Essential role of the nonreducing terminal α‐mannosyl residues of the N‐linked carbohydrate chain of bovine zona pellucida glycoproteins in sperm‐egg binding

Amari, S.; Yonezawa, Naoto; Mitsui, Shinji; Katsumata, Toshiyuki; Hamano, Seizo; Kuwayama, Masashige; Hashimoto, Yasuhiro; Suzuki, Akemi; Takeda, Yoshiro; Nakano, Minoru

doi:10.1002/mrd.1026

Cited by 54 publications

(57 citation statements)

References 24 publications

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“…The highest luminosity of the oocyte treated with LCA and GNL lectins showed a high concentration (respect to the other monosaccharides and controls) of the Glc and Man respectively on the oocytes at all levels of oocyte maturation. This result agrees with previous studies carried out on oocyte envelopes in the shrimp Sicyonia ingentis (Pillai & Clark, 1990;Glas et al, 1996), the sea urchin Strongylocentrotus purpuratus (Correa & Carroll, 1997) and in cattle (Amari et al, 2001), in which the oocyte envelopes had high mannose values.…”

Section: Discussionsupporting

confidence: 93%

Role of egg surface glycoconjugate in the fertilization of the rock shrimp Rhynchocinetes typus (Milne Edwards, 1837)

Dupré¹,

Gomez²,

G³

et al. 2012

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ABSTRACT. During first gamete interaction, oligosaccharides on the glycoproteins present in oocyte envelopes of the rock shrimp, Rhynchocinetes typus, play an important role in spermatozoon recognition prior to the onset of penetration. These oligosaccharides have terminal monosaccharides that may be recognized by means of specific lectins. A variety of marine species have monosaccharides on their oocyte envelopes, allowing them to interact with the spermatozoa. The number and location of the monosaccharides varies during oocyte maturation. However, this phenomenon has not been studied in shrimp. The present study evaluates the presence and location of monosaccharides on oocyte envelopes during maturation using seven specific lectins conjugated to FITC (GNL, LCA, Con-A BS-1, LTA, GLS-II,DBA); these recognize mannose (α 1-3) mannose, α-mannose, α-glucose, glucose, galactose, fucose, N-acetyl-glucosamine, and N-acetylgalactosamine, respectively. Participation of these carbohydrates in the fertilization process was determined through the insemination of fresh oocytes with spermatozoa previously incubated with the different monosaccharides that block the active sites of the spermatozoa, inhibiting fertilization. The results showed the presence of N-acetyl-glucosamine and mannose on the oocyte envelopes, indicating that these sugars could be the receptors during the first gamete interaction. The results also suggested that glucose could be a complementary receptor to N-acetyl-glucosamine and mannose since, despite the low concentration of glucose on the envelope, this sugar generated a high degree of fertilization inhibition. Keywords: gametes, oocyte recognition, sperm receptors, lectins, vitelline coat, chorion. El rol de los glicoconjugados de las cubiertas ovocitarias en la fecundación del camarón de roca Rhynchocinetes typus (Milne-Edwards, 1837)RESUMEN. Durante la primera interacción gamética, los oligosacaridos unidos a las glicoproteínas de las cubiertas ovocitarias del camarón de roca Rhynchocinetes typus tienen un importante rol en el reconocimiento del espermatozoide antes de iniciar la penetración. Estos oligosacáridos presentan en su zona terminal, monocacáridos que pueden ser reconocidos por lectinas específicas. Diversas especies marinas tienen monosacáridos en la cubierta externa de sus ovocitos que le permiten interactuar con los espermatozoides y su número y localización presenta cambios durante la maduración, sin embargo este fenómeno no ha sido estudiado en camarones. El presente estudio evalúa la presencia y localización de monosacáridos sobre la cubierta de los ovocitos durante su maduración usando siete lectinas específicas conjugadas con FITC (GNL, LCA , Con-A BS-1, LTA, GLS-II y DBA) las cuales reconocen manosa (α 1-3) manosa, α-manosa, α-glucosa, glucosa, galactosa, fucosa, N-acetil-glucosamina y N-acetilgalactosamina respectivamente. La participación de estos carbohidratos en el proceso de fecundación fue determinada mediante la inseminación de ovocitos frescos con espermatozoides incubados...

