Cryostorage and Oxidative Stress in Mammalian Spermatozoa

Meyers, Stuart A.

doi:10.1007/978-1-61779-776-7_3

Cited by 11 publications

(12 citation statements)

References 105 publications

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“…The radical NO is a free radical with a relatively long half‐life and the product of the oxidation of l ‐arginine to l ‐citrulline by the enzyme nitric oxide synthases (NOS, Roessner et al ., ). In a study, although nitric oxide production remains unchanged during sperm cooling, a sudden burst of nitric oxide radical production was observed during defrosting (Meyers, ), which may explain the results obtained in this experiment. Physiological nitrite concentrations could have some physiological role in the sperm cell, as it has been observed in to be related to human sperm motility (Lewis et al ., ).…”

Section: Discussionsupporting

confidence: 51%

“…The ROS, mainly the superoxide anion (O 2 − ) and hydrogen peroxide (H 2 O 2 ), are formed as products of the oxidative metabolism of cells such as the spermatozoa and leucocytes in the semen (Ball, ). However, spermatozoon and seminal plasma contain enzymes and low molecular weight antioxidants, which scavenge ROS, preventing cellular damage (Meyers, ). ROS at high concentrations can cause lipid peroxidation, loss of motility and viability, and DNA fragmentation (Baumber et al ., ).…”

Section: Introductionmentioning

confidence: 99%

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Milk, caseinate and lactoferrin addition to equine semen cooling extenders

et al. 2016

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Cooled semen has been used routinely to prolong sperm viability until artificial insemination time. However, spermatozoa are subjected to oxidative stress. The aim of the present work was to investigate the protective and antioxidant effect of the milk proteins lactoferrin (Lf) and caseinate added to equine semen cooling extenders. Semen from six stallions was cooled at 5 °C after resuspension with C1) milk- and glucose-based, C2) 0.6% caseinate, C3) C2 + Lf 200 μg ml , C4) C2 + Lf 500 μg ml and C5) C2 + Lf 1000 μg ml extenders, and kept at 5 °C for 24 h. Sperm motility characteristics and intact membrane rates were not different among the treatments (P > 0.05). As a result of the cooling process, the nitrite concentration increased significantly in the cooled semen (69.6 ± 78.9 μm per ×10 spermatozoa) compared with the fresh semen (8.6 ± 1.9 μm per ×10 spermatozoa). In contrast, the H O concentrations were lower in the 0.6% caseinate extender (265.9 ± 221.3 μm per ×10 spermatozoa) than in the milk extender (430.9 ± 199.8 μm per ×10 spermatozoa, P < 0.05), showing an antioxidative effect of the caseinate compared with the milk. However, in all groups, hydrogen peroxide concentrations were similar to the undiluted fresh semen (332.8 ± 151.3 μm per ×10 spermatozoa). Caseinate showed to be as efficient as milk to protect equine-cooled spermatozoon.

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Section: Discussionsupporting

confidence: 51%

Section: Introductionmentioning

confidence: 99%

Milk, caseinate and lactoferrin addition to equine semen cooling extenders

et al. 2016

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“…Since glycolysis is less efficient than OxPhos (producing two ATP per molecule of glucose whereas OxPhos produces 30 ATP per ETC cycle), this could at least partially explain the decrease in motility seen in both cryopreservation and ageing. In the ageing testicle, there is decreased antioxidant buffering capacity which includes decreased superoxide dismutase enzyme activity as well as less active intra‐mitochondrial catalase and peroxidase (Meyers, ).This leaves sperm more susceptible to oxidative cell and DNA damage which could lead to decreased OxPhos.…”

Section: Function Of Sperm Mitochondriamentioning

confidence: 99%

Sperm mitochondrial regulation in motility and fertility in horses

Meyers

Bulkeley

Foutouhi

2019

Reprod Domestic Animals

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The biological nature of age‐related declines in fertility in males of any species, including stallions, has been elusive. In horses, the economic costs to the breeding industry are frequently extensive. Mitochondrial function in ejaculated sperm, which is essential for sperm motility, is reflected by adenosine triphosphate production, mitochondrial oxidative efficiency and production of reactive oxygen species, and that this balance may become compromised in ageing stallions and during the process of cryopreservation. This presentation will focus on mitochondrial integrity and function as an avenue for understanding the pathophysiology of sperm when undergoing cryopreservation and male ageing. We discuss the importance of understanding the differences and similarities of sperm mitochondria to that of somatic cells regarding structure and mitochondrial biochemistry relating to sperm function. The roles of oxidative phosphorylation and glycolysis in sperm mitochondria are outlined as is the method of determining oxygen consumption and calcium homoeostasis in sperm mitochondria. Further, we outline the role of oxidative stress and reactive oxygen species.

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“…65,66 It is believed that leukocytes and spermatozoa share a similar mechanism for ROS generation: an NADPH oxidase located in or near the cell membrane. 67 Although controversy exists regarding the form of this enzyme, 68 exogenous gangliosides undeniably decrease the extracellular production of superoxide radicals.…”

Section: Gangliosides and Spermatozoamentioning

confidence: 99%

Protective effects of exogenous gangliosides on ROS-induced changes in human spermatozoa

Gavella¹,

Lipovac²

2013

Asian J Androl

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This article summarizes the available evidence on the efficacy of gangliosides to reduce the degree of reactive oxygen species (ROS)-mediated damage. The antioxidative efficacy of exogenous gangliosides in protecting different cells encouraged us to examine their ability to protect human spermatozoa. Gangliosides are sialic acid-containing glycosphingolipids with strong amphiphilic character due to the bulky headgroup made of several sugar rings with sialic acid residues and the double-tailed hydrophobic lipid moiety. The amphiphilicity of gangliosides allows them to exist as micelles in aqueous media when they are present at a concentration above their critical micellar concentration. The protective effect of ganglioside micelles on spermatozoa is believed to stem from their ability to scavenge free radicals and prevent their damaging effects. In our study, we particularly focused our attention on the protective effect of ganglioside micelles on DNA in human spermatozoa exposed to cryopreservation. The results indicate that ganglioside micelles can modulate the hydrophobic properties of the sperm membrane to increase tolerance to DNA fragmentation, thus protecting the DNA from cryopreservation-induced damage. Further actions of ganglioside micelles, which were documented by biochemical and biophysical studies, included (i) the modulation of superoxide anion generation by increasing the diffusion barrier for membrane events responsible for signal translocation to the interior of the cell; (ii) the inhibition of iron-catalysed hydroxyl radical formation due to the iron chelation potential of gangliosides; and (iii) inhibition of hydrogen peroxide diffusion across the sperm membrane.

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Cryostorage and Oxidative Stress in Mammalian Spermatozoa

Cited by 11 publications

References 105 publications

Milk, caseinate and lactoferrin addition to equine semen cooling extenders

Milk, caseinate and lactoferrin addition to equine semen cooling extenders

Sperm mitochondrial regulation in motility and fertility in horses

Protective effects of exogenous gangliosides on ROS-induced changes in human spermatozoa

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