Molecular cloning of bovine zona pellucida glycoproteins ZPA and ZPB and analysis for sperm‐binding component of the zona

Yonezawa, Naoto; Fukui, Norio; Kuno, Masako; Shinoda, Mitsutaka; Goko, Satoshi; Mitsui, Shinji; Nakano, Minoru

doi:10.1046/j.1432-1327.2001.02269.x

Cited by 31 publications

(49 citation statements)

References 27 publications

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“…5). In the cow, ZPB exhibits the strongest sperm-binding activity among the components and ZPC exhibits sperm-binding activity approximately one-sixth that of ZPB [18]. However, it is still unclear whether bovine ZPA plays a role in sperm-zona binding.…”

Section: Discussionmentioning

confidence: 99%

“…However, it is still unclear whether bovine ZPA plays a role in sperm-zona binding. That is, ZPA exhibits weak sperm-binding activity in the competition assay, but does not exhibit activity in the sperm-bead binding assay [18]. Table 1 shows that bovine ZPA possesses the spermligand active high-mannose-type chain, but there is very In 83A1, 191A1 and 527A1, nonreducing terminal b-Gal residue attaches to GlcNAc residue of the a1-6 branch (*) or of the a1-3 branch (**).…”

Section: Discussionmentioning

confidence: 99%

“…The putative processing site for furin or furin-like enzymes is double underlined. Closed area of Leu366-Ser632 indicates ZP domain [18,25] and the putative transmembrane domain is from Thr683 to Leu697. At least half of the ZPA molecules are specifically cleaved by an unknown protease during preparation, giving rise to N-terminal 21 kDa fragment and C-terminal 63 kDa fragment, which are crosslinked through a disulfide bond.…”

Section: Sugar Mapping Of the Carbohydrate Chains From Each N-glycosymentioning

confidence: 99%

“…Sperm-binding activity is mainly ascribed to ZPB, while ZPC has weak activity. However, it is unclear whether ZPA possesses sperm-binding activity using in vitro competition and sperm-bead binding assays [18]. We deduced the amino acid sequence of the bovine ZPA by cDNA cloning and sequencing, and revealed that bovine ZPA has four potential N-glycosylation sites [18], whereas porcine ZPA has six potential sites [3].…”

mentioning

confidence: 98%

“…When they are digested with endob-Galactosidase to remove the acidic N-acetyllactosamine repeat, the three components become separable [16][17][18]. Sperm-binding activity is mainly ascribed to ZPB, while ZPC has weak activity.…”

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confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Sugar Mapping Of the Carbohydrate Chains From Each N-glycosymentioning

confidence: 99%

mentioning

confidence: 98%

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confidence: 99%

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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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Mammalian Zona Pellucida Proteins

Litscher¹,

Wassarman²

2015

A Guide to Zona Pellucida Domain Proteins

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Specific maternal transcripts in bovine oocytes and cleavaged embryos: Identification with novel DDRT‐PCR methods

Hwang

Park

et al. 2005

Molecular Reproduction Devel

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We used annealing control primer (ACP)-based differential display reverse transcription polymerase chain reaction (DDRT-PCR) to isolate differentially expressed amplicons in bovine germinal vesicle (GV) stage oocytes, 8-cell stage embryos produced in vitro, and blastocyst stage embryos produced in vitro. Four expressed sequence tags (ESTs) of genes that were specifically and predominantly expressed in GV oocytes were cloned and sequenced. We have used a fluorescence monitored real-time quantitative PCR (qPCR) to quantify and analyzed the temporal expression of the target differentially expressed transcripts throughout the preimplantation stages from oocytes to blastocysts. The cloned genes or ESTs all exhibited significant sequence similarity with known bovine genes (98%-100%; DNCL1 and ZP2) or ESTs (81%-97%; FANK1 and GTL3) of other species. As revealed by real-time qRT-PCR, DNCL1, FANK1, GTL3, and ZP2 transcripts were observed in the GV stage oocytes and expression gradually decreased up to the 8-cell stage embryo and the transcripts were not detected in later stages. Similarly, upregulation was observed in GV stage mouse oocytes and metaphase II, suggesting that these four differentially expressed orthologous genes play important roles in early preimplantation, as maternally-derived transcripts.

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Molecular cloning of bovine zona pellucida glycoproteins ZPA and ZPB and analysis for sperm‐binding component of the zona

Cited by 31 publications

References 27 publications

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

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

Mammalian Zona Pellucida Proteins

Specific maternal transcripts in bovine oocytes and cleavaged embryos: Identification with novel DDRT‐PCR methods

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