Cryopreservation increases coating of bull sperm by seminal plasma binder of sperm proteins BSP1, BSP3, and BSP5

Ardón, Florencia; Suárez, Susan S.

doi:10.1530/rep-12-0468

Cited by 39 publications

(23 citation statements)

References 51 publications

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“…33 Procedures to prepare the sperm from the frozen samples are described in Ardon et al . 34 Briefly, the straws were first thawed in a 37°C water bath, and then seminal plasma, extender, and dead sperm were removed from live sperm by density gradient centrifugation (300 x g for 10 min) through two layers (40–80%) of BoviPure diluted in BoviDilute (Spectrum Technologies, Inc., Healdsburg, CA, USA). The sperm pellet was then washed in 3 mL TALP (300 x g, 3 min).…”

Section: Experimental Methodsmentioning

confidence: 99%

Cooperative roles of biological flow and surface topography in guiding sperm migration revealed by a microfluidic model

et al. 2014

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Successful reproduction in mammals requires sperm to swim against a fluid flow and through the long and complex female reproductive tract before reaching the egg in the oviduct. Millions of them do not make it. Despite the clinical importance, the roles played in sperm migration by the diverse biophysical and biochemical microenvironments within the reproductive tract are largely unknown. In this article, we present the development of a double layer microfluidic device that recreates two important biophysical environments within female reproductive tract: fluid flow and surface topography. The unique feature of the device is that it enables one to study the cooperative roles of fluid flow and surface topography in guiding sperm migration. Using bull sperm as a model system, we found that microfluidic grooves embedded on a channel surface facilitate sperm migration against fluid flows. These findings suggest ways to design in vitro fertilization devices to treat infertility and to develop non-invasive contraceptives that use microarchitectural design to entrap sperm.

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Section: Experimental Methodsmentioning

confidence: 99%

Cooperative roles of biological flow and surface topography in guiding sperm migration revealed by a microfluidic model

et al. 2014

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“…The freezing and thawing processes of sperm cryopreservation inevitably cause structural and functional alterations, thereby reducing fertility [5–7]. Although the bovine is regarded as a model of successful cryopreservation among various species, the process causes up to 50% loss of viable spermatozoa [8].…”

Section: Introductionmentioning

confidence: 99%

Proteomic identification of cryostress in epididymal spermatozoa

Yoon

Rahman

Kwon

et al. 2016

J Animal Sci Biotechnol

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Background: Cryopreservation of epididymal spermatozoa is important in cases in which it is not possible to collect semen using normal methods, as the sudden death of an animal or a catastrophic injury. However, the freezing and thawing processes cause stress to spermatozoa, including cold shock, osmotic damage, and ice crystal formation, thereby reducing sperm quality. We assessed the motility (%), motion kinematics, capacitation status, and viability of spermatozoa using computer-assisted sperm analysis and Hoechst 33258/chlortetracycline fluorescence staining. Moreover, we identified proteins associated with cryostress using a proteomic approach and performed western blotting to validate two-dimensional electrophoresis (2-DE) results using two commercial antibodies. Results: Cryopreservation reduced viability (%), motility (%), straight-line velocity (VSL), average path velocity (VAP), amplitude of lateral head displacement (ALH), and capacitated spermatozoa, whereas straightness (STR) and the acrosome reaction increased after cryopreservation (P < 0.05). Nine proteins were differentially expressed (two proteins decreased and seven increased) (>3 fold, P < 0.05) before and after cryopreservation. The proteins differentially expressed following cryopreservation are putatively related to several signaling pathways, including the ephrinR-actin pathway, the ROS metabolism pathway, actin cytoskeleton assembly, actin cytoskeleton regulation, and the guanylate cyclase pathway.

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“…Cryopreservation has been applied to various species, including humans, swine, cattle, cats, and dogs (Mota Filho et al, 2014). Although sperm cryopreservation preserves sperm motility, metabolic functions, and fertility, but, still the freeze-thawing process causes irreversible damage to spermatozoa and reduces fertility (Ardon and Saurez, 2013). Even though cryopreservation helps in prolonged storage of semen, but cryo-capacitation is one of the major factors associated with reduced longevity and poor survivability of cryopreserved spermatozoa in female reproductive tract (Watson, 2000), resulting in reduced fertility of frozen-thawed semen.…”

Section: Introductionmentioning

confidence: 99%

Seminal Plasma Heparin Binding Proteins Improve Semen Quality by Reducing Oxidative Stress during Cryopreservation of Cattle Bull Semen

Patel

Gandotra

Cheema

et al. 2015

Asian Australas. J. Anim. Sci

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Heparin binding proteins (HBPs) are produced by accessory glands. These are secreted into the seminal fluid, bind to the spermatozoa at the time of ejaculation, favour capacitation, acrosome reaction, and alter the immune system response toward the sperm. The present study was conducted with an objective to assess the effect of purified seminal plasma-HBPs (SP-HBPs) on cross bred cattle bull sperm attributes during two phases of cryopreservation: Pre freezing and freezing-thawing. SP-HBPs were purified from pooled seminal plasma by heparin affinity chromatography. Three doses of SP-HBPs i.e. 10, 20, 40 μg/mL semen were standardized to find out the optimum dose and 20 μg/mL was found to be an optimum dose. Semen as such and treated with SP-HBPs was diluted with sodium citrate-egg yolk diluter and cryopreserved as per the standard protocol. Sperm parameters i.e. motility, viability, Hypo-osmotic swelling test (HOST), acrosome damage, in vitro capacitation and lipid peroxidation were evaluated in SP-HBP treated and untreated (control) semen at both phases of cryopreservation. A considerable variation in percent sperm motility, viability, membrane integrity (HOST), acrosome damage, acrosome reaction and lipid peroxidation was observed at both phases among the bulls irrespective of the treatment. Incubation of neat semen with 20 μg/mL SP-HBP before processing for cryopreservation enhanced the average motility, viability, membrane integrity by 7.2%, 1.5%, 7.9%, and 5.6%, 6.6%, 7.4% in pre-frozen and frozen-thawed semen in comparison to control. There was also an average increase of 4.1%/3.9% in in vitro capacitation and acrosome reaction in SP-HBPs-treated frozen-thawed semen as compared to control. However, binding of SP-HBPs to the sperm declined acrosome damage and lipid peroxidation by 1.3%/4.1% and 22.1/32.7 μM/109 spermatozoa in SP-HBP treated pre-frozen/frozen-thawed semen as compared to control, respectively. Significant (p<0.05) effects were observed only in motility, HOST and in vitro acrosome reaction. It can be concluded that treatment of neat semen with SP-HBPs before cryopreservation minimized the cryoinjury by decreasing the generation of reactive oxygen species.

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Cryopreservation increases coating of bull sperm by seminal plasma binder of sperm proteins BSP1, BSP3, and BSP5

Cited by 39 publications

References 51 publications

Cooperative roles of biological flow and surface topography in guiding sperm migration revealed by a microfluidic model

Cooperative roles of biological flow and surface topography in guiding sperm migration revealed by a microfluidic model

Proteomic identification of cryostress in epididymal spermatozoa

Seminal Plasma Heparin Binding Proteins Improve Semen Quality by Reducing Oxidative Stress during Cryopreservation of Cattle Bull Semen

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