Alterations to the Bull Sperm Surface Proteins That Bind Sperm to Oviductal Epithelium1

Hung, Pei-Hsuan; Suárez, Susan S.

doi:10.1095/biolreprod.112.099721

Cited by 39 publications

(41 citation statements)

References 62 publications

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“…Indeed, our results show a positive effect of temperature on SOD and GPX1 activity that at the same time seems to have an indirect effect on sperm quality likely to maintain a constant fitness for reproductive success ( Figure 6). Addition of SP in a range of 5-50% (v/v) to the extender minimized cryopreservation-induced membrane damage [5,9,38] or early onset of acrosome responsiveness post-thaw [16,38] due to stabilizing proteins or antioxidant enzymes in SP that provide protection to the sperm cells [6,13,31]. Results in our study indicate that addition of SP to frozen-thawed semen ameliorated the negative effects of cryopreservation compared with control sperm as reflected in higher EN as well as HOST percent values (Figures 7 and 8).…”

Section: Discussionmentioning

confidence: 99%

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Antioxidant Effects of Seminal Plasma on Cellular Morphological Viability of Swine Semen Post-Cryopreservation

Barrientos¹

2015

J Veterinar Sci Technol

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The aims of this study were to measure the antioxidant enzyme activity of superoxide dismutase (SOD) and glutathione peroxidase (GPX1) in seminal plasma (SP), the influence of temperature overtime on such enzymes and, to assess post-thaw viability of semen supplemented with autologous or homologous SP by eosin-nigrosin (EN) and hypoosmotic tests (HOST). A total of 48 sperm-rich fractions from 8 boars were collected and equally divided for SP antioxidant activity determination or cryopreservation experiments. Marked differences in SP antioxidant activity were found amongst individuals. SOD values ranged from 7.88 ± 0.04 U/g to 12.01 ± 0.07 U/g. Restricted maximum likelihood variance components estimates (REML) indicated that 98% of the variation resided between individuals (p<0.05). In addition, GPX1 activity ranged from 0.03 ± 0.001 U/g to 0.05 ± 0.005 U/g with a REML between and within individual of 58% and 42%, respectively (p<0.05). Further, temperature largely influenced SOD and GPX1 activity (Spearman's ρ ≥ 0.77; main effect p<0.01). Regardless, sperm viability improved significantly in groups supplemented with 20% (v/v) SP compared with control as per EN 27 ± 0.59 % vs. 26 ± 0.23 % or HOST 28 ± 0.27 % vs. 18 ± 0.27 % (p<0.05). Although there was an additive effect of SP on sperm viability, the antioxidant levels were not strongly correlated to sperm morphology. Therefore, other factors in seminal plasma are contributing to sperm viability and overall fitness towards a successful fertilization.

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Section: Discussionmentioning

confidence: 99%

“…The protective effects of SP may be attributed to critical components such as antioxidant enzymes and other stabilizing proteins capable of modulating sperm function [12][13][14]. However, SP is removed prior cryopreservation to dilute the semen at a specific concentration in the extender.…”

Section: Introductionmentioning

confidence: 99%

Antioxidant Effects of Seminal Plasma on Cellular Morphological Viability of Swine Semen Post-Cryopreservation

Barrientos¹

2015

J Veterinar Sci Technol

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“…This binding inhibits premature capacitation and enhances the viability of spermatozoa [41,42]. Further to this, BSP1 has been shown to remain present on spermatozoa even after capacitation, suggesting a function in the binding of spermatozoa to the epithelium of the ampulla [43]. More work is required in order to know mechanisms underlying the actions performed by GBPs during sperm reservoir formation.…”

Section: Establishment Of Sperm Reservoir In Oviductmentioning

confidence: 96%

“…The exact molecular mechanism by which the reversal of these deleterious effects during cryopreservation is achieved is not fully understood. In several studies, it has been reported that SP proteins are adsorbed onto the surfaces of boar spermatozoa and that this may allow damaged spermatozoa surfaces to retain their original shape during cryopreservation [43,50].…”

