Primary structures and Lewis blood-group-dependent expression of major sialylated saccharides from mucus glycoproteins of human seminal plasma

Hanisch, Franz‐Georg; Egge, Heinz; Peter‐Katalinić, Jasna; Uhlenbruck, G.; Dienst, C.; Fangmann, Ruth

doi:10.1111/j.1432-1033.1985.tb09204.x

Cited by 32 publications

(12 citation statements)

References 19 publications

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“…However, it is significant that Lewis y is known to occur on normal glycoproteins in seminal plasma. Thus, O-linked oligosaccharides expressing the Lewis y sequence have been derived from mucinlike proteins in this secretion (34,35). Furthermore, ␥-seminoprotein isolated from seminal plasma carries the Lewis y epitope on its N-linked glycans (36).…”

Section: Discussionmentioning

confidence: 99%

Gender-specific Glycosylation of Human Glycodelin Affects Its Contraceptive Activity

Morris

Dell

Easton

et al. 1996

Journal of Biological Chemistry

142

136

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We have recently demonstrated that a human amniotic fluid-derived glycoprotein, glycodelin-A (GdA; previously known as PP14 or PAEP), potently inhibits gamete binding in an established sperm-egg binding system and expresses immunosuppressive activities directed against a variety of different immune cell types. GdA has high mannose-, hybrid-, and complex-type biantennary oligosaccharides including structures with fucosylated or sialylated N,N-diacetyllactosediamine (GalNAc␤1-4GlcNAc) sequences, which are rare in other human glycoproteins. We now report the characterization of glycodelin-S (GdS). This is a human seminal plasma glycoprotein that is immunologically indistinguishable from GdA, but unlike the latter, does not inhibit human sperm-zona pellucida binding under hemizona assay conditions. Analysis of the N-glycans of GdS by mass spectrometry revealed that all glycoforms of GdS are different from those of GdA. GdS glycans are unusually fucose-rich, and the major complex-type structures are biantennary glycans with Lewis x (Gal␤1-4(Fuc␣1-3)GlcNAc) and Lewis y (Fuc␣1-2Gal␤1-4 (Fuc␣1-3)GlcNAc) antennae. It is probable that these highly fucosylated epitopes contribute to the immunosuppressive activity of human seminal plasma and to the low immunogenicity of sperm. This study provides the first evidence for gender-specific glycosylation that may serve to regulate key processes involved in human reproduction.

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Section: Discussionmentioning

confidence: 99%

Gender-specific Glycosylation of Human Glycodelin Affects Its Contraceptive Activity

Morris

Dell

Easton

et al. 1996

Journal of Biological Chemistry

142

136

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“…NeuAca NeuAca among the 0-linked chains of glycophorin A from Cad antigen-positive erythrocytes (Blanchard et al, 1983), and the identification of chondroitin sulphate-related sequences as antigens of nerve adhesion molecules (Chou et al, 1985;Kruse et al, 1985) and as target antigens of autoantibodies associated with polyneuropathy (Kabat et al, 1984 (Hanisch et al, 1985). Although all glycoprotein oligosaccharide sequences are potential antigens, the antigenic determinants characterized thus far largely involve the backbone and peripheral domains common to 0-and N-linked chains and the core regions of O-linked chains (Rahman & Longenecker, 1982;Steuden et al, 1985;Hirohashi et al, 1985).…”

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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“…Besides, this type of linkage has been found in respiratory mucus glycoproteins of a patient suffering from bronchiectasis [39], in 0-glycans of mucus glycoproteins from human seminal plasma [40], rat and human colonic mucins [41,42], human meconium [43,44], as well as in mucus glycoproteins and oligosaccharides from human milk [45 -541. However, this structure determinant is rarely found in Nglycans of healthy tissues.…”

Section: Discussionmentioning

confidence: 99%

Occurrence of α1‐2‐fucosylation in membrane glycoproteins of Morris hepatoma 7777 but not in liver

Nuck

Orthen

Reutter

1992

European Journal of Biochemistry

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A comparative study was undertaken to characterize the linkages of L-fucose in N-glycans of plasma membrane glycoproteins from Morris hepatoma 7777, host liver and kidney cortex, as well as from rat serum.After in-vivo radiolabelling of rats with ~-[6-~H]fucose, the asparagine-linked carbohydrate chains were released from delipidated plasma membrane glycoproteins, as well as from serum glycoproteins, by enzymic digestion with peptide-N4-(N-acetyl-~-glucosaminyl)asparagine amidase from Flavobacterium meningosepticum. They were then converted to their corresponding oligosaccharide alditols by reduction with sodium borohydride.Two specific a-L-fucosidases from almond emulsin and from Aspergillus niger, combined with affinity HPLC on immobilized Aleuria aurantia lectin were used to study the linkage of L-fucose in the oligosaccharide chains.Fucose a1-2 linked to galactose, was present only in the plasma membrane of hepatoma 7777 (18% of total ~-[~H]fucose in N-glycans), but was not expressed in host liver, kidney cortex and serum. None of the investigated sources contained an appreciable amount of fucose al-3/4 linked to N-acetyl-D-glucosamine. All the radioactively labelled oligosaccharides from host liver, kidney cortex and serum, but only 82% of these oligosaccharides from hepatoma, contained a-fucosyl residues linked at the C6 position of the proximal N-acetyl-D-glucosamine.Several differences have been found in the structure of sugar chains of glycoconjugates produced in normal and malignant cells [l -31. One of the most frequently found phenomena in malignant cells is an increased degree of branching and quite often, due to repeating units, an elongation of the outer chains of N-linked oligosaccharides in glycoproteins, paralleled by an increased activity of p-N-acetylglucosaminyltransferase V [4]. A bisecting N-acetyl-D-glucosamine residue, pl-4 linked to the mannosyl-chitobiose core, is also possibly the result of an altered, tumour-associated glycosylation [S].Furthermore, malignant transformation has been reported to be accompanied by alterations in the content and linkage of the terminal sugar residues, L-fucose and sialic acid [2, 6, 71, which play an important role in blood-group antigens [8].

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Primary structures and Lewis blood-group-dependent expression of major sialylated saccharides from mucus glycoproteins of human seminal plasma

Cited by 32 publications

References 19 publications

Gender-specific Glycosylation of Human Glycodelin Affects Its Contraceptive Activity

Gender-specific Glycosylation of Human Glycodelin Affects Its Contraceptive Activity

Carbohydrates as antigenic determinants of glycoproteins

Occurrence of α1‐2‐fucosylation in membrane glycoproteins of Morris hepatoma 7777 but not in liver

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