Sentences with phrase «phosphorylation level of»

The idea that both STAT2 and IRF - 9 were basic components necessary for RIG - G expression was also supported by the fact that ATRA could not only induce the total amounts of STAT2 and IRF - 9 proteins but also increase the tyrosine phosphorylation level of STAT2 in NB4 cells (Fig. 1A).
Thus, we examined whether VPA treatment could increase the acetylation level of Akt and, in turn, decrease the phosphorylation level of Akt.
In this study, we demonstrate that VPA treatment ameliorated GVHD in a mouse BMT model by downregulating Th1 and Th17 cells and reducing inflammatory cytokine levels via inhibition of the phosphorylation level of Akt in CD4 + T cells.
(H) Spleen CD4 + T cells harvested from VPA recipients and control mice on day 21 were analyzed by Western blot assay for the expression and phosphorylation level of Akt and downstream target proteins.
We isolated spleen CD4 + T cells from VPA recipients and vehicle recipients and assessed the phosphorylation level of Akt.
Spleen CD4 + T cells were harvested from mice 21 d after transplantation and cultured or not with VPA for 24 h. Western blot assay showed that VPA attenuated the phosphorylation level of Akt in a dose - dependent manner (Fig. 4F).
We observed that the phosphorylation level of AKT significantly correlated with the phosphorylation level of mTOR and rpS6 as well as with expression of total 4E - BP1 and eIF4E in ALK + ALCL tumors.
Treatment of the Karpas 299 and SU - DHL1 cell lines with increasing concentrations of rapamycin, an inhibitor of the mTOR - raptor complex, resulted in a marked concentration - dependent decrease of the phosphorylation levels of mTOR, p70S6K, 4E - BP1, and total eIF4E (Fig. 4A).
The phosphorylation levels of downstream target proteins of Akt also were downregulated in parallel (Fig. 4F).
As shown in Fig. 4H, the phosphorylation levels of Akt, as well as the downstream target proteins, were reduced in the VPA - treated group compared with vehicle - control group.

