Characterization of an Oviductal Glycoprotein Associated with the Ovulated Hamster Oocyte1

Robitaille, Gilles; St‐Jacques, Sylvie; Potier, Michel; Bleau, G.

doi:10.1095/biolreprod38.3.687

Cited by 79 publications

(54 citation statements)

References 22 publications

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“…After immunoblotting, the anti-rhaOv m antibody detected a broad band starting at ‫ف‬ 160 kD in the HPA-purified hamster oviductin sample. This band corresponds to the mature, fully glycosylated form of oviductin as previously reported after detection with a monoclonal antibody (Robitaille et al 1988;StJacques and Bleau 1988;Malette and Bleau 1993). There were several bands observed in the oviduct total protein homogenates, including the high molecular weight polydispersed band beginning at ‫ف‬ 160 kD corresponding to the band observed with HPA-purified oviductin.…”

Section: Discussionsupporting

confidence: 79%

Detection of Nascent and/or Mature Forms of Oviductin in the Female Reproductive Tract and Post-ovulatory Oocytes by Use of a Polyclonal Antibody Against Recombinant Hamster Oviductin

McBride

Boisvert

Bleau

et al. 2004

J Histochem Cytochem.

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S U M M A R YOviductins belong to a family of glycoproteins that have been suggested to play several roles during the early processes of reproduction. Recently, a polyclonal antibody was raised against recombinant hamster oviductin (rhaOv m ). Here the anti-rhaOv m antibody was used to investigate the sites of localization of oviductin in the female golden hamster. In the hamster oviduct, immunolabeling was restricted to the content of the Golgi saccules and secretory granules of the non-ciliated oviduct cells. After its release into the lumen, oviductin becomes associated with the zona pellucida of post-ovulatory oocytes. In unfertilized oocytes, oviductin was also detected in membrane invaginations along the oolemma and in some vesicles within the ooplasm. Furthermore, oviductin was detected over the microvilli and within multivesicular bodies of uterine epithelial cells. Western blotting analysis revealed the presence of oviductin in the hamster oviduct but not in the uterus or ovary. In the oviduct, the anti-rhaOv m antibody detected a polydispersed band corresponding to native oviductin (160-350 kD) and several lower molecular weight bands ( Ͻ 100 kD) corresponding to nascent and partially glycosylated forms of oviductin. The anti-rhaOv m antibody provides an additional tool for investigation into the cytochemical and biochemical properties of different forms of hamster oviductin in the female reproductive tract.

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Section: Discussionsupporting

confidence: 79%

Detection of Nascent and/or Mature Forms of Oviductin in the Female Reproductive Tract and Post-ovulatory Oocytes by Use of a Polyclonal Antibody Against Recombinant Hamster Oviductin

McBride

Boisvert

Bleau

et al. 2004

J Histochem Cytochem.

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“…Composed of two major domains, a catalytically inactive chitinase domain and a C-terminal O-glycosylation domain, OGP is expressed in response to estrogen stimulation in the oviduct of numerous mammals, including pig (Buhi et al, 1990), hamster (Robitaille et al, 1988), baboon (Boice et al, 1990), bovine , mice (Kapur and Johnson, 1985) and humans (Verhage et al, 1988). Co-incubation of OGP or media conditioned with OGP (i.e.…”

Section: Discussionmentioning

confidence: 99%

Mouse oviduct-specific glycoprotein is an egg-associated ZP3-independent sperm-adhesion ligand

Lyng

Shur

2009

Journal of Cell Science

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Mouse sperm-egg binding requires a multiplicity of receptorligand interactions, including an oviduct-derived, high molecular weight, wheat germ agglutinin (WGA)-binding glycoprotein that associates with the egg coat at ovulation. Herein, we report the purification and identification of this sperm-binding ligand. WGA-binding, high molecular weight glycoproteins isolated from hormonally primed mouse oviduct lysates competitively inhibit sperm-egg binding in vitro. Within this heterogeneous glycoprotein preparation, a distinct 220 kDa protein selectively binds to sperm surfaces, and was identified by sequence analysis as oviduct-specific glycoprotein (OGP). The sperm-binding activity of OGP was confirmed by the loss of sperm-binding following immunodepletion of OGP from oviduct lysates, and by the ability of both immunoprecipitated OGP and natively purified OGP to competitively inhibit spermegg binding. As expected, OGP is expressed by the secretory cells of the fimbriae and infundibulum; however, in contrast to previous reports, OGP is also associated with both the zona pellucida and the perivitelline space of mouse oocytes. Western blot analysis and lectin affinity chromatography demonstrate that whereas the bulk of OGP remains soluble in the ampullar fluid, distinct glycoforms associate with the cumulus matrix, zona pellucida and perivitelline space. The sperm-binding activity of OGP is carbohydrate-dependent and restricted to a relatively minor peanut agglutinin (PNA)-binding glycoform that preferentially associates with the sperm surface, zona pellucida and perivitelline space, relative to other more abundant glycoforms. Finally, pretreatment of two-cell embryos, which do not normally bind sperm, with PNA-binding OGP stimulates sperm binding.

