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Abstract:

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.

Registro:

Documento: Artículo
Título:Participation of glycosylated residues in the human sperm acrosome reaction: Possible role of N-acetylglucosaminidase
Autor:Brandelli, A.; Miranda, P.V.; Tezon, J.G.
Filiación:Instituto de Biologia y Medicina Experimental (IBYME), Obligado 2490, 1428 Buenos Aires, Argentina
Palabras clave:(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
Año:1994
Volumen:1220
Número:3
Página de inicio:299
Página de fin:304
DOI: http://dx.doi.org/10.1016/0167-4889(94)90152-X
Título revista:BBA - Molecular Cell Research
Título revista abreviado:Biochim. Biophys. Acta Mol. Cell Res.
ISSN:01674889
CODEN:BAMRD
CAS:Acetylglucosaminidase, EC 3.2.1.30; Egtazic Acid, 67-42-5; Glycoproteins; Serum Albumin, Bovine
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01674889_v1220_n3_p299_Brandelli

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Citas:

---------- APA ----------
Brandelli, A., Miranda, P.V. & Tezon, J.G. (1994) . Participation of glycosylated residues in the human sperm acrosome reaction: Possible role of N-acetylglucosaminidase. BBA - Molecular Cell Research, 1220(3), 299-304.
http://dx.doi.org/10.1016/0167-4889(94)90152-X
---------- CHICAGO ----------
Brandelli, A., Miranda, P.V., Tezon, J.G. "Participation of glycosylated residues in the human sperm acrosome reaction: Possible role of N-acetylglucosaminidase" . BBA - Molecular Cell Research 1220, no. 3 (1994) : 299-304.
http://dx.doi.org/10.1016/0167-4889(94)90152-X
---------- MLA ----------
Brandelli, A., Miranda, P.V., Tezon, J.G. "Participation of glycosylated residues in the human sperm acrosome reaction: Possible role of N-acetylglucosaminidase" . BBA - Molecular Cell Research, vol. 1220, no. 3, 1994, pp. 299-304.
http://dx.doi.org/10.1016/0167-4889(94)90152-X
---------- VANCOUVER ----------
Brandelli, A., Miranda, P.V., Tezon, J.G. Participation of glycosylated residues in the human sperm acrosome reaction: Possible role of N-acetylglucosaminidase. Biochim. Biophys. Acta Mol. Cell Res. 1994;1220(3):299-304.
http://dx.doi.org/10.1016/0167-4889(94)90152-X