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Arylsulfatase A Remodeling during Human Sperm In Vitro Capacitation Using Field Emission Scanning Electron Microscopy (FE-SEM)

Capacitation drives sperm biophysical and biochemical changes for sperm-oocyte interactions. It is a well-known fact that the molecular complex arylsulfatase A (ARSA), hyaluronidase sperm adhesion molecule 1 (SPAM1), and heat shock protein 2 (HSPA2) plays a significant role in sperm–zona pellucida (...

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Autores principales: Gómez-Torres, María José, Huerta-Retamal, Natalia, Robles-Gómez, Laura, Sáez-Espinosa, Paula, Aizpurua, Jon, Avilés, Manuel, Romero, Alejandro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7912702/
https://www.ncbi.nlm.nih.gov/pubmed/33498624
http://dx.doi.org/10.3390/cells10020222
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author Gómez-Torres, María José
Huerta-Retamal, Natalia
Robles-Gómez, Laura
Sáez-Espinosa, Paula
Aizpurua, Jon
Avilés, Manuel
Romero, Alejandro
author_facet Gómez-Torres, María José
Huerta-Retamal, Natalia
Robles-Gómez, Laura
Sáez-Espinosa, Paula
Aizpurua, Jon
Avilés, Manuel
Romero, Alejandro
author_sort Gómez-Torres, María José
collection PubMed
description Capacitation drives sperm biophysical and biochemical changes for sperm-oocyte interactions. It is a well-known fact that the molecular complex arylsulfatase A (ARSA), hyaluronidase sperm adhesion molecule 1 (SPAM1), and heat shock protein 2 (HSPA2) plays a significant role in sperm–zona pellucida (ZP) binding. However, the time-dependent capacitation effects on the sperm surface ARSA presence and specific topographic distributions remain to be elucidated. Here, we quantified the ARSA density and specific membrane domain locations before (US) and after in vitro capacitation (one and four hours; CS1–CS4) in human sperm using high-resolution field emission scanning electron microscopy (FE-SEM) and immunogold labeling. Our results showed a significant and progressive capacitation-mediated increase of labeled spermatozoa from the US (37%) to CS4 (100%) physiological conditions. In addition, surface mapping revealed a close relationship between the ARSA residues and their acrosomal repositioning. Compared with the ARSA surface heterogeneous distribution found in US, the CS1–4 conditions exhibited clustering on the peri-acrosomal region, showing that time-dependent capacitation also induced a ARSA residue dramatic translocation on sperm surfaces. Our findings provide novel insights into the molecular remodeling events preceding sperm-oocyte interactions.
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spelling pubmed-79127022021-02-28 Arylsulfatase A Remodeling during Human Sperm In Vitro Capacitation Using Field Emission Scanning Electron Microscopy (FE-SEM) Gómez-Torres, María José Huerta-Retamal, Natalia Robles-Gómez, Laura Sáez-Espinosa, Paula Aizpurua, Jon Avilés, Manuel Romero, Alejandro Cells Communication Capacitation drives sperm biophysical and biochemical changes for sperm-oocyte interactions. It is a well-known fact that the molecular complex arylsulfatase A (ARSA), hyaluronidase sperm adhesion molecule 1 (SPAM1), and heat shock protein 2 (HSPA2) plays a significant role in sperm–zona pellucida (ZP) binding. However, the time-dependent capacitation effects on the sperm surface ARSA presence and specific topographic distributions remain to be elucidated. Here, we quantified the ARSA density and specific membrane domain locations before (US) and after in vitro capacitation (one and four hours; CS1–CS4) in human sperm using high-resolution field emission scanning electron microscopy (FE-SEM) and immunogold labeling. Our results showed a significant and progressive capacitation-mediated increase of labeled spermatozoa from the US (37%) to CS4 (100%) physiological conditions. In addition, surface mapping revealed a close relationship between the ARSA residues and their acrosomal repositioning. Compared with the ARSA surface heterogeneous distribution found in US, the CS1–4 conditions exhibited clustering on the peri-acrosomal region, showing that time-dependent capacitation also induced a ARSA residue dramatic translocation on sperm surfaces. Our findings provide novel insights into the molecular remodeling events preceding sperm-oocyte interactions. MDPI 2021-01-23 /pmc/articles/PMC7912702/ /pubmed/33498624 http://dx.doi.org/10.3390/cells10020222 Text en © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Communication
Gómez-Torres, María José
Huerta-Retamal, Natalia
Robles-Gómez, Laura
Sáez-Espinosa, Paula
Aizpurua, Jon
Avilés, Manuel
Romero, Alejandro
Arylsulfatase A Remodeling during Human Sperm In Vitro Capacitation Using Field Emission Scanning Electron Microscopy (FE-SEM)
title Arylsulfatase A Remodeling during Human Sperm In Vitro Capacitation Using Field Emission Scanning Electron Microscopy (FE-SEM)
title_full Arylsulfatase A Remodeling during Human Sperm In Vitro Capacitation Using Field Emission Scanning Electron Microscopy (FE-SEM)
title_fullStr Arylsulfatase A Remodeling during Human Sperm In Vitro Capacitation Using Field Emission Scanning Electron Microscopy (FE-SEM)
title_full_unstemmed Arylsulfatase A Remodeling during Human Sperm In Vitro Capacitation Using Field Emission Scanning Electron Microscopy (FE-SEM)
title_short Arylsulfatase A Remodeling during Human Sperm In Vitro Capacitation Using Field Emission Scanning Electron Microscopy (FE-SEM)
title_sort arylsulfatase a remodeling during human sperm in vitro capacitation using field emission scanning electron microscopy (fe-sem)
topic Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7912702/
https://www.ncbi.nlm.nih.gov/pubmed/33498624
http://dx.doi.org/10.3390/cells10020222
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