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Section: Discussionsupporting

confidence: 93%

Role of egg surface glycoconjugate in the fertilization of the rock shrimp Rhynchocinetes typus (Milne Edwards, 1837)

Dupré¹,

Gomez²,

G³

et al. 2012

lajar

View full text Add to dashboard Cite

show abstract

“…Although a considerable amount of knowledge has been gained especially in human and mouse (Almeida et al 1995, Bronson & Fusi 1996, Fusi et al 1996a, 1996b, Nixon et al 2007, Vjugina & Evans 2008, the exact mechanisms of the molecules involved in bovine fertilization are not unequivocally identified at present. Carbohydrates and glycoproteins are assumed to modulate adhesion and binding events during consecutive reproductive processes, like sperm-oviduct adhesion (Lefebvre et al 1997, Suarez et al 1998, Revah et al 2000, Talevi & Gualtieri 2001, Sostaric et al 2005, Ignotz et al 2007, sperm-oocyte interactions (Tulsiani et al 1997, Gougoulidis et al 1999, Amari et al 2001, Tanghe et al 2004a, 2004b, and embryo implantation (Whyte & Allen 1985, Biermann et al 1997.…”

Section: Introductionmentioning

confidence: 99%

Expression and putative function of fibronectin and its receptor (integrin α5β1) in male and female gametes during bovine fertilization in vitro

Thys¹,

Nauwynck²,

Maes³

et al. 2009

Reproduction

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Fibronectin (Fn) is a 440 kDa glycoprotein assumed to participate in sperm-egg interaction in human. Recently, it has been demonstrated that Fn -when present during bovine IVF -strongly inhibits sperm penetration. The present study was conducted firstly to evaluate the expression of Fn and its integrin receptor (a 5 b 1 ) on male and female bovine gametes using indirect immunofluorescence and secondly, to determine the function of Fn during bovine IVF. Endogenous Fn was detected underneath the zona pellucida (ZP) and integrin a 5 on the oolemma of cumulus-denuded oocytes. Bovine spermatozoa displayed integrin a 5 at their equatorial segment after acrosome reaction. We established that the main inhibitory effect of exogenously supplemented Fn was located at the sperm-oolemma binding, with a (concurrent) effect on fusion, and this can probably be attributed to the binding of Fn to spermatozoa at the equatorial segment, as shown by means of Alexa Fluor 488-conjugated Fn. Combining these results, the inhibitory effect of exogenously supplemented Fn seemed to be exerted on the male gamete by binding to the exposed integrin a 5 b 1 receptor after acrosome reaction. The presence of endogenous Fn underneath the ZP together with integrin a 5 expression on oolemma and acrosome-reacted (AR) sperm cell surface suggests a 'velcro' interaction between the endogenous Fn ligand and corresponding receptors on both (AR) sperm cell and oolemma, initiating sperm-egg binding.

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“…However, participation of the sialic acids in bovine sperm-zona binding has not been demonstrated. Bovine sperm-binding activity is mainly ascribed to the high-mannose-type chain with five mannose residues [15].…”

Section: Discussionmentioning

confidence: 99%

“…The neutral chain is a high-mannosetype chain with five mannose residues (Man 5 GlcNAc 2 ). This high-mannose-type chain exhibits sperm-binding activity and inhibits in vitro fertilization [15].The native bovine zona proteins cannot be separated into their three components because their molecular masses are almost identical (74 kDa) and their carbohydrate chains are very heterogeneous [16]. When they are digested with endob-Galactosidase to remove the acidic N-acetyllactosamine repeat, the three components become separable [16][17][18].…”

