scholarly journals Functional insights into the role of seminal plasma proteins on sperm motility of buffalo

2018 ◽  
Vol 195 ◽  
pp. 251-258 ◽  
Author(s):  
Viviane Maria Codognoto ◽  
Paulo Henrique Yamada ◽  
Rúbia Alves Schmith ◽  
Felipe Rydygier de Ruediger ◽  
Caroline Scott ◽  
...  
2009 ◽  
Vol 10 (1) ◽  
pp. 51 ◽  
Author(s):  
Jaime Antonio Cardozo ◽  
Patricia Grasa ◽  
María Teresa Muiño B. ◽  
José Álvaro Cebrián P.

<p>Este estudio se adelantó para evaluar el efecto de la adición de proteínas del plasma seminal de cordero en la criopreservación sobre la motilidad e integridad de la membrana espermática, y los cambios en el perfil electroforético de las proteínas de la membrana espermática inducidos por la criopreservación. Se usaron eyaculados de ocho corderos adultos de la raza rasa aragonesa, se les determinó su viabilidad y motilidad espermáticas y posteriormente se sometieron a un procedimiento de congelación. Las proteínas se separaron por el método de electroforesis en geles de acrilamida en dos dimensiones. Se obtuvo un mejoramiento significativo (<em>p </em>&lt; 0,05) en la calidad del semen congelado, cuando se adicionaron proteínas del plasma seminal. El análisis bidimensional comparativo entre el semen fresco y el congelado evidenció la pérdida de 8 puntos de proteína en el espermatozoide descongelado. La concentración de un punto de proteína de membrana espermática, de bajo peso molecular (punto 2), fue más alta (<em>p </em>&lt; 0,05) en el espermatozoide descongelado al que se adicionaron proteínas del plasma seminal. Se encontraron correlaciones entre algunos puntos de proteína y la motilidad y viabilidad espermáticas, lo cual sugiere que pueden jugar papeles importantes en el mantenimiento de la integridad y funcionalidad del espermatozoide. Se puede concluir que la adición de proteínas del plasma seminal en la congelación mejora la integridad del espermatozoide descongelado, y que la criopreservación del semen de cordero produce variaciones en la composición de las proteínas de membrana.  </p><p> </p><p><strong>Effect of seminal plasma proteins at freezing on ram sperm motility and viability</strong>  </p><p>The aim of the study was to evaluate the cryoprotective effect of seminal plasma proteins on ram sperm motility, membrane integrity and the changes in the profile of ram sperm membrane proteins induced by cryopreservation. Fresh ejaculates from 8 mature Rasa aragonesa rams were used. Sperm motility and cell viability was assessed. The freezing procedure was based on the method described by Fiser <em>et al</em>. (1987). Proteins extracted from fresh and frozen-thawed semen were subjected to the Two-dimensional polyacrilamide gel electrophoresis. A significant improvement in the quality of frozenthawed sperm was obtained after addition of seminal plasma proteins (<em>p </em>&lt; 0.05). Comparative two-dimensional polyacrilamide gel electrophoresis analysis between fresh and frozen semen, either with or without seminal plasma proteins in the cryopreservation medium, revealed that eight protein spots were lost in frozen-thawed sperm. The concentration of one sperm membrane protein spot of low Mr (spot 2) was higher (<em>p </em>&lt; 0.05) in proteinadded frozen sperm. Correlations found between certain protein spots sperm motility and viability suggests that these proteins could play important roles in the maintenance of sperm integrity and functionality. In conclusion, the addition of seminal plasma proteins to freezing extender improved frozen-thawed ram sperm integrity quality and cryopreservation of ram semen produced variations in the sperm membrane protein composition. </p>


SPERMOVA ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 83-95
Author(s):  
María Alejandra Cardozo ◽  
◽  
Jaime Antonio Cardozo ◽  
Fabian Rueda

Bovine livestock is one of the most important economic and social sectors for many countries. In this sense, the development of strategies to improve reproductive bull fertility and reproduction rates is relevant. It's highlighted the role of seminal plasma proteins (SPP) in reproductive fertility, so it has found close relationships among studies on the structure and biological activity of SPP, with seminal quality, including viability, sperm motility, and morphology. In addition, they have been found to regulate sperm functions such as capacitation, acrosome reaction, and they are even related to protecting sperm against thermal and oxidative stress. Moreover, the methods of separation and protein identification and their contribution to characterizing the bovine SP proteome should be also highlighted. In this sense, the most recent studies have been directed towards developing supplements with SPP that improve quality sperm subjected to cryopreservation processes. Research has begun and should forward to establish how the networks or sets of proteins are related to the functioning and fertility of sperm, the search for biomarkers of fertility, and the use of proteins in biotechnological processes, to increase efficiency reproductive.


2020 ◽  
Vol 19 (6) ◽  
pp. 1035-1046 ◽  
Author(s):  
Yunlei Li ◽  
Yanyan Sun ◽  
Aixin Ni ◽  
Lei Shi ◽  
Panlin Wang ◽  
...  

