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Data show that sulfatase 1 (hSulf-1 (show SULF1 Proteins)) overexpression in melanoma cells can inhibit cell proliferation and induce cell cycle arrest and apoptosis by decreasing the protein kinase B (AKT) phosphorylation and limiting cyclin dependent kinase 4 (CDK4 (show CDK4 Proteins)) nuclear import.
In summary, we demonstrate that ADAMTS18 (show ADAMTS18 Proteins) silencing in breast cancer is significantly correlated with promoter CpG methylation. ADAMTS18 (show ADAMTS18 Proteins) acts as an antagonist of AKT and NF-kappaB (show NFKB1 Proteins) signaling, further suppressing EMT (show ITK Proteins) and metastasis of breast cancer cells.
eIF3d (show EIF3D Proteins) promotes gallbladder cancer (GBC) progression mainly via eIF3d (show EIF3D Proteins)-GRK2 (show ADRBK1 Proteins)-AKT axis and it may be used as a prognostic factor. The therapeutic targeting of eIF3d (show EIF3D Proteins)-GRK2 (show ADRBK1 Proteins) axis may be a potential treatment approach for GBC.
Study demonstrates that ROS (show ROS1 Proteins)-mediated oxidative modification of Akt1 contributes to synaptic dysfunction in Alzheimer's disease, seen as loss of activity-dependent protein translation that is essential for synaptic plasticity and maintenance.
High AKT1 expression is associated with breast cancer.
The results demonstrate that in renal cells, NHE1 (show SLC9A1 Proteins) is associated with several regulatory proteins including Hsp90 (show HSP90 Proteins), and that Hsp90 (show HSP90 Proteins) affects its function possibly through altered phosphorylation of the protein via the AKT kinase.
SMYD3 (show SMYD3 Proteins)-mediated methylation of AKT1 at lysine 14 is essential for AKT1 activation and that SMYD3 (show SMYD3 Proteins)-mediated AKT1 methylation appears to be a good target for development of anti-cancer therapy.
Intra-tumour activation of the PTEN/Akt/COX-2 pathway modulates colorectal cancer (CRC (show CALR Proteins)) progression and invasive capacity.
BTK (show BTK Proteins)-mediated signaling was found to be highly attenuated accompanied by a shift in PI3K (show PIK3CA Proteins)/AKT and apoptosis regulation-associated genes/proteins. Cytotoxicity studies using the AKT inhibitor, MK2206+/-ibrutinib, and the Bcl-2 (show BCL2 Proteins)-specific inhibitor, venetoclax+/-ibrutinib, demonstrated synergistic loss of cell viability
This study for the first time demonstrated that HDAC8 (show HDAC8 Proteins) activity determines susceptibility to cell cycle arrest induced by Anthrax Lethal Toxin, through regulating the PI3K (show PIK3CA Proteins)-PTEN-AKT signaling axis.
both AKT phosphorylation and RAC-dependent membrane ruffling were markedly reduced by depletion of either APPL1 or MYO6. These results place MYO6 and its binding partners at a central nexus in cellular signaling linking actin dynamics at the cell surface and endosomal signaling in the cell cortex.
TXNIP (show TXNIP Proteins) is a direct substrate of protein kinase B (AKT) and is responsible for mediating AKT-dependent acute glucose influx after growth factor stimulation.
Influence of 1mM MbetaCD on the fenoterol-driven changes in both contractility and NO level was strongly attenuated by inhibition of Gi-protein (pertussis toxin), Akt (Akt 1/2 kinase inhibitor) or NO-synthase (L-NAME)..Obtained results suggest that slight cholesterol depletion upregulates Gi-protein/Akt/NO-synthase signaling that attenuates the positive inotropic response to b2-adrenergic stimulation
Akt1 conditions the normal circadian rhythm in the vasculature more so than in other peripheral tissues where other AKT isoforms or kinases might be important for daily rhythms.
