated via a G protein, since prior injection of guanosine 5'-O-(2-thiodiphosphate) (GDP-beta-S) totally inhibited the effect of the agonist. Pertussis toxin (PT) had no effect on the Ca2+ transients induced by acetylcholine, suggesting that the signal transduction pathway involved a PT-insensitive G protein. Electron microscopy revealed that in the injected oocytes, acetylcholine induced cortical granule exocytosis. The oocytes were released from meiotic arrest as evidenced by the decrease in H1 kinase activity measured in the oocytes during the histone H1 kinase assay. After resuming meiosis they entered interphase: 58.8% of the injected oocytes formed pronuclei after incubation with the agonist. Injection without subsequent acetylcholine treatment, or acetylcholine incubation without prior injection with the receptor mRNA, did not cause these changes. The results provide further evidence that the components of a G protein-mediated signal transduction pathway exist in porcine oocytes and that the activation of this pathway via an exogenously supplied G protein-coupled receptor results in a full complement of oocyte activation events. Whether this pathway transduces the activating signal at sperm-induced oocyte activation requires further examination.

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“…It has been demonstrated in an invertebrate, Urechis caupo, that a protein isolated from sperm acrosomes activates the egg, with accompanying changes in potential quite similar to those seen at fertilization (8,9,10). It has recently been reported in sea urchin that antiserum against a fragment of an egg receptor for sperm causes the activation of a small percentage of the eggs (6). These results suggest that some molecules on the sperm membrane or among the acrosomal contents are involved in the process of egg activation via an egg receptor on the egg plasma membrane.…”

Section: Discussionmentioning

confidence: 99%

“…The acrosomal protein activates the egg in a voltage-insensitive manner that resembles activation by sperm. Recently, in sea urchin eggs, a receptor on the egg plasma membrane was characterized as a transmembrane glycoprotein (7) and treatment with antiserum against a fragment of the receptor caused the egg to undergo cortical exocytosis (6). Furthermore, in guineapig sperm, a fusion protein similar to viral fusion proteins is localized on the sperm surface and is involved in the fusion of sperm and egg (2,31).…”

Section: Introductionmentioning

confidence: 99%

Activation of Xenopus Eggs by an Extract of Cynops Sperm

et al. 1994

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An extract obtained from Cynops sperm induced the activation of both Cynops and Xenopus eggs with accompanying changes in the potential of the egg membrane that were quite similar to those caused by the Cynops sperm, The activation-inducing properties of the extract were abolished by treatment with proteinase K or by heating (60°C, 15 min) and were associated with a protease activity against peptidyl Arg-MCA substrates. The activation of Xenopus eggs by the extract was inhibited by those substrates, or by protease inhibitors, aprotinin or leupeptin. The protease activity was localized in the acrosomal region of Cynops sperm. The activation of Xenopus eggs by the extract was prevented when the exterior concentration of Ca2+ ions, [Ca2+],, was reduced to 1.5 pM, but it was enhanced when [Ca"], was increased to 340 pM. The activation of Xenopus eggs by the extract was not affected by positive clamping when [Ca2+lO was 340 p M . These results suggest that the sperm extract contains a protease that causes an increase in the influx of Ca2+ ions that results in voltage-insensitive activation of the egg.

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Identification of the sea urchin egg receptor for sperm using an antiserum raised against a fragment of its extracellular domain.

Cited by 52 publications

References 46 publications

Characterization of the main egg envelope proteins of the sea bass Dicentrarchus labrax L. (teleostea, serranidae)

Characterization of the main egg envelope proteins of the sea bass Dicentrarchus labrax L. (teleostea, serranidae)

Activation of Porcine Oocytes Via an Exogenously Introduced Rat Muscarinic M1 Receptor1

Activation of Xenopus Eggs by an Extract of Cynops Sperm

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