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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Publicado:	1994
Materias:	(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 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
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
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_01674889_v1220_n3_p299_Brandelli
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spelling	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

Participation of glycosylated residues in the human sperm acrosome reaction: Possible role of N-acetylglucosaminidase

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