Inhibition of phosphatidylinositol 3-kinase modifies boar sperm motion parameters

Aparicio, I.M.; Gil, María Concepción Robles; García-Herreros, Manuel; Peña, Fernando J.; García‐Marín, Luis J.

doi:10.1530/rep.1.00447

Cited by 41 publications

(34 citation statements)

References 30 publications

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“…2). As previously described (Aparicio et al 2005), our results showed that incubation with 8Br-cAMP induced, in porcine spermatozoa, a significant increase in the percentage of rapid-and mediumspeed spermatozoa and in the curvilinear velocity (VCL), straight linear velocity (VSL), average path velocity (VAP), linearity coefficient (LIN), and wobble coefficient (WOB). In these conditions, no significant effects were detected in the percentage of static and low-speed spermatozoa and in the straightness (STR), amplitude of lateral head displacement (ALH) and frequency of head displacement (or beat crossfrequency, BCF), when compared with porcine spermatozoa incubated at 38 8C in TBM alone (Table 2).…”

Section: Identification Of Gsk3 Protein In Porcine Spermatozoasupporting

confidence: 85%

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Porcine sperm motility is regulated by serine phosphorylation of the glycogen synthase kinase-3α

Aparicio¹,

Bragado²,

Gil³

et al. 2007

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Sperm functions are critically controlled through the phosphorylation state of specific proteins. Glycogen synthase kinase-3 (GSK3) is a serine/threonine kinase with two different isoforms (a and b), the enzyme activity of which is inhibited by serine phosphorylation. Recent studies suggest that GSK3 is involved in the control of bovine sperm motility. Our aim was to investigate whether GSK3 is present in porcine spermatozoa and its role in the function of these cells. This work shows that both isoforms of GSK3 are present in whole cell lysates of porcine sperm and are phosphorylated on serine in spermatozoa stimulated with the cAMP analog, 8Br-cAMP. A parallel increase in serine phosphorylation of the isoform GSK3a, but not in the isoform GSK3b, is observed after treatments that also induce a significant increase in porcine sperm velocity parameters. Therefore, a significant positive correlation among straight-line velocity, circular velocity, average velocity, rapid-speed spermatozoa, and GSK3a serine phosphorylation levels exists. Inhibition of GSK3 activity by alsterpaullone leads to a significant increase in the percentage of rapid-and medium-speed spermatozoa as well as in all sperm velocity parameters and coefficients. Moreover, pretreatment of porcine spermatozoa with alsterpaullone significantly increased the percentage of capacitated porcine spermatozoa and presents no effect in the number of acrosome-reacted porcine spermatozoa. Our work suggests that the isoform GSK3a plays a negative role in the regulation of porcine sperm motility and points out the possibility that sperm motile quality might be modulated according the activity state of GSK3a. Reproduction (2007) 134 435-444

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Section: Identification Of Gsk3 Protein In Porcine Spermatozoasupporting

confidence: 85%

“…Spermatozoa-capacitating medium, Tyrode's complete medium (TCM; Aparicio et al 2005),which consisted of 96 mM NaCl, 4.7 mM KCl, 0.4 mM MgSO 4 , 0.3 mM NaH 2 PO 4 , 5.5 mM glucose, 1 mM sodium pyruvate, 21.6 mM sodium lactate, 1 mM CaCl 2 , 10 mM NaHCO 3 , 20 mM HEPES (pH 7.45), and 3 mg/ml BSA. TCM was equilibrated with 5% CO 2 .…”

Section: Mediamentioning

confidence: 99%

Porcine sperm motility is regulated by serine phosphorylation of the glycogen synthase kinase-3α

Aparicio¹,

Bragado²,

Gil³

et al. 2007

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“…The inhibition of PIK3CA increases cAMP levels and tyrosine phosphorylation of the PKA-anchoring protein AKAP3 in human spermatozoa, suggesting a negative role for PI3K in the regulation of motility (Luconi et al 2001, du Plessis et al 2004, Luconi et al 2005. Moreover, studies using pig spermatozoa showed no effect of PIK3CA on the percentage of motile or progressive motile spermatozoa, but showed an increase in sperm velocity (Aparicio et al 2005). In addition, both Wortmannin and LY294002 lack specificity and provoke different responses from spermatozoa (Nauc et al 2004).…”

