Reactive oxygen species promote tyrosine phosphorylation and capacitation in equine spermatozoa

Baumber, Julie; Sabeur, Khalida; Vo, Anthony; Ball, Barry A.

doi:10.1016/s0093-691x(03)00144-4

Cited by 109 publications

(67 citation statements)

References 29 publications

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“…The characterization of NOX5 and its putative role in ROS production are important to understand the relationship between the redox state and the biological function of sperm. A growing body of evidence indicates a role for ROS in a variety of sperm functions, including capacitation (Leclerc et al 1997), tyrosine phosphorylation (Aitken et al 1996, Leclerc et al 1997, Baumber et al 2003, O'Flaherty et al 2006, chromatin condensation (Godeas et al 1997), regulation of intracellular pH ) and acrosomal exocytosis (Rivlin et al 2004). Several studies including ours (Aitken & Clarkson 1987, Aitken et al 1995, Tselkas et al 2000, O'Flaherty et al 2003, Sabeur & Ball 2006 have shown that mammalian spermatozoa are capable of generating ROS but the biochemical mechanisms by which ROS are generated in mammalian spermatozoa are not fully understood.…”

Section: Discussionmentioning

confidence: 99%

“…Several laboratories have shown that sperm capacitation, hyperactivation, acrosomal exocytosis, nuclear condensation and mitochondrial stability are redox-regulated events (De Lamirande & Gagnon 1993a, 1993b, Aitken et al 1995, 1998, Baumber et al 2003. Although a number of studies define an important role for ROS generation in the regulation of sperm function, the mechanism(s) responsible for the production of ROS by spermatozoa remains controversial (Baker et al 2003, Ford 2004.…”

Section: Introductionmentioning

confidence: 99%

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Characterization of NADPH oxidase 5 in equine testis and spermatozoa

Sabeur¹,

Ball²

2007

Reproduction

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Reactive oxygen species (ROS) play an important role in normal sperm function, and spermatozoa possess specific mechanisms for ROS generation via an NAD(P)H-dependent oxidase. The aim of this study was to identify the presence of an NADPH oxidase 5 (NOX5) in equine testis and spermatozoa. The mRNA of NOX5 was expressed in equine testis as detected by northern blot probed with human NOX5 cDNA and by RT-PCR. Immunoblotting with affinity purified a-NOX5 revealed one major protein in equine testis and other tissues. Immunolocalization of NOX5 showed labeling over the rostral sperm head with some labeling in the equatorial and post-acrosomal regions. In the testis, there was abundant staining in the adluminal region of the seminiferous tubules associated with round and elongating spermatids. The RT-PCR and sequence analysis revealed a high homology with human NOX5. This study demonstrates that NOX5 is present in equine spermatozoa and testes and therefore represents a potential mechanism for ROS generation in equine spermatozoa.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterization of NADPH oxidase 5 in equine testis and spermatozoa

Sabeur¹,

Ball²

2007

Reproduction

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“…Among all the ROS produced by equine sperm, hydrogen peroxide has been claimed to be the most harmful being involved in enhanced acrosome reaction and induction PY induction in fresh equine sperm (Baumber et al, 2003b) and has also been shown to affect detrimentally the motility of fresh equine sperm (Baumber et al, 2000). It has also been demonstrated that ROS addition was associated with a marked increase of protein tyrosine phosphorylation (PY) in fresh equine semen (Baumber et al, 2003b). PY has been related to sperm fertilization ability and, more specifically, is known to be a final hallmark of mammalian sperm capacitation (Visconti et al, 1995).…”

Section: Semen Collection and Processingmentioning

confidence: 99%

Effect of genistein addition to equine sperm freezing extender

Macías‐García

Guimarães

Lopes

et al. 2018

J Hellenic Vet Med Soc

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Cryopreservation negatively affects equine sperm quality post-thaw: an excessive release of reactive oxygen species (ROS) and increased protein tyrosine phosphorylation (known as cryocapacitation) have been demonstrated in frozenthawed equine sperm diminishing its lifespan. The objective of this study was to determine the possible beneficial effect of genistein addition (a ROS scavenger and protein tyrosine kinase inhibitor) to a commercial freezing extender. Equine sperm were frozen in the presence of different genistein concentrations ranging from 0 to 800 μM. After thawing, the sperm viability (eosinnigrosin), acrosome integrity using peanut agglutinin (PNA), protein tyrosine phosphorylation (PY) and motility were assessed at times 0 and 1 hr. In addition PY was studied in fresh and frozen sperm incubated in Modified Whitten’s (MW) medium with 25 mM Bicarbonate (MW+Bic). Genistein did not affect the viability, total or progressive motility or acrosome status of frozenthawed equine sperm. Immediately after thawing, positive PY staining in the equatorial band was observed and genistein addition did not exert any change in PY. Fresh sperm incubated in MW+Bic showed a significant increase in PY staining along the tail compared to frozen-thawed sperm. In our study sperm viability immediately post-thaw was 58.25% ± 5.35 and progressive motility 14.46% ± 5.7 (mean ± S.E.M.) and genistein did not improve the post-thaw quality of equine sperm. In addition, cryopreservation did not induce PY immediately post-thaw or enhanced frozen-thawed equine sperm susceptibility to PY induction.

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“…This suggests a role of reactive oxygen species (ROS) in sperm protein phosphorylation and capacitation. Reactive oxygen species have been shown to promote capacitation in hamster [Bize et al 1991], murine [Ecroyd et al 2003], rat [Lewis and Aitkent 2001], horse [Baumber et al 2003], ram and bull [Brener et al 2003] spermatozoa. Controversy surrounds the concept of whether spermatozoa are capable of producing ROS.…”

Section: Protein Phosphorylationmentioning

confidence: 99%

Current Concepts of Molecular Events During Bovine and Porcine Spermatozoa Capacitation

Vadnais

Galantino‐Homer

Althouse

2007

Archives of Andrology

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Spermatozoa are required to undergo the processes of capacitation before they obtain fertilizing ability. The molecular changes of capacitation are still not fully understood. However, it is accepted that capacitation is a sequential process involving numerous physiological changes including destabilization of the plasma membrane, alterations of intracellular ion concentrations and membrane potential, and protein phosphorylation. There are no known morphological changes that occur to the spermatozoon during capacitation. The purpose of this review is to summarize current evidence on the molecular aspects of capacitation both in vivo and in vitro in bovine and porcine spermatozoa. For the purpose of this review, the process of sperm capacitation will encompass maturational events that occur following ejaculation up to binding to the zona pellucida, that triggers acrosomal exocytosis and initiates fertilization.

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Reactive oxygen species promote tyrosine phosphorylation and capacitation in equine spermatozoa

Cited by 109 publications

References 29 publications

Characterization of NADPH oxidase 5 in equine testis and spermatozoa

Characterization of NADPH oxidase 5 in equine testis and spermatozoa

Effect of genistein addition to equine sperm freezing extender

Current Concepts of Molecular Events During Bovine and Porcine Spermatozoa Capacitation

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