Sentences with phrase «decreased phosphorylation»

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).

However, depletion of ABL kinases decreased the phosphorylation of STAT5 (Fig. 7D and fig.

TAZ knockdown with two distinct shRNAs decreased the phosphorylation of STAT5 and, to a lesser extent, total STAT5 protein abundance (fig.

We also show that inhibition of mTOR with rapamycin, as well as silencing mTOR gene product expression using mTOR - specific small interfering RNA, decreased phosphorylation of mTOR signaling proteins and induced cell cycle arrest and apoptosis in ALK + ALCL cells.

Decreased phosphorylation of PDGFR - ß impairs the angiogenic potential of expanded endothelial progenitor cells via the inhibition of PI3K / Akt signaling.

Double knockdown of ABL1 and ABL2 was required to decrease the phosphorylation of CrkL by more than 90 %, which indicates inactivation of the endogenous ABL kinases (Fig. 2K).

Thus, we examined whether VPA treatment could increase the acetylation level of Akt and, in turn, decrease the phosphorylation level of Akt.

Not exact matches

This results in cells having less mitochondrial DNA, decreased mitochondrial membrane potential and a faulty process in cell metabolism called oxidative phosphorylation.

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.

We discovered that 2 hours cyclic stretching increased the phosphorylation of moesin, elongation factor eEF1D and leprecan, while the phosphorylation of elongation factor eEF1B decreased after cellular stretching.

Mutation of Hof1 PEST motif phosphorylation sites leads to retention of Hof1 at the bud neck and a decrease in the rate of myosin contraction.

C and D, inhibition of AKT1 expression or activity decreases mTOR phosphorylation.

Because treatment with rapamycin also led to decreased AKT phosphorylation in ALK + ALCL cells in our in vitro study, it is tempting to speculate that an effector protein downstream of mTOR - raptor may contribute directly or indirectly to AKT activation.

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).

Since the expression of genes representing oxidative phosphorylation is decreased in adipose tissue of T2D twins (Table 2 and Fig. 1A), we quantified mtDNA content to follow up these results.

Silencing of total mTOR gene expression by siRNA decreased AKT phosphorylation.

Of note, treatment of ALCL cell lines with rapamycin also resulted in a slight decrease of Ser473 phosphorylation of AKT.

We showed that inactivation of the ABL kinases in breast cancer cells resulted in decreased expression of genes in the JAK / STAT and cytokine / cytokine receptor pathway signatures, which may be due to decreased STAT5A mRNA expression and reduced STAT5 phosphorylation in ABL1 / ABL2 - depleted breast cancer cells.

We found that ~ 90 % knockdown of ABL1 alone resulted in enhanced ABL2 expression and did not produce a significant decrease in the phosphorylation of CrkL, a reporter for the activation state of the ABL kinases (Fig. 2K), and did not inhibit metastasis (Fig. 2, L and M).

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.

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.

Phosphorylation of mTOR is increased in response to leucine [20], an excellent substrate for SLC6A14; as such, our findings that mTOR phosphorylation is markedly decreased in Slc6a14 − / − tumours indicate that the tumours suffer from amino acPhosphorylation of mTOR is increased in response to leucine [20], an excellent substrate for SLC6A14; as such, our findings that mTOR phosphorylation is markedly decreased in Slc6a14 − / − tumours indicate that the tumours suffer from amino acphosphorylation is markedly decreased in Slc6a14 − / − tumours indicate that the tumours suffer from amino acid deprivation.

Phosphorylation of AKT decreased after treatment with ActD for 10 minutes in the 293, 293T, and Hepa - 1c1c7 cells, but still increased after treatment with ActD (10 and 30 nM) for 10 minutes in the HepG2 cells.

Twelve - hour exposure of 3T3 - L1 adipocytes to H (2) O (2) or TNF - alpha resulted in the increase of c - Jun NH (2)- terminal kinase (JNK) activation and insulin receptor substrate 1 (IRS1) serine 307 phosphorylation, concomitantly with the decrease in insulin - stimulated IRS1 tyrosine phosphorylation and cellular glucose uptake.

Furthermore, Cy -3-g substantially induced AMPK downstream target ACC phosphorylation and inactivation, and then decreased malonyl CoA contents, leading to stimulation of CPT - 1 expression and significant increase of fatty acid oxidation in HepG2 cells.

Moreover, C3G treatment decreased c - Jun N - terminal kinase activation and promoted phosphorylation and nuclear exclusion of forkhead box O1 after refeeding.

Therefore, the hyperinsulinemia registered in vivo and in vitro, associated with the impairment of glucose tolerance and the decrease in AKT phosphorylation, make clear the occurrence of peripheral insulin resistance.