Calcium signalling in early embryos

Whitaker, Michael

doi:10.1098/rstb.2008.2259

Cited by 62 publications

(43 citation statements)

References 316 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…We measured dissociation constants (K d ) in the range of 100 nM for S100A1, S100A2, S100A4 and S100A6, and 2.8 mM for S100B (Table 1). The observed affinities were significantly higher than for the homologous p53TET peptide (Fernandez-Fernandez et al, 2005, 2008. Similarly to p53TET, the affinity to p63TET was highly dependent on the concentration of the labelled peptide used in the anisotropy titration experiments, as illustrated by the binding of S100A4 to 0.1, 0.5, 1 and 2 mM p63TET (Figure 1a).…”

Section: S100 Proteins Bind the P63 Tetramerization Domain In Differementioning

confidence: 95%

“…In addition, a subset of the protein family binds to the negative regulatory domain (367-393) of the tumor suppressor. Further, S100 proteins have been shown to potentially activate as well as inhibit p53 (Baudier et al, 1992;Scotto et al, 1998Scotto et al, , 1999Rustandi et al, 2000;Grigorian et al, 2001;Lin et al, 2001Lin et al, , 2004Fernandez-Fernandez et al, 2005, 2008Mueller et al, 2005;Salama et al, 2008;Slomnicki et al, 2009;van Dieck et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Molecular basis of S100 proteins interacting with the p53 homologs p63 and p73

et al. 2010

View full text Add to dashboard Cite

S100 proteins modulate p53 activity by interacting with its tetramerization (p53TET, residues 325-355) and transactivation (residues 1-57) domains. In this study, we characterized biophysically the binding of S100A1, S100A2, S100A4, S100A6 and S100B to homologous domains of p63 and p73 in vitro by fluorescence anisotropy, analytical ultracentrifugation and analytical gel filtration. We found that S100A1, S100A2, S100A4, S100A6 and S100B proteins bound different p63 and p73 tetramerization domain variants and naturally occurring isoforms with varying affinities in a calcium-dependent manner. Additional interactions were observed with peptides derived from the p63 and p73 N-terminal transactivation domains. Importantly, S100 proteins bound p63 and p73 with different affinities in their different oligomeric states, similarly to the differential modes of binding to p53. On the basis of our data, we hypothesize that S100 proteins regulate the oligomerization state of all three p53 family members and their isoforms, with a potential physiological relevance in developmental and disease-related processes. The regulation of the p53 family by S100 is complicated and depends on the target preference of each individual S100 protein, the concentration of the proteins and calcium, as well as the splicing variation of p63 or p73. Our results outlining the complexity of the interaction should be considered when studying the functional effects of S100 proteins in their biological context.

show abstract

Section: S100 Proteins Bind the P63 Tetramerization Domain In Differementioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

Molecular basis of S100 proteins interacting with the p53 homologs p63 and p73

et al. 2010

View full text Add to dashboard Cite

show abstract

“…In addition, mitochondria play a vital role in signal transduction, oxygen sensing and maintenance of the cellular homeostasis especially calcium oscillations (Gutierrez et al, 2006;Quintero et al, 2006). Calcium oscillations are very important for fertilization, embryonic cell-cycle transition and embryonic axis establishment (Whitaker, 2008). So, melatonin by enhancing the mitochondrial healthy condition might share indirectly in all of these processes.…”

Section: Discussionmentioning

confidence: 99%

Evidences for the Role of Melatonin as a Protective Additive During Buffalo Semen Freezing

Raey¹,

Badr²,

Rawash³

et al. 2014

American Journal of Animal and Veterinary Sciences

View full text Add to dashboard Cite

Till now, the exact role of melatonin in male infertility hasn't been fully discovered. Moreover, the intracellular signaling pathways activated by melatonin in buffalo spermatozoa especially on the level of cryopreservation process haven't been reported. The current study aimed simply to clarify the precise role of this hormone during buffalo semen cryopreservation. Semen samples were obtained randomly from 6 fertile buffalo bulls (aged 3 to 5 years). Weekly, two consecutive ejaculates were collected from each bull for successive six weeks duration using an artificial vagina. The ejaculates were pooled to eliminate variability between the evaluated samples. After that, semen samples were subjected to extension with Tris-based extender supplemented with different concentrations of melatonin (0.1, 0.25, 0.5, 0.75 and 1 mM) Vs. Trisbased extender only (control). Then they were processed to cryopreservation and thawing to assess the different semen characteristics. It had been found that 0.1 mM of melatonin significantly (p<0.05) improved post thawing motility, viability index, acrosomal integrity, total antioxidant capacity, superoxide dismutase and glutathione reductase activity. On the other hand, it significantly (p<0.05) decreased the rate of lipid peroxidation, aspartate amino transferase, alanine aminotransferase, alkaline phosphatase and DNA fragmentation. All of these previously enhanced semen characteristics were reflected positively on its in vitro fertilizing capacity, as well as the percent of harvested embryos. In conclusion melatonin supplementation to the extension media of buffalo semen during processing significantly enhanced its characteristics. Moreover, the preceding results focusing more light on the potential roles of melatonin in regulating male reproduction.