UVB-irradiated or aged mice skin revealed that mTORC2 (show CRTC2 Proteins) activity was significantly upregulated which in turn increased Akt activation and Akt-dependent IkappaB kinase alpha (show CHUK Proteins) (IKKalpha (show CHUK Proteins)) phosphorylation, and The increased mTORC2 (show CRTC2 Proteins) signaling pathway during skin aging were associated to NF-kappaB (show NFKB1 Proteins) activation.
this study reveals the function of IL-15 (show IL15 Proteins) in astrocyte survival via Akt phosphorylation in response to OGD (show FGFR1 Proteins)-induced damage.
This study demonstrates the neuroprotective effect of TSG (show TWSG1 Proteins) on APP (show APP Proteins) expression, suggesting that TSG (show TWSG1 Proteins) may be beneficial for AD prevention and treatment.
Data show that NEDL2 regulates GDNF/Ret/Akt pathway depends on its Nedd8 ligase activity rather than ubiquitin ligase activity.
Despite higher endogenous insulin (show INS Proteins) concentrations following feeding, arcuate nucleus phosphorylation of Akt (pAkt) levels were significantly lower in the pregnant group compared with the nonpregnant group.
Setdb1 (show SETDB1 Proteins) regulates PTEN/AKT/FOXO1 (show FOXO1 Proteins) pathway to inhibit Spermatogonial stem cells apoptosis.
The metabolic defects of cycG (show CCNG1 Proteins) mutant animals are abrogated by a concomitant loss of Wdb, CycG (show CCNG1 Proteins) presumably influences Akt1 activity at the PP2A (show PPP2R2B Proteins) nexus; Well rounded (Wrd), another B' subunit of PP2A (show PPP2R2B Proteins) in Drosophila, binds CycG (show CCNG1 Proteins) similar to Wdb, and that its loss ameliorates some, but not all, of the metabolic defects of cycG (show CCNG1 Proteins) mutants.
Our findings demonstrated that lovastatin restored LRRK2-G2019S neurite degeneration by augmenting Akt/NRF2 pathway and inhibiting downstream GSK3b activity, which decreased phospho-tau levels. We suggested that lovastatin is a potential disease-modifying agent for LRRK2-G2019S parkinsonism.
These findings revise the existing spermiation model in Drosophila and suggest that somatic cells can actively oppose mechanical cell invasion attempts using calibrated F-actin dynamics in situ
subtle manipulation of foxo through Akt1 can enhance survival during adverse nutrient conditions in Drosophila.
The developmental delay of these novel Akt1 hypomorphs results in a latent phenotype uncovered by generation of somatic clones
these data show that Drosophila Trbl has a conserved role to bind Akt and block Akt-mediated insulin signaling, and implicate Trib proteins as novel sites of signaling pathway integration that link nutrient availability with cell growth and proliferation
AKT1 and caspase-dependent regulation of Acn stability adjusts basal autophagy levels.
Akt1 governs two critical elements of synapse development, neurotransmitter receptor (show GRIN1 Proteins) localization, and postsynaptic membrane elaboration
Tsc2 mutants showed a dramatic decrease in the levels of phosphorylated Akt, and interestingly, Akt mutants phenocopied Tsc2 mutants, leading to the hypothesis that Tsc2 and Akt might work via the same genetic pathway to regulate synapse growth.
Hippo signaling not only blocks cell division and promotes apoptosis, but also regulates cellular growth by inhibiting the Akt pathway activity.
This study showed that beta-actin (show ACTB Proteins), L32 (show RPL32 Proteins) ribosomal protein, and ATP5B (show ATP5B Proteins) proteins were the most stabily expressed genes in cryopreserved horse semen.
the measurement of levels of PI3K-Akt pathway components in FCs from ovarian follicles carrying oocytes with distinct developmental competences is a useful tool to identify putative molecular pathways involved in the acquisition of oocyte competence.
These results demonstrate that activation of AKT is required for gonadotropin regulation of CTNNB1 (show CTNNB1 Proteins) accumulation and subsequent ovarian E2 production.
