Receptor function of mouse sperm surface galactosyltransferase during fertilization.

Lopez, Linda C.; Bayna, Evelyn; Litoff, David; Shaper, Nancy L.; Shaper, Joël H.; Shur, Barry D.

doi:10.1083/jcb.101.4.1501

Cited by 248 publications

(135 citation statements)

References 32 publications

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“…31, in many species (Cherr et al, 1986;Florman and First, 1988a;Wassarman, 1987Wassarman, , 1988. Binding of the mouse sperm to the zona pellucida involves galactosyltransferase (GT), a sperm surface enzyme (Lopez et al, 1985;Shur and Hall, 1982b). The zona pellucida glycoprotein ZP3 is responsible for initial binding of sperm and induction of the acrosome reaction possibly by interacting with GT (Bleil and Wassarman, 1980a;Wassarman, 1987Wassarman, , 1988.…”

Section: Introductionmentioning

confidence: 99%

Carbohydrates and fertilization in animals

Miller

1990

Molecular Reproduction Devel

120

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A frequently used mechanism for sperrn-egg recognition in many species involves complementary protein-carbohydrate interaction. The usual paradigm includes complex glycoconjugates in reproductive tract fluids or on the eggs which are recognized by carbohydratebinding proteins on the sperm surface. Various glycoconjugates are utilized in the steps of sperm capacitation, sperm binding to the egg extracellular matrix and vitelline membrane and induction of the acrosome reaction. Several types of complex glycoconjugates are involved in these processes, including proteoglycans, lactosaminoglycans, sulfated fucose-containing glycoconiugates, and glycoproteins. There appear to be some structural similarities between active glycoconjugates; they are large in molecular weight and complex, and they are often sulfated, fucosylated, and attached to a protein through serine or threonine residues. In some species, the protein core of the glycoconjugates also participates in the interaction by limiting the binding of carbohydrates to sperm only of the relevant species, likely by providing the proper steric arrangement for the interaction. In other cases the protein core seems to serve more as a crosslinker of the carbohydrate moieties. This review discusses the types of glycoconjugates implicated in fertilization and the complementary lectinlike proteins found on sperm.Key Words: Sperm, Eggs, Glycosaminoglycans, Glycoconjugates, Glycoproteins, Zona pellucida, Capacitation, Acrosorne reaction, Fertilization cess differ between species, there is remarkable conservation in the ability of sperm to use glycoconjugates in reproductive tract secretions or in the egg extracellular matrix and vitelline membrane for fertilization-related events. This review summarizes research from various animals in which glycoconjugates are important in sperm-egg interaction. It contrasts differences between species at the point of the fertilization process where carbohydrates interact with sperm. Furthermore, a structural comparison between each of the carbohydrates is presented.An understanding of fertilization-related events is necessary prior to a discussion of the potential molecules involved in sperm-egg interaction. There are differences between species in the events occurring both before and during sperm-egg interaction. These events are best understood in sea urchins and mice, although there is recent information from other species. A diagram of sperm-egg interaction in sea urchins is shown in Figure

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Section: Introductionmentioning

confidence: 99%

Carbohydrates and fertilization in animals

Miller

1990

Molecular Reproduction Devel

120

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“…The resulting membrane pellet was then lyophilized and stored at -70°C until used. For chromatography, alkalinestripped membranes were homogenized in 75 mM sodium phosphate buffer, pH 7.2 (PB), containing 16 mM CHAPS and protease inhibitors (10 pg/ml aprotinin, 1 pg/ml leupeptin, 2 fig/ml antipain, 10 &ml benzamidine, 1 &ml chymostatin, and 1 fig/ml pepstatin A; Lopez et al, 1985). The CHAPS soluble fraction (supematant) was obtained after centrifugation at 160,000 x g for 2 hr and applied to a hydroxylapatite column (1.5 x 12 cm) equilibrated in 75 mM PB and 16 mM CHAPS.…”

Section: Immunocytochemistrymentioning

confidence: 99%

A nerve terminal protein with a selective distribution in spinal cord and brain

1989

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A monoclonal antibody, designated S-7B8, recognizes a protein antigen localized to highly selected populations of nerve terminals in spinal cord and brain. The antibody produces dense immunocytochemical staining of primary afferent endings that synapse in superficial laminae of the spinal cord dorsal horn. Electron microscopy shows staining to be localized in nerve terminals where reaction product is associated primarily with spherical vesicles. In brain, S-7B8 immunoreactivity occurs in nerve terminals in sensory relay nuclei, most thalamic nuclei, and other selected areas, including the cerebellar molecular layer, the substantia nigra, the globus pallidus, and certain synaptic layers of the hippocampus and dentate gyrus. Endocrine glands and other tissues do not exhibit S-7B8 immunoreactivity. Although the antibody localizes to certain populations of nerve terminals that may use excitatory amino acid neurotransmitters, the distribution of S-7B8 immunoreactivity in the CNS does not correspond to that of any previously identified nerve terminal protein. Experiments to characterize the S-7B8 antigen indicate it may be an integral membrane component since extraction of synaptosomes with alkaline pH or high ionic strength does not release the antigen from the membranes. To identify the molecular weight of the S-7B8 antigen, synaptosomal membranes were solubilized in CHAPS and sequentially chromatographed on hydroxylapatite and then on DEAE anion-exchange resin to produce enriched fractions. When enriched fractions were separated on SDS-PAGE and Western blotted, the S-7B8 antibody specifically stained a protein migrating at 75,000 Da. This protein has been designated NT75. Preliminary studies of developing pathways show that the appearance of S-7B8 immunoreactivity in growing nerve endings corresponds closely to the time when synaptic connections are formed. Thus, the NT75 protein recognized by the S-7B8 antibody may have a role in the development and maintenance of specific synaptic endings.

