Flow-sorted ram spermatozoa are highly susceptible to hydrogen peroxide damage but are protected by seminal plasma and catalase

2010 ◽  
Vol 22 (7) ◽  
pp. 1131 ◽  
Author(s):  
T. Leahy ◽  
P. Celi ◽  
R. Bathgate ◽  
G. Evans ◽  
W. M. C. Maxwell ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Hydrogen Peroxide ◽  
Seminal Plasma ◽  
Plasma Proteins ◽  
Fluorescein Isothiocyanate ◽  
Oxygen Species ◽  
Merocyanine 540 ◽  
Propidium Iodide Staining ◽  
Flow Sorting ◽  
Seminal Plasma Proteins

To determine whether flow sorting increased the susceptibility of spermatozoa to reactive oxygen species (ROS), ram semen was either diluted with Tris medium (100 × 106 spermatozoa mL–1; D) or highly diluted (106 spermatozoa mL–1) before being centrifuged (DC) at 750g for 7.5 min at 21°C or flow-sorted (S) before cryopreservation. Thawed spermatozoa were resuspended in graded concentrations of hydrogen peroxide to induce oxidative stress. In Experiment 1, following exposure to 30 or 45 μM hydrogen peroxide (H2O2), the total motility (%) of DC (41.0 ± 7.3 or 25.7 ± 6.7, respectively) and S spermatozoa (33.8 ± 6.3 or 20.1 ± 6.3, respectively) was lower (P < 0.001) than that of D spermatozoa (58.7 ± 5.6 or 44.5 ± 6.7, respectively). In Experiment 2, supplementation of samples containing H2O2 with catalase (150 IU mL–1) or seminal plasma proteins (4 mg protein per 108 spermatozoa) negated oxidative stress, resulting in comparable values to samples receiving no H2O2in terms of the proportion of spermatozoa with stable plasmalemma (as determined using merocyanine-540 and Yo-Pro-1) in the D and S groups, the proportion of viable, acrosome-intact spermatozoa (as determined by fluorescein isothiocyanate and propidium iodide staining) in the D group and the motility of control (undiluted) and S spermatozoa. Neither H2O2 nor sperm type (i.e. D, DC or S) had any effect on intracellular concentrations of ROS. These results show that flow sorting increases the susceptibility of spermatozoa to ROS, but the inclusion of anti-oxidants or seminal plasma as part of the sorting protocol improves resistance to oxidative stress.

Proteomic analysis of spermatozoa reveals caseins play a pivotal role in preventing short-term periods of subfertility in stallions

2022 ◽  
Author(s):  
Róisín Ann Griffin ◽  
Aleona Swegen ◽  
Mark A Baker ◽  
Rachel Ann Ogle ◽  
Nathan Smith ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Plasma Proteins ◽  
Low Fertility ◽  
High Fertility ◽  
Short Term ◽  
Sperm Binding ◽  
Merocyanine 540 ◽  
Seminal Plasma Proteins ◽  
Assessment Strategies

Abstract Stallions experience transient fluctuations in fertility throughout the breeding season. Considering pregnancy diagnoses cannot be ascertained until ~14 days post-breeding, the timely detection of decreases in stallion fertility would enhance industry economic and welfare outcomes. Therefore, this study aimed to identify the proteomic signatures reflective of short-term fertility fluctuations, and to determine the biological mechanisms governing such differences. Using LC–MS/MS, we compared the proteomic profile of semen samples collected from commercially “fertile” stallions, during high- and low-fertility periods. A total of 1702 proteins were identified, of which, 38 showed a significant change in abundance (p ≤ 0.05). Assessment of intra- and inter-stallion variability revealed that caseins (namely κ-, α-S1-, and α-S2-casein), were significantly more abundant during “high-fertility” periods, while several epididymal, and seminal plasma proteins (chiefly, epididymal sperm binding protein 1 [ELSPbP1], horse seminal plasma protein 1 [HSP-1] and clusterin), were significantly more abundant during “low-fertility” periods. We hypothesised that an increased abundance of caseins offers greater protection from potentially harmful seminal plasma proteins, thereby preserving cell functionality and fertility. In vitro exposure of spermatozoa to casein resulted in decreased levels of lipid scrambling (Merocyanine 540), higher abundance of sperm-bound caseins (α-S1-, α-S2-, and κ-casein), and lower abundance of sperm-bound HSP-1 (p ≤ 0.05). This study demonstrates key pathways governing short-term fertility fluctuations in the stallion, thereby providing a platform to develop robust, fertility assessment strategies into the future.

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

2020 ◽  
Vol 19 (6) ◽  
pp. 1035-1046 ◽  
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.

Identification of seminal plasma proteins in men with oxidative stress utilizing proteomic tools

2012 ◽  
Vol 98 (3) ◽  
pp. S239
Author(s):  
R. Sharma ◽  
A. Agarwal ◽  
A.J. Hamada ◽  
S.S. Du Plessis ◽  
S.P. Yadav ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Seminal Plasma ◽  
Plasma Proteins ◽  
Seminal Plasma Proteins

Genetic Polymorphism of Boar Seminal Plasma Proteins

1993 ◽  
Vol 64 (3) ◽  
pp. 221-227
Author(s):  
Soichi TSUJI ◽  
Masatoshi ASAO ◽  
Hiroshi KUSUNOKI ◽  
Takao OISHI
Keyword(s):  
Genetic Polymorphism ◽  
Seminal Plasma ◽  
Plasma Proteins ◽  
Seminal Plasma Proteins

Seasonal differences in seminal plasma proteins from two bovine breeds adapted to a subtropical climate

2021 ◽  
Vol 53 (1) ◽  
Author(s):  
Paula Lorena Souto ◽  
Lilian Silveira Travassos Carmouy ◽  
Cristiane Santos ◽  
Edison Martins ◽  
Vera Martins ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Plasma Proteins ◽  
Subtropical Climate ◽  
Seasonal Differences ◽  
Seminal Plasma Proteins

scholarly journals Intracellular Sources of ROS/H2O2 in Health and Neurodegeneration: Spotlight on Endoplasmic Reticulum

Cells ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 233
Author(s):  
Tasuku Konno ◽  
Eduardo Pinho Melo ◽  
Joseph E. Chambers ◽  
Edward Avezov
Keyword(s):  
Oxidative Stress ◽  
Reactive Oxygen Species ◽  
Hydrogen Peroxide ◽  
Endoplasmic Reticulum ◽  
Neurodegenerative Diseases ◽  
Antioxidative Enzymes ◽  
Redox Reactions ◽  
Ros Production ◽  
Oxygen Species ◽  
Specific Target

Reactive oxygen species (ROS) are produced continuously throughout the cell as products of various redox reactions. Yet these products function as important signal messengers, acting through oxidation of specific target factors. Whilst excess ROS production has the potential to induce oxidative stress, physiological roles of ROS are supported by a spatiotemporal equilibrium between ROS producers and scavengers such as antioxidative enzymes. In the endoplasmic reticulum (ER), hydrogen peroxide (H2O2), a non-radical ROS, is produced through the process of oxidative folding. Utilisation and dysregulation of H2O2, in particular that generated in the ER, affects not only cellular homeostasis but also the longevity of organisms. ROS dysregulation has been implicated in various pathologies including dementia and other neurodegenerative diseases, sanctioning a field of research that strives to better understand cell-intrinsic ROS production. Here we review the organelle-specific ROS-generating and consuming pathways, providing evidence that the ER is a major contributing source of potentially pathologic ROS.

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