Antibodies against epididymal glycoproteins block fertilizing ability in rat

Cuasnicú, Patricia S.; Echeverrı́a, Fernanda Gonzalez; Piazza, Alejandra; Cameo, Mónica S.; Blaquier, Jörge A.

doi:10.1530/jrf.0.0720467

Cited by 95 publications

(36 citation statements)

References 18 publications

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“…This suggests that ADAMs could function in redundant roles, consistent with the fact that ADAMs have similar adhesionmediating motifs to interact with integrins via their disintegrin domain (D in the diagram) [124,[126][127][128]. Cysteine-rich Secretory Protein 1 was implicated in sperm-oocyte fusion by antibody studies in the 1980s [129,130], and the Crisp1 knockout was recently reported. Sperm from Crisp1 -/-males show a modest decrease in sperm-oocyte fusion in in vitro fertilization assays, although male fertility appears normal [131].…”

Section: Gamete Membrane Fusion and The Oocyte-to-embryo Transitionmentioning

confidence: 70%

Membrane Fusions During Mammalian Fertilization

Gadella

Evans

2011

Advances in Experimental Medicine and Biology

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Successful completion of fertilization in mammals requires three different types of membrane fusion events. Firstly, the sperm cell will need to secrete its acrosome contents (acrosome exocytosis; also known as the acrosome reaction); this allows the sperm to penetrate the extracellular matrix of the oocyte (zona pellucida) and to reach the oocyte plasma membrane, the site of fertilization. Next the sperm cell will bind and fuse with the oocyte plasma membrane (also known as the oolemma), which is a different type of fusion in which two different cells fuse together. Finally, the fertilized oocyte needs to prevent polyspermic fertilization, or fertilization by more than one sperm. To this end, the oocyte secretes the contents of cortical granules by exocytotic fusions of these vesicles with the oocyte plasma membrane over the entire oocyte cell surface (also known as the cortical reaction or cortical granule exocytosis). The secreted cortical contents modify the zona pellucida, converting it to a state that is unreceptive to sperm, constituting a block to polyspermy. In addition, there is a block at the level of the oolemma (also known as the membrane block to polyspermy). IntroductionFertilization of the oocyte involves three membrane fusion events [1] namely, (1) a preparative series of secretion membrane fusions at the apical sperm surface known as acrosome exocytosis [2]. The membrane fusions are induced when the sperm cell binds to specific zona binding proteins at the sperm surface [3][4][5][6][7]. The acrosome exocytosis is a multipoint membrane fusion event between the sperm plasma membrane and the outer acrosomal membrane (see Fig. 5.1 [8,9]) and the exposed acrosomal content is required for sperm to penetrate the zona pellucida [10][11][12]. This so-called zona drilling effectively takes place because the sperm at this stage also has acquired hyperactivated motility [13]. (2) After zona penetration the sperm enters the perivitelline space where it can bind and fuse with the oocyte plasma membrane [14,15]. This is the actual fertilization fusion in which the contents of the sperm are delivered into the oocyte cytoplasm. The plasma membrane of the equatorial segment (see Fig. 5.1) is the site where proteins are located that orchestrate sperm-oocyte binding and fusion [16]. (3) In order to prevent polyspermy the oocyte has to activate defense systems to block redundant sperm-oocyte fusion [17]. To this end the first fertilizing sperm delivers activation factors

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Section: Gamete Membrane Fusion and The Oocyte-to-embryo Transitionmentioning

confidence: 70%

Membrane Fusions During Mammalian Fertilization

Gadella

Evans

2011

Advances in Experimental Medicine and Biology

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“…Before the acrosome reaction occurs, DE is localized on the dorsal region of the rat sperm acrosome and subsequently migrates to the equatorial segments, where sperm begins to fuse with an oocyte . Polyclonal anti-DE antibodies significantly prevented sperm from fusing with zona-free oocytes without changing either the mobility or binding ability of the sperm (Cuasnicu et al 1984). A purified DE protein could bind to the entire surface of oocytes except the region over the meiotic spindle, where sperm rarely fuse , suggesting that there is a receptor for DE on the surface of oocytes for promoting the sperm -oocyte fusion.…”

