The role of calcium/calmodulin-dependent protein kinase II on the inactivation of MAP kinase and p34cdc2 kinase during fertilization and activation in pig oocytes

Ito, Junya; Kawano, Naoki; Hirabayashi, Masumi; Shimada, M.

doi:10.1530/rep.1.00230

Cited by 21 publications

(19 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Interestingly, except for CDC25B, these genes responded to PTHrP-(67-86) in the same way as to siPTHrP. Collectively, the data suggest that PTHrP affects gene expression in MDA-MB-231 cells in at least three different ways as follows: one that depends on the PTH/PTHrP-receptor, a second that is sensitive to the PTHrP peptide 67-86, and a third that did not depend on PTH1R nor was sensitive to PTHrP- (67)(68)(69)(70)(71)(72)(73)(74)(75)(76)(77)(78)(79)(80)(81)(82)(83)(84)(85)(86).…”

Section: Pthrp Acts Through Different Pathways To Modulate Gene Exprementioning

confidence: 70%

See 1 more Smart Citation

Parathyroid Hormone-related Protein Regulates Tumor-relevant Genes in Breast Cancer Cells

Dittmer¹,

Vetter²,

Schunke³

et al. 2006

Journal of Biological Chemistry

View full text Add to dashboard Cite

The effect of endogenous parathyroid hormone-related protein (PTHrP) on gene expression in breast cancer cells was studied. We suppressed PTHrP expression in MDA-MB-231 cells by RNA interference and analyzed changes in gene expression by microarray analysis. More than 200 genes showed altered expression in response to a PTHrP-specific small interfering (si) RNA (siPTHrP). Cell cycle-regulating gene CDC2 and genes (CDC25B and Tome-1) that control CDC2 activity showed increased expression in the presence of siPTHrP. CDC2 activity was also found to be higher in siPTHrP-treated cells. Studies with PTHrP peptides 1-34 and 67-86, forskolin, and a PTH1 receptor (PTH1R)-specific siRNA showed that PTHrP regulates CDC2 and CDC25B, at least in part, via PTH1R in a cAMP-independent manner. Other siPTHrP-responsive genes included integrin ␣6 (ITGA6), KISS-1, and PAI-1. When combined, siRNAs against ITGA6, PAI-1, and KISS-1 could mimic the negative effect of siPTHrP on migration, whereas siKISS-1 and siPTHrP similarly reduced the proliferative activity of the cells. Comparative expression analyses with 50 primary breast carcinomas revealed that the RNA level of ITGA6 correlates with that of PTHrP, and higher CDC2 and CDC25B values are found at low PTHrP expression. Our data suggest that PTHrP has a profound effect on gene expression in breast cancer cells and, as a consequence, contributes to the regulation of important cellular activities, such as migration and proliferation.

show abstract

Section: Pthrp Acts Through Different Pathways To Modulate Gene Exprementioning

confidence: 70%

“…Instead, calcium may be involved, which seems to be a preferred target of PTH1R in the more progressed breast cancer cells (10). Interestingly, calcium has been shown to have a negative effect on CDC2 by activating calcium/calmodulindependent protein kinase II (68).…”

Section: Discussionmentioning

confidence: 99%

Parathyroid Hormone-related Protein Regulates Tumor-relevant Genes in Breast Cancer Cells

Dittmer¹,

Vetter²,

Schunke³

et al. 2006

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…CaMKII plays a crucial role in Xenopus [5,6], mouse [10,25,26], and pig [27] fertilization. It has , and cdc2 and p-cdc2 (C) in the MII-oocytes (A and B) and the oocytes treated with vanadate for 2 h (C), respectively (defined as 100%).…”

Section: Discussionmentioning

confidence: 99%

The Regulation of Calcium/Calmodulin-dependent Protein Kinase II during Oocyte Activation in the Rat

