IndraLab
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"AKT signaling is important in endothelial-to-mesenchymal transition and myofibroblastic transformation in fibroblasts from the heart and lungs.32, 33 miR-486 may upregulate AKT activity through negative regulation of PTEN expression.43 The phosphoinositide phosphatase PTEN converts PIP3 to PIP2 and thereby negatively modulates AKT activity,31 thus downregulation of PTEN can upregulate AKT phosphorylation.43, 53 We evaluated the role of the AKT pathway in mediating alpha-SMA expression induced by miR-486 mimic."
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"Our in vitro and in vivo data showed that activation of PTEN increased Foxo1 activity, whereas myeloid specific PTEN deficiency increased Akt phosphorylation, which in turn phosphorylated Foxo1, resulting in increasing its exportation from the nucleus to the cytoplasm and reducing its DNA binding capacity, thereby inhibiting Foxo1 transcriptional activity."
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"Taken together, the -dependent PTP1B activation mediates IGF-1 and AKT suppression at the step ofIGF-1Rbeta dephosphorylation, while PTEN recruitment and activation at the plasma membrane enhance the dephosphorylation of its phospholipid substrate PIP3 to PIP2, thus suppressing the phosphorylation (activation) of AKT."
rlimsp
"Taken together, it is suggested that suppression of cerebral ischemic injury by 17 beta-estradiol may be ascribed to the maxi-K channel opening-coupled downregulation of PTEN phosphorylation and upregulation of Akt and CREB phosphorylation with resultant increase in Bcl-2 protein and decrease in Bax protein and cytochrome c release."
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"As such, phosphatase and tensin homolog (PTEN) not only counteracts PKB and Akt activity by reducing phosphatidylinositol 3,4,5-trisphosphate (PIP 3) levels but also reverses the PKB and Akt dependent phosphorylation of IP 3 Rs, particularly at the MAMs where IP 3 R3 becomes dephosphorylated and de-repressed."
sparser
"This study has demonstrated the following novel findings: (1) Zn treatment can significantly improve diabetes-induced renal functional and pathological changes in OVE26 and Akt2-KO diabetic models; (2) the therapeutic effect of Zn treatment on the diabetic kidney is associated with the stimulation of MT expression and Akt-mediated metabolic signaling; (3) preservation of Akt-mediated metabolic signaling by Zn treatment may be associated with Zn-mediated suppression of Akt negative regulators PTEN phosphorylation and PTP1B and TRB3 expression, under diabetic conditions; (4) deletion of the Akt2 gene had no effect on Zn’s ability to provide renal protection against diabetes-induced functional and pathologic changes; furthermore, deletion of the Akt2 gene had no effect on Zn-induced stimulation of Akt-mediated metabolic signaling; (5) however, Zn-induced stimulation of Akt-related metabolic signaling is MT dependent, at least under normal physiological conditions."
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"Both Pten protein and mRNA in migrasomes can transfer into the recipient cells, and Pten protein modulates Akt phosphorylation in the recipient cell at earlier time points, while Pten mRNA plays a more important role at later time points; in which time, it can translate into Pten protein [2]."
sparser
"Currently, PD-L1 is the main target for tumor immunotherapy, and some PD-L1 monoclonal antibodies, such as durvalumab and atezolizumab, have shown good clinical therapeutic effects. xref , xref In addition to factors that directly regulate PD-L1 mRNA, studies have shown that the transcription and expression of PD-L1 in tumor cells are strongly dependent on the interferon-γ (IFN–γ) signaling pathway (Fig. xref ). xref , xref In addition, PD-L1 is also regulated by the phosphatase and tensin homolog deleted on chromosome ten (PTEN)/phosphatidylinositide 3-kinase (PI3K)/AKT/mammalian target of rapamycin (mTOR) signaling pathway in tumor cells (Fig. xref ). xref The absence of PTEN promotes AKT and mTOR phosphorylation, which in turn leads to increased PD-L1 translation (Fig. xref ). xref miRNAs can affect PD-L1 expression in tumor cells by directly targeting the PD-L1 mRNA or targeting the intermediate links of related signaling pathways (Table xref , Fig. xref )."
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"Kunliang Guan et al provided evidences that YAP mediates the major effects of the Hippo pathway by regulating gene expression, and among the YAP target genes is the miR-29 family, which inhibits PTEN, a tumor suppressor that inhibits the phosphorylation of Akt by targeting its 3 ' UTR [XREF_BIBR]."
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"As such, phosphatase and tensin homolog (PTEN) not only counteracts PKB and Akt activity by reducing phosphatidylinositol 3,4,5-trisphosphate (PIP 3) levels but also reverses the PKB and Akt dependent phosphorylation of IP 3 Rs, particularly at the MAMs where IP 3 R3 becomes dephosphorylated and de-repressed."
sparser
"Thus, the presence of a wild-type PTEN protein results in the reduction of Akt activity/phosphorylation leading to the inhibition of IκB phosphorylation and the sequestration of NF-κB. On the opposite, the presence of a mutated PTEN protein enables Akt phosphorylation, which in turn may phosphorylate IκB allowing NF-κB to be translocated to the nucleus to induce transcription of genes involved in cell survival."
