Protein kinase C and meiotic regulation in isolated mouse oocytes

Downs, Stephen M.; Cottom, Joshua E.; Hunzicker-Dunn, Mary

doi:10.1002/1098-2795(200101)58:1<101::aid-mrd13>3.0.co;2-j

Cited by 76 publications

(45 citation statements)

References 108 publications

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“…Participation of the EGFR, Src, and Ca 2+ in ERK activation in granulosa cells is evidenced by the abilities of the EGFR inhibitor AG1478, the Src inhibitor PP1, and the Ca 2+ chelator EGTA to abrogate FSH-stimulated ERK activity [27]. Moreover, FSHstimulated ERK activation is mimicked by the Ca 2+ ionophore A23187 [45]. As shown in Fig.…”

Section: Protein Tyrosine Phosphatase (Ptp) Sl-like Ptpmentioning

confidence: 86%

FSH signaling pathways in immature granulosa cells that regulate target gene expression: Branching out from protein kinase A

Hunzicker-Dunn

Maizels

2006

Cellular Signalling

319

240

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Follicle-stimulating hormone (FSH) is necessary and sufficient to induce maturation of ovarian follicles to a mature, preovulatory phenotype in the intact animal, resulting in the generation of mature eggs and production of estrogen. FSH accomplishes these actions by inducing a complex pattern of gene expression in target granulosa cells that is regulated by input from many different signaling cascades, including those for the extracellular regulated kinases (ERKs), p38 mitogen-activated protein kinases (MAPKs), and phosphatidylinositol-3 kinase (PI3K). The upstream kinase that appears to be responsible for initiating all of the signaling that regulates gene expression in these epithelial cells is protein kinase A (PKA). PKA not only signals to directly phosphorylate transcription factors like cAMP response element binding protein and to promote chromatin remodeling by phosphorylating histone H3, this versatile kinase also enhances the activity of the p38 MAPK, ERK, and PI3K pathways. Additionally, accumulating evidence suggests that activation of a single signaling cascade downstream of PKA is not sufficient to activate target gene expression. Rather, cross-talk between and among signaling cascades is required. We will review the signaling cascades activated by FSH in granulosa cells and how these cascades contribute to the regulation of select target gene expression. KeywordsFollicle-stimulating hormone; Mitogen-activated protein kinase; Female reproduction; Hypoxiainduced factor 1; Histone H3; Protein kinase A Abbreviations AKAP, A kinase anchoring protein; Aromatase, P450 aromatase; CBP, CREB binding protein; ChIP, chromatin immunoprecipitation assay; CREB, cAMP response element binding protein; EGF, epidermal growth factor; Egr-1, early growth response protein-1; ERK, extracellular regulated kinase; Epac, exchange proteins activated by cAMP; FSH, follicle-stimulating hormone; GIOT-1, gonadotropin-inducible ovarian transcription factor-1; GPCR, G-protein-coupled receptor; HIF-1, hypoxia-induced factor-1; IGF, insulin-like growth factor; LH, luteinizing hormone; LRH-1, liver receptor homolog-1; MAP2D, microtubule-associated protein 2D; MAPK, mitogen-activated protein kinase; MEK, mitogen-and extracellular-regulated kinase kinase; MK, MAPK-activated protein kinases; MNK, MAPK-interacting kinase; mTOR, mammalian target of rapamycin; p70S6K, p70 ribosomal S6 kinase; PDE, phosphodiesterase; PI3K, phosphatidylinositol 3-kinase; PKA, protein kinase A; PKC, protein kinase C; PKI, PKA inhibitor peptide; PTP, protein tyrosine phosphatase; R, PKA regulatory subunits; RSK, p90 ribosomal S6 protein kinase; SCC, P450 cholesterol side chain cleavage; SF-1, steroidogenic factor-1; SGK, serum glucocorticoid kinase; Sp1/Sp3, specific

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Section: Protein Tyrosine Phosphatase (Ptp) Sl-like Ptpmentioning

confidence: 86%

FSH signaling pathways in immature granulosa cells that regulate target gene expression: Branching out from protein kinase A

Hunzicker-Dunn

Maizels

2006

Cellular Signalling

319

240

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“…Pauken & Capco (2000) detected PKCs a, g, d, l, m, and z by Western blot and immunocytochemistry, but not PKC b. While Luria et al (2000) found that PKCs a, bI and bII were present by immunocytochemistry, and Downs et al (2001) found that PKCs a, bI, d, and z, but not 1 were present by Western blot. Luria et al (2000), Eliyahu & Shalgi (2002) and Baluch et al (2004) have supported some of the results with PKC activator/inhibitor studies.…”

Section: Introductionmentioning

confidence: 93%

“…Several studies have established involvement of PKC in egg activation, fertilization, and progression through the meiotic cycles in mice and rats (Gallicano et al 1995, Raz et al 1998, Downs et al 2001, Viveiros et al 2001, Eliyahu & Shalgi 2002, Quan et al 2003. However, there is less known of the role of the PKC during early cleavage.…”

Section: Introductionmentioning

confidence: 99%

Expression profile of protein kinase C isozymes in preimplantation mouse development

Dehghani¹,

Hahnel²

2005

Reproduction

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In the preimplantation mouse embryo, the protein kinase C (PKC) family has been implicated in regulation of egg activation, progression of meiotic and mitotic cell cycles, embryo compaction, and blastulation, but the involvement of the individual isozymes is largely unknown. Here, using semiquantitative immunocytochemistry and confocal microscopy we analyze the relative amount and subcellular distribution of ten isozymes of PKC (a, bI, bII, g, d, 1, h, u, z, i/l) and a PKC-anchoring protein, receptor for activated C-kinase 1 (RACK1). Our results show that all of these isoforms of PKC are present between the twocell and blastocyst stages of mouse preimplantation development, and that each has a distinct, dynamic pattern and level of expression. The data suggest that different complements of the isozymes are involved in various steps of preimplantation development, and will serve as a framework for further functional studies of the individual isozymes. In particular, there was a transient increase in the nuclear concentration of several isozymes at the early four-cell stage, suggesting that some of the PKC isozymes might be involved in regulation of nuclear organization and function in the early mouse embryo.

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“…Several authors reported the presence of isotypes PKC-α, -β I , -β II , -γ, -δ, -ε, -µ, -λ, and -ζ in rodent oocytes at the stage of metaphase II (Gangeswaran and Jones, 1997;Raz et al, 1998;Luria et al, 2000;Pauken and Capco, 2000;Downs et al, 2001;Eliyahu et al, 2001;Eliyahu and Shalgi, 2002;Viveiros et al, 2003) and mRNA for PKC-α, -δ, and -λ (Gangeswaran and Jones, 1997;Raz et al, 1998) although the data on the PKC isotype spectrum and their mRNA are different. Fan et al (2002a,b) demonstrated PKC-α, -β I , -γ isotypes in both immature and mature porcine oocytes.…”

mentioning

confidence: 99%

Effects of protein kinase C on parthenogenetic activation of pig oocytes using calcium ionophore or nitric oxide-donor

Petr¹,

Eva²,

Dörflerová³

et al. 2007

CZECH J ANIM SCI

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Porcine oocytes matured in vitro were activated for parthenogenetic development using either calcium ionophore (50µM for 10 min) or nitric oxide donor SNAP (2mM for 23.5 hours). Protein kinase C (PKC) inhibitors, bisindolylmaleimide I or rottlerin, are able to inhibit parthenogenetic activation induced by calcium ionophore. The rate of activated oocytes decreased from 69% to 2% (P < 0.05) under the effect of bisindolylmaleimide I at a concentration of 0 or 20nM, respectively. The activation rate decreased from 68% to 0% (P < 0.05) under the influence of 0 or 20µM rottlerin, respectively. PKC inhibitors Go6976 or hispidin had no effect on the oocyte activation using calcium ionophore or on oocytes activated by a nitric oxide donor. The activation of oocytes by a nitric oxide donor is not significantly influenced even under the effects of bisindolylmaleimide I or rottlerin. Based on these data we can conclude that the oocyte activation induced by calcium ionophore depends on PKC, especially on PKC-δ. On the other hand, the oocyte activation induced by nitric oxide is independent of the tested isotypes of PKC.

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Protein kinase C and meiotic regulation in isolated mouse oocytes

Cited by 76 publications

References 108 publications

FSH signaling pathways in immature granulosa cells that regulate target gene expression: Branching out from protein kinase A

FSH signaling pathways in immature granulosa cells that regulate target gene expression: Branching out from protein kinase A

Expression profile of protein kinase C isozymes in preimplantation mouse development

Effects of protein kinase C on parthenogenetic activation of pig oocytes using calcium ionophore or nitric oxide-donor

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