show abstract

“…Mitochondria form aggregates with the smooth endoplasmic reticulum (SER), Cummins et al, 1997;Cox and Spradling, 2003;Mitochondrial distribution Wilding et al, 2001Torner et al, 2004;Nishi et al, 2003Mitochondrial movement van Blerkom, 1991Cox and Spradling, 2003;mtDNA content Reynier et al, 2001Spikings et al, 2007mtDNA mutation Yesodi et al, 2002Hsieh et al, 2004Mitochondrial polarity van Blerkom et al, 2003 2007 Function in calcium regulation Machaty et al, 1997;Krisher, 2004;Whitaker, 2008 Mitochondrial dysfunction Tarín, 1996;Eichenlaub-Ritter, 1998;Yin et al, 1998;Ottolenghi et al, 2004;Thouas et al, 2004;Zhang et al, 2006Mitochondria transfer Pinkert et al, 1997Malter and Cohen, 2002;Kong et al, 2004;Yi et al, 2007 a Studies involved in oocytes and embryos and these aggregates are apparently involved in the energy production and deposition before fertilization (Torner et al, 2004). Mammalian oocyte maturation relies not only on a high level of ATP for nuclear envelope breakdown, but also on intracellular calcium, which is derived from the endoplasmic reticulum (ER) and mitochondria (Krisher, 2004).…”

Section: Calcium Signaling In Mitochondriamentioning

confidence: 99%

“…Inositol 1,4,5-trisphosphate (IP3) and ryanodine receptors were found to localize on the surface of the ER, which are active from the germinal vesicle stage to oocyte maturation (Machaty et al, 1997 (Berridge et al, 2000;Smaili et al, 2000). Whitaker (2008) recently reviewed that calcium may perform an important function in embryonic cell-cycle transition and embryonic axis establishment.…”

Section: Calcium Signaling In Mitochondriamentioning

confidence: 99%

Mitochondrial functions on oocytes and preimplantation embryos

Wang

Zou

et al. 2009

J. Zhejiang Univ. Sci. B

134

View full text Add to dashboard Cite

Oocyte quality has long been considered as a main limiting factor for in vitro fertilization (IVF). In the past decade, extensive observations demonstrated that the mitochondrion plays a vital role in the oocyte cytoplasm, for it can provide adenosine triphosphate (ATP) for fertilization and preimplantation embryo development and also act as stores of intracellular calcium and proapoptotic factors. During the oocyte maturation, mitochondria are characterized by distinct changes of their distribution pattern from being homogeneous to heterogeneous, which is correlated with the cumulus apoptosis. Oocyte quality decreases with the increasing maternal age. Recent studies have shown that low quality oocytes have some age-related dysfunctions, which include the decrease in mitochondrial membrane potential, increase of mitochondrial DNA (mtDNA) damages, chromosomal aneuploidies, the incidence of apoptosis, and changes in mitochondrial gene expression. All these dysfunctions may cause a high level of developmental retardation and arrest of preimplantation embryos. It has been suggested that these mitochondrial changes may arise from excessive reactive oxygen species (ROS) that is closely associated with the oxidative energy production or calcium overload, which may trigger permeability transition pore opening and subsequent apoptosis. Therefore, mitochondria can be seen as signs for oocyte quality evaluation, and it is possible that the oocyte quality can be improved by enhancing the physical function of mitochondria. Here we reviewed recent advances in mitochondrial functions on oocytes.

show abstract

Calcium signalling in early embryos

Cited by 62 publications

References 316 publications

Molecular basis of S100 proteins interacting with the p53 homologs p63 and p73

Molecular basis of S100 proteins interacting with the p53 homologs p63 and p73

Evidences for the Role of Melatonin as a Protective Additive During Buffalo Semen Freezing

Mitochondrial functions on oocytes and preimplantation embryos

Contact Info

Product

Resources

About