Protein kinase C initially inhibits the induction of meiotic cell division in xenopus oocytes

Stith, Bradley J.; Goalstone, Marc L.; Kirkwood, Allan J.

doi:10.1016/0898-6568(92)90034-6

Cited by 11 publications

(11 citation statements)

References 52 publications

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“…One interesting possibility is that the kinase involved is PKC as shown in mammalian cells [5] and this may have a major functional role in oocyte maturation. In Xenopus oocytes, progesterone is known to act synergistically to [35] or via [9] PKC. In this work, the 29-kDa protein appears before the 'white-spot' stage, suggesting that during oogenesis, p27 BBP /eIF6 phosphorylation occurs at the onset of the major Mos/MPF activation events.…”

Section: Discussionmentioning

confidence: 99%

Phosphorylation of p27BBP/eIF6 and its association with the cytoskeleton are developmentally regulated in Xenopus oogenesis

Carotenuto

Marco

Biffo

et al. 2005

CMLS, Cell. Mol. Life Sci.

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p27BBP/eIF6 is an evolutionarily conserved regulator of ribosomal function. It is necessary for 60S biogenesis and impedes improper joining of 40S and 60S subunits, regulated by protein kinase C or Efl1p. No data on p27BBP/eIF6 during early development of Metazoa are available. We studied the distribution, post-translational changes and association with the cytoskeleton of p27BBP/ eIF6 during Xenopus oogenesis and early development. Results indicate that p27BBP/eIF6 is present throughout oogenesis, partly associated with 60S subunits, partly free and with little cytoskeleton bound. During prophase I, p27BBP/eIF6 is detected as a single band of 27-kDa. Upon maturation induced by progesterone or protein kinase C, a serine-phosphorylated 29 kDa isoform appears and is kept throughout development to the neurula stage. Confocal microscopy showed that the distribution of p27BBP/eIF6 and its association with the cytoskeleton varies according to oogenesis stages. Briefly, in stage 6 oocytes, p27BBP/eIF6 has a limited dot-like distribution, and does not co-localize with cytokeratin, whereas upon maturation it spreads throughout the cytoplasm. After fertilization, a large fraction coalesces around cytomembranes and a cytochalasin B-sensitive co-localization with cytokeratin occurs. RNAse removes p27BBP/eIF6 from the cytokeratin fibres. Developmental data suggest a role of p27BBP/eIF6 in controlling ribosomal availability or regulating cross-talk between ribosomes and the cytoskeleton.

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Section: Discussionmentioning

confidence: 99%

Phosphorylation of p27BBP/eIF6 and its association with the cytoskeleton are developmentally regulated in Xenopus oogenesis

Carotenuto

Marco

Biffo

et al. 2005

CMLS, Cell. Mol. Life Sci.

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“…These observations indicate that MIH-dependent meiotic resumption in croaker oocytes does not involve PKC and that premature PKC activation may be inhibitory or toxic to maturation. A maturation-suppressing effect of PKC was also suggested for mouse oocytes [17] and Xenopus oocytes [16]. Conversely, pharmacological activation of PKC was reported to promote oocyte maturation in species such as the rat [18], the amphibian Rana dybowskii [19], and the teleost killifish [20,21].…”

Section: Maturationmentioning

confidence: 95%

“…For example, negative [16,17] as well as positive [18][19][20][21] regulation of meiotic resumption by PKC has been reported in several different species. Nevertheless, general agreement is found in the literature that ovulation in most vertebrates, including teleost fishes, requires PKC-dependent pathways [10,[22][23][24][25][26][27].…”

Section: Introductionmentioning

confidence: 96%

Role of Arachidonic Acid and Protein Kinase C During Maturation-Inducing Hormone-Dependent Meiotic Resumption and Ovulation in Ovarian Follicles of Atlantic Croaker1

