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


Por: Hernandez-Silva, Gabriela, Fabian Lopez-Araiza, Jorge Elias, López-Torres A.S., Larrea, Fernando, Torres-Flores, Victor, Chirinos, Mayel

Publicada: 1 ene 2019
Resumen:
Background: 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. Objectives: 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. Materials and Methods: 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. Results: 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. Discussion and Conclusions: 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. © 2019 American Society of Andrology and European Academy of Andrology

Filiaciones:
Hernandez-Silva, Gabriela:
 Departamento de Biología de la Reproducción Dr. Carlos Gual Castro, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, Ciudad de México, Mexico

 Posgrado en Ciencias Biológicas, Universidad Nacional Autónoma de México, Ciudad de Mexico, Mexico

 Inst Nacl Ciencias Med & Nutr Salvador Zubiran, Dept Biol Reprod Dr Carlos Gual Castro, Vasco de Quiroga 15, Tlalpan 14080, Ciudad De Mexic, Mexico

 Univ Nacl Autonoma Mexico, Posgrad Ciencias Biol, Ciudad De Mexico, Mexico

Fabian Lopez-Araiza, Jorge Elias:
 Laboratorio de Biomembranas, Facultad de Medicina, Universidad Nacional Autónoma de México, Ciudad de México, Mexico

 Univ Nacl Autonoma Mexico, Fac Med, Lab Biomembranas, Ciudad De Mexico, Mexico

López-Torres A.S.:
 Departamento de Biología de la Reproducción Dr. Carlos Gual Castro, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, Ciudad de México, Mexico

Larrea, Fernando:
 Departamento de Biología de la Reproducción Dr. Carlos Gual Castro, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, Ciudad de México, Mexico

 Inst Nacl Ciencias Med & Nutr Salvador Zubiran, Dept Biol Reprod Dr Carlos Gual Castro, Vasco de Quiroga 15, Tlalpan 14080, Ciudad De Mexic, Mexico

Torres-Flores, Victor:
 Laboratorio de Biomembranas, Facultad de Medicina, Universidad Nacional Autónoma de México, Ciudad de México, Mexico

 Univ Nacl Autonoma Mexico, Fac Med, Lab Biomembranas, Ciudad De Mexico, Mexico

Chirinos, Mayel:
 Departamento de Biología de la Reproducción Dr. Carlos Gual Castro, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, Ciudad de México, Mexico

 Inst Nacl Ciencias Med & Nutr Salvador Zubiran, Dept Biol Reprod Dr Carlos Gual Castro, Vasco de Quiroga 15, Tlalpan 14080, Ciudad De Mexic, Mexico
ISSN: 20472919
Editorial
WILEY-BLACKWELL, 111 RIVER ST, HOBOKEN 07030-5774, NJ USA, Reino Unido
Tipo de documento: Article
Volumen: 8 Número: 1
Páginas: 171-180
WOS Id: 000505871200018
ID de PubMed: 31002753