Caveolin-1 (show CAV1 Proteins) scaffolding domain residue phenylalanine 92 modulates Akt signaling
TG2 (show TGM2 Proteins) contributes to 5-hydroxytryptamine-induced distal pulmonary artery smooth muscle cell proliferation via promotion of AKT signaling, likely via its serotonylation.
results suggest that PI3K-Akt activity is important for the internalization of S. aureus and phosphorylation of GSK-3alpha, GSK-3beta, and NF-kappaB (show NFKB1 Proteins).
The current study was designed to determine mechanisms underlying 20-hydroxyeicosatetraenoic acid -stimulated nitric oxide (NO) release, and particularly the role of NADPH oxidase (show NOX1 Proteins), reactive oxygen species, and PI3-kinase (show PIK3CA Proteins) in stimulated NO release.
PI3K/Akt and p53 (show TP53 Proteins) are redox-regulated in bovine aortic endothelial cells exposed to hydrogen peroxide
Thus our data demonstrate that hypoxia-induced adventitial fibroblast proliferation requires activation and interaction of PI3K, Akt, mTOR, p70S6K, and ERK1/2.
Gab1 tyrosine phosphorylation is stimulated by flow shear stress to mediate protein kinase B and endothelial nitric-oxide synthase (show NOS3 Proteins) activation in endothelial cells
Losartan metabolite stimulates eNOS (show NOS3 Proteins) phosphorylation and suppresses tumor necrosis factor alpha (show TNF Proteins)-induced endothelial cell apoptosis by activating AKT1.
These findings highlight novel and essential roles of PFKFB4 (show PFKFB4 Proteins) activity in later stages of neural crest (NC) development that are wired into the NC gene regulatory network.
SCF (show KITLG Proteins) is a critical regulatory factor for conceptus development and implantation during pregnancy in pigs.
These results indicate glycine enhances muscle protein mass under an inflammatory condition. The beneficial roles of glycine on the muscle are closely associated with maintaining Akt-mTOR-FOXO1 signaling and suppressing the activation of TLR4 and/or NOD2 signaling pathways.
Data show that homocysteine (Hcy) can ameliorate the endothelium-independent hypoxic coronary vasoconstriction, in which the inhibition of PI3K/Akt signaling pathway may be involved.
In pigs, lactose synthesis was significantly elevated with the increase of milk production and AKT1 could positively regulate lactose synthesis.
In conclusion, our observations reveal that PRRSV triggers the activation of FAK-PI3K-AKT-Rac1 signaling pathway to facilitate its entry into cells.
Host PI3K and Akt1 play a role in viral gene expression, leading to an increase in porcine reproductive and respiratory syndrome virus replication.
Activity of AKT is not essential for induction of germinal vesicle breakdown in porcine oocytes but plays a substantial role during progression of meiosis to MI/MII-stage.
IL-4 induced activation of Akt/SREBP-1/lipid biosynthesis in EC, resulting in protection against membrane attack complex and melittin, in association with mitochondrial protection.
findings show that megalin (show LRP2 Proteins) is the sensor that determines whether cells will be protected or injured by albumin (show ALB Proteins); it binds protein kinase B (PKB) in a D-3-phosphorylated phospholipid-insensitive manner, anchoring PKB in the luminal plasma membrane [
protein kinase B (PKB/Akt)was localized in the granulosa cells of primordial follicles and in the basal layers of the granulosa cells of preantral and antral follicles, but were not localized in atretic follicles and corpora lutea
CIPK23 and AtKC1 exhibit distinct effects; however, they act synergistically and balance K(+) uptake/leakage to modulate AKT1-mediated low potassium responses in Arabidopsis.
results suggest that NO decreases K(+) absorption by promoting the synthesis of vitamin B6 PLP (show FNTA Proteins), which further represses the activity of K(+) channel (show KCNC4 Proteins) AKT1 in Arabidopsis.
Examination of the athak5 atakt1 double mutant, revealing novel aspects of an uptake system as yet unidentified by genetic means.
AKT1 is regulated by CIPK23 in guard cells and is involved in water stress responses.