Ito

Kaneko

Hirabayashi

2006

Journal of Reproduction and Development

Self Cite

View full text Add to dashboard Cite

Abstract. Increases in intracellular Ca2+ are required for oocyte activation and subsequent development. Calmodulin-dependent protein kinase II (CaMKII) plays a crucial role in oocyte activation. However, how CaMKII is regulated during this process is not well characterized. We show here for the first time in rat oocytes that CaMKII is phosphorylated during oocyte activation. CaMKII phosphorylation was suppressed by KN93, a CaMKII inhibitor, but not KN92, which is the inactive analogue of KN93. Electrical stimulation of rat oocytes resulted in degradation of both cyclin B and Mos, presumably due a rise in Ca 2+ induced by the electrical pulse. KN93 blocked the degradation of both proteins induced by the electrical pulse. Addition of a protein phosphatase inhibitor, okadaic acid (OA), further increased the amount of CaMKII and also increased the amount of phosphorylated enzyme. Importantly, in oocytes undergoing spontaneous activation, accumulation and phosphorylation of CaMKII also occurs in a time-dependent manner. Consistent with this, addition of KN93 inhibited spontaneous activation. Collectively, our results show that CaMKII is phosphorylated during oocyte activation and that this phosphorylation is involved in inactivation of p34 cdc2 kinase and somewhat involved in degradation of Mos. Furthermore, CaMKII phosphorylation is negatively regulated by a protein phosphatase.

show abstract

“…The calcium transients drive the resumption of the cell cycle by decreasing the activity of both M-phase promoting factor (MPF) and cytostatic factor (Jones 2004). The destruction of MPF, triggered by [Ca 2þ ] i rise, is mediated by calmodulin (CaM) and by Ca 2þ /CaM-dependent protein kinase II (CaMKII; Fan et al 2003, Ito et al 2004. Incubation of mouse eggs in the presence of a CaM antagonist prior to in vitro insemination, delayed both the fertilization-associated decrease in histone H1 kinase activity and the emission of the second polar body (PBII), but did not block CGE (Xu et al 1996).…”

Section: Introductionmentioning

confidence: 99%

Association between myristoylated alanin-rich C kinase substrate (MARCKS) translocation and cortical granule exocytosis in rat eggs

Eliyahu¹,

Shtraizent²,

Tsaadon³

et al. 2006

Reproduction

View full text Add to dashboard Cite

Cortical granule exocytosis (CGE), following egg activation, is a secretory process that blocks polyspermy and enables successful embryonic development. CGE can be triggered independently by either a rise in intracellular calcium concentration ([Ca 21 ] i ) or activation of protein kinase C (PKC). The present study investigates the signal transduction pathways leading to CGE through activation of PKC or stimulation of a rise in [Ca 21 ] i . Using Western blot analysis, co-immunoprecipitation and immunohistochemistry, combined with various inhibitors or activators, we investigated the link between myristoylated alaninrich C kinase substrate (MARCKS) translocation and CGE. We were able to demonstrate translocation of MARCKS from the plasma membrane to the cortex, in fertilized as well as in parthenogenetically activated eggs. MARCKS phosphorylation was demonstrated upon PKC activation, whereas a PKC inhibitor (myrPKCc) prevented both MARCKS translocation and CGE in 12-O-tetradecanoyl phorbol-13-acetate (TPA)-activated eggs. We have further shown that upon egg activation the amount of phosphorylated MARCKS (p-MARCKS) and the amount of calmodulin bound to MARCKS were increased. MARCKS translocation in ionomycin activated eggs was also inhibited by the calmodulin inhibitor N-(6-aminohexyl)-5-chloro-1-napthalenesulfonamide hydrochloride (W7). These results complement other studies showing MARCKS requirement for exocytosis and imply that upon fertilization, MARCKS translocation is followed by CGE. These findings present a significant contribution to our understanding of CGE in mammalian eggs in particular, as well as cellular exocytosis in general.

show abstract

The role of calcium/calmodulin-dependent protein kinase II on the inactivation of MAP kinase and p34cdc2 kinase during fertilization and activation in pig oocytes

Cited by 21 publications

References 26 publications

Parathyroid Hormone-related Protein Regulates Tumor-relevant Genes in Breast Cancer Cells

Parathyroid Hormone-related Protein Regulates Tumor-relevant Genes in Breast Cancer Cells

The Regulation of Calcium/Calmodulin-dependent Protein Kinase II during Oocyte Activation in the Rat

Association between myristoylated alanin-rich C kinase substrate (MARCKS) translocation and cortical granule exocytosis in rat eggs

Contact Info

Product

Resources

About