Implication of the human Binder of SPerm Homolog 1 (BSPH1) protein in capacitation
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Abstract:
Binder of SPerm (BSP) proteins are a family of proteins expressed exclusively in the male reproductive tract (seminal vesicles or epididymis) of several mammalian species. They are known to promote capacitation, a sperm maturation step essential for fertilization. Our recent studies have shown that in human, the Binder of SPerm Homolog 1 (BSPH1) is expressed solely in epididymal tissues. The goal of the current study was to characterize BSPH1 and evaluate its effect on different sperm functions. A human recombinant BSPH1 (rec-BSPH1) was produced, purified and refolded. Rec-BSPH1 was found to share many characteristics with other members of the BSP superfamily, as it was able to bind gelatin and heparin as well as capacitate sperm. Rec-BSPH1 had no effect on sperm acrosome reaction or any sperm motility parameters. Native BSPH1 was localized on the equatorial segment, post-acrosomal segment and neck of ejaculated human sperm. Rec-BSPH1, following incubation with washed ejaculated human sperm, exhibited binding patterns similar to the native protein. These results show that the human epididymal BSPH1 shares many biochemical and functional characteristics with BSP proteins secreted by seminal vesicles of ungulates, and behaves similarly to its murine epididymal orthologue BSPH1. This study of human BSPH1 brings us one step closer to understanding the importance of this protein in male fertility.Keywords:
Capacitation
Acrosome reaction
Hyperactivation
Acrosome reaction
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Acrosome reaction
Capacitation
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Capacitation
Acrosome reaction
Hyperactivation
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Capacitation
Acrosome reaction
Bovine serum albumin
Hyperactivation
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Capacitation
Acrosome reaction
Phalloidin
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Abstract Hamster epididymal spermatozoa were isolated in the caput, corpus and cauda regions for one, two and three days. Sperm suspensions from these regions were assessed for morphology, motility, viability; and for fertility by A.I. The ability to capacitate was tested by checking for acrosome reactions when the sperm were cultured under defined capacitating conditions at 37°C in vitro. Normal, mature cauda sperm were highly fertile (overall 77% of ova fertilized) and showed 50–80% incidence of acrosome reactions after six hours in culture. Isolation for up to three days had no effect. Immature sperm from the caput and corpus were poorly motile, infertile, and did not manifest an acrosome reaction. Isolation for one and two days produced improvements in motility, and distal migration of the cytoplasmic droplet akin to normal maturation, however the sperm remained infertile and did not capacitate in vitro. Survival after three days isolation was poor. Thus the development of fertilizing ability in hamster epididymal spermatozoa is closely related to the ability to manifest an acrosome reaction in vitro; however it is only poorly correlated with motility and morphology. Completion of sperm maturation in this species appears to require the environment of the cauda epididymidis.
Acrosome reaction
Mesocricetus
Capacitation
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There are many protocols for horse sperm cryopreservation, but results are inconsistent; sperm survival after freeze-thawing is usually poor; in consequence, fertility is low. The objective of this work was to see whether slow cooling before freezing to minus 3 °C instead of +5 °C, the traditional target temperature, could improve horse sperm cryosurvival, capability to carry out capacitation and the acrosome reaction induced by progesterone. Spermatozoa from five stallions were packaged in straws and slowly cooled to +5 °C. Half of the straws were frozen directly and the other half was further cooled to −3 °C before freezing. Progressive motility, viability, plasma membrane integrity, acrosome integrity and capacitation status were assessed. After thawing, there were no differences between cooling treatments on motility, viability, acrosome integrity and capacitation status; however, there was difference (P < 0.05) regarding plasma membrane integrity. Acrosome integrity decreased as incubation, without or with progesterone (2 μg ml−1), progressed, but there were no differences between cooling treatments regardless of progesterone. Both capacitated and acrosome-reacted spermatozoa increased as incubation progressed, but there were no differences between cooling treatments regardless of progesterone. Slow cooling to −3 °C before freezing did not improve horse sperm cryosurvival or capability to undergo the acrosome reaction.
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Ejaculated mammalian sperm must undergo a maturation process called capacitation before they are able to fertilize an egg. Several studies have suggested a role for members of the secreted phospholipase A2 (sPLA2) family in capacitation, acrosome reaction (AR), and fertilization, but the molecular nature of these enzymes and their specific roles have remained elusive. Here, we have demonstrated that mouse group X sPLA2 (mGX) is the major enzyme present in the acrosome of spermatozoa and that it is released in an active form during capacitation through spontaneous AR. mGX-deficient male mice produced smaller litters than wild-type male siblings when crossed with mGX-deficient females. Further analysis revealed that spermatozoa from mGX-deficient mice exhibited lower rates of spontaneous AR and that this was associated with decreased in vitro fertilization (IVF) efficiency due to a drop in the fertilization potential of the sperm and an increased rate of aborted embryos. Treatment of sperm with sPLA2 inhibitors and antibodies specific for mGX blocked spontaneous AR of wild-type sperm and reduced IVF success. Addition of lysophosphatidylcholine, a catalytic product of mGX, overcame these deficiencies. Finally, recombinant mGX triggered AR and improved IVF outcome. Taken together, our results highlight a paracrine role for mGX during capacitation in which the enzyme primes sperm for efficient fertilization and boosts premature AR of a likely phospholipid-damaged sperm subpopulation to eliminate suboptimal sperm from the pool available for fertilization.
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The conditions for stimulation of in vitro capacitation and the acrosome reaction of ejaculated buffalo sperm has been determined. Washed ejaculated sperm were successfully capacitated in BWW medium supplemented with bovine serum albumin (BSA) and a sperm motility factor(s) (SMF(s) isolated from the adrenal glands of rats. The acrosome reaction was induced in capacitated sperm by introducing Ca ++ ions (final concentration 5 mM) into the medium. Supplementation of BWW medium with SMF(s) in the presence of BSA significantly increased the percentage of sperm showing capacitation and the acrosome reaction. SMF(s) also significantly increased the percentage motility, the percentage forward motility and maintained a higher percentage of live sperm in BWW medium under the conditions used in this study. The significance of the present findings is discussed.
Capacitation
Acrosome reaction
Bovine serum albumin
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