Involvement of the PKC family in regulation of early development

Kalive, Madhavi; Faust, James J.; Koeneman, Brian A.; Capco, David G.

doi:10.1002/mrd.21112

Cited by 38 publications

(31 citation statements)

References 72 publications

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“…The lack of effect of these compounds suggests that PKC and/or SLC26A6 do not have a significant involvement in these processes. It is worth mentioning that, although the cAMP/PKA signaling cascade has been shown to play an important role during capacitation [58], other kinases, such as PKC, are also present in mammalian spermatozoa and may participate in motility and during the AR [59]. Immunolocalization experiments have indicated the presence of PKC, both in the equatorial segment and in the principal piece of human sperm [60].…”

Section: Discussionmentioning

confidence: 99%

Participation of the Cl−/HCO3− Exchangers SLC26A3 and SLC26A6, the Cl− Channel CFTR, and the Regulatory Factor SLC9A3R1 in Mouse Sperm Capacitation1

Chávez

Hernández‐González

Wertheimer

et al. 2012

Biology of Reproduction

106

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Sperm capacitation is required for fertilization and involves several ion permeability changes. Although Cl(-) and HCO(3)(-) are essential for capacitation, the molecular entities responsible for their transport are not fully known. During mouse sperm capacitation, the intracellular concentration of Cl(-) ([Cl(-)](i)) increases and membrane potential (Em) hyperpolarizes. As in noncapacitated sperm, the Cl(-) equilibrium potential appears to be close to the cell resting Em, opening of Cl(-) channels could not support the [Cl(-)](i) increase observed during capacitation. Alternatively, the [Cl(-)](i) increase might be mediated by anion exchangers. Among them, SLC26A3 and SLC26A6 are good candidates, since, in several cell types, they increase [Cl(-)](i) and interact with cystic fibrosis transmembrane conductance regulator (CFTR), a Cl(-) channel present in mouse and human sperm. This interaction is known to be mediated and probably regulated by the Na(+)/H(+) regulatory factor-1 (official symbol, SLC9A3R1). Our RT-PCR, immunocytochemistry, Western blot, and immunoprecipitation data indicate that SLC26A3, SLC26A6, and SLC9A3R1 are expressed in mouse sperm, localize to the midpiece, and interact between each other and with CFTR. Moreover, we present evidence indicating that CFTR and SLC26A3 are involved in the [Cl(-)](i) increase induced by db-cAMP in noncapacitated sperm. Furthermore, we found that inhibitors of SLC26A3 (Tenidap and 5099) interfere with the Em changes that accompany capacitation. Together, these findings indicate that a CFTR/SLC26A3 functional interaction is important for mouse sperm capacitation.

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Section: Discussionmentioning

confidence: 99%

Participation of the Cl−/HCO3− Exchangers SLC26A3 and SLC26A6, the Cl− Channel CFTR, and the Regulatory Factor SLC9A3R1 in Mouse Sperm Capacitation1

Chávez

Hernández‐González

Wertheimer

et al. 2012

Biology of Reproduction

106

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“…All these three mechanisms seem to have a role in fine-tuning the function of the kinase. 63 PKC was found to be localized mainly in the equatorial segment of the human sperm. 59,74 In bull sperm, PKC is concentrated mainly in the postacrosomal and upper region of the acrosome.…”

Section: Protein Kinases a And Cmentioning

confidence: 96%

“…There are three broad categories of PKC based on their requirements for activity, and the structure of their regulatory domains at the NH 2 terminus. 63 First, the conventional PKCs, namely PKCa, bI, bII and c are dependent on diacylglycerol (DAG), phospholipids and calcium, with their regulatory domains containing a C1 domain, which binds DAG/PMA, and a C2 domain that binds anionic phospholipids in a calcium-dependent manner. Second, the novel PKCs are DAG and phospholipid-dependent, but are calciumindependent, and include PKCd, e, m, g and h; their regulatory domains contain two C1 and one C2 domains, with the C2 domains lacking the calcium-coordinating acidic residues.…”

Section: Protein Kinases a And Cmentioning

confidence: 99%

“…As a result, gelsolin is activated and translocated to the head of the sperm. 63 Nevertheless, the elevation of PIP 2(4,5) levels and gelsolin phosphorylation maintain gelsolin in an inactive state, allowing actin polymerization to occur. Prior to the AR, the intracellular Ca 21 concentration is further elevated: PLC is activated and hydrolyzes PIP 2 (4,5) resulting in the release of gelsolin to the cytosol.…”

Section: -89mentioning

confidence: 99%

See 1 more Smart Citation

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

Ickowicz¹,

Finkelstein²,

Breitbart³

2012

Asian J Androl

200

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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“…Little is known about the functions for members of the PKC superfamily in bovine embryos. In mice, multiple members of the PKC superfamily exist during preimplantation development (Pauken and Capco 2000; and various PKCs are implicated in controlling numerous processes during gamete development and maturation, fertilisation and early embryonic development (Kalive et al 2010).…”

Section: Introductionmentioning

confidence: 99%

The requirement for protein kinase C delta (PRKCD) during preimplantation bovine embryo development

Yang

Ozawa

Zhang

et al. 2016

Reprod. Fertil. Dev.

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Protein kinase C (PKC) delta (PRKCD) is a member of the novel PKC subfamily that regulates gene expression in bovine trophoblast cells. Additional functions for PRKCD in early embryonic development in cattle have not been fully explored. The objectives of this study were to describe the expression profile of PRKCD mRNA in bovine embryos and to examine its biological roles during bovine embryo development. Both PRKCD mRNA and protein are present throughout early embryo development and increases in mRNA abundance are evident at morula and blastocyst stages. Phosphorylation patterns are consistent with detection of enzymatically active PRKCD in bovine embryos. Exposure to a pharmacological inhibitor (rottlerin) during early embryonic development prevented development beyond the eight- to 16-cell stage. Treatment at or after the 16-cell stage reduced blastocyst development rates, total blastomere numbers and inner cell mass-to-trophoblast cell ratio. Exposure to the inhibitor also decreased basal interferon tau (IFNT) transcript abundance and abolished fibroblast growth factor-2 induction of IFNT expression. Furthermore, trophoblast adhesion and proliferation was compromised in hatched blastocysts. These observations provide novel insights into PRKCD mRNA expression profiles in bovine embryos and provide evidence for PRKCD-dependent regulation of embryonic development, gene expression and post-hatching events.

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Involvement of the PKC family in regulation of early development

Cited by 38 publications

References 72 publications

Participation of the Cl−/HCO3− Exchangers SLC26A3 and SLC26A6, the Cl− Channel CFTR, and the Regulatory Factor SLC9A3R1 in Mouse Sperm Capacitation1

Participation of the Cl−/HCO3− Exchangers SLC26A3 and SLC26A6, the Cl− Channel CFTR, and the Regulatory Factor SLC9A3R1 in Mouse Sperm Capacitation1

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

The requirement for protein kinase C delta (PRKCD) during preimplantation bovine embryo development

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