Section: Cryopreservationmentioning

confidence: 99%

Gelatin Binding Proteins in Reproductive Physiology

Kumar¹,

Tinson²,

Mulligan³

et al. 2016

Indian J Microbiol

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In order to advance the assisted reproductive technologies used in animals and human beings, it is important to accumulate basic informations about underlying molecular mechanisms that shape the biological processes of reproduction. From within seminal plasma, proteins perform a wide variety of distinct functions that regulate major reproductive events such as fertilization. The ability of such proteins to bind and interact with different antagonistic ions and biomolecules such as polysaccharides, lipids, and other proteins present in the male and female reproductive tract define these capabilities. Over the last two decades, extensive work has been undertaken in an attempt to define the role of seminal plasma proteins, of which, Gelatin binding proteins (GBPs) represent a large family. GBPs comprise of known group of Bovine seminal plasma (BSP) protein family, matrix metallo proteinases (MMP 2 and MMP 9) and fibronectin, which have been widely studied. The presence of a type II repeat is a characteristic feature of GBPs, which is similar in structure to the fibronectin type II domain (fn2), which has ability to bind multiple ligands including gelatin, glycosaminoglycans, choline phospholipids, and lipoproteins. Two fn2 domains are present within the BSP protein family, while, three fn2 domains are found in gelatinases (MMP-2 and MMP9), and ELSPBP1 (Epididymosomes Transfer Epididymal Sperm Binding Protein 1) contains four long fn2 domains. For the most part BSP proteins are exclusively expressed in seminal vesicles although mBSPH1, mBSPH2 and hBSPH1 are all expressed in the epididymis. The expression of gelatinases has been demonstrated in several organs and tissues such as the prostate, testis, epididymis, ovary, human placenta, cervix and endometrial wall. This review intends to bring current updates on the role of GBPs in reproductive physiology to light, which may act as basis for future studies on GBPs.

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“…To achieve this physiological process in bovine sperm by heparin requires heparin binding to sperm and the culture media must contain HCO 3− , Ca 2+ and have a pH of 7.0 or greater for at least 4 h during in vitro incubation conditions (Bergqvist et al, 2007). Thus, heparin is considered a physiological capacitation inducer in bovine sperm and for instance a strong inducer of the acrosome reaction (Hung and Suarez, 2012). Understanding the specific role of biophysical factors is important for fertility investigations and for improving the success of assisted reproductive technologies.…”

Section: Introductionmentioning

confidence: 99%

Sperm volumetric dynamics during in vitro capacitation process in bovine spermatozoa

García-Herreros

Leal

2015

Animal

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Previous studies have demonstrated that sperm head morphometry can be used as a potential diagnostic tool for detecting biophysical changes associated with sperm viability in bovine spermatozoa. In this study, sperm head morphometry was used to investigate its value as a biophysical marker for detecting volumetric changes in bovine spermatozoa under in vitro capacitating and non-capacitating incubation conditions. To further test this hypotesis, aliquots of pooled, washed bovine sperm were incubated in either Tyrode's complete medium with heparin (TCMH; a capacitating medium containing Ca 2+ , NaHCO 3 and heparin), Tyrode's complete medium heparin-free (TCM; a medium containing just Ca 2+ and NaHCO 3 ) or Tyrode's basal medium (TBM; a non-capacitating medium free of Ca 2+ , NaHCO 3 and heparin, used as control). Aliquots of sperm were processed for morphometric analysis at different incubation-time intervals (0, 3 and 6 h at 38°C), and the chlortetracycline assay was used simultaneously to confirm the ability of the sperm to undergo capacitation (B pattern) and the acrosome reaction (AR pattern) status in each medium. After 3 h of incubation under TCMH conditions, a significant increase was observed in the percentage of B and AR patterns and a significant decrease was found in all sperm morphometric parameters ( P < 0.01). Interestingly, after 6 h of incubation in TCMH, the percentage of B and AR patterns increased drastically over time and marked differences were found in the dimensional and shape parameters, which were significantly smaller compared with TBM or TCM media ( P < 0.001). Significant correlations were observed between sperm size and AR pattern (r = −0.875, P < 0.01). In conclusion, sperm head morphometry can be used as a potential biophysical marker for detecting volumetric changes during capacitation process in bovine spermatozoa.

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Alterations to the Bull Sperm Surface Proteins That Bind Sperm to Oviductal Epithelium1

Cited by 39 publications

References 62 publications

Antioxidant Effects of Seminal Plasma on Cellular Morphological Viability of Swine Semen Post-Cryopreservation

Antioxidant Effects of Seminal Plasma on Cellular Morphological Viability of Swine Semen Post-Cryopreservation

Gelatin Binding Proteins in Reproductive Physiology

Sperm volumetric dynamics during in vitro capacitation process in bovine spermatozoa

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