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dc.contributor.author
Mayorga, Luis Segundo  
dc.contributor.author
Altamirano, Karina Noel  
dc.contributor.author
Zanni Ruiz, Emilia  
dc.contributor.author
Pavarotti, Martin Alejandro  
dc.date.available
2020-07-28T02:41:23Z  
dc.date.issued
2020-03  
dc.identifier.citation
Mayorga, Luis Segundo; Altamirano, Karina Noel; Zanni Ruiz, Emilia; Pavarotti, Martin Alejandro; Human sperm capacitation is necessary for SNARE assembly in neurotoxin‐resistant complexes; John Wiley and Sons Inc.; Andrology; 8; 2; 3-2020; 442-449  
dc.identifier.issn
2047-2919  
dc.identifier.uri
http://hdl.handle.net/11336/110386  
dc.description.abstract
Capacitation is not a well‐defined process, required for the acrosome reaction triggered by physiological stimuli. In vitro, capacitation is achieved by sperm incubation in artificial media supplemented with HCO3ˉ, Ca2+, and albumin. The role of capacitation in the membrane fusion machinery required for acrosomal exocytosis is not well known. SNAREs proteins are fundamental for intracellular membrane fusion and acrosomal exocytosis. We have previously shown that in capacitated sperm, the fusion machinery is maintained in an inactive state until the acrosome reaction is initiated. In particular, SNARE proteins are assembled in neurotoxin‐resistant complexes.Objective:This work aimed to study the dynamic changes of SNARE complexes during capacitation.Materials and Methods: The light chain of tetanus and botulinum neurotoxin has been widely used to study the configuration of SNARE proteins. For this purpose, we developed a recombinant light chain of tetanus neurotoxin linked to a polyarginine peptide. This membrane permeant protein was able to cleave cytosolic VAMP2 (a SNARE protein required for acrosome reaction) when present in a monomeric configuration.Results: The results show that the VAMP2 is cleaved by the membrane permeant tetanus neurotoxin in non‐capacitated sperm, indicating that, before capacitation, SNAREs are not assembled in stable toxin‐resistant complexes. However, 2 h of incubation in a capacitation medium containing albumin was sufficient to render VAMP2 insensitive to the toxin. Discussion: We conclude that during capacitation, the SNARE proteins become engaged in stable fully assembled cis SNARE complexes. This step is likely essential to prevent untimely activation of the membrane fusion machinery.ConclusionWe propose that capacitation promotes the stabilization of the membrane fusion machinery required for acrosomal exocytosis in preparation for the stimulus‐triggered acrosome reaction.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
John Wiley and Sons Inc.  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
SPERM  
dc.subject
CAPACITATION  
dc.subject
SNARE  
dc.subject
NEUROTOXIN  
dc.subject.classification
Bioquímica y Biología Molecular  
dc.subject.classification
Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Human sperm capacitation is necessary for SNARE assembly in neurotoxin‐resistant complexes  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2020-06-30T14:23:50Z  
dc.journal.volume
8  
dc.journal.number
2  
dc.journal.pagination
442-449  
dc.journal.pais
Estados Unidos  
dc.journal.ciudad
New Jersey  
dc.description.fil
Fil: Mayorga, Luis Segundo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas; Argentina. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina  
dc.description.fil
Fil: Altamirano, Karina Noel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina  
dc.description.fil
Fil: Zanni Ruiz, Emilia. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina. Universidad Nacional de Cuyo; Argentina  
dc.description.fil
Fil: Pavarotti, Martin Alejandro. Universidad Nacional de Cuyo; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina  
dc.journal.title
Andrology  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/andr.12706  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1111/andr.12706