Patiño

Yoshizaki

Bolamba

et al. 2003

Biology of Reproduction

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The roles of arachidonic acid (AA) and protein kinase C (PKC) during in vitro maturation-inducing hormone (MIH)-dependent meiotic resumption (maturation) and ovulation were studied in ovarian follicles of Atlantic croaker (Micropogonias undulatus). The requirement for cyclooxygenase (COX) metabolites of AA was examined using a nonspecific COX inhibitor, indomethacin (IM), as well as two COX products, prostaglandin (PG) F(2alpha) and PGE(2), whereas the role of lipoxygenase (LOX) was investigated using a specific LOX inhibitor, nordihydroguaiaretic acid (NDGA). The involvement of PKC was examined using phorbol 12-myristate 13-acetate (PMA), a PKC activator, as well as GF109203X (GF), a specific inhibitor of PKC and 1-(5-isoquinolinesulfonyl)-2-methylpiperazine (H7), nonspecific inhibitor of protein kinases. Genomic mechanisms were examined with the transcription-inhibitor actinomycin D (ActD) and the functionality of heterologous (oocyte-granulosa) gap junctions (GJ) with a dye transfer assay. The AA (100 microM) and PGF(2alpha) (5 microM) did not induce maturation, and NDGA (10 microM) did not affect MIH-dependent maturation. However, IM (100 microM) partially inhibited MIH-dependent maturation. Conversely, AA and both PGs induced, and IM and NDGA inhibited, MIH-dependent ovulation in matured follicles. The PMA (1 microg/ml) did not induce maturation but caused ovulation in matured follicles, whereas PKC inhibitors (GF, 5 microM; H7, 50 microM) did not affect MIH-dependent maturation but inhibited MIH- and PMA-dependent ovulation. The PMA-dependent ovulation was inhibited by IM but not by NDGA. In addition, ActD (5 microM) blocked MIH-dependent, but not PMA-dependent, ovulation, and PGF(2alpha) restored MIH-dependent ovulation in ActD-blocked follicles. The AA and PGs did not induce, and GF did not inhibit, MIH-dependent heterologous GJ uncoupling. In conclusion, AA and PKC mediate MIH-dependent ovulation but not meiotic resumption or heterologous GJ uncoupling in croaker follicles, but a permissive role of COX products of AA during maturation is possible. A novel model of MIH-dependent ovulation is proposed in which 1). LOX and COX metabolites of AA are both required for ovulation, but at upstream and downstream sites of the pathway, respectively, relative to PKC, and 2). PKC is downstream of genomic activation.

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“…2). As discussed below, a comparison of the increases of IP3 (Stith et al, 1992a; Stith et al, 1994; Stith et al, 1993) and DAG (Stith et al, 1992b; Stith et al, 1991; Stith et al, 1997) provide insight into lipid signaling during these crucial developmental periods. Our summary (Table 1) highlights the relative high levels of PA and DAG (pmol/cell) versus the lower levels of IP 3 (fmol/cell).…”

Section: Levels Of Plc Activation In Development: Ip3 Mass Changesmentioning

confidence: 99%

“…Injection of PKC did not induce oocyte maturation but accelerated insulin (but not progesterone) induction of meiosis by 25% (Stith and Maller, 1987). Subsequent studies (Stith et al, 1992b) artificially elevated DAG and reduced PKC activity with two different inhibitors to find that PKC is initially inhibitory to the induction of maturation by either hormone. Perhaps reflecting different PKC isoforms, at ~2 hours after hormone addition, PKC activity changes to facilitating oocyte maturation.…”

Section: Dag Changes In Developmentmentioning

confidence: 99%

Phospholipase C and D regulation of Src, calcium release and membrane fusion during Xenopus laevis development

Stith

2015

Developmental Biology

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This review emphasizes how lipids regulate membrane fusion and the proteins involved in three developmental stages: oocyte maturation to the fertilizable egg, fertilization and during first cleavage. Decades of work show that phosphatidic acid (PA) releases intracellular calcium, and recent work shows that the lipid can activate Src tyrosine kinase or phospholipase C during Xenopus fertilization. Numerous reports are summarized to show three levels of increase in lipid second messengers inositol 1,4,5-trisphosphate and sn 1,2-diacylglycerol (DAG) during the three different developmental stages. In addition, possible roles for PA, ceramide, lysophosphatidylcholine, plasmalogens, phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 4,5-bisphosphate, membrane microdomains (rafts) and phosphatidylinositol 3,4,5-trisphosphate in regulation of membrane fusion (acrosome reaction, sperm-egg fusion, cortical granule exocytosis), inositol 1,4,5-trisphosphate receptors, and calcium release are discussed. The role of six lipases involved in generating putative lipid second messengers during fertilization is also discussed: phospholipase D, autotaxin, lipin1, sphingomyelinase, phospholipase C, and phospholipase A2. More specifically, proteins involved in developmental events and their regulation through lipid binding to SH3, SH4, PH, PX, or C2 protein domains is emphasized. New models are presented for PA activation of Src (through SH3, SH4 and a unique domain), that this may be why the SH2 domain of PLCγ is not required for Xenopus fertilization, PA activation of phospholipase C, a role for PA during the calcium wave after fertilization, and that calcium/calmodulin may be responsible for the loss of Src from rafts after fertilization. Also discussed is that the large DAG increase during fertilization derives from phospholipase D production of PA and lipin dephosphorylation to DAG.

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Protein kinase C initially inhibits the induction of meiotic cell division in xenopus oocytes

Cited by 11 publications

References 52 publications

Phosphorylation of p27BBP/eIF6 and its association with the cytoskeleton are developmentally regulated in Xenopus oogenesis

Phosphorylation of p27BBP/eIF6 and its association with the cytoskeleton are developmentally regulated in Xenopus oogenesis

Role of Arachidonic Acid and Protein Kinase C During Maturation-Inducing Hormone-Dependent Meiotic Resumption and Ovulation in Ovarian Follicles of Atlantic Croaker1

Phospholipase C and D regulation of Src, calcium release and membrane fusion during Xenopus laevis development

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