Cell surface carbohydrates of embryonal carcinoma cells: Polysaccharidic side chains of F9 antigens and of receptors to two lectins, FBP and PNA

Muramatsu, Takashi; Gachelin, Gabriel; Damonneville, Martine; Delarbre, Christiane; Jacob, François

doi:10.1016/0092-8674(79)90367-2

Cited by 204 publications

(65 citation statements)

References 25 publications

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“…LAGS are unsulfated, branched heteropolymers of galactose and N-acetylglucosamine, some of which may be fucosylated (Muramatsu et al, 1979). They are often attached to protein and the carbohydrate chains are variable in length, similar to keratan sulfate proteoglycans.…”

Section: Sperm-zona Interaction In Rabbitsmentioning

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: Sperm-zona Interaction In Rabbitsmentioning

confidence: 99%

Carbohydrates and fertilization in animals

Miller

1990

Molecular Reproduction Devel

120

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“…The structures of the F9 antigenic determinant(s) were not established; however, it was shown that undifferentiated teratocarcinoma cells and embryonic cells are rich in glycoproteins with long carbohydrate chains of poly-N-acetyl-lactosamine type which react with antibodies to F9 antigen (Muramatsu et al, 1979). Work with monoclonal antibodies has shown that several carbohydrate antigens which change dramatically at successive stages of differentiation are borne on poly-N-acetyl-lactosamine chains of polydisperse, high-Mr glycoproteins .…”

Section: Glycoprotein Oligosaccharides As Major Antigens Of Whole Cellsmentioning

confidence: 99%

Carbohydrates as antigenic determinants of glycoproteins

Feizi

Childs

1987

Biochemical Journal

261

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“…FBP (105 mg) were coupled to 10 ml of Affi-gel 10 (Bio-Rad) in 0.1 M Mops buffer (pH 7.5) containing 80 mM CaC12 at 4°C for 4 h. Residual active sites of the beads were blocked by incubating with 0.1 M ethanolamine (pH 7.5) for 1 h. N4-1 [25] are embryonal carcinoma cell lines derived from teratocarcinoma OTT6050 and STT-2, respectively. The cells were labeled by culturing with radioactive sugars for 24 h as described previously [7]. The labeled cells were harvested in Dulbecco's phosphate-buffered saline by pipetting and extracted for 30 min at 4°C with 1% Triton X-100 in 0.01 M Tris/HCl buffer (pH 7.6) containing 0.15 M NaCl, 3 mM MgCI2 and 1 mM phenylmethylsulfonyl fluoride.…”

Section: Methodsmentioning

confidence: 99%

“…The cells were labeled by culturing with radioactive sugars for 24 h as described previously [7]. The labeled cells were harvested in Dulbecco's phosphate-buffered saline by pipetting and extracted for 30 min at 4°C with 1% Triton X-100 in 0.01 M Tris/HCl buffer (pH 7.6) containing 0.15 M NaCl, 3 mM MgCI2 and 1 mM phenylmethylsulfonyl fluoride.…”

Section: Methodsmentioning

confidence: 99%

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Receptors for fucose-binding proteins of Lotus tetragonolobus isolated from mouse embryonal carcinoma cells. Structural characteristics of the poly (N-acetyllactosamine)-type glycan

Kamada¹,

Arita²,

Ogata³

et al. 1987

Eur J Biochem

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Receptors for fucose-binding proteins of Lotus tetragonolobus were isolated from N4-1 and F9 embryonal carcinoma cells. They were glycoproteins, whose major components had apparent relative molecular masses of more than 100000. Carbohydrates released from the receptors of N4-1 cells by hydrazinolysis were separated into three fractions by gel filtration. Binding activity to the lectin was detected in the high-molecular-mass fraction. The composition of the large glycan was characteristic of the poly(N-acetyl1actosamine)-type, and glucosamine was identified as the sugar involved in the protein-carbohydrate linkage. The glycan has one fucosyl residue per four N-acetyllactosamine units. Most of the fucose was linked to the C-3 hydroxyl group of N-acetylglucosamine. No Fucal-+2Gal or Fucal+4GlcNAc linkage was detected. The glycan had a relative molecular mass of 9000 or more and the poly(N-acetyllactosamine) units were branched. N-Acetylgalactosamine residues were detected in non-reducing ends of at least a part of the glycan. Therefore, the glycan has a more complex structure than the related one from human granulocytes, although both of them have F u c a l~3 G l c N A c termini.Cell-surface carbohydrates undergo marked alterations during differentiation and development [l - MATERIALS AND METHODS MaterialsFucose-binding proteins of Lotus tetragonolobus were prepared as described by Ogata et al. [18]; the components that had the ability to bind to mucin-agarose were used. FBP (105 mg) were coupled to 10 ml of Affi-gel 10 (Bio-Rad) in 0.1 M Mops buffer (pH 7.5) containing 80 mM CaC12 at 4°C for 4 h. Residual active sites of the beads were blocked by incubating with 0.1 M ethanolamine (pH 7.5) for 1 h. N4-1 [25] are embryonal carcinoma cell lines derived from teratocarcinoma OTT6050 and STT-2, respectively. The cells were labeled by culturing with radioactive sugars for 24 h as described previously [7]. The labeled cells were harvested in Dulbecco's phosphate-buffered saline by pipetting and extracted for 30 min at 4°C with 1% Triton X-100 in 0.01 M Tris/HCl buffer (pH 7.6) containing 0.15 M NaCl, 3 mM MgCI2 and 1 mM phenylmethylsulfonyl fluoride. The extracts were applied to a column containing

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Cell surface carbohydrates of embryonal carcinoma cells: Polysaccharidic side chains of F9 antigens and of receptors to two lectins, FBP and PNA

Cited by 204 publications

References 25 publications

Carbohydrates and fertilization in animals

Carbohydrates and fertilization in animals

Carbohydrates as antigenic determinants of glycoproteins

Receptors for fucose-binding proteins of Lotus tetragonolobus isolated from mouse embryonal carcinoma cells. Structural characteristics of the poly (N-acetyllactosamine)-type glycan

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