Evidence for the participation of β-hexosaminidase in human sperm-zona pellucida interaction in vitro

Mammalian sperm-zona pellucida (ZP) interaction is mediated by sperm lectin-like proteins and ZP glycoproteins. We have previously reported the participation of binding sites for N-acetylglucosamine (GIcNAc) residues in human sperm function, including sperm interaction with the ZP. Additionally, pre...

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Autores principales: Miranda, P.V., González-Echeverría, F., Blaquier, J.A., Mahuran, D.J., Tezón, J.G.
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_13609947_v6_n8_p699_Miranda
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spelling todo:paper_13609947_v6_n8_p699_Miranda2023-10-03T16:10:52Z Evidence for the participation of β-hexosaminidase in human sperm-zona pellucida interaction in vitro Miranda, P.V. González-Echeverría, F. Blaquier, J.A. Mahuran, D.J. Tezón, J.G. Fertilization Sperm-zona binding Spermatozoa Zona pellucida β-Hexosaminidase beta n acetylhexosaminidase glycoprotein glycosidase article binding affinity binding site CHO cell electrophoresis enzyme activation fertilization in vitro human human cell male mammal nonhuman priority journal protein binding semen analysis signal transduction Western blotting zona pellucida Mammalia Mammalian sperm-zona pellucida (ZP) interaction is mediated by sperm lectin-like proteins and ZP glycoproteins. We have previously reported the participation of binding sites for N-acetylglucosamine (GIcNAc) residues in human sperm function, including sperm interaction with the ZP. Additionally, previous results from our laboratory suggested that some of these events may be mediated by the glycosidase N-acetylglucosaminidase (β-hexosaminidase, Hex, in mammals). In this study, we report the possible participation of Hex in human sperm-ZP interaction. Human recombinant Hex (hrHex) was obtained by expression in a stable transfected CHO cell line. When the recombinant enzyme was present during hemizona (HZ) assays, the number of sperm bound per HZ was significantly reduced. The same result was obtained when HZ were preincubated with hrHex. Additionally, the presence of a Hex-specific substrate during the HZ assay produced the same inhibitory effect. These results suggest the participation of a sperm Hex in the interaction with human ZP in vitro. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_13609947_v6_n8_p699_Miranda
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Fertilization
Sperm-zona binding
Spermatozoa
Zona pellucida
β-Hexosaminidase
beta n acetylhexosaminidase
glycoprotein
glycosidase
article
binding affinity
binding site
CHO cell
electrophoresis
enzyme activation
fertilization in vitro
human
human cell
male
mammal
nonhuman
priority journal
protein binding
semen analysis
signal transduction
Western blotting
zona pellucida
Mammalia
spellingShingle Fertilization
Sperm-zona binding
Spermatozoa
Zona pellucida
β-Hexosaminidase
beta n acetylhexosaminidase
glycoprotein
glycosidase
article
binding affinity
binding site
CHO cell
electrophoresis
enzyme activation
fertilization in vitro
human
human cell
male
mammal
nonhuman
priority journal
protein binding
semen analysis
signal transduction
Western blotting
zona pellucida
Mammalia
Miranda, P.V.
González-Echeverría, F.
Blaquier, J.A.
Mahuran, D.J.
Tezón, J.G.
Evidence for the participation of β-hexosaminidase in human sperm-zona pellucida interaction in vitro
topic_facet Fertilization
Sperm-zona binding
Spermatozoa
Zona pellucida
β-Hexosaminidase
beta n acetylhexosaminidase
glycoprotein
glycosidase
article
binding affinity
binding site
CHO cell
electrophoresis
enzyme activation
fertilization in vitro
human
human cell
male
mammal
nonhuman
priority journal
protein binding
semen analysis
signal transduction
Western blotting
zona pellucida
Mammalia
description Mammalian sperm-zona pellucida (ZP) interaction is mediated by sperm lectin-like proteins and ZP glycoproteins. We have previously reported the participation of binding sites for N-acetylglucosamine (GIcNAc) residues in human sperm function, including sperm interaction with the ZP. Additionally, previous results from our laboratory suggested that some of these events may be mediated by the glycosidase N-acetylglucosaminidase (β-hexosaminidase, Hex, in mammals). In this study, we report the possible participation of Hex in human sperm-ZP interaction. Human recombinant Hex (hrHex) was obtained by expression in a stable transfected CHO cell line. When the recombinant enzyme was present during hemizona (HZ) assays, the number of sperm bound per HZ was significantly reduced. The same result was obtained when HZ were preincubated with hrHex. Additionally, the presence of a Hex-specific substrate during the HZ assay produced the same inhibitory effect. These results suggest the participation of a sperm Hex in the interaction with human ZP in vitro.
format JOUR
author Miranda, P.V.
González-Echeverría, F.
Blaquier, J.A.
Mahuran, D.J.
Tezón, J.G.
author_facet Miranda, P.V.
González-Echeverría, F.
Blaquier, J.A.
Mahuran, D.J.
Tezón, J.G.
author_sort Miranda, P.V.
title Evidence for the participation of β-hexosaminidase in human sperm-zona pellucida interaction in vitro
title_short Evidence for the participation of β-hexosaminidase in human sperm-zona pellucida interaction in vitro
title_full Evidence for the participation of β-hexosaminidase in human sperm-zona pellucida interaction in vitro
title_fullStr Evidence for the participation of β-hexosaminidase in human sperm-zona pellucida interaction in vitro
title_full_unstemmed Evidence for the participation of β-hexosaminidase in human sperm-zona pellucida interaction in vitro
title_sort evidence for the participation of β-hexosaminidase in human sperm-zona pellucida interaction in vitro
url http://hdl.handle.net/20.500.12110/paper_13609947_v6_n8_p699_Miranda
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AT blaquierja evidencefortheparticipationofbhexosaminidaseinhumanspermzonapellucidainteractioninvitro
AT mahurandj evidencefortheparticipationofbhexosaminidaseinhumanspermzonapellucidainteractioninvitro
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