Capacitation Is Associated with Tyrosine Phosphorylation and Tyrosine Kinase-Like Activity of Pig Sperm Proteins1

Tardif, Steve; Dubé, Charlotte; Chevalier, Simone; Bailey, Janice L.

doi:10.1095/biolreprod65.3.784

Cited by 187 publications

(156 citation statements)

References 60 publications

Supporting

Mentioning

136

Contrasting

Unclassified

Order By: Relevance

“…The situation of phosphorylated proteins at the principal piece of the flagellum has been related to motility hyperactivation and to the presence of A-kinase anchoring proteins (which anchor PKA) located in the fibrous sheath of the sperm flagellum in several species (Carrera et al 1996, Mandal et al 1999, Jha & Shivaji 2002a, Pommer et al 2003. Conversely, a capacitation-related redistribution of phosphotyrosine residues to the acrosome has been reported in humans (Naz et al 1991), boars (Tardif et al 2001, Dube et al 2005, bulls (Cormier & Bailey 2003) and buffalo (Roy & Atreja 2008). Moreover, other studies have revealed that certain tyrosine phosphoproteins become localized to the sperm surface overlying the acrosome during capacitation suggesting a key role of these proteins in sperm-zona binding (Asquith et al 2004, Piehler et al 2006.…”

Section: Discussionmentioning

confidence: 99%

“…In addition, a capacitation-associated redistribution of phosphotyrosine residues to the acrosome has been reported in boars (Petrunkina et al 2001, Tardif et al 2001, bulls (Cormier & Bailey 2003) and buffalo (Roy & Atreja 2008), and specific phosphotyrosine proteins localized over the acrosomal region have been postulated to be involved in the zona pellucida interaction and/or fusion events (Leyton & Saling 1989, Naz et al 1991, Ficarro et al 2003, Dube et al 2005.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Changes in content and localization of proteins phosphorylated at tyrosine, serine and threonine residues during ram sperm capacitation and acrosome reaction

Grasa

Colás²,

Gallego³

et al. 2009

Reproduction

View full text Add to dashboard Cite

Previously, we reported the involvement of tyrosine phosphorylation in events that lead to ram sperm capacitation. In this study, we carried out a comparative analysis of the localization of tyrosine, serine and threonine phosphoproteins in different functional stages of ram spermatozoa (after the swim-up procedure, in vitro capacitation, and ionophore-induced acrosome reaction) by immunofluorescence, immunocytochemistry and confocal microscopy. Capacitation increased protein tyrosine, serine and threonine phosphorylation whereas the induction of the acrosome reaction resulted in significantly decreased phosphorylation, mainly in those proteins that increased following capacitation. Control samples showed tyrosine-phosphorylated proteins restricted to the head, mainly distributed at the equatorial region with some cells also displaying an acrosomal and/or post-acrosomal localization. In vitro capacitation promoted both tail and acrosome phosphorylation, and the acrosome reaction induced the loss of labeling on the acrosome and the subsequent increase in the post-acrosomal region and flagellum. The preferential localization of serine-and threonine-phosphorylated proteins in the equatorial and acrosomal regions found in control samples changed during capacitation, which induced tail phosphorylation in a sequential manner. After the acrosome reaction, the labeling of both phosphoamino acids decreased in the acrosome and increased in the post-acrosome. The obtained results were proved by two immunodetection techniques and strengthened by confocal microscopy, and indicate that changes in phosphorylated proteins during capacitation and acrosome reaction of ram spermatozoa may have physiological significance in consolidating certain phosphorylated proteins to specific sperm regions involved in acrosomal exocytosis and zona pellucida recognition, binding and penetration. Reproduction (2009) 137 655-667

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Changes in content and localization of proteins phosphorylated at tyrosine, serine and threonine residues during ram sperm capacitation and acrosome reaction