Not exact matches

«Now, we need to better understand how this works at the molecular level so we can perhaps design therapeutics to prevent phosphorylation of that site.»
The phosphorylation of eIF2alpha, which decreases protein synthesis, was previously found at elevated levels in both humans diagnosed with Alzheimer's and in Alzheimer's Disease (AD) model mice.
Klann and his colleagues hypothesized that abnormally high levels of eIF2alpha phosphorylation could become detrimental because, ultimately, protein synthesis would diminish, thereby undermining the ability to form long - term memories.
To test potential remedies, the researchers examined phosphorylation of eIF2alpha in mice lacking PERK, hypothesizing that removal of this kinase would return protein synthesis to normal levels.
In recent years, researchers have found that both humans with Alzheimer's Disease and AD model mice have relatively high levels of eIF2alpha phosphorylation.
Such modifications, including methylation, acetylation, ubiquitination, and phosphorylation, often result in the alteration of gene expression levels that determine cell fate.
In vitro, Pkn1 — / — Cgcs exhibited deregulated axonal outgrowth, elevated AKT phosphorylation, and higher levels of neuronal differentiation - 2 (NeuroD2), a transcription factor preventing presynaptic maturation.
At a molecular level, loss of insulin signaling in astrocytes impaired tyrosine phosphorylation of Munc18c.
Embryos that expressed the mutant R206H ACVR1 showed increased levels of Smad1 / 5 phosphorylation relative to embryos expressing the control ACVR1 (Figure 3M).
The enhanced hiPS - HEP cells respond to insulin with phosphorylation of protein kinase B - α (Akt), even at low insulin concentrations, and the genes involved in glycogen metabolism, gluconeogenesis, and insulin signaling are expressed at similar levels as in hphep cells.
Stimulation of BP with the Tie2 ligand Ang1 resulted in detectable Tie2 phosphorylation, albeit again at considerably lower levels as in EC (Fig. 1e — h).
Here, we show that enhanced hiPS - HEP cells respond to insulin with phosphorylation of protein kinase B - α (Akt), even at low insulin concentrations (Figure 4, Panels E and F), and that the genes involved in glycogen metabolism, gluconeogenesis, and insulin signaling are expressed at similar levels as in hphep cells (Figure 4, Panels B, C, and D).
Thus the phosphorylation of CREB by J147 could increase the levels of BDNF, which consequently may increase BDNF responsive proteins.
Infection of both cell lines with adeno - myrAkt resulted in substantially increased of Ser473p - AKT levels (A) associated with increased phosphorylation (activation) of mTOR, p70S6K, and rpS6 (B).
That is high levels of PTP1B in the cell can lead to reduction in insulin receptor activation or phosphorylation; reduction in IRS - 1, IRS - 2 phosphorylation; reduction in activation of PI - 3 kinase.
Finally, in a mouse model of tauopathy, mice subjected to the flickering - light treatment had lower levels of tau phosphorylation associated with formation of neurotoxic tangles.
Measuring the levels of AKT phosphorylation and FoxO transcriptional activity provide two useful readouts of IIS levels.
Although p53 protein levels decreased after reaching the maximal level with treatment of 30 nM ActD, phosphorylation of p53 still increased with treatment of high doses (100 and 300 nM) of ActD.
The results revealed that the supernatant of 72 - hour ATRA - treated NB4 cells was sufficient to induce the tyrosine phosphorylation of STAT2 and the endogenous RIG - G level in U3A cells, in comparison with the relative consistent level of total STAT2 (Fig. 3B).
Low levels of glutathione peroxidase 1 activity in selenium - deficient mouse liver affect c - Jun N - terminal kinase activation and p53 phosphorylation on Ser - 15 in pro-oxidant-induced aponecrosis.
As lethal toxin treatment led to reduced levels of MEK1 / 2 and MKK3 / 6 and reduced phosphorylation of ERK1 / 2 and p38, we examined the role of these two MAPK kinases in IL - 22 production in ILC3s.
Although p53 protein levels decreased after reaching the maximal level with treatment of 100 nM ActD, phosphorylation of p53 still increased with treatment of a high dose (300 nM) of ActD.
Similarly, increased level of STAT2 tyrosine phosphorylation was detected as well in IRF - 1 — transfected HT1080 cells (Fig. 4B).
In the dosage studies, the expression and phosphorylation of p53 reached a maximal level with treatment of 10 nM ActD for 24 h in the 293 and 293T cells (Fig. 1B).
In contrast, treatment with ActD (10 nM) distinctly induced the expression and phosphorylation of p53 at 3 h, reaching a maximal response at 6 h, and maintaining a high level of p53 for up to 12 h in the HepG2 cells.
Stimulation of gamma waves reduced levels of amyloid - β, decreased phosphorylation of tau, and led the brain's immune cells — microglia — to perform their usual housekeeping role, clearing away cellular debris, including amyloid - β (as opposed mounting an inflammatory response as microglia do in Alzheimer's disease, Tanzi explained).
In the Hepa - 1c1c7 cells, treatment with ActD (10 nM) distinctly induced the expression and phosphorylation of p53 at 6 h, and a high level of p53 was maintained for up to 12 h (Fig. 1A).
We also found high levels of strA and strB, two resistance genes encoding for the aminoglycoside phosphotransferases APH (3 ″)- Ib and APH (6)- Id which inactivates streptomycin by phosphorylation [26].
We find comparable levels of STAT5 phosphorylation (p = 0.5) and total STAT5a (p = 0.2) in the mammary gland at lactation day 12 regardless of whether the pregnancy is «early» or «late» (Figure 8 — figure supplement 1A, B of the revised submission).
In particular, our results demonstrate that LA increases reactive oxygen species levels, stimulates the phosphorylation of EGFR, ERK and c - Jun and induces the expression of c - fos.
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