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confidence: 99%

Localization of N‐linked carbohydrate chains in glycoprotein ZPA of the bovine egg zona pellucida

Ikeda

Yonezawa

Naoi

et al. 2002

European Journal of Biochemistry

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The zona pellucida, a transparent envelope surrounding the mammalian oocyte, consists of three glycoproteins, ZPA, ZPB and ZPC, and plays a role in sperm-egg interactions. In bovines, these glycoproteins cannot be separated unless the acidic N-acetyllactosamine regions of the carbohydrate chains are removed by endo-b-Galactosidase digestion. Endo-b-Galactosidase-digested ZPB retains stronger spermbinding activity than ZPC. It is still unclear whether ZPA possesses significant activity. Recently, we reported that bovine sperm binds to Man 5 GlcNAc 2 , the neutral N-linked chain in the cow zona proteins. In this study, we investigated the localization of the sperm-ligand active high-mannosetype chain and the acidic complex-type chains in bovine ZPA. Three N-glycopeptides of ZPA, containing an N-glycosylation site at Asn83, Asn191 and Asn527, respectively, were obtained from endo-b-Galactosidase-digested ZPA. Of these glycosylation sites, only Asn527 is present in the ZP domain common to all the zona proteins. The carbohydrate structures of the N-linked chains obtained from each N-glycopeptide were characterized by two-dimensional sugar mapping analysis, while considering the structures of the N-linked chains of the zona protein mixture reported previously. Acidic complex-type chains were found at all three N-glycosylation sites, while Man 5 GlcNAc 2 was found at Asn83 and Asn191, but there was very little of this spermligand active chain at Asn527 in the ZP domain of ZPA.Keywords: glycoprotein; N-linked carbohydrate chain; sperm ligand; zona pellucida; ZP domain.The mammalian oocyte is coated with a transparent matrix called the zona pellucida. This matrix plays various roles in the early phase of fertilization: species-specific sperm binding, blocking polyspermy, and protecting the embryo until implantation [1,2]. The zona is composed of three glycoproteins, called ZPA, ZPB and ZPC in the order of the size of their cDNAs [3], and their carbohydrate chains are responsible for species-specific sperm-zona binding [1,4].In the pig, the carbohydrate structures of O-linked chains of zona protein mixture [5,6] and the acidic and neutral N-linked chains of ZPB/ZPC mixture [7,8] are well characterized. Sperm-binding activity has been ascribed to the O-linked chains of the zona protein mixture [9] or to the neutral N-linked chains obtained from the ZPB/ZPC mixture [8]. We have shown that the triantennary/tetraantennary chains of the ZPB/ZPC mixture possess greater activity than the diantennary chains [10]. The triantennary/ tetraantennary chains of ZPB are localized at Asn220 in the N-terminal region [10]. Moreover, the isolated N-terminal peptide of ZPB including Asn220 has sperm-binding activity [11]. Yurewicz et al. [12] showed that ZPB and ZPC form heterocomplexes that have sperm-binding activity, but that monomeric ZPB or ZPC does not exhibit this activity. These results suggest that ZPC contributes to the expression of the sperm-binding activity of the neutral N-linked chain of ZPB. In ZPC, the triantennary/tetraante...

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Essential role of the nonreducing terminal α‐mannosyl residues of the N‐linked carbohydrate chain of bovine zona pellucida glycoproteins in sperm‐egg binding

Cited by 54 publications

References 24 publications

Role of egg surface glycoconjugate in the fertilization of the rock shrimp Rhynchocinetes typus (Milne Edwards, 1837)

Role of egg surface glycoconjugate in the fertilization of the rock shrimp Rhynchocinetes typus (Milne Edwards, 1837)

Expression and putative function of fibronectin and its receptor (integrin α5β1) in male and female gametes during bovine fertilization in vitro

Localization of N‐linked carbohydrate chains in glycoprotein ZPA of the bovine egg zona pellucida

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