Cloning of rat sp56, the homologue of mouse sperm ZP3 receptor–sp56

He, Xiao; Yuan, Yan; Li, Yi Ping; Koide, S. S.

doi:10.1038/sj.cr.7290156

Cited by 6 publications

(3 citation statements)

References 12 publications

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“…It should be noted that most studies of the function of ZP3R have been performed in the mouse. An orthologue has been identified in the guinea pig (AM67) [12] and the rat [16]. An inference has been made to a putative human orthologue, but no sequence data were provided or any repository accession information cited [17].…”

Section: Introductionmentioning

confidence: 99%

Function of the Acrosomal Matrix: Zona Pellucida 3 Receptor (ZP3R/sp56) Is Not Essential for Mouse Fertilization1

Muro

Buffone

Okabe

et al. 2012

Biology of Reproduction

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In mammalian fertilization, sperm-zona pellucida binding is considered to be a critical aspect of gamete interaction. In this study, we examine the mouse sperm acrosomal matrix protein zona pellucida 3 receptor (ZP3R; formerly called sp56) because of our interest in defining the function of the acrosomal matrix, the particulate compartment within the sperm secretory acrosome. Using targeted deletion of the Zp3r gene by homologous recombination, we examined the fertility of nullizygous animals. Our experiments showed that males and females homozygous for the affected gene exhibited no differences in litter sizes compared to wild-type and heterozygous animals. Testis weights of nullizygous males were equivalent to those of wild-type and heterozygous males, and no differences in the number of sperm produced by mice of three genotypes were found. In vitro fertilization rates using cumulus-intact and cumulus-free oocytes were also equivalent. Examination of sperm-binding zonae of unfertilized eggs and the ability of the sperm to undergo acrosomal exocytosis in response to calcium ionophore A23187 displayed no differences between wild-type, heterozygous, and nullizygous mouse sperm. These results provide further evidence that either ZP3R is not involved in sperm-zona pellucida binding or this process might be functionally redundant, involving multiple proteins for gamete interactions.

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Section: Introductionmentioning

confidence: 99%

Function of the Acrosomal Matrix: Zona Pellucida 3 Receptor (ZP3R/sp56) Is Not Essential for Mouse Fertilization1

Muro

Buffone

Okabe

et al. 2012

Biology of Reproduction

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“…ZP3R is a member of the complement regulatory superfamily. Other than guinea pig AM67 and rat ZP3R, mouse ZP3R is most closely related to the alpha chain of complement 4-binding protein (Foster et al, 1997;He et al, 2003). Both of these proteins form high order oligomers (six to eight monomers of ZP3R per protein complex and seven alpha and one beta subunits in human C4BP) that contain both intra-and inter-chain disulfides (Kask et al, 2002).…”

Section: Consequences Of the Structural Homologies Of Zp3r And C4bpmentioning

confidence: 99%

Functional consequences of cleavage, dissociation and exocytotic release of ZP3R, a C4BP-related protein, from the mouse sperm acrosomal matrix

Buffone

Kim

Doak

et al. 2009

Journal of Cell Science

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The acrosome is an exocytotic vesicle located on the apical tip of the sperm head. In addition to having different morphological regions, two biochemically distinct compartments can be defined within the acrosome: a particulate acrosomal matrix and a soluble partition. The domains within the acrosome participate in the release of acrosomal proteins from the sperm during exocytosis, depending on whether the proteins partition into either the soluble or matrix compartments of the acrosome. We have examined the mechanism of differential release by evaluating the solubilization of acrosomal matrix protein ZP3R (sp56) from mouse sperm during the course of spontaneous acrosomal exocytosis. Using indirect immunofluorescence and immunoblotting, we found that the ZP3R monomer is processed from 67,000 Mr to 43,000 Mr by proteases coincident with release from the acrosome. Sperm require a maturational step, termed capacitation, before they are competent for acrosomal exocytosis and the processing of ZP3R is dramatically reduced under non-capacitating conditions. The cleavage probably takes place in complement control protein domain (CCP) 6 or the bridge region between CCP6 and CCP7, which is not present in the guinea pig orthologue AM67. The cleaved form of ZP3R does not bind to unfertilized eggs. We have incorporated these structural considerations into a model to explain the functional consequences of acrosomal exocytosis on sperm-zona interactions.

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“…ZP3R was initially isolated by ZPC-affinity chromatography in mice [66], and was also found in guinea pigs [AM67, [67]], and rats [68], but no sequence data are available for a human orthologue. ZP3R is a component of the acrosomal matrix; following maturation, ZP3R becomes transiently associated with the sperm surface [69].…”

Section: Sperm Recognition Of the Zpmentioning

confidence: 99%

Protein-Carbohydrate Interaction between Sperm and the Egg-Coating Envelope and Its Regulation by Dicalcin, a Xenopus laevis Zona Pellucida Protein-Associated Protein

Miwa

2015

Molecules

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Protein-carbohydrate interaction regulates multiple important processes during fertilization, an essential biological event where individual gametes undergo intercellular recognition to fuse and generate a zygote. In the mammalian female reproductive tract, sperm temporarily adhere to the oviductal epithelium via the complementary interaction between carbohydrate-binding proteins on the sperm membrane and carbohydrates on the oviductal cells. After detachment from the oviductal epithelium at the appropriate time point following ovulation, sperm migrate and occasionally bind to the extracellular matrix, called the zona pellucida (ZP), which surrounds the egg, thereafter undergoing the exocytotic acrosomal reaction to penetrate the envelope and to reach the egg plasma membrane. This sperm-ZP interaction also involves the direct interaction between sperm carbohydrate-binding proteins and carbohydrates within the ZP, most of which have been conserved across divergent species from mammals to amphibians and echinoderms. This review focuses on the carbohydrate-mediated interaction of sperm with the female reproductive tract, mainly the interaction between sperm and the ZP, and introduces the fertilization-suppressive action of dicalcin, a Xenopus laevis ZP protein-associated protein.The action of dicalcin correlates significantly with a dicalcin-dependent change in the lectin-staining pattern within the ZP, suggesting a unique role of dicalcin as an inherent protein that is capable of regulating the affinity between the lectin and oligosaccharides attached on its target glycoprotein.

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Cloning of rat sp56, the homologue of mouse sperm ZP3 receptor–sp56

Cited by 6 publications

References 12 publications

Function of the Acrosomal Matrix: Zona Pellucida 3 Receptor (ZP3R/sp56) Is Not Essential for Mouse Fertilization1

Function of the Acrosomal Matrix: Zona Pellucida 3 Receptor (ZP3R/sp56) Is Not Essential for Mouse Fertilization1

Functional consequences of cleavage, dissociation and exocytotic release of ZP3R, a C4BP-related protein, from the mouse sperm acrosomal matrix

Protein-Carbohydrate Interaction between Sperm and the Egg-Coating Envelope and Its Regulation by Dicalcin, a Xenopus laevis Zona Pellucida Protein-Associated Protein

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