Fucosylated glycoconjugates of the human spermatozoon. Comparison of the domains of these glycoconjugates with the α-fucosyl binding sites, and with lactosaminic glycoconjugates and β-D-galactosyl binding site domains
Fucosylated glycoconjugates play an important role in fertilization as the recognition signal of the zona pellucida. In this work, using "critical" concentrations of either, FITC Lotus tetragonolobus lectin or FITC α-L-fucosyl-BSA neoglycoprotein as molecular probes, population densities o...
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todo:paper_03279545_v20_n1_p11_DeCerezo2023-10-03T15:25:06Z Fucosylated glycoconjugates of the human spermatozoon. Comparison of the domains of these glycoconjugates with the α-fucosyl binding sites, and with lactosaminic glycoconjugates and β-D-galactosyl binding site domains De Cerezo, J.M.S. Marquínez, A.C. Sarchi, M.I. Cerezo, A.S. Fucose Glycoconjugates Human spermatozoon aminosugar fluorescein isothiocyanate follitropin fucose galactose glycoconjugate lactosamine lectin luteinizing hormone article binding site chemistry comparative study human male metabolism physiology protein tertiary structure spermatozoon ultrastructure Amino Sugars Binding Sites Fluorescein-5-isothiocyanate Follicle Stimulating Hormone Fucose Galactose Glycoconjugates Humans Lectins Luteinizing Hormone Male Protein Structure, Tertiary Spermatozoa Fucosylated glycoconjugates play an important role in fertilization as the recognition signal of the zona pellucida. In this work, using "critical" concentrations of either, FITC Lotus tetragonolobus lectin or FITC α-L-fucosyl-BSA neoglycoprotein as molecular probes, population densities of fucosylated glycoconjugates and of their "complementary" molecules (carrying fucosyl receptors), were found all over the sperm surface with higher population densities in post acrosomal sheath, neck and midpiece. These results were compared with previously reported data on the population densities of lactosaminic compounds and their "complementary" molecules, obtained on same samples of spermatozoa. Statistical data demonstrate that fucosylated glycoconjugates share the same domains with biantennary N-acetyllactosaminic oligosaccharides carrying outer galactose and bisected N-acetylglucosamine residues. These domains highly differ with those of the lactosaminic glycoproteins carrying tri and tetraantennary N-acetyllactosaminic oligosaccharides. These studies also show that the domains of fucosylated glycoconjugates and their "complementary" molecules (carrying fucosyl receptors) locate in different zones of the spermatozoon than those of the compounds carrying β-galactosyl receptors. Besides, the results suggest structural differences between fucosylated glycoconjugates of the acrosome, equatorial zone and post acrosomal sheath. This may be relevant to the different biological behavior of these compounds and zones, in fertilization. Fil:Marquínez, A.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Sarchi, M.I. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Cerezo, A.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03279545_v20_n1_p11_DeCerezo |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Fucose Glycoconjugates Human spermatozoon aminosugar fluorescein isothiocyanate follitropin fucose galactose glycoconjugate lactosamine lectin luteinizing hormone article binding site chemistry comparative study human male metabolism physiology protein tertiary structure spermatozoon ultrastructure Amino Sugars Binding Sites Fluorescein-5-isothiocyanate Follicle Stimulating Hormone Fucose Galactose Glycoconjugates Humans Lectins Luteinizing Hormone Male Protein Structure, Tertiary Spermatozoa |
| spellingShingle |
Fucose Glycoconjugates Human spermatozoon aminosugar fluorescein isothiocyanate follitropin fucose galactose glycoconjugate lactosamine lectin luteinizing hormone article binding site chemistry comparative study human male metabolism physiology protein tertiary structure spermatozoon ultrastructure Amino Sugars Binding Sites Fluorescein-5-isothiocyanate Follicle Stimulating Hormone Fucose Galactose Glycoconjugates Humans Lectins Luteinizing Hormone Male Protein Structure, Tertiary Spermatozoa De Cerezo, J.M.S. Marquínez, A.C. Sarchi, M.I. Cerezo, A.S. Fucosylated glycoconjugates of the human spermatozoon. Comparison of the domains of these glycoconjugates with the α-fucosyl binding sites, and with lactosaminic glycoconjugates and β-D-galactosyl binding site domains |