These findings provide further insights into the signaling network consisting of CBL (show CBL Proteins)-CIPK-PP2C interactions in the activation of the AKT1 channel.
Electrophysiological results showed that AtKC1 inhibited the AKT1-mediated inward K(+) currents and negatively shifted the voltage dependence of AKT1 channels.
AtHAK5 and AKT1 are vital for plant growth and development at low K+ concentrations.
In the range between 0.01 and 0.05 mM K+ AtHAK5 and AtAKT1 are the only contributors to K+ acquisition. At higher K+ concentrations, unknown systems come into operation and participate together with AtAKT1 in low-affinity K+ uptake.
CIPK23 directly phosphorylates the K+ transporter AKT1
Data show that interacting calcium sensors (CBL1 and CBL9) together with CIPK23, but not either alone, activated the AKT1 channel in a Ca(2 (show CA2 Proteins)+)-dependent manner, connecting the Ca(2 (show CA2 Proteins)+) signal to K(+) uptake through activation of a K(+) channel (show KCNC4 Proteins).
the LIN-28/let-7/AKT/DAF-16 axis is a program that plays an important role in balancing reproduction and somatic maintenance.
this study shows that akt-1 and akt-2 negatively regulate DNA-damage-induced apoptosis in the C. elegans germline and the antiapoptotic activity of akt-1 is independent of its target gene daf-16 but dependent on cep-1/p53 (show TP53 Proteins).
Modulation of pptr-1 affects insulin (show INS Proteins)/IGF-1 (show IGF1 Proteins) signaling pathway-associated phenotypes including life span, dauer, stress resistance, and fat storage; study shows that PPTR-1 functions by regulating worm AKT-1 phosphorylation at Thr (show TRH Proteins) 350.
Exogenous AKT was transcribed, and AKT was overexpressed, inducing the phosphorylation of p70S6K (show RPS6KB1 Proteins) (Thr389) and 4E-BP1 (show EIF4EBP1 Proteins) (Thr37/46) in goat fetal fibroblasts.
findings suggested that the expressions of the cardiac CACNA1C (show CACNA1C Proteins) were under the CLOCK-BMAL1 (show ARNTL Proteins) regulation, probably through the PI3K-Akt signal pathway
Overexpression of human Akt1 enhances adipogenesis and leads to lipoma formation in zebrafish.
The serine-threonine protein kinase encoded by the AKT1 gene is catalytically inactive in serum-starved primary and immortalized fibroblasts. AKT1 and the related AKT2 are activated by platelet-derived growth factor. The activation is rapid and specific, and it is abrogated by mutations in the pleckstrin homology domain of AKT1. It was shown that the activation occurs through phosphatidylinositol 3-kinase. In the developing nervous system AKT is a critical mediator of growth factor-induced neuronal survival. Survival factors can suppress apoptosis in a transcription-independent manner by activating the serine/threonine kinase AKT1, which then phosphorylates and inactivates components of the apoptotic machinery. Mutations in this gene have been associated with the Proteus syndrome. Multiple alternatively spliced transcript variants have been found for this gene.
, RAC-alpha serine/threonine-protein kinase
, protein kinase B alpha
, proto-oncogene c-Akt
, rac protein kinase alpha
, AKT1 kinase
, protein kinase B-alpha
, proto-oncogene c-AKT
, related to A and C kinases
, actin, cytoplasmic 1
, Akt kinase
, dAkt kinase
, protein kinase B
, related to PKA to PKC protein kinases
, related to the A and C kinases
, 5C actin
, actin 5 C
, actin 5C
, actin 5c
, actin A1
, cellular cytoskeletal beta-actin
, gamma non-muscle actin
, beta actin
, RAC protein kinase alpha RAC-PK alpha
, murine thymoma viral (v-akt) oncogene homolog 1
, thymoma viral proto-oncogene 1
, v-akt murine thymoma viral oncogene-like protein 1
, serine/threonine protein kinase
, protein kinase Akt-1
, protein kinase B, alpha
, v-akt murine thymoma viral oncogene homolog 1
, v-akt murine thymoma viral oncogene-like 1