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dc.contributor.author
Sari, Luciana María
dc.contributor.author
Castro Gonzalez, Ximena Aixa
dc.contributor.author
Zampini, Renato
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Apichela, Silvana Andrea
dc.contributor.author
Ratto, Marcelo Hector
dc.contributor.author
Argañaraz, Martin Eduardo
dc.date.available
2024-04-23T10:21:33Z
dc.date.issued
2023-03
dc.identifier.citation
Sari, Luciana María; Castro Gonzalez, Ximena Aixa; Zampini, Renato; Apichela, Silvana Andrea; Ratto, Marcelo Hector; et al.; Characterization of proteases in the seminal plasma and spermatozoa of llama; Elsevier Science Inc.; Theriogenology; 199; 3-2023; 30-42
dc.identifier.issn
0093-691X
dc.identifier.uri
http://hdl.handle.net/11336/233812
dc.description.abstract
Camelids´ semen has peculiar characteristics that differentiate it from other species, including the highly viscous aspect of seminal plasma that greatly difficult sperm manipulation and the development of techniques such as cryopreservation, artificial insemination, and/or in vitro fertilization. The presence of proteases in the seminal plasma is responsible for semen liquefaction, and sperm functionality to achieve fertilization. The enzymatic and molecular composition of the semen of llama remains unknown. Therefore, the goal of the study was to characterize the protease activity and composition of the seminal plasma and sperm of llama semen. The proteolytic activity was performed using gelatine zymography and the composition by mass-spectrometry.Metallo-proteases were the major source of gelatinolytic activity in seminal plasma, while serine-peptidases were the main enzymes of sperm cells. Matrix Metalloproteinase 2 (MMP2) was the most prominent metallo-protease of llama seminal plasma characterized under the exposure of different inhibitors (EDTA and benzamidine) and by a specific immunodetection. Moreover, the prostate and epididymis were identified as potential sites of its synthesis and secretion.Outstandingly, this metalloproteinase was undetectable in llama sperm. Regarding, the molecular composition of semen by mass-spectrometry, 4 metallo-, 9 serine-, 8 threonine-, and 1 aspartic-peptidases were identified alongside 15 regulators in the sperm cell; where 24 were directly or indirectly interacting. Whereas 6 metallo-, 12 serine-, 3 cysteine-, and 1 aspartic-peptidases were identified, besides 7 inhibitors and 5 regulators in llama seminal plasma where 30 of them were directly or indirectly interconnected. This is the first study describing a partial degradome of llama seminal plasma and spermatozoa suggesting significant differences especially the absence of MMP2 in spermatozoa in contrast to data observed in other species. The characterization of proteases in llama semen will provide a better understanding of the molecular mechanisms involved in the in vivo or in vitro fertilization process in this species.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science Inc.
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Seminal plasma
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Sperm
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New world camelids
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Proteases
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MMP2
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Biología Reproductiva
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Characterization of proteases in the seminal plasma and spermatozoa of llama
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2024-04-22T11:39:24Z
dc.journal.volume
199
dc.journal.pagination
30-42
dc.journal.pais
Estados Unidos
dc.description.fil
Fil: Sari, Luciana María. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
dc.description.fil
Fil: Castro Gonzalez, Ximena Aixa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
dc.description.fil
Fil: Zampini, Renato. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
dc.description.fil
Fil: Apichela, Silvana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina. Universidad Nacional de Tucuman. Facultad de Agronomia y Zootecnia. Cátedra de Zootecnia General I; Argentina
dc.description.fil
Fil: Ratto, Marcelo Hector. Universidad Austral de Chile; Chile
dc.description.fil
Fil: Argañaraz, Martin Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
dc.journal.title
Theriogenology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0093691X23000092
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.theriogenology.2023.01.009
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