scholarly journals Cryopreservation Differentially Alters the Proteome of Epididymal and Ejaculated Pig Spermatozoa

2019 ◽  
Vol 20 (7) ◽  
pp. 1791 ◽  
Author(s):  
Cristina Perez-Patiño ◽  
Isabel Barranco ◽  
Junwei Li ◽  
Lorena Padilla ◽  
Emilio A. Martinez ◽  
...  
Keyword(s):  
Quantitative Proteomics ◽  
Reactive Oxygen Species Generation ◽  
Sperm Function ◽  
Oxygen Species ◽  
Mitochondria Membrane Potential ◽  
Progressive Motility ◽  
Epididymal Spermatozoa ◽  
Proteome Changes ◽  
Sexually Mature ◽  
Mammalian Spermatozoa

Cryopreservation induces differential remodeling of the proteome in mammalian spermatozoa. How these proteome changes relate to the loss of sperm function during cryopreservation remains unsolved. The present study aimed to clarify this issue evaluating differential changes in the proteome of fresh and frozen-thawed pig spermatozoa retrieved from the cauda epididymis and the ejaculate of the same boars, with clear differences in cryotolerance. Spermatozoa were collected from 10 healthy, sexually mature, and fertile boars, and cryopreserved using a standard 0.5 mL-straw protocol. Total and progressive motility, viability, and mitochondria membrane potential were higher and membrane fluidity and reactive oxygen species generation lower in frozen-thawed (FT) epididymal than ejaculated spermatozoa. Quantitative proteomics of fresh and FT spermatozoa were analyzed using a LC-ESI-MS/MS-based Sequential Window Acquisition of All Theoretical Spectra approach. Cryopreservation quantitatively altered more proteins in ejaculated than cauda epididymal spermatozoa. Differential protein–protein networks highlighted a set of proteins quantitatively altered in ejaculated spermatozoa, directly involved in mitochondrial functionality which would explain why ejaculated spermatozoa deteriorate during cryopreservation.

Free radicals, lipid peroxidation and sperm function

1995 ◽  
Vol 7 (4) ◽  
pp. 659 ◽  
Author(s):  
RJ Aitken
Keyword(s):  
Reactive Oxygen Species ◽  
Lipid Peroxidation ◽  
Reactive Oxygen ◽  
Human Spermatozoa ◽  
Sperm Function ◽  
Oxygen Species ◽  
Normal Sperm ◽  
Oxidative Processes ◽  
Mammalian Spermatozoa

The cellular generation of reactive oxygen species was first observed in mammalian spermatozoa in the late 1940s. The field then remained dormant for 30 years until Thaddeus Mann and Roy Jones published a series of landmark papers in the 1970s in which the importance of lipid peroxidation as a mechanism for damaging mammalian spermatozoa was first intimated. The subsequent demonstration that human spermatozoa produce reactive oxygen species and are susceptible to peroxidative damage has triggered intense interest in the role of oxidative stress in the aetiology of male infertility. Moreover, data have recently been obtained to indicate that, although excessive exposure to reactive oxygen species may be harmful to spermatozoa, in physiological amounts these molecules are of importance in the control of normal sperm function. This review considers the dualistic role of reactive oxygen species and sets out the current understanding of the importance of oxidative processes in both the physiology and the pathology of the human spermatozoon. Extra keywords: human spermatozoa, reactive oxygen species.

scholarly journals GENERATION OF REACTIVE OXYGEN SPECIES IN RAT EPIDIDYMAL SPERMATOZOA AFTER CYCLOPHOSPHAMIDE TREATMENT

2018 ◽  
Vol 11 (4) ◽  
pp. 437
Author(s):  
Kashmiri Zn ◽  
Sastry Ms
Keyword(s):  
Reactive Oxygen Species ◽  
Sperm Morphology ◽  
Reactive Oxygen ◽  
Wistar Rat ◽  
Sperm Function ◽  
Oxygen Species ◽  
Cyclophosphamide Treatment ◽  
Epididymal Spermatozoa ◽  
Vehicle Treated Control ◽  
Different Doses

 Objective: The aim of this study was to examine the effect of an anticancer drug cyclophosphamide (CPA) on generation of reactive oxygen species (ROS) in epididymal spermatozoa of Wistar rat, Rattus norvegicus. Methods: For this purpose, the rats were injected intraperitoneally with different doses of CPA (5 mg, 15 mg, and 20 mg/Kg BW for 2 weeks).Results: Treatment resulted into significantly increased level of ROS in CPA-treated groups when compared to the vehicle-treated control group.Conclusion: The results revealed that CPA has deleterious effect on the sperm morphology and physiology, which is dose and duration dependent and at certain doses cause the production of a number of reactive molecules and free radicals derived from molecular oxygen consequently resulting into adverse effect on the sperm function and hence on reproduction.

Redox regulation of tyrosine phosphorylation in human spermatozoa and its role in the control of human sperm function

1995 ◽  
Vol 108 (5) ◽  
pp. 2017-2025 ◽  
Author(s):  
R.J. Aitken ◽  
M. Paterson ◽  
H. Fisher ◽  
D.W. Buckingham ◽  
M. van Duin
Keyword(s):  
Reactive Oxygen Species ◽  
Tyrosine Phosphorylation ◽  
Redox Regulation ◽  
Reactive Oxygen Species Generation ◽  
Reactive Oxygen ◽  
Human Sperm ◽  
Human Spermatozoa ◽  
Sperm Function ◽  
Ionophore A23187 ◽  
Oxygen Species

The redox status of human spermatozoa was found to have a profound influence on the fertilizing potential of these cells in association with qualitative and quantitative changes in the patterns of tyrosine phosphorylation. In general, oxidizing conditions enhanced tyrosine phosphorylation and stimulated sperm function, whereas reducing conditions had the opposite effect. Unstimulated human spermatozoa exhibited low levels of spontaneous acrosomal exocytosis and sperm-oocyte fusion and minimal reactive oxygen species generation, while phosphotyrosine expression was largely confined to a single protein of 116 kDa. However, if the spermatozoa were exposed to oxidizing conditions through the addition of exogenous H2O2, or the stimulation of endogenous NADPH-dependent reactive oxygen species generation, then a dramatic increase in tyrosine phosphorylation was observed (major phosphotyrosyl bands at 222 kDa, 200 kDa, 159 kDa, 133 kDa, 116 kDa and 82 kDa) in concert with the functional activation of the spermatozoa. A causal association between reactive oxygen species generation, tyrosine phosphorylation and sperm function was indicated by studies with the ionophore, A23187, which induced high rates of spermoocyte fusion together with enhanced rates of reactive oxygen species production and the increased expression of phosphotyrosyl proteins. This functional response to A23187 could be abrogated, without any concomitant change in sperm motility or viability, by using membrane permeant thiols or catalase to suppress the reactive oxygen species-induced increase in phosphotyrosine expression. The fact that the biological responses of human spermatozoa to biological agonists (recombinant human ZP3 and progesterone) could also be inhibited by catalase indicated the general relevance of these findings.(ABSTRACT TRUNCATED AT 250 WORDS)

Роль оксида азота в реализации антиоксидантного эффекта неопиатного аналога лей-энкефалина в сердце новорожденных белых крыс

2019 ◽  
pp. 61-64
Keyword(s):  
Reactive Oxygen Species ◽  
Reactive Oxygen Species Generation ◽  
Reactive Oxygen ◽  
Postnatal Period ◽  
Oxide System ◽  
No Synthase ◽  
Albino Rats ◽  
Oxygen Species ◽  
Control Parameters ◽  
Synthase Inhibitor

The eff ect of the non-opiate analog of leu-enkephalin (peptide NALE: Phe – D – Ala – Gly – Phe – Leu – Arg) on the reactive oxygen species generation in the heart of albino rats in the early postnatal period was studied. Peptide NALE was administered intraperitoneally in the dose of 100 μ/kg daily from 2 to 6 days of life. Reactive oxygen species generation was assessed by chemiluminescence in the heart homogenates of 7-day-old animals. Decreasing of reactive oxygen species generation nearly by 30 % and an increasing in antioxidant system activity by the 20-27 %, compared with the control parameters, were found. The antioxidant eff ect of peptide NALE is associated with the presence of the amino acid Arg in the structure of the peptide. An analogue of NALE peptide, devoid of Arg (peptide Phe – D – Ala – Gly – Phe – Leu – Gly), had a signifi cant lower antioxidant eff ect. The NO-synthase inhibitor NG-nitro-L-arginine methyl ester (L-NAME) in the dose 50 mg/kg, administered with NALE peptide, reduced the severity of the NALE antioxidant eff ect. The results of the study suggest that the pronounced antioxidant eff ect of NALE peptide in the heart of albino rats, at least in part, is due to the interaction with the nitric oxide system.

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