Section: De On Spermmentioning

confidence: 97%

The mechanism of sperm–oocyte fusion in mammals

Kaji¹,

Kudo²

2004

Reproduction

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Sperm-oocyte fusion is one of the most impressive events in sexual reproduction, and the elucidation of its molecular mechanism has fascinated researchers for a long time. Because of the limitation of materials and difficulties in analyzing membrane protein -protein interactions, many attempts have failed to reach this goal. Recent studies involving gene targeting have clearly demonstrated the various molecules that are involved in sperm-oocyte binding and fusion. Sperm ADAMs (family of proteins with a disintegrin and metalloprotease domain), including fertilin a, fertilin b and cyritestin, have been investigated and found to be important for binding rather than for fusion and painstaking studies have raised suspicions that their putative receptors, oocyte integrins, are necessary for the sperm -oocyte interaction. Recently, several studies have focused the spotlight on CD9 and glycosylphosphatidylinositol (GPI)-anchored proteins on oocytes, and epididymal protein DE on sperm, as candidate molecules involved in sperm-oocyte fusion. Lack of, or interference with the function of, these proteins can disrupt the sperm -oocyte fusion without changing the binding. In this review we highlight the candidate molecules involved in the sperm-oocyte interaction suggested from the recent progress in this research field.

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“…Sperm coating glycoprotein is known to associate with the acrosomal region of spermatozoa after secretion from the epididymis [22]. Antibodies against the protein were able to block fertilization of an ovum [23], indicating a role for sperm coating glycoprotein in the penetration by spermatozoa of the extracellular matrix-like zona pellucida, which surrounds the ovum. A role of SGP28 in degradation of the extracellular matrix during neutrophil migration is possible and suggested by its localization in specific granules, where other matrix degradative enzymes are stored [1][2][3]5].…”

Section: -Ementioning

confidence: 99%

SGP28, a novel matrix glycoprotein in specific granules of human neutrophils with similarity to a human testis‐specific gene product and to a rodent sperm‐coating glycoprotein

et al. 1996

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A novel 28 kDa glycoprotein was purified from exocytosed material from human nentrophils and its primary structure partially determined. Degenerate oligonucleotide primers were used to amplify cDNA clones from a human bone marrow cDNA library. The deduced 245 amino acid sequence of the 2124 bp full-length cDNA showed high degrees of similarity to the deduced sequences of the human gene TPX-1 and of sperm coating glycoprotein from rat and mouse. Subcellular fractionation of human neutrophils indicated that the protein is localized in specific granules. The protein was named SGP28 (specific granule protein of 28 kDa).Key words: TPX-1; Acidic epididymal glycoprotein; Pathogenesis related protein 1; Subcellular fractionation Materials and methods Purification of SGP28Isolated neutrophils were resuspended in Krebs-Ringer phosphate at approximately 5 x 108 cells/ml and preincubated at 37°C for 5 min. Phorbol myristate-acetate (PMA, Sigma) was added at 5 ~tg/ml and the neutrophils stimulated for 20 min. Protease inhibitors were added (phenylmethylsulfonylfluoride (1 mM), aprotinin (200 KIE/ml), pepstatin (1 mM)) and the cells pelleted by centrifugation. After precipitation in 18% PEG, removal of PEG from non-precipitated proteins by addition of 0.5 M K2HPO4, and a change of buffer to 0.05 M sodium acetate, the PEG supernatant was subjected to cation exchange-chromatography on Mono S using FPLC (Pharmacia) (all procedures as described in [8]). Fractions containing SGP28, as evaluated by SDS-PAGE, were pooled and re-chromatographed on MonoS and the eluate subjected to gel filtration on Superose 12 (Pharmacia), using 25 mM Tris-HCl, pH 8.0, 100 mM NaC1 as buffer.

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Antibodies against epididymal glycoproteins block fertilizing ability in rat

Cited by 95 publications

References 18 publications

Membrane Fusions During Mammalian Fertilization

Membrane Fusions During Mammalian Fertilization

The mechanism of sperm–oocyte fusion in mammals

SGP28, a novel matrix glycoprotein in specific granules of human neutrophils with similarity to a human testis‐specific gene product and to a rodent sperm‐coating glycoprotein

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