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"As previously reported, the p110beta selective inhibitor TGX221 strongly impaired PI3K signaling in PTEN deficient cancer cell lines, whereas the p110alpha selective inhibitor A66 significantly inhibited AKT phosphorylation in cancer cell lines with wild-type PTEN (data not shown)."
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"10 In PCa the most common mechanism of PI3K pathway activation is the deletion of the gene encoding the phosphatase and tensin homolog (PTEN) protein, whose inactivation in turns leads to phosphorylations of AKT and of the S6 ribosomal subunit, which are therefore powerful biomarkers of PI3K activation."
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"Inhibitors of reactive oxygen species and phosphatase and tensin homolog restored AKT phosphorylation but abolished ERK 1/2 phosphorylation, suggesting that the reactive oxygen species dependent increase in phosphatase and tensin homolog activity in reperfusion period relieves ERK 1/2 from inhibition of AKT."
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"Moreover, inactivation of phosphatase and tensin homolog increased Akt phosphorylation in quiescent muscle satellite cells and induced cytoplasmic translocation of Forkhead box protein O1 (FOXO1) -- a major substrate of phosphorylated Akt -- while repressing Notch signaling, causing muscle satellite cells to exit quiescence and leading to depletion of the SC pool [XREF_BIBR, XREF_BIBR]."
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"To investigate the signaling events governing PGF2alpha induced VSMC hypertrophy we examined the ability of the PGF2alpha analog, fluprostenol to elicit phosphorylation of Akt, the mammalian target of rapamycin (mTOR), ribosomal protein S6 kinase (p70S6k), glycogen synthase kinase-3beta (GSK-3beta), phosphatase and tensin homolog (PTEN), extracellular signal regulated kinase 1/2 (ERK1/2) and Jun N-terminal kinase (JNK) in growth arrested A7r5 VSMC."
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"As shown in XREF_FIG, although all three growth factors and PTEN depletion induced comparable Akt phosphorylation detected by WB (not shown), analysis of samples by cIEF showed striking differences between the changes in Ser (P) 473 -Akt in response to growth factors or PTEN depletion (XREF_FIG A)."
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"However, we did not find correlation between PTEN and p-Akt (as a measurement of Akt activation) immunostaining in most of the tumors, suggesting the existence of PTEN independent mechanisms driving Akt phosphorylation and activation in CCRCC, as previously proposed by others [XREF_BIBR]."
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"The original hypothesis based on data obtained from these cells is that ligand activation of PPARbeta and delta increases expression of 3-phosphoinositide-dependent-protein kinase 1 (PDPK1) and integrin linked kinase (ILK) and decreases expression of phosphatase and tensin homolog deleted on chromosome Ten (PTEN) causing increased phosphorylation of protein kinase B (AKT) leading to anti-apoptotic signaling and enhanced cell survival (XREF_TABLE and XREF_TABLE)."
sparser
"PTEN silencing increased the phosphorylation of AKT and the expression of PI3K but decreased the phosphorylation of IRS1, which increased the phosphorylation levels of glycogen synthase kinase-3β (GSK-3β) and expression of sterol regulatory element-binding protein-1c (SREBP-1c)."
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"Moreover, p53-induced PTEN dephosphorylates phosphatidylinositol 3,4,5-trisphosphate (PIP3) and indirectly represses the phosphorylation of Akt, thereby preventing nuclear entry of Mdm2c [34,36], enclosing another positive feedback loop.The expression of each target gene by p53 is represented by a Hill function, and the Hill coefficient is set to 4 given that p53 functions as a transcription factor in a tetrameric form [37]."
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"Our results also showed that the dual mutations of tp53 and pten greatly increased Akt phosphorylation and obviously induced the features of nonalcoholic steatohepatitis (NASH), including infiltration of inflammatory cells, collagen deposition, and abnormal lipid accumulation [7, 87], in tumours derived from liver tissues in zebrafish (Fig. 4d-g)."
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"Decreased microRNA (miR) -144 expression and increased PTEN expression after TPL treatment were demonstrated, and TPL enhanced p85alpha-PTEN complexes and inhibitory effects on Akt (Ser 473) phosphorylation and S phase arrest were suppressed by ectopic PTEN short hairpin RNA or miR-144 expression."
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"Different mechanisms of action may explain those findings in un-irradiated skin, such as the inhibition of phosphorylation of AKT by PTEN may be impaired through its somatic mutation and inactivation, without alteration in protein expression as previously found in a number of malignancies including melanoma [ xref ]."
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"Korkaya and colleagues demonstrated that phosphatase and tensin homolog knockdown increased phosphorylation of Akt, leading to enriched normal and malignant mammary stem and progenitor cells, and that this Akt driven process was mediated by the Wnt and beta-catenin pathway [XREF_BIBR]."