Molecular mechanisms underlying sperm motility have not been fully explained, particularly in chickens. The objective was to identify seminal plasma proteins associated with chicken sperm motility by comparing the seminal plasma proteomic profile of roosters with low sperm motility (LSM, n = 4) and high sperm motility (HSM, n = 4). Using a label-free MS-based method, a total of 522 seminal plasma proteins were identified, including 386 (∼74%) previously reported and 136 novel ones. A total of 70 differentially abundant proteins were defined, including 48 more-abundant, 15 less-abundant, and seven proteins unique to the LSM group (specific proteins). Key secretory proteins like less-abundant adhesion G-protein coupled receptor G2 (ADGRG2) and more-abundant serine peptidase inhibitor Kazal-type 2 (SPINK2) in the LSM suggested that the corresponding secretory tissues played a crucial role in maintaining sperm motility. Majority (80%) of the more-abundant and five specific proteins were annotated to the cytoplasmic domain which might be a result of higher plasma membrane damage and acrosome dysfunction in LSM. Additionally, more-abundant mitochondrial proteins were detected in LSM seminal plasma associated with lower spermatozoa mitochondrial membrane potential (ΔΨm) and ATP concentrations. Further studies showed that the spermatozoa might be suffering from oxidative stress, as the amount of spermatozoa reactive oxygen species (ROS) were largely enhanced, seminal malondialdehyde (MDA) concentrations were increased, and the seminal plasma total antioxidant capacity (T-AOC) were decreased. Our study provides an additional catalogue of chicken seminal plasma proteome and supports the idea that seminal plasma could be as an indicator of spermatozoa physiology. More-abundant of acrosome, mitochondria and sperm cytoskeleton proteins in the seminal plasma could be a marker of sperm dysfunction and loss of motility. The degeneration of spermatozoa caused by the reduced seminal T-AOC and enhanced oxidative stress might be potential determinants of low sperm motility. These results could extend our understanding of sperm motility and sperm physiology regulation.


2019 ◽  
Vol 26 (4) ◽  
pp. 238-250 ◽  
Author(s):  
Archana Kumar ◽  
T.B. Sridharn ◽  
Kamini A. Rao

Seminal plasma proteins contributed by secretions of accessory glands plays a copious role in fertilization. Their role is overlooked for decades and even now, as Artificial Reproduction Techniques (ART) excludes the plasma components in the procedures. Recent evidences suggest the importance of these proteins starting from imparting fertility status to men, fertilization and till successful implantation of the conceptus in the female uterus. Seminal plasma is rich in diverse proteins, but a major part of the seminal plasma is constituted by very lesser number of proteins. This makes isolation and further research on non abundant protein a tough task. With the advent of much advanced proteomic techniques and bio informatics tools, studying the protein component of seminal plasma has become easy and promising. This review is focused on the role of seminal plasma proteins on various walks of fertilization process and thus, the possible exploitation of seminal plasma proteins for understanding the etiology of male related infertility issues. In addition, a compilation of seminal plasma proteins and their functions has been done.


Andrologia ◽  
2018 ◽  
Vol 51 (4) ◽  
pp. e13222 ◽  
Author(s):  
Franciele L. De Lazari ◽  
Elistone R. Sontag ◽  
Alexander Schneider ◽  
Arlindo A. A. Moura ◽  
Fábio R. Vasconcelos ◽  
...  

Author(s):  
Gemma Gaitskell-Phillips ◽  
Francisco E. Martín-Cano ◽  
José M. Ortiz-Rodríguez ◽  
Eva da Silva-Álvarez ◽  
Javier Massot ◽  
...  

2013 ◽  
Vol 109 (2-3) ◽  
pp. 94-100 ◽  
Author(s):  
M.A.M. Rodrigues ◽  
C.E.A. Souza ◽  
J.A.M. Martins ◽  
J.P.A. Rego ◽  
J.T.A. Oliveira ◽  
...  

2021 ◽  
Vol 53 (2) ◽  
Author(s):  
Janyaporn Rungruangsak ◽  
Junpen Suwimonteerabutr ◽  
Kakanang Buranaamnuay ◽  
Sariya Asawakarn ◽  
Naphat Chantavisoote ◽  
...  

The present study was performed to compare the expression of sperm proteins, i.e. triosephosphate isomerase (TPI) and acrosin binding protein (ACRBP) and seminal plasma proteins, i.e. glutathione peroxidase 5 (GPX5) and fibronectin 1 (FN1), in boar semen with good, moderate and poor freezability. The study was conducted by determining the protein contents in 32 sperm samples and 38 seminal plasma samples of semen. The ejaculated semen was divided into two portions: the first portion was centrifuged to separate the pellet of sperm from the seminal plasma and the second portion was cryopreserved. After thawing, the ejaculates were classified into three groups according to their post-thawed sperm motility: good (60.2 ± 1.7%), moderate (29.3 ± 2.0%) and poor (16.6 ± 2.2%) freezabilities. The expressions of GPX5 and FN1 in seminal plasma and TPI and ACRBP in sperm were determined using Western blot analysis. It was found that, for sperm proteins, the level of TPI was negatively correlated with the post-thawed total sperm motility (r = -0.38, P = 0.029). For seminal plasma proteins, the level of FN1 in the seminal plasma was positively correlated with the post-thawed total sperm motility (r = 0.37, P = 0.021) and progressive motility (r = 0.39, P = 0.016). The expression of GPX5 was not correlated with any of the frozen–thawed sperm qualities (P &gt; 0.05). In conclusions, boar semen containing a high level of FN1 in seminal plasma has better freezability. Frozen–thawed sperm motility was positively correlated with the level of FN1 in boar seminal plasma and negatively correlated with TPI in boar spermatozoa.


1993 ◽  
Vol 64 (3) ◽  
pp. 221-227
Author(s):  
Soichi TSUJI ◽  
Masatoshi ASAO ◽  
Hiroshi KUSUNOKI ◽  
Takao OISHI

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