Participation of glycosylated residues in the human sperm acrosome reaction: Possible role of N-acetylglucosaminidase
Sperm binding to the egg zona pellucida is mediated by complementary protein-carbohydrate interaction. This binding results in the exocytosis of the sperm acrosome, or acrosome reaction (AR). We report the effect of different neoglycoproteins (sugar residues covalently bound to bovine serum albumin)...
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1994
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01674889_v1220_n3_p299_Brandelli http://hdl.handle.net/20.500.12110/paper_01674889_v1220_n3_p299_Brandelli |
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paper:paper_01674889_v1220_n3_p299_Brandelli2023-06-08T15:16:26Z Participation of glycosylated residues in the human sperm acrosome reaction: Possible role of N-acetylglucosaminidase (Human) Acrosome Acrosome reaction Exocytosis N-Acetylglucosaminidase Spermatozoon acetylglucosaminidase glycosylated protein mannose acrosome article binding site controlled study exocytosis human human cell male priority journal spermatozoon Acetylglucosaminidase Acrosome Egtazic Acid Female Glycoproteins Glycosylation Human Male Serum Albumin, Bovine Sperm Capacitation Sperm-Ovum Interactions Structure-Activity Relationship Support, Non-U.S. Gov't Zona Pellucida Bovinae Sperm binding to the egg zona pellucida is mediated by complementary protein-carbohydrate interaction. This binding results in the exocytosis of the sperm acrosome, or acrosome reaction (AR). We report the effect of different neoglycoproteins (sugar residues covalently bound to bovine serum albumin) on the human sperm AR. p-Aminophenyl-N-acetyl-β-d-glucosaminide-BSA (BSA-GlcNAc) and p-aminophenyl-α-d-mannopyranoside-BSA (BSA-Man) at 1 μg/ml were capable of inducing the greatest percentages of AR (3-fold stimulation with respect to controls), while other NeoGPs had only a weak effect on this process. The BSA-GlcNAc-induced acrosome reaction was inhibited by N-acetylglucosamine (GlcNAc), p-nitrophenyl-GlcNAc, and purified soluble β-N-acetylglucosaminidase (βNAG). The induction of the AR with BSA-Man could be inhibited by mannose, while soluble α-mannosidase was only partially effective. These data suggest that binding sites for GlcNAc and mannose may be involved in the induction of the AR in human sperm. The characteristics of the BSA-GlcNAc induction suggest that the βNAG molecule may be the mediator of this effect. © 1994. 1994 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01674889_v1220_n3_p299_Brandelli http://hdl.handle.net/20.500.12110/paper_01674889_v1220_n3_p299_Brandelli |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
(Human) Acrosome Acrosome reaction Exocytosis N-Acetylglucosaminidase Spermatozoon acetylglucosaminidase glycosylated protein mannose acrosome article binding site controlled study exocytosis human human cell male priority journal spermatozoon Acetylglucosaminidase Acrosome Egtazic Acid Female Glycoproteins Glycosylation Human Male Serum Albumin, Bovine Sperm Capacitation Sperm-Ovum Interactions Structure-Activity Relationship Support, Non-U.S. Gov't Zona Pellucida Bovinae |
spellingShingle |
(Human) Acrosome Acrosome reaction Exocytosis N-Acetylglucosaminidase Spermatozoon acetylglucosaminidase glycosylated protein mannose acrosome article binding site controlled study exocytosis human human cell male priority journal spermatozoon Acetylglucosaminidase Acrosome Egtazic Acid Female Glycoproteins Glycosylation Human Male Serum Albumin, Bovine Sperm Capacitation Sperm-Ovum Interactions Structure-Activity Relationship Support, Non-U.S. Gov't Zona Pellucida Bovinae Participation of glycosylated residues in the human sperm acrosome reaction: Possible role of N-acetylglucosaminidase |
topic_facet |
(Human) Acrosome Acrosome reaction Exocytosis N-Acetylglucosaminidase Spermatozoon acetylglucosaminidase glycosylated protein mannose acrosome article binding site controlled study exocytosis human human cell male priority journal spermatozoon Acetylglucosaminidase Acrosome Egtazic Acid Female Glycoproteins Glycosylation Human Male Serum Albumin, Bovine Sperm Capacitation Sperm-Ovum Interactions Structure-Activity Relationship Support, Non-U.S. Gov't Zona Pellucida Bovinae |
description |
Sperm binding to the egg zona pellucida is mediated by complementary protein-carbohydrate interaction. This binding results in the exocytosis of the sperm acrosome, or acrosome reaction (AR). We report the effect of different neoglycoproteins (sugar residues covalently bound to bovine serum albumin) on the human sperm AR. p-Aminophenyl-N-acetyl-β-d-glucosaminide-BSA (BSA-GlcNAc) and p-aminophenyl-α-d-mannopyranoside-BSA (BSA-Man) at 1 μg/ml were capable of inducing the greatest percentages of AR (3-fold stimulation with respect to controls), while other NeoGPs had only a weak effect on this process. The BSA-GlcNAc-induced acrosome reaction was inhibited by N-acetylglucosamine (GlcNAc), p-nitrophenyl-GlcNAc, and purified soluble β-N-acetylglucosaminidase (βNAG). The induction of the AR with BSA-Man could be inhibited by mannose, while soluble α-mannosidase was only partially effective. These data suggest that binding sites for GlcNAc and mannose may be involved in the induction of the AR in human sperm. The characteristics of the BSA-GlcNAc induction suggest that the βNAG molecule may be the mediator of this effect. © 1994. |
title |
Participation of glycosylated residues in the human sperm acrosome reaction: Possible role of N-acetylglucosaminidase |
title_short |
Participation of glycosylated residues in the human sperm acrosome reaction: Possible role of N-acetylglucosaminidase |
title_full |
Participation of glycosylated residues in the human sperm acrosome reaction: Possible role of N-acetylglucosaminidase |
title_fullStr |
Participation of glycosylated residues in the human sperm acrosome reaction: Possible role of N-acetylglucosaminidase |
title_full_unstemmed |
Participation of glycosylated residues in the human sperm acrosome reaction: Possible role of N-acetylglucosaminidase |
title_sort |
participation of glycosylated residues in the human sperm acrosome reaction: possible role of n-acetylglucosaminidase |
publishDate |
1994 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01674889_v1220_n3_p299_Brandelli http://hdl.handle.net/20.500.12110/paper_01674889_v1220_n3_p299_Brandelli |
_version_ |
1768542687792726016 |