Grasa

Colás²,

Gallego³

et al. 2009

Reproduction

View full text Add to dashboard Cite

show abstract

“…Only sperm samples with over 95% of the sperm showing progressive motility were used for the experiments. Sperm capacitation was induced according to the method reported by of Tardif et al (2001), with slight modifications. The washed sperm were incubated either in 15 ml of Non-cap medium or in Cap medium (5!10 6 cells/ml) at 37 8C for 3 h in a 5% CO 2 atmosphere.…”

Section: Preparation Of Cauda Epididymal Sperm and Induction Of Capacmentioning

confidence: 99%

Porcine sperm capacitation involves tyrosine phosphorylation and activation of aldose reductase

Katoh¹,

Takebayashi²,

Kikuchi³

et al. 2014

Reproduction

View full text Add to dashboard Cite

Mammalian sperm must be activated in the tubal isthmus through capacitation to induce the acrosome reaction and subsequent fertilization. Although the molecular mechanisms involved in capacitation have yet to be fully elucidated, increased concentrations of reactive oxygen species (ROS) and the extent of tyrosine phosphorylation of proteins have been suggested to play central roles in the completion of capacitation. In this study, aldose reductase was for the first time identified as one of the tyrosine-phosphorylated proteins involved in the capacitation of porcine cauda epididymal sperm. Both tyrosine phosphorylation and activity of aldose reductase associated with the particulate fraction of sperm cells were significantly enhanced during capacitation. Alrestatin, a membranepermeable and specific inhibitor of aldose reductase, plays a role in the inhibition of aldose reductase activity, elevation of intracellular levels of ROS, and induction of hyperactivated motility, all at similar dose dependencies. Alrestatin canceled both the increase in the tyrosine phosphorylation of aldose reductase and the decrease in the glutathione levels in sperm-induced during capacitation. The hyperactivated motility was induced to a higher extent in the presence of glucose than in the presence of fructose. These results indicate that aldose reductase plays an important role in induction of hyperactivation and capacitation of sperm through the elevation of ROS in sperm cells. Furthermore, aldose reductase was shown to be added to sperm during transit through the epididymis, suggesting that aldose reductase is one of the key proteins that support the functional maturation of sperm.

show abstract

“…The noncapacitating medium (NCM) contained 2.7 mM KCl, 1.5 mM KH 2 PO 4 , 8.1 mM Na 2 HPO 4 , 137 mM NaCl, 5.55 mM glucose, and 2 mM pyruvate (pH 7.4). Both media have been described previously (Tardif, 2001). …”

Section: Mediamentioning

confidence: 99%

Effects of Seminal Plasma on Cooling‐Induced Capacitative Changes in Boar Sperm

Vadnais

Roberts

2007

Journal of Andrology

View full text Add to dashboard Cite

Porcine seminal plasma (SP) has been shown to contain factors that have a decapacitative or capacitation-inhibiting effect on sperm. The objectives of the present study were to compare the capacitative changes observed in cooled sperm with those seen in sperm after in vitro capacitation and to determine whether SP could prevent these changes. Sperm were subjected to incubation or to slow cooling under noncapacitating or capacitating conditions. The effect of SP on protein tyrosine phosphorylation and the ability of the sperm to undergo an acrosome reaction (AR) were determined. Cooled sperm displayed an increased level of tyrosine phosphorylation and a higher percentage of induced AR sperm compared to incubated sperm. The addition of SP inhibited the number of ARs that occurred during incubation and cooling. These results suggest that cooling of sperm augments the capacitative changes in sperm, and that SP contains a factor(s) that effectively prevents these changes.

show abstract

Capacitation Is Associated with Tyrosine Phosphorylation and Tyrosine Kinase-Like Activity of Pig Sperm Proteins1

Cited by 187 publications

References 60 publications

Changes in content and localization of proteins phosphorylated at tyrosine, serine and threonine residues during ram sperm capacitation and acrosome reaction

Changes in content and localization of proteins phosphorylated at tyrosine, serine and threonine residues during ram sperm capacitation and acrosome reaction

Porcine sperm capacitation involves tyrosine phosphorylation and activation of aldose reductase

Effects of Seminal Plasma on Cooling‐Induced Capacitative Changes in Boar Sperm

Contact Info

Product

Resources

About