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AKT role in the melanoma drug resistance.T
High phosphorylated AKT expression is associated with Esophageal Squamous Cell Cancer.
These results suggest that the classical metabolic PI3K pathway and not the canonical proliferation ERK pathway is involved in the insulin/insulin-like growth factor-1-induced increase in crypt proliferation in obese humans, which may contribute to abnormal tissue renewal and function.
High AKT1 expression is associated with hepatocellular carcinoma.
the results indicated that JB inhibits glycolysis by down-regulating HK2 expression through inactivating the Akt/mTOR pathway in non-small cell lung cancer (NSCLC) cells, suggesting that JB might be a potential therapeutic agent for the treatment of NSCLC.
PIK3CA silencing inhibited Nalm-6 cell proliferation and invasion, and promoted their apoptosis and sensitivity to chemotherapeutic drugs, potentially through regulation of the PI3K/AKT signaling pathway.
CIP2A- and SETBP1-mediated PP2A inhibition reveals AKT S473 phosphorylation to be a new biomarker in AML.
findings provided a comprehensive mutation profiling of AKT1, PIK3CA, PTEN and TP53 genes in Chinese breast cancer patients, which have potential implications in clinical management.
This study unravels an anti-metastatic role of AKT1 in the NSCLC cells with KRAS or EGFR mutations, and establishes an AKT1-MARCKS-LAMC2 feedback loop in this regulation.
LASP1 may function as an oncogene in glioblastoma and regulate cell proliferation and chemosensitivity in a PI3K/AKT-dependent mechanism.
Knockdown studies revealed that AKT sustained BCL-2 expression in uterine leiomyoma.
These data revealed that CXCR4-mediated Akt activation and signaling require endocytosis and the Rab5-effector EEA1 but not APPL1, suggesting a role for EEA1-positive endosomes in Akt signaling.
EGFR inhibition can only sensitize EGFR-high cells for chemotherapy, while AKT inhibition increases chemosensitivity in EGFR-low cells. By understanding these mechanisms, we can take advantage of the cellular context to individualize antineoplastic therapy. Finally, our data also suggest targeting of EFFRI1 in EGFR-low cancer as a promising therapeutic approach
This study presents further evidence to show that TRPM4 regulates beta-catenin signaling and enhances the proliferation of prostate cancer cell lines, through a calcium-dependent regulation of Akt1 and GSK-3beta activity.
miRNA-520a reduced hepatitis b virus transcription and replication by reducing AKT levels.
DDX5 promotes hepatocellular carcinoma tumorigenesis via Akt signaling pathway.
High AKT1 expression is associated with cholangiocarcinoma metastasis.
These results highlight an Arf GAP-independent function of ARAP2 in regulating Akt activity.
High AKT expression is associated with metastasis of hepatocellular carcinoma.
Data show that Y-box binding protein-1 (YBX1) promoted tumorigenesis and progression in spinal chordoma via the epidermal growth factor receptor (EGFR)/proto-oncogene proteins c-akt (AKT) pathway.
The role of Akt signaling in the hemangioendothelioma growth.
Akt1 deficiency leads to growth retardation.
CD36 knockdown in C2C12 myotubes accelerated insulin-stimulated Akt activation.
CLOCK phosphorylation by AKT on Ser-845 regulates its nuclear translocation and the expression levels of certain core circadian genes in insulin-sensitive tissues.
Exosomes derived from pancreatic cancer cells induce insulin resistance in C2C12 myotube cells through the Pik3cd/Akt/FoxO1 pathway.
Endothelial Akt1 signaling is necessary for ischemic resolution post-injury and likely reflects the consequence of NO insufficiency critical for vascular repair.
Akt1 plays a critical role in regulating satellite cell proliferation during load-induced muscle hypertrophy.
PIP5K1alpha was found to be required for AKT activation and calcium release, both of which were important for skeletal muscle differentiation.
Kcnj13 mutants exhibit a shorter trachea as well as defective smooth muscle cell alignment and polarity. Kcnj13 is essential to maintain ion homeostasis in tracheal smooth cells, which is required for actin polymerization and is mediated, at least in part, through activation of the actin regulator, AKT.
M-CSF-evoked ERK1/2 activation was decreased, whereas AKT activation was enhanced in SHP2-deficient BMMs. ERK1/2, via its downstream target RSK2, mediates this negative feedback by negatively regulating phosphorylation of M-CSF receptor at Tyr721 and, consequently, its binding to p85 subunit of PI3K and PI3K activation.
Site-directed mutagenesis of Akt at Cys224 revealed that S-nitrosylation at this site was pivotal for the reduced phosphorylation at Akt Ser473, which led to impaired Akt signaling. Furthermore, on HHcy challenge, as compared with GSNOR(+/+)ApoE(-/-) littermate controls, GSNOR(-/-)ApoE(-/-) double knockout mice showed reduced T-cell activation with concurrent reduction of atherosclerosis.
the present study suggested that Pulsed electromagnetic fields (PEMFs) reduced osteoclast formation from RAW264.7 macrophages via inhibition of the Akt/mTOR signaling pathway. These findings provided novel insight into the mechanisms through which PEMFs suppress osteoclast differentiation.
findings uncover a new function of p53 in the regulation of Akt signaling and reveal how p53, ASS1, and Akt are interrelated to each other.
Here, we describe a role for PI3K/AKT in the regulation of TRF1, an essential component of the shelterin complex. PI3K and AKT chemical inhibitors reduce TRF1 telomeric foci and lead to increased telomeric DNA damage and fragility. TRF1 is phosphorylated by AKT regulating TRF1 protein stability and TRF1 binding to telomeric DNA in vitro and are important for in vivo TRF1 telomere location and cell viability.
High AKT1 expression is associated with cardiac hypertrophy.
CTRP1 protected against Dox-induced cardiotoxicity via activation of AKT
Noise exposure led to enhanced JNK phosphorylation and IRS1 serine phosphