scholarly journals Expression profile of protein kinase C isozymes in preimplantation mouse development

Reproduction ◽  
2005 ◽  
Vol 130 (4) ◽  
pp. 441-451 ◽  
Author(s):  
Hesam Dehghani ◽  
Ann C Hahnel
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Mouse Embryo ◽  
Mitotic Cell ◽  
Preimplantation Development ◽  
Mouse Development ◽  
Cell Stage ◽  
Kinase C ◽  
Preimplantation Mouse ◽  
The Individual

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 (α, βI, βII, γ, δ, ε, η, 𝛉, ζ, ι/λ) 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 two-cell 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.

Activation of protein kinase C triggers premature compaction in the four-cell stage mouse embryo

1990 ◽  
Vol 138 (1) ◽  
pp. 1-15 ◽  
Author(s):  
Glen K. Winkel ◽  
James E. Ferguson ◽  
Masatoshi Takeichi ◽  
Richard Nuccitelli
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Mouse Embryo ◽  
Cell Stage ◽  
Kinase C

scholarly journals Protein kinase C acts downstream of calcium at entry into the first mitotic interphase of Xenopus laevis.

1990 ◽  
Vol 1 (3) ◽  
pp. 315-326 ◽  
Author(s):  
W M Bement ◽  
D G Capco
Keyword(s):  
Cell Cycle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Xenopus Laevis ◽  
Mitotic Cell ◽  
Cortical Granule ◽  
Mitotic Cell Cycle ◽  
Cleavage Furrow ◽  
Kinase C ◽  
Cortical Granule Exocytosis

Transit into interphase of the first mitotic cell cycle in amphibian eggs is a process referred to as activation and is accompanied by an increase in intracellular free calcium [( Ca2+]i), which may be transduced into cytoplasmic events characteristic of interphase by protein kinase C (PKC). To investigate the respective roles of [Ca2+]i and PKC in Xenopus laevis egg activation, the calcium signal was blocked by microinjection of the calcium chelator BAPTA, or the activity of PKC was blocked by PKC inhibitors sphingosine or H7. Eggs were then challenged for activation by treatment with either calcium ionophore A23187 or the PKC activator PMA. BAPTA prevented cortical contraction, cortical granule exocytosis, and cleavage furrow formation in eggs challenged with A23187 but not with PMA. In contrast, sphingosine and H7 inhibited cortical granule exocytosis, cortical contraction, and cleavage furrow formation in eggs challenged with either A23187 or PMA. Measurement of egg [Ca2+]i with calcium-sensitive electrodes demonstrated that PMA treatment does not increase egg [Ca2+]i in BAPTA-injected eggs. Further, PMA does not increase [Ca2+]i in eggs that have not been injected with BAPTA. These results show that PKC acts downstream of the [Ca2+]i increase to induce cytoplasmic events of the first Xenopus mitotic cell cycle.

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

2016 ◽  
Vol 28 (4) ◽  
pp. 482 ◽  
Author(s):  
Qi-En Yang ◽  
Manabu Ozawa ◽  
Kun Zhang ◽  
Sally E. Johnson ◽  
Alan D. Ealy
Keyword(s):  
Gene Expression ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Embryonic Development ◽  
Embryo Development ◽  
Early Embryonic Development ◽  
Bovine Embryo ◽  
Bovine Embryos ◽  
Cell Stage ◽  
Kinase C

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.

scholarly journals Subcellular localization of protein kinase C δ and ε affects transcriptional and post-transcriptional processes in four-cell mouse embryos

Reproduction ◽  
2005 ◽  
Vol 130 (4) ◽  
pp. 453-465 ◽  
Author(s):  
Hesam Dehghani ◽  
Cara Reith ◽  
Ann C Hahnel
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Subcellular Localization ◽  
Cajal Bodies ◽  
Message Processing ◽  
Mrna Transcription ◽  
Cell Stage ◽  
Kinase C ◽  
Sm Protein ◽  
Small Nuclear Ribonucleoproteins

During mouse preimplantation development, two isozymes of protein kinase C (PKC), δ and ε, transiently localize to nuclei at the early four-cell stage. In order to study their functions at this stage, we altered the subcellular localization of these isozymes (ratio of nuclear to cytoplasmic concentrations) with peptides that specifically activate or inhibit translocation of each isozyme. The effects of altering nuclear concentration of each isozyme on transcription (5-bromouridine 5′-triphosphate (BrUTP) incorporation), amount and distribution of small nuclear ribonucleoproteins (snRNPs), nucleolar dynamics (immunocytochemistry for Smith antigen (Sm) protein) and the activity of embryonic alkaline phosphatase (EAP; histochemistry) were examined. We found that nuclear concentration of PKC ε correlated with total mRNA transcription. Higher nuclear concentrations of both PKC δ and ε decreased storage of snRNPs in Cajal bodies and decreased the number of nucleoli, but did not affect the nucleoplasmic concentration of snRNPs. Inhibiting translocation of PKC δ out of the nucleus at the early four-cell stage decreased cytoplasmic EAP activity, whereas inhibiting translocation of PKC ε increased EAP activity slightly. These results indicate that translocation of PKC δ and ε in and out of nuclei at the early four-cell stage in mice can affect transcription or message processing, and that sequestration of these PKC in nuclei can also affect the activity of a cytoplasmic protein (EAP).

The effects of phorbol ester on mouse blastomeres: a role for protein kinase C in compaction?

Development ◽  
1989 ◽  
Vol 106 (1) ◽  
pp. 159-171
Author(s):  
T.L. Bloom
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Polarity ◽  
Myristate Acetate ◽  
Experimental Conditions ◽  
Cell Stage ◽  
Cytoskeletal Organization ◽  
Kinase C ◽  
Early Embryos ◽  
Interphase Cells

The effects of phorbol myristate acetate (PMA) and other activators of protein kinase C on the cytoskeletal organization of mouse oocytes and early embryos have been examined. The effects observed depended on the developmental stage on exposure to PMA. PMA had little effect on the cytoskeletal or microvillous organization of unfertilized oocytes. Interphase cells from embryos prior to compaction showed limited disruption and loss of microvilli when exposed to PMA and foci of polymerized actin remained visible in the cytocortex of embryos up to the early 8-cell stage. When compacted late 8-cell embryos were exposed to PMA, most microvilli were lost and little polymerized actin remained in the cytocortex. PMA also caused loss of microtubules from compact 8-cell embryos under some experimental conditions. Intercellular flattening was both prevented and reversed. The relevance of these observations to the rearrangement of cell-cell contacts and cytoskeletal organization seen during compaction at the 8-cell stage is discussed and a possible role for protein kinase C in the generation of cell polarity proposed.

scholarly journals Protein kinase C isoforms play differential roles in the regulation of adipocyte differentiation

1998 ◽  
Vol 333 (3) ◽  
pp. 719-727 ◽  
Author(s):  
Iona FLEMING ◽  
Simon J. MacKENZIE ◽  
Richard G. VERNON ◽  
Neil G. ANDERSON ◽  
Miles D. HOUSLAY ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Adipocyte Differentiation ◽  
Inhibitory Influence ◽  
Differentiation Process ◽  
Kinase C ◽  
Pkc Isoforms ◽  
Pkc Ζ ◽  
The Individual ◽  
Adipocyte Development

In this study we first established, by immunoblotting with specific antibodies, the temporal changes in cellular levels of protein kinase C (PKC) isoforms during differentiation of 3T3-F442A pre-adipocytes. Both pre-adipocyte and adipocyte 3T3-F442A cells were found to express PKC-α, -γ, -δ, -ε, -ζ and -µ. However we were unable to detect PKC-β, -η or -θ. The same PKC isoform expression profile was found in rat adipocytes. The α, δ and γ isoforms displayed similar temporal patterns of expression during differentiation of 3T3-F442A cells; all increased rapidly, peaking at day 2 of differentiation. Subsequently, the expression of these isoforms decreased, resulting in lower levels in fully differentiated adipocytes than in pre-adipocytes. The expression of PKC-ε increased steadily during differentiation, resulting in markedly elevated levels in adipocytes. Although expression of PKC-µ increased during differentiation, this was attributable to prolonged confluence rather than to the differentiation process itself. No change was observed in PKC-ζ levels during adipocyte development. Anti-sense oligodeoxynucleotides (ODNs) were used to deplete selectively the individual PKC subtypes. Each of the ODNs used effectively depleted the specific isoforms to undetectable levels and did not affect expression of the other PKC subtypes. This approach indicated that pre-adipocyte differentiation is not dependent upon PKC-ζ but that PKC-α,-δ and -µ each exert an inhibitory influence upon differentiation. Use of anti-sense ODNs to deplete PKC-ε and -γ revealed that pre-adipocyte differentiation is dependent upon each of these isoforms. However, PKC-γ, but not PKC-ε, appeared to be necessary for the clonal expansion of differentiating cells, suggesting that PKC-ε is required at a later phase in the differentiation process, when its expression is elevated, for the attainment and maintenance of the adipocyte phenotype.

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