Seminal plasma proteins as potential biomarkers for sperm motility and velocities

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 (p < 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 (p < 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. Effect of seminal plasma proteins at freezing on ram sperm motility and viability 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 et al. (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 (p < 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 (p < 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.

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Seminal Plasma Proteome as an Indicator of Sperm Dysfunction and Low Sperm Motility in Chickens

Molecular & Cellular Proteomics ◽

10.1074/mcp.ra120.002017 ◽

2020 ◽

Vol 19 (6) ◽

pp. 1035-1046 ◽

Cited By ~ 3

Author(s):

Yunlei Li ◽

Yanyan Sun ◽

Aixin Ni ◽

Lei Shi ◽

Panlin Wang ◽

...

Keyword(s):

Oxidative Stress ◽

Sperm Motility ◽

Seminal Plasma ◽

Plasma Proteins ◽

Molecular Mechanisms ◽

Membrane Damage ◽

Plasma Proteome ◽

Specific Proteins ◽

Seminal Plasma Proteins ◽

Sperm Dysfunction

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.

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Seminal plasma proteins and their relationship with sperm motility and morphology in boars

Andrologia ◽

10.1111/and.13222 ◽

2018 ◽

Vol 51 (4) ◽

pp. e13222 ◽

Cited By ~ 7

Author(s):

Franciele L. De Lazari ◽

Elistone R. Sontag ◽

Alexander Schneider ◽

Arlindo A. A. Moura ◽

Fábio R. Vasconcelos ◽

...

Keyword(s):

Sperm Motility ◽

Seminal Plasma ◽

Plasma Proteins ◽

Seminal Plasma Proteins

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Identification of seminal plasma proteins as potential biomarkers in men with primary infertility

10.26226/morressier.5af300ae738ab10027aa9316 ◽

2018 ◽

Author(s):

Ashok Agarwal ◽

Luna Samanta ◽

Damayanthi Durairajanayagam

Keyword(s):

Seminal Plasma ◽

Plasma Proteins ◽

Primary Infertility ◽

Seminal Plasma Proteins ◽

Potential Biomarkers

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Seminal plasma proteins and their relationship with sperm motility in Santa Ines rams

Small Ruminant Research ◽

10.1016/j.smallrumres.2012.07.032 ◽

2013 ◽

Vol 109 (2-3) ◽

pp. 94-100 ◽

Cited By ~ 29

Author(s):

M.A.M. Rodrigues ◽

C.E.A. Souza ◽

J.A.M. Martins ◽

J.P.A. Rego ◽

J.T.A. Oliveira ◽

...

Keyword(s):

Sperm Motility ◽

Seminal Plasma ◽

Plasma Proteins ◽

Seminal Plasma Proteins ◽

Santa Inês

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Difference of seminal plasma and sperm proteins in good and poor freezability boar ejaculates

Veterinarska stanica ◽

10.46419/vs.53.2.8 ◽

2021 ◽

Vol 53 (2) ◽

Author(s):

Janyaporn Rungruangsak ◽

Junpen Suwimonteerabutr ◽

Kakanang Buranaamnuay ◽

Sariya Asawakarn ◽

Naphat Chantavisoote ◽

...

Keyword(s):

Sperm Motility ◽

Seminal Plasma ◽

Plasma Proteins ◽

Triosephosphate Isomerase ◽

Progressive Motility ◽

Sperm Proteins ◽

Seminal Plasma Proteins ◽

Boar Semen ◽

High Level ◽

Boar Spermatozoa

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 > 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.

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