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Cells
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Molecular Physiology of Human Sperm Cells
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Molecular Physiology of Human Sperm Cells

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Stem Cells".

Deadline for manuscript submissions: closed (10 April 2022) | Viewed by 18384

Special Issue Editors

Prof. Dr. Robert John Aitken

E-Mail Website
Guest Editor
School of Environmental and Life Sciences, College of Engineering, Science and Environmental Science, University of Newcastle, Callaghan, NSW 2308, Australia
Interests: oxidative stress; antioxidants; reproductive biology; fertilization; demography
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Brett Nixon

E-Mail Website
Guest Editor
1. School of Environmental and Life Sciences, Faculty of Science and Priority Research Centre in Reproductive Science, University of Newcastle, Callaghan, NSW 2308, Australia
2. Hunter Medical Research Institute, New Lambton Heights, NSW 2305, Australia
Interests: sperm physiology; evolution; sperm-egg recognition; epididymal maturation

Special Issue Information

Dear Colleagues,

The purpose of this issue is to summarize our current understanding of the molecular basis of normal sperm function, the way in which these mechanisms become perturbed in cases of male infertility and the development of effective methods to detect and treat this distressingly common condition. The detailed scope of this issue will encompass the molecular modelling of spermatozoa during epididymal transit in order to generate functionally competent cells, the intricacies of sperm transport to the site of fertilization and the complex cascade of intercellular interactions that lead to the recognition and fusion of male and female gametes and the formation of a developmentally-competent zygote. We will also examine the extent to which defective sperm function is genetically or environmentally induced, including an assessment of the role played by oxidative stress in the genesis of male infertility. Recent developments in the methods employed to detect and treat impaired sperm function will be reviewed with particular focus on the way in which we are using our fundamental knowledge of sperm physiology to fashion new approaches to infertility diagnosis and management. Finally, we will highlight the dramatic impact that sperm quality has on the developmental competence of the embryo and the health and wellbeing of the offspring.

Prof. Robert John Aitken
Prof. Brett Nixon
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Cells is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • sperm physiology
  • male infertility
  • epididymal maturation
  • DNA damage
  • sperm–egg recognition
  • fertilization
  • paternal impacts on development

Published Papers (4 papers)

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Research

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20 pages, 2025 KiB  
Article
Epithelial and Neural Cadherin in Mammalian Fertilization: Studies in the Mouse Model
by Gustavo Luis Verón, María Florencia Veiga, Mónica Cameo, Clara Isabel Marín-Briggiler and Mónica Hebe Vazquez-Levin
Cells 2022, 11(1), 102; https://doi.org/10.3390/cells11010102 - 29 Dec 2021
Cited by 1 | Viewed by 2620
Abstract
Successful mammalian fertilization requires a well-orchestrated sequence of molecular events leading to gamete fusion. Since this interaction involves Ca2+-dependent adhesion events, the participation of the Ca+2-dependent cell-cell adhesion proteins Epithelial (E-cad) and Neural (N-cad) cadherin is envisaged. We have [...] Read more.
Successful mammalian fertilization requires a well-orchestrated sequence of molecular events leading to gamete fusion. Since this interaction involves Ca2+-dependent adhesion events, the participation of the Ca+2-dependent cell-cell adhesion proteins Epithelial (E-cad) and Neural (N-cad) cadherin is envisaged. We have previously reported the expression of E-cad and N-cad in human gametes and showed evidence of their involvement in sperm-oocyte adhesion events leading to fertilization. To overcome ethical limitations associated with the use of human gametes in fertilization-related studies, the mouse has been selected worldwide as the experimental model for over 4 decades. Herein, we report a detailed study aimed at characterizing the expression of E-cad and N-cad in murine gametes and their involvement in murine fertilization using specific antibodies and blocking peptides towards both adhesion proteins. E-cad and N-cad protein forms, as well as other members of the adhesion complex, specifically β-catenin and actin, were identified in spermatozoa, cumulus cells and oocytes protein extracts by means of Western immunoblotting. In addition, subcellular localization of these proteins was determined in whole cells using optical fluorescent microscopy. Gamete pre-incubation with anti-E-cad (ECCD-1) or N-cad (H-63) antibodies resulted in decreased (p < 0.05) In Vitro Fertilization (IVF) rates, when using both cumulus-oocytes complexes and cumulus-free oocytes. Moreover, IVF assays done with denuded oocytes and either antibodies or blocking peptides against E-cad and N-cad led to lower (p < 0.05) fertilization rates. When assessing each step, penetration of the cumulus mass was lower (p < 0.05) when spermatozoa were pre-incubated with ECCD-1 or blocking peptides towards E-cad or towards both E- and N-cad. Moreover, sperm-oolemma binding was impaired (p < 0.0005) after sperm pre-incubation with E-cad antibody or blocking peptide towards E-cad, N-cad or both proteins. Finally, sperm-oocyte fusion was lower (p < 0.05) after sperm pre-incubation with either antibody or blocking peptide against E-cad or N-cad. Our studies demonstrate the expression of members of the adherent complex in the murine model, and the use of antibodies and specific peptides revealed E-cad and N-cad participation in mammalian fertilization. Full article
(This article belongs to the Special Issue Molecular Physiology of Human Sperm Cells)
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6 pages, 1064 KiB  
Communication
Arylsulfatase A Remodeling during Human Sperm In Vitro Capacitation Using Field Emission Scanning Electron Microscopy (FE-SEM)
by María José Gómez-Torres, Natalia Huerta-Retamal, Laura Robles-Gómez, Paula Sáez-Espinosa, Jon Aizpurua, Manuel Avilés and Alejandro Romero
Cells 2021, 10(2), 222; https://doi.org/10.3390/cells10020222 - 23 Jan 2021
Cited by 9 | Viewed by 2433
Abstract
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. [...] Read more.
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. Full article
(This article belongs to the Special Issue Molecular Physiology of Human Sperm Cells)
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20 pages, 15120 KiB  
Article
Protamine-2 Deficiency Initiates a Reactive Oxygen Species (ROS)-Mediated Destruction Cascade during Epididymal Sperm Maturation in Mice
by Simon Schneider, Farhad Shakeri, Christian Trötschel, Lena Arévalo, Alexander Kruse, Andreas Buness, Ansgar Poetsch, Klaus Steger and Hubert Schorle
Cells 2020, 9(8), 1789; https://doi.org/10.3390/cells9081789 - 27 Jul 2020
Cited by 20 | Viewed by 3795
Abstract
Protamines are the safeguards of the paternal sperm genome. They replace most of the histones during spermiogenesis, resulting in DNA hypercondensation, thereby protecting its genome from environmental noxa. Impaired protamination has been linked to male infertility in mice and humans in many studies. [...] Read more.
Protamines are the safeguards of the paternal sperm genome. They replace most of the histones during spermiogenesis, resulting in DNA hypercondensation, thereby protecting its genome from environmental noxa. Impaired protamination has been linked to male infertility in mice and humans in many studies. Apart from impaired DNA integrity, protamine-deficient human and murine sperm show multiple secondary effects, including decreased motility and aberrant head morphology. In this study, we use a Protamine-2 (Prm2)-deficient mouse model in combination with label-free quantitative proteomics to decipher the underlying molecular processes of these effects. We show that loss of the sperm’s antioxidant capacity, indicated by downregulation of key proteins like Superoxide dismutase type 1 (SOD1) and Peroxiredoxin 5 (PRDX5), ultimately initiates an oxidative stress-mediated destruction cascade during epididymal sperm maturation. This is confirmed by an increased level of 8-OHdG in epididymal sperm, a biomarker for oxidative stress-mediated DNA damage. Prm2-deficient testicular sperm are not affected and initiate the proper development of blastocyst stage preimplantation embryos in vitro upon intracytoplasmic sperm injection (ICSI) into oocytes. Our results provide new insight into the role of Prm2 and its downstream molecular effects on sperm function and present an important contribution to the investigation of new treatment regimens for infertile men with impaired protamination. Full article
(This article belongs to the Special Issue Molecular Physiology of Human Sperm Cells)
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Review

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36 pages, 1005 KiB  
Review
Ligands and Receptors Involved in the Sperm-Zona Pellucida Interactions in Mammals
by Lucie Tumova, Michal Zigo, Peter Sutovsky, Marketa Sedmikova and Pavla Postlerova
Cells 2021, 10(1), 133; https://doi.org/10.3390/cells10010133 - 12 Jan 2021
Cited by 27 | Viewed by 8638
Abstract
Sperm-zona pellucida (ZP) interaction, involving the binding of sperm surface ligands to complementary carbohydrates of ZP, is the first direct gamete contact event crucial for subsequent gamete fusion and successful fertilization in mammals. It is a complex process mediated by the coordinated engagement [...] Read more.
Sperm-zona pellucida (ZP) interaction, involving the binding of sperm surface ligands to complementary carbohydrates of ZP, is the first direct gamete contact event crucial for subsequent gamete fusion and successful fertilization in mammals. It is a complex process mediated by the coordinated engagement of multiple ZP receptors forming high-molecular-weight (HMW) protein complexes at the acrosomal region of the sperm surface. The present article aims to review the current understanding of sperm-ZP binding in the four most studied mammalian models, i.e., murine, porcine, bovine, and human, and summarizes the candidate ZP receptors with established ZP affinity, including their origins and the mechanisms of ZP binding. Further, it compares and contrasts the ZP structure and carbohydrate composition in the aforementioned model organisms. The comprehensive understanding of sperm-ZP interaction mechanisms is critical for the diagnosis of infertility and thus becomes an integral part of assisted reproductive therapies/technologies. Full article
(This article belongs to the Special Issue Molecular Physiology of Human Sperm Cells)
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