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“…In fact, oviductal glycoprotein secretions are known to permeate the zona pellucida, and, at least in hamster, there is evidence to suggest that the ovulated zona pellucida has biological activities that are distinctly different from those in the ovarian zona pellucida (Boatman and Magnoni, 1995;Kan et al, 1990;Robitaille et al, 1988;St-Jacques et al, 1992). All of these observations necessitate a re-examination of the simple premise that spermegg binding involves a single receptor-ligand interaction.…”

Section: Discussionmentioning

confidence: 99%

“…The most extensively studied of the oviduct-derived glycoproteins is oviduct-secreted glycoprotein (OGP), which, in hamster, is secreted at the time of ovulation, adheres to the zona pellucida and may promote zona-binding and penetration (Boatman and Magnoni, 1995;Kan et al, 1990;Robitaille et al, 1988;St-Jacques et al, 1992). We therefore tested directly whether OGP functions as the ZP3-independent ligand identified here.…”

Section: The Zp3-independent Ligand Is Not Oviduct-secreted Glycoprotmentioning

confidence: 99%

Characterization of a novel ZP3-independent sperm-binding ligand that facilitates sperm adhesion to the egg coat

Rodeheffer

Shur

2004

Development

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During mammalian fertilization, sperm adhere to the extracellular coat of the egg, or zona pellucida, in a species-specific manner. In mouse, evidence suggests that sperm recognize and bind to specific oligosaccharide ligands within the zona pellucida glycoprotein, ZP3, viaβ1,4-galactosyltransferase I (GalT I), a lectin-like receptor on the sperm surface. Although in vitro experiments using isolated gametes lend support to this model, recent in vivo studies of genetically altered mice question whether ZP3 and/or GalT I are solely responsible for sperm-egg binding. In this regard, sperm from GalT I-null mice bind poorly to ZP3 and fail to undergo a zona-induced acrosome reaction; however, they still bind to the ovulated egg coat in vitro. In this report, we characterize a novel ZP3- and GalT I-independent mechanism for sperm adhesion to the egg coat. Results show that the ovulated zona pellucida contains at least two distinct ligands for sperm binding: a ZP3-independent ligand that is peripherally associated with the egg coat and facilitates gamete adhesion; and a ZP3-dependent ligand that is present in the insoluble zona matrix and is recognized by sperm GalT I to facilitate acrosomal exocytosis. The ZP3-independent ligand is not a result of contamination by egg cortical granules, nor is it the mouse homolog of oviduct-specific glycoprotein. It behaves as a 250 kDa, WGA-reactive glycoprotein with a basic isoelectric point, distinguishing it from the acidic glycoproteins that form the insoluble matrix of the egg coat. When eluted from isoelectric focusing gels, the acidic matrix glycoproteins possess sperm-binding activity for wild-type sperm, but not for GalT I-null sperm,whereas the basic glycoprotein retains sperm-binding activity for both wild-type and GalT I-null sperm. Thus, GalT I-null sperm are able to resolve gamete recognition into at least two distinct binding events, leading to the characterization of a novel, peripherally associated, sperm-binding ligand on the ovulated zona pellucida.

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Characterization of an Oviductal Glycoprotein Associated with the Ovulated Hamster Oocyte1

Cited by 79 publications

References 22 publications

Detection of Nascent and/or Mature Forms of Oviductin in the Female Reproductive Tract and Post-ovulatory Oocytes by Use of a Polyclonal Antibody Against Recombinant Hamster Oviductin

Detection of Nascent and/or Mature Forms of Oviductin in the Female Reproductive Tract and Post-ovulatory Oocytes by Use of a Polyclonal Antibody Against Recombinant Hamster Oviductin

Mouse oviduct-specific glycoprotein is an egg-associated ZP3-independent sperm-adhesion ligand

Characterization of a novel ZP3-independent sperm-binding ligand that facilitates sperm adhesion to the egg coat

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