The Addition of Mitogen-Activated Protein Kinase and p34cdc2Kinase Substrate Peptides Inhibits the Flagellar Motility of Demembranated Fowl Spermatozoa

Ashizawa, Koji; Hashimoto, Kei; Higashio, Mari; Tsuzuki, Yasuhiro

doi:10.1006/bbrc.1997.7626

Cited by 34 publications

(25 citation statements)

References 38 publications

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“…This conclusion is also supported by the evidence that MAP kinase is localized in the neck and tail of ejaculated human sperm, and that PD 098059, a specific MEK inhibitor, reduced sperm motility [21]. Phosphorylation of axonemal and/or accessory cytoskeletal protein mediated by MAP kinases and p34 cdc2 kinase may be involved in the regulation of flagellar movement of foul sperm [3].…”

mentioning

confidence: 72%

Expression and Phosphorylation of Mitogen-Activated Protein Kinases During Spermatogenesis and Epididymal Sperm Maturation in Mice

Lü

Sun

Breitbart

et al. 1999

Archives of Andrology

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mentioning

confidence: 72%

Expression and Phosphorylation of Mitogen-Activated Protein Kinases During Spermatogenesis and Epididymal Sperm Maturation in Mice

Lü

Sun

Breitbart

et al. 1999

Archives of Andrology

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“…The role of ERK in sperm motility is controversial. A positive role for ERK was suggested in fowl sperm (43). ERK was shown to be gradually activated throughout the transition of mouse spermatozoa from the caput (immotile) to the vas deferens (fully motile) (10).…”

Section: Discussionmentioning

confidence: 99%

Identification of Extracellular Signal-regulated Kinase 1/2 and p38 MAPK as Regulators of Human Sperm Motility and Acrosome Reaction and as Predictors of Poor Spermatozoan Quality

Almog

Lazar

Reiss

et al. 2008

Journal of Biological Chemistry

106

127

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Mature spermatozoa acquire progressive motility only after ejaculation. Their journey in the female reproductive tract also includes suppression of progressive motility, reactivation, capacitation, and hyperactivation of motility (whiplash), the mechanisms of which are obscure. MAPKs are key regulatory enzymes in cell signaling, participating in diverse cellular functions such as growth, differentiation, stress, and apoptosis. Here we report that ERK1/2 and p38 MAPK are primarily localized to the tail of mature human spermatozoa. Surprisingly, c-Jun N-terminal kinase 1/2, which is thought to be ubiquitously expressed, could not be detected in mature human spermatozoa. ERK1/2 stimulation is downstream to protein kinase C (PKC) activation, which is also present in the human sperm tail (PKC␤I and PKC⑀). ERK1/2 stimulates and p38 inhibits forward and hyperactivated motility, respectively. Both ERK1/2 and p38 MAPK are involved in the acrosome reaction. Using a proteomic approach, we identified ARHGAP6, a RhoGAP, as an ERK substrate in PMA-stimulated human spermatozoa. Inverse correlation was obtained between the relative expression level of ERK1 or the relative activation level of p38 and sperm motility, forward progression motility, sperm morphology, and viability. Therefore, increased expression of ERK1 and activated p38 can predict poor human sperm quality.

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“…Ashizawa et al [17,29] showed the presence of PKC in avian spermatozoa and showed its possible inhibitory effect on the acrosome reaction. The same authors also suggested the existence of MAPK in chicken spermatozoa by indirect measurement of activity [22]. However, studies of the signaling pathways involved in the induction of the acrosome reaction are still very incomplete in this species, despite major interest in understanding the internal fertilization process.…”

Section: Discussionmentioning

confidence: 99%

“…These include PKA, PIK3, MAPK3/1, and MAPK14 in mammals [20,21]. In the chicken, MAPK/p34 cdc2 substrate has been reported to inhibit flagellar motility of demembranated chicken spermatozoa, suggesting a positive role for MAPK3/1 in motility [22]. In contrast, PKC could negatively regulate the motility of chicken spermatozoa [17].…”

Section: Introductionmentioning

confidence: 99%

Potential Involvement of Several Signaling Pathways in Initiation of the Chicken Acrosome Reaction1

Lemoine¹,

Dupont²,

Guillory³

et al. 2009

Biology of Reproduction

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Avian sperm biology has demonstrated specific features in preparation for fertilization. For example, capacitationlike processes and motility hyperactivation do not exist in the form described in mammals. The present study investigated the potential involvement of several signaling pathways, including protein kinase A (PKA), phosphatidylinositol 3 kinase (PIK3), mitogen-activated protein kinase 3/1 (MAPK3/1), and MAPK14 in the chicken acrosome reaction (AR). The presence in chicken spermatozoa of key proteins involved in these signaling pathways (i.e., cAMP-responsive element-binding protein [CREB], AKT, MAPK1, and MAPK14 and their respective phosphorylated forms) was detected using immunoblotting and localized by immunocytochemistry, mainly in the heads. The potential involvement of these pathways in the AR induced by inner perivitelline layer (IPVL) and Ca(2+) was then examined using specific inhibitors and phosphorylation status measurements. The effects of the specific inhibitors on motility were also measured. Phosphorylations of AKT, CREB, and MAPK1, but not MAPK14, were increased at the time of AR. Phosphorylation of AKT was increased in the presence of IPVL alone, whereas both IPVL and Ca(2+) were needed to increase CREB and MAPK1 phosphorylations. Inhibition of the three corresponding pathways blocked the increase in phosphorylation and significantly decreased AR. Inhibitions of the PKA and MAPK1 pathways also significantly decreased motility, whereas MAPK14 and PIK3 inhibition had no effect on motility. Our results suggest that the AR could be mediated by activation of the PKA, PIK3, and MAPK1 pathways through a sequential action involving, successively, PIK3 and then PKA and MAPK1 activations.

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The Addition of Mitogen-Activated Protein Kinase and p34cdc2Kinase Substrate Peptides Inhibits the Flagellar Motility of Demembranated Fowl Spermatozoa

Cited by 34 publications

References 38 publications

Expression and Phosphorylation of Mitogen-Activated Protein Kinases During Spermatogenesis and Epididymal Sperm Maturation in Mice

Expression and Phosphorylation of Mitogen-Activated Protein Kinases During Spermatogenesis and Epididymal Sperm Maturation in Mice

Identification of Extracellular Signal-regulated Kinase 1/2 and p38 MAPK as Regulators of Human Sperm Motility and Acrosome Reaction and as Predictors of Poor Spermatozoan Quality

Potential Involvement of Several Signaling Pathways in Initiation of the Chicken Acrosome Reaction1

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