Section: Discussionmentioning

confidence: 99%

“…Growing evidence suggests that AKT is also involved in the regulation of sperm motility and survival (Aparicio et al 2005, Aquila et al 2007, Parte et al 2012. Although the first component of this pathway, phosphatidylinositide 3-kinase (PIK3CA (PI3K)), has been the subject of several studies in sperm biology, AKT has received insufficient attention despite recent research identifying it as a key factor for sperm survival after ejaculation.…”

Section: Introductionmentioning

confidence: 99%

Phosphorylated AKT preserves stallion sperm viability and motility by inhibiting caspases 3 and 7

Bolaños¹,

Silva²,

Muñoz³

et al. 2014

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AKT, also referred to as protein kinase B (PKB or RAC), plays a critical role in controlling cell survival and apoptosis. To gain insights into the mechanisms regulating sperm survival after ejaculation, the role of AKT was investigated in stallion spermatozoa using a specific inhibitor and a phosphoflow approach. Stallion spermatozoa were washed and incubated in Biggers-Whitten-Whittingham medium, supplemented with 1% polyvinyl alcohol (PVA) in the presence of 0 (vehicle), 10, 20 or 30 mM SH5, an AKT inhibitor. SH5 treatment reduced the percentage of sperm displaying AKT phosphorylation, with inhibition reaching a maximum after 1 h of incubation. This decrease in phosphorylation was attributable to either dephosphorylation or suppression of the active phosphorylation pathway. Stallion spermatozoa spontaneously dephosphorylated during in vitro incubation, resulting in a lack of a difference in AKT phosphorylation between the SH5-treated sperm and the control after 4 h of incubation. AKT inhibition decreased the proportion of motile spermatozoa (total and progressive) and the sperm velocity. Similarly, AKT inhibition reduced membrane integrity, leading to increased membrane permeability and reduced the mitochondrial membrane potential concomitantly with activation of caspases 3 and 7. However, the percentage of spermatozoa exhibiting oxidative stress, the production of mitochondrial superoxide radicals, DNA oxidation and DNA fragmentation were not affected by AKT inhibition. It is concluded that AKT maintains the membrane integrity of ejaculated stallion spermatozoa, presumably by inhibiting caspases 3 and 7, which prevents the progression of spermatozoa to an incomplete form of apoptosis.Free Spanish abstract A Spanish translation of this abstract is freely available at

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“…Tyrode's complete medium (TCM) was used as spermatozoa's capacitating medium (Aparicio et al, 2005) and consisted of 96 mM NaCl, 4.7 mM KCl, 0.4 mM MgSO 4 , 0.3 mM NaH 2 PO 4 , 5.5 mM glucose, 1 mM sodium pyruvate, 21.6 mM sodium lactate, 1 mM CaCl 2 , 10 mM NaHCO 3 , 20 mM HEPES (pH 7.45) and 3 mg/mL BSA. TCM was equilibrated with 95% O 2 and 5% CO 2 .…”

Section: Sperm Incubation Mediamentioning

confidence: 99%

Protein kinase C activity in boar sperm

et al. 2017

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SUMMARYMale germ cells undergo different processes within the female reproductive tract to successfully fertilize the oocyte. These processes are triggered by different extracellular stimuli leading to activation of protein phosphorylation. Protein kinase C (PKC) is a key regulatory enzyme in signal transduction mechanisms involved in many cellular processes. Studies in boar sperm demonstrated a role for PKC in the intracellular signaling involved in motility and cellular volume regulation. Experiments using phorbol 12-myristate 13-acetate (PMA) showed increases in the Serine/Threonine phosphorylation of substrates downstream of PKC in boar sperm. In order to gain knowledge about those cellular processes regulated by PKC, we evaluate the effects of PMA on boar sperm motility, lipid organization of plasma membrane, integrity of acrosome membrane and sperm agglutination. Also, we investigate the crosstalk between PKA and PKC intracellular pathways in spermatozoa from this species. The results presented here reveal a participation of PKC in sperm motility regulation and membrane fluidity changes, which is probably associated to acrosome reaction and to agglutination. Also, we show the existence of a hierarchy in the kinases pathway. Previous works on boar sperm suggest a pathway in which PKA is positioned upstream to PKC and this new results support such model.

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Inhibition of phosphatidylinositol 3-kinase modifies boar sperm motion parameters

Cited by 41 publications

References 30 publications

Porcine sperm motility is regulated by serine phosphorylation of the glycogen synthase kinase-3α

Porcine sperm motility is regulated by serine phosphorylation of the glycogen synthase kinase-3α

Phosphorylated AKT preserves stallion sperm viability and motility by inhibiting caspases 3 and 7

Protein kinase C activity in boar sperm

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