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PMID: 31002753 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Proteomic characterization of human sperm plasma membrane-associated proteins and their role in capacitation.

Andrology ·Vol. 8 ·No. 1 ·2020-00-00 ·Pages 171-180

Hernández-Silva G, Fabián López-Araiza JE, López-Torres AS, Larrea F, Torres-Flores V, Chirinos M

Abstract

Plasma membranes of ejaculated sperm are covered by epididymal and accessory glands secreted proteins that must be released from sperm surface during the female reproductive tract passage in order to capacitate and fertilize the oocyte. As human sperm plasma membrane-associated proteins (SMAP) have not yet been investigated, the aim of this study was to characterize the SMAP released during in vitro human capacitation and to study their possible role as decapacitation factors. SMAP were characterized by 2-dimensional electrophoresis and mass spectrometry analysis. Besides, we explored SMAP effects on motility, protein tyrosine phosphorylation, and calcium ionophore-induced acrosome reaction of spermatozoa either incubated for 6 h in capacitating medium ± SMAP or for 5 h in capacitating medium alone followed by incubation for 1 h ± SMAP. Mass spectrometry analysis allowed the identification of 29 proteins, all of which have previously been identified in the human seminal fluid. Spermatozoa incubated for 6 h under capacitating conditions in the presence of the SMAP showed a significant decrease in the incidence of non-progressive motility, hyperactivation, protein tyrosine phosphorylation, and calcium ionophore-induced acrosome reaction. However, spermatozoa incubated for 5 h in capacitating medium and further incubated for 1 h with the SMAP showed a lower percentage of spermatozoa with non-progressive motility and hyperactivated cells but no effects on protein tyrosine phosphorylation were detected. Our results indicate that SMAP inhibit the progress of human sperm capacitation, but only motility changes related to capacitation may be reversed by these proteins. The study of the identified proteins on sperm function and their mechanisms of action on this cell may contribute to the understanding of their role during capacitation.

Keywords
capacitation decapacitation factor male reproductive tract spermatozoa
MeSH Terms
Cell Membrane/metabolism Humans Male Membrane Proteins/metabolism Proteome Sperm Capacitation Spermatozoa/metabolism
Chemicals
Membrane Proteins Proteome
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Hernández-Silva Gabriela
Departamento de Biología de la Reproducción Dr. Carlos Gual Castro, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, Ciudad de México, México. | Posgrado en Ciencias Biológicas, Universidad Nacional Autónoma de México, Ciudad de México, México.
Fabián López-Araiza Jorge Elías
Laboratorio de Biomembranas, Facultad de Medicina, Universidad Nacional Autónoma de México, Ciudad de México, México.
López-Torres Aideé Saray
Departamento de Biología de la Reproducción Dr. Carlos Gual Castro, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, Ciudad de México, México.
Larrea Fernando
Departamento de Biología de la Reproducción Dr. Carlos Gual Castro, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, Ciudad de México, México.
Torres-Flores Víctor
Laboratorio de Biomembranas, Facultad de Medicina, Universidad Nacional Autónoma de México, Ciudad de México, México.
Chirinos Mayel ORCID
Departamento de Biología de la Reproducción Dr. Carlos Gual Castro, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, Ciudad de México, México.
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Article Info
Journal
Andrology
Abbr.
Andrology
ISSN
2047-2927
DOI
10.1111/andr.12627
Published
2020-00-00
Epub
2019-00-19
Pages
171-180
Language
English
Region
England
NLM ID
101585129
Subset
IM
Grants
Consejo Nacional de Ciencia y Tecnología · 154923 · International
External Links
PubMed source DOI: 10.1111/andr.12627 View journal details
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