Tyrosine phosphorylation of a 38‐kDa capacitation‐associated buffalo (<i>Bubalus bubalis</i>) sperm protein is induced by <scp>L</scp>‐arginine and regulated through a cAMP/PKA‐independent pathway

Roy, Sudhir C.; Atreja, S. K.

doi:10.1111/j.1365-2605.2007.00745.x

Cited by 32 publications

(22 citation statements)

References 44 publications

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“…2). Such a dose-dependent increase of broadly distributed protein tyrosine phosphorylation during sperm capacitation has also been reported in cattle and buffalo, by using other capacitation inducers [20, 21, 24, 25]. It has been accepted that cAMP elevation and subsequent PKA activation is necessary for protein tyrosine phosphorylation in sperm [26].…”

Section: Discussionmentioning

confidence: 75%

Exogenous neurotensin modulates sperm function in Japanese Black cattle

Umezu

Hiradate

Oikawa³

et al. 2016

Journal of Reproduction and Development

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Recently, the conception rates after artificial insemination have been pointed out to decline continuously. To overcome this problem, the control of frozen and thawed sperm quality is required. However, the mechanism of bovine sperm functional regulation is still largely unknown. In mammals, the ejaculated sperm are capable of showing fertilizing ability during migration in the female reproductive organs. It is well known that these female organs secrete several factors contributing to sperm capacitation. We previously reported that neurotensin (NT) secreted from the oviduct and cumulus cells enhanced sperm capacitation and acrosome reaction in mice. In this study, we confirmed the expression of the NT receptor (NTR1) in the bovine sperm neck region and the secretion of NT in the bovine uterus and oviduct. The similar expression patterns of NT and NTR1 suggests a conserved mechanism of sperm functional regulation between mouse and cattle. Thus, we examined the effects of exogenous NT on the bovine sperm functions. First, we showed that NT induced sperm protein tyrosine phosphorylation in a dose-dependent manner, suggesting that NT enhances sperm capacitation. Second, we showed that NT induced acrosome reactions of capacitated sperm in a dose-dependent manner, suggesting that NT facilitates acrosome reaction. Finally, we used a computer-aided sperm analysis system to show that NT did not have a great effect on sperm motility. These results suggest that NT acts as a facilitator of sperm capacitation and acrosome reaction in the female reproductive tracts in cattle, highlighting the importance of NT-mediated signaling to regulate sperm functions.

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Section: Discussionmentioning

confidence: 75%

Exogenous neurotensin modulates sperm function in Japanese Black cattle

Umezu

Hiradate

Oikawa³

et al. 2016

Journal of Reproduction and Development

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“…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%

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

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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

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“…14,15 Although both serine/threonine phosphorylation and tyrosine phosphorylation of proteins have been reported in spermatozoa, the tyrosine phosphorylation of a number of protein substrates has been associated with capacitation in the spermatozoa of most mammalian species, and is considered a hallmark event of capacitation. [16][17][18][19][20][21] Several tyrosine phosphoproteins in capacitated buffalo and cattle spermatozoa were identified using 2D immunoblotting and mass spectrometry. These include serine/threonine-protein phosphatase PP1c2 catalytic subunit, the MGC157332 protein, alpha-enolase, 3-oxoacid CoA transferase 2 and actin-like protein 7A.…”

Section: Protein Tyrosine Phosphorylationmentioning

confidence: 99%

Mechanism of sperm capacitation and the acrosome reaction: role of protein kinases

Ickowicz¹,

Finkelstein²,

Breitbart³

2012

Asian J Androl

204

130

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Mammalian sperm must undergo a series of biochemical and physiological modifications, collectively called capacitation, in the female reproductive tract prior to the acrosome reaction (AR). The mechanisms of these modifications are not well characterized though protein kinases were shown to be involved in the regulation of intracellular Ca 21 during both capacitation and the AR. In the present review, we summarize some of the signaling events that are involved in capacitation. During the capacitation process, phosphatidyl-inositol-3-kinase (PI3K) is phosphorylated/activated via a protein kinase A (PKA)-dependent cascade, and downregulated by protein kinase C a (PKCa). PKCa is active at the beginning of capacitation, resulting in PI3K inactivation. During capacitation, PKCa as well as PP1c2 is degraded by a PKA-dependent mechanism, allowing the activation of PI3K. The activation of PKA during capacitation depends mainly on cyclic adenosine monophosphate (cAMP) produced by the bicarbonate-dependent soluble adenylyl cyclase. This activation of PKA leads to an increase in actin polymerization, an essential process for the development of hyperactivated motility, which is necessary for successful fertilization. Actin polymerization is mediated by PIP 2 in two ways: first, PIP 2 acts as a cofactor for phospholipase D (PLD) activation, and second, as a molecule that binds and inhibits actin-severing proteins such as gelsolin. Tyrosine phosphorylation of gelsolin during capacitation by Src family kinase (SFK) is also important for its inactivation. Prior to the AR, gelsolin is released from PIP 2 and undergoes dephosphorylation/activation, resulting in fast F-actin depolymerization, leading to the AR.

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Tyrosine phosphorylation of a 38‐kDa capacitation‐associated buffalo (Bubalus bubalis) sperm protein is induced by L‐arginine and regulated through a cAMP/PKA‐independent pathway

Cited by 32 publications

References 44 publications

Exogenous neurotensin modulates sperm function in Japanese Black cattle

Exogenous neurotensin modulates sperm function in Japanese Black cattle

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

Mechanism of sperm capacitation and the acrosome reaction: role of protein kinases

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