Sperm from a Variety of Mammalian Species Express β1,4-Galactosyltransferase on their Surface1

Larson, Jennine L.; Miller, David J.

doi:10.1095/biolreprod57.2.442

Cited by 41 publications

(17 citation statements)

References 1 publication

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“…Consistent with this notion, GalT is present on all mammalian sperm assayed and has the proper location expected of a zona-binding protein [Fayrer-Hosken et al, 1991;Huszar et al, 1997;Larson and Miller, 1997]. AntiGalT antibodies and other GalT-specific perturbations inhibit sperm-egg binding in other species, most notably bovine (unpubl.…”

Section: Galt In Fertilization Of Other Speciesmentioning

confidence: 74%

Galactosyltransferase Function during Mammalian Fertilization

Nixon¹,

Lu²,

Wassler³

et al. 2000

Cells Tissues Organs

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Gamete recognition has been studied extensively in the mouse. In this system, it is generally believed that sperm bind to a class of O-linked oligosaccharides on the zona pellucida glycoprotein, ZP3. The best characterized sperm receptor for ZP3 is β1,4-galactosyltransferase (GalT), which functions in a lectin-like capacity by binding to N-terminal N-acetylglucosamine residues on ZP3 oligosaccharides. Multivalent oligosaccharides on ZP3, as well as synthetic polymers terminating in N-acetylglucosamine aggregate GalT, leading to activation of a heterotrimeric G protein cascade and culminating in the acrosome reaction. Following fertilization, cortical granules release N-acetylglucosaminidase, which removes the binding site for sperm GalT and facilitates the zona block to polyspermic binding. Genetic manipulation of GalT expression has confirmed its function as a ZP3 receptor. Overexpressing GalT on sperm leads to increased binding of ZP3, increased G protein activation, and precocious acrosome reactions. In contrast, sperm from mice made null for GalT by homologous recombination are refractory to ZP3, in that they are unable to bind soluble ZP3 and fail to undergo the acrosome reaction in response to zona glycoproteins. Surprisingly, GalT null sperm still bind to the zona and achieve low rates of fertilization in vitro. This then suggests that sperm-egg binding involves receptor-ligand interactions independent of GalT and ZP3. The current model suggests that GalT functions as the ZP3 receptor that is responsible for inducing the acrosome reaction, whereas initial sperm-zona binding is dictated by other sperm surface receptors. Consistent with this, at least three other zona pellucida monosaccharides have been implicated in sperm binding, and novel sperm surface glycoproteins have been suggested to function in gamete binding. A large scaffolding protein has been identified that associates with the GalT cytoplasmic domain and may be responsible for orchestrating its signal transduction capacities that lead to the acrosome reaction.

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Section: Galt In Fertilization Of Other Speciesmentioning

confidence: 74%

Galactosyltransferase Function during Mammalian Fertilization

Nixon¹,

Lu²,

Wassler³

et al. 2000

Cells Tissues Organs

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“…It binds specifically to the N-terminal N-acetylglucosamine residues of ZP3 but not to the other zona pellucida proteins [24,61]. The enzyme is present in the head region of all mammalian sperm studied, including human, consistent with a role in gamete recognition [24,49,62,63]. Reagents blocking the activity of the enzyme, including UDP-Gal and alpha-lactalbumin, inhibit sperm-zona pellucida binding [24,49,64].…”

Section: Discussionmentioning

confidence: 96%

The Contribution of d-Mannose, l-Fucose, N-Acetylglucosamine, and Selectin Residues on the Binding of Glycodelin Isoforms to Human Spermatozoa1

Chiu

Tsang

Koistinen

et al. 2004

Biology of Reproduction

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Previous data showed that glycodelin-A from amniotic fluid and glycodelin-F from follicular fluid inhibited sperm-zona pellucida binding. Solubilized zona pellucida reduced the binding of glycodelin-F to sperm extract dose dependently. This study demonstrated that the zona pellucida proteins also reduced the binding of glycodelin-A to sperm extract. Ionophore-induced acrosome reaction reduced the binding of iodinated glycodelin-A and -F to sperm, indicating that the glycodelin-binding sites are on the outer acrosomal membrane or on the sperm plasma membrane overlying the acrosome. While the binding of glycodelin-A to sperm was suppressed by mannose and fucose neoglycoproteins, that of glycodelin-F was also reduced by acetylglucosamine neoglycoprotein. Pretreatment of sperm with inhibitors of mannosidase and acetylglucosaminidase reduced the binding of glycodelin-F to sperm. On the other hand, inhibitor of mannosidase but not of acetylglucosaminidase inhibited the binding of glycodelin-A. In a competition binding assay, mannosidase reduced both glycodelin-A and -F binding whereas acetylglucosaminidase reduced only glycodelin-F binding. While fucosidase reduced the binding of both glycodelins, fucosidase inhibitor was marginally active in suppressing the binding of glycodelins to human sperm. Among the selectins tested, only E-selectin had a slight inhibitory effect on the binding of glycodelin-A to sperm. The binding of glycodelin-F was unaffected by selectins and their antibodies. In conclusion, the binding of glycodelin-A to sperm involves mannose, fucose, and possibly E- selectin residues, while that of glycodelin-F involves mannose, fucose, and N-acetylglucosamine but not the selectin residue.

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“…Others have confirmed the participation of GalT during mouse sperm-egg binding (Benau et al, 1990) and GalT has been detected on the surface of all mammalian sperm thus far assayed, including rat, guinea pig, rabbit, equine, bovine, porcine and human (FayerHosken et al, 1991;Larson and Miller, 1997;Huszar et al, 1997) although its role, if any, during sperm-ZP binding in these species remains unknown.…”

Section: Evidence Implicating Sperm Galt As An Inducer Of Acrosomal Ementioning

confidence: 87%

Reassessing the role of protein-carbohydrate complementarity during sperm-egg interactions in the mouse

Shur

2008

Int. J. Dev. Biol.

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Despite years of intense study by many investigators, it may appear that we have made little progress towards a molecular understanding of mammalian sperm binding to the egg zona pellucida. An abundance of evidence derived from in vitro assays suggests that sperm-zona pellucida binding is dependent upon sperm recognition of specific glycan moieties on the zona pellucida glycoproteins. However, there is considerable disagreement regarding the identity of the zona pellucida sugars thought to mediate sperm binding, as well as disagreement over the identity of the sperm receptors themselves. Moreover, results from in vivo gene-targeting strategies fail to support a role for many, if not all, of the sperm receptors and their zona pellucida ligands implicated from in vitro assays. Nevertheless, a retrospective view of the literature suggests that some common principles are emerging regarding the molecular basis of mammalian sperm-zona binding, both with respect to the nature of the components that mediate binding, as well as the involvement of distinct receptor-ligand interactions, that involve both protein-and carbohydrate-dependent mechanisms of binding.

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Sperm from a Variety of Mammalian Species Express β1,4-Galactosyltransferase on their Surface1

Cited by 41 publications

References 1 publication

Galactosyltransferase Function during Mammalian Fertilization

Galactosyltransferase Function during Mammalian Fertilization

The Contribution of d-Mannose, l-Fucose, N-Acetylglucosamine, and Selectin Residues on the Binding of Glycodelin Isoforms to Human Spermatozoa1

Reassessing the role of protein-carbohydrate complementarity during sperm-egg interactions in the mouse

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