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“…In support of this model, ␤4GT has been localized immunocytochemically with a polyclonal antiserum to the sperm plasma membrane that overlies the acrosome (6). Biochemical and immunological probes that can potentially interact with cell surface ␤4GT block the ability of sperm to bind zona-intact eggs in vitro (6). The activity of ZP3 in a competitive sperm-ZP binding assay was reduced either by enzymatic removal or ␤4-galactosylation of terminal GlcNAc residues (5).…”

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confidence: 99%

“…The first model posits that sperm surface ␤1,4-galactosyltransferase (␤4GT) binds its acceptor sugar substrate, an N-acetylglucosaminyl residue (GlcNAc), located at the nonreducing terminus of an O-linked oligosaccharide on ZP3 (5,6). In support of this model, ␤4GT has been localized immunocytochemically with a polyclonal antiserum to the sperm plasma membrane that overlies the acrosome (6). Biochemical and immunological probes that can potentially interact with cell surface ␤4GT block the ability of sperm to bind zona-intact eggs in vitro (6).…”

mentioning

confidence: 99%

Murine Sperm-Zona Binding, A Fucosyl Residue Is Required for a High Affinity Sperm-binding Ligand

Johnston

Wright

Shaper

et al. 1998

Journal of Biological Chemistry

121

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An essential initial step in murine fertilization is the binding of acrosome-intact sperm to specific O-linked oligosaccharides on zona pellucida glycoprotein 3. While there is agreement on the primary role of O-linked glycans in this process, there is a lack of consensus on both the terminal monosaccharide(s) required for a functional sperm binding site and the corresponding protein on the sperm cell surface that recognizes this ligand. Much current debate centers on an essential role for either a terminal N-acetylglucosaminyl or, alternatively, a terminal ␣-galactosyl residue. To gain insight into the terminal saccharides required to form a functional sperm-binding ligand, dose-response curves were generated for a series of related tri-and tetrasaccharides to evaluate their relative effectiveness to competitively inhibit the in vitro binding of murine sperm to zona pellucida-enclosed eggs. A GlcNAc-capped trisaccharide, GlcNAc␤1,4GlcNAc␤1,4GlcNAc,was inactive (1-72 M range). In contrast, a ␤4-galactosyl-capped trisaccharide (Gal␤1,4GlcNAc␤1, 4GlcNAc) and an ␣3-galactosyl-capped trisaccharide (Gal␣1,3Gal␤1,4 GlcNAc) inhibited sperm-zona binding with low or moderate affinity (ED 50 ‫؍‬ 42 M and 5.3 M, respectively). The addition of an ␣3-fucosyl residue to each of these two competitive inhibitors, forming Gal␤1,4[Fuc␣1,3] GlcNAc␤1,4GlcNAc or Gal␣1,3Gal␤1, 4[Fuc␣1,3]Glc NAc, resulted in ligands with 85-and 12-fold higher affinities for sperm, respectively (ED 50 ‫؍‬ 500 and 430 nM). Thus, the presence of a fucosyl residue appears to be obligatory for an oligosaccharide to bind sperm with high affinity. Last, mixing experiments with pairs of competitive inhibitors suggest that murine sperm-zona binding is mediated by two independent oligosaccharide-binding sites on sperm. The first (apparently high affinity) site binds both the ␣3-galactosyl-capped trisaccharide and the two fucosylated tetrasaccharides. The second (apparently low affinity) site binds a nonfucosylated ␤-galactosyl-capped trisaccharide.The initial event in mammalian fertilization is the binding of a sperm to the zona pellucida (ZP), 1 the extracellular glycoprotein matrix surrounding the egg. In the mouse, capacitated, acrosome-intact sperm initially bind to zona pellucida glycoprotein 3 (ZP3), one of three glycoproteins comprising the ZP (1, 2). The sperm binding activity of ZP3 is localized to a subset of O-linked oligosaccharides on ZP3 with an estimated molecular mass of about 3.9 kDa (3-5). While there is general agreement that the nonreducing terminal monosaccharides are critical for binding (4,5), there is a lack of agreement on the identity of the terminal monosaccharide(s) required for a functional spermbinding ligand and the corresponding binding site(s) on the sperm surface.Two different models of murine sperm-ZP binding have been proposed that address the basic requirements for both a functional sperm-binding ligand and for the corresponding sperm surface ZP-binding protein. The first model posits that sperm surface ␤1,4-galactosyltransf...

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Receptor function of mouse sperm surface galactosyltransferase during fertilization.

Cited by 248 publications

References 32 publications

Carbohydrates and fertilization in animals

Carbohydrates and fertilization in animals

A nerve terminal protein with a selective distribution in spinal cord and brain

Murine Sperm-Zona Binding, A Fucosyl Residue Is Required for a High Affinity Sperm-binding Ligand

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