| topic_facet |
Fucose Glycoconjugates Human spermatozoon aminosugar fluorescein isothiocyanate follitropin fucose galactose glycoconjugate lactosamine lectin luteinizing hormone article binding site chemistry comparative study human male metabolism physiology protein tertiary structure spermatozoon ultrastructure Amino Sugars Binding Sites Fluorescein-5-isothiocyanate Follicle Stimulating Hormone Fucose Galactose Glycoconjugates Humans Lectins Luteinizing Hormone Male Protein Structure, Tertiary Spermatozoa |
| description |
Fucosylated glycoconjugates play an important role in fertilization as the recognition signal of the zona pellucida. In this work, using "critical" concentrations of either, FITC Lotus tetragonolobus lectin or FITC α-L-fucosyl-BSA neoglycoprotein as molecular probes, population densities of fucosylated glycoconjugates and of their "complementary" molecules (carrying fucosyl receptors), were found all over the sperm surface with higher population densities in post acrosomal sheath, neck and midpiece. These results were compared with previously reported data on the population densities of lactosaminic compounds and their "complementary" molecules, obtained on same samples of spermatozoa. Statistical data demonstrate that fucosylated glycoconjugates share the same domains with biantennary N-acetyllactosaminic oligosaccharides carrying outer galactose and bisected N-acetylglucosamine residues. These domains highly differ with those of the lactosaminic glycoproteins carrying tri and tetraantennary N-acetyllactosaminic oligosaccharides. These studies also show that the domains of fucosylated glycoconjugates and their "complementary" molecules (carrying fucosyl receptors) locate in different zones of the spermatozoon than those of the compounds carrying β-galactosyl receptors. Besides, the results suggest structural differences between fucosylated glycoconjugates of the acrosome, equatorial zone and post acrosomal sheath. This may be relevant to the different biological behavior of these compounds and zones, in fertilization. |
| format |
JOUR |
| author |
De Cerezo, J.M.S. Marquínez, A.C. Sarchi, M.I. Cerezo, A.S. |
| author_facet |
De Cerezo, J.M.S. Marquínez, A.C. Sarchi, M.I. Cerezo, A.S. |
| author_sort |
De Cerezo, J.M.S. |
| title |
Fucosylated glycoconjugates of the human spermatozoon. Comparison of the domains of these glycoconjugates with the α-fucosyl binding sites, and with lactosaminic glycoconjugates and β-D-galactosyl binding site domains |
| title_short |
Fucosylated glycoconjugates of the human spermatozoon. Comparison of the domains of these glycoconjugates with the α-fucosyl binding sites, and with lactosaminic glycoconjugates and β-D-galactosyl binding site domains |
| title_full |
Fucosylated glycoconjugates of the human spermatozoon. Comparison of the domains of these glycoconjugates with the α-fucosyl binding sites, and with lactosaminic glycoconjugates and β-D-galactosyl binding site domains |
| title_fullStr |
Fucosylated glycoconjugates of the human spermatozoon. Comparison of the domains of these glycoconjugates with the α-fucosyl binding sites, and with lactosaminic glycoconjugates and β-D-galactosyl binding site domains |
| title_full_unstemmed |
Fucosylated glycoconjugates of the human spermatozoon. Comparison of the domains of these glycoconjugates with the α-fucosyl binding sites, and with lactosaminic glycoconjugates and β-D-galactosyl binding site domains |
| title_sort |
fucosylated glycoconjugates of the human spermatozoon. comparison of the domains of these glycoconjugates with the α-fucosyl binding sites, and with lactosaminic glycoconjugates and β-d-galactosyl binding site domains |
| url |
http://hdl.handle.net/20.500.12110/paper_03279545_v20_n1_p11_DeCerezo |
| work_keys_str_mv |
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