Carbohydrate determinants involved in mammalian fertilization

Ahuja, Kamal

doi:10.1002/aja.1001740304

Cited by 74 publications

(39 citation statements)

References 68 publications

(64 reference statements)

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“…Accordingly, the inhibitory saccharides could block sperm-egg adhesion by competitively blocking the sperm adhesion sites on the zona pellucida. Similar results have been obtained in mouse, rat, and guinea pig spermatozoa [see Ahuja, 1985a, for a review].…”

Section: Zona-binding Sites On the Sperm Surfacesupporting

confidence: 73%

Metabolic and surface events in fertilization

Fraser

Ahuja

1988

Gamete Research

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Section: Zona-binding Sites On the Sperm Surfacesupporting

confidence: 73%

Metabolic and surface events in fertilization

Fraser

Ahuja

1988

Gamete Research

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“…The chemical nature of these complementary recognition sites is poorly understood, although there is growing evidence that carbohydrate moieties on surface membrane glycoconjugates are involved in these interactions (1,34).…”

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confidence: 99%

Novel alpha-D-mannosidase of rat sperm plasma membranes: characterization and potential role in sperm-egg interactions.

Tulsiani

Skudlarek

Orgebin‐Crist

1989

The Journal of Cell Biology

130

100

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Abstract. During the course of a study of glycoprotein processing mannosidases in the rat epididymis, we have made an intriguing discovery regarding the presence of a novel ot-o-mannosidase on the rat sperm plasma membranes. Unlike the sperm acrosomal "acid" mannosidase which has a pH optimum of 4.4, the newly discovered Ot-D-mannosidase has a pH optimum of 6.2, and 6.5 when assayed in sperm plasma membranes and intact spermatozoa, respectively. In addition, the two enzymes show different substrate specificity. The acrosomal Ot-D-mannosidase is active mainly towards synthetic substrate, p-nitrophenyl a-Dmannopyranoside, whereas the sperm plasma membrane O~-D-mannosidase shows activity mainly towards mannose-containing oligosaccharides. Evidence is presented which suggest that the sperm plasma membrane Ot-D-mannosidase is different from several processing mannosidases previously characterized from the rat liver.The newly discovered a-D-mannosidase appears to be an intrinsic plasma membrane component, since washing of the purified membranes with buffered 0.4 M NaCI did not release the enzyme in soluble form. The enzyme requires nonionic detergent (Triton X-100) for complete solubilization. The enzyme is activated by Co 2+ and Mn 2÷. However, Cu 2÷ and Zn 2÷ are potent inhibitors of the sperm plasma membrane Ot-D-mannosidase. At a concentration of 0.1 mM, these divalent cations caused nearly complete inactivation of the sperm enzyme. In addition methyl-c~-D-mannoside, methyl-ot-D-glucoside, mannose, 2-deoxy-D-glucose, and D-mannosamine are inhibitors of the sperm surface a-D-mannosidase. The physiological role of the newly discovered enzyme is not yet known. Several published reports in three species, including the rat, suggest that the sperm surface c~-o-mannosidase may have a role in binding to mannose-containing saccharides presumably present on the zona pellucida.I X is generally accepted that one step in the fertilization process requires interaction between complementary molecules present on the surface of the spermatozoon and the zona pellucida. The chemical nature of these complementary recognition sites is poorly understood, although there is growing evidence that carbohydrate moieties on surface membrane glycoconjugates are involved in these interactions (1, 34).In mammals, several sperm proteins have been suggested to bind to zona pellucida (28). Some of these macromolecules have enzymatic activity and are thought to form a stable enzyme-substrate complex by binding to the oligosaccharide units present on the zona pellucida glycoproteins. In mice, galactosyltransferase present on the head region of the spermatozoa mediates sperm-egg binding by interacting with its substrate on the zona pellucida (23). There is also evidence that trypsin-like protease present on spermatozoa of mouse (4, 31) initiates sperm-egg binding. Mouse spermatozoa also contain sialyltransferase (13) and fucosyltransferase (30). The latter enzyme has been suggested to be involved in some aspect of sperm-egg recognition (Apter, E M., ...

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“…Specific carbohydrate upon hydration. Thus modifications of the anuran egg extracelmoieties mediate sperm-zona pellucida interaction in mice [2], lular matrix are fundamental processes that regulate sperm-egg hamsters [3], and rats [4]. Alves et al [5] have shown that sul-interaction in fertilization.…”

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confidence: 99%

Structural analysis of oligosaccharide‐alditols released by reductive β‐elimination from the jelly coats of the anuran Bufo arenarum

Morelle

Cabada

Strecker

1998

European Journal of Biochemistry

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Amphibian egg jelly coats are formed by components secreted along the oviduct. These secretion products overlay the oocytes as they are transported toward the cloaca. Mucin type glycoproteins are the major constituents of the egg jelly coats. In this study, the O-linked carbohydrate chains of the jelly coat surrounding the eggs of Bufo arenarum were released by alkaline borohydride treatment. Fractionation of the mixture of O-linked oligosaccharide-alditols was achieved by a combination of chromatographic techniques comprising gel-permeation chromatography, ion-exchange chromatography and high-performance liquid chromatography using an amino-bonded silica column, afforded 11 fractions. The primary structures of these O-glycans were determined by one-dimensional and two-dimensional 1 H-NMR spectroscopy in conjunction with matrix-assisted laser-desorption-ionizationϪtime-of-flight mass spectrometry. 11 oligosaccharide structures, possessing a core consisting of Galβ1→3GalNAc-ol with or without branching through a GlcNAc residue linked β1→6 to the GalNAc residue (core type 2 or core type 1, respectively) are described. These oligosaccharide-alditols with these types of cores have been identified previously in mammalian mucins or in oviducal amphibian jellies. These glycans contain blood group determinants such as H, A or Cad antigens.Keywords : amphibian egg jelly coats; Bufo arenarum; NMR; oligosaccharide.Mature eggs of most animal species are surrounded by extra-space, which separates the envelope from the egg plasma memcellular coats or vestments such as the vitelline envelope, the brane. Jelly coat layers are synthesized by specific regions of zona pellucida, and the jelly coat through which fertilizing the oviduct (the long pars recta convoluta portion of the oviduct) sperm have to penetrate before fusing with the egg plasma mem-and are sequentially deposited as the egg is transported toward brane. Fertilization is a fundamentally significant event, which the cloaca. Interest in these oviductally derived investments has has been intensely studied. A number of studies have shown that centered on their obligatory participation in the early events of the specific recognition between gametes is mediated by surface-fertilization. Oocytes whose jelly coat has been removed, or that located macromolecules. Much of the experimental evidence have not travelled down the oviduct are not fertilized when inavailable points to a major role for carbohydrates in sperm-egg seminated [6]. The particular properties of the jelly which make interaction. Carbohydrate moieties present within the zona pellu-its presence essential to fertilization are largely unknown. Howcida and corresponding carbohydrate-binding proteins on the ever, jelly layers become a blocking site to sperm penetration sperm surface [1] regulate this interaction. Specific carbohydrate upon hydration. Thus modifications of the anuran egg extracelmoieties mediate sperm-zona pellucida interaction in mice [2], lular matrix are fundamental processes that regulate sper...

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Carbohydrate determinants involved in mammalian fertilization

Cited by 74 publications

References 68 publications

Metabolic and surface events in fertilization

Metabolic and surface events in fertilization

Novel alpha-D-mannosidase of rat sperm plasma membranes: characterization and potential role in sperm-egg interactions.

Structural analysis of oligosaccharide‐alditols released by reductive β‐elimination from the jelly coats of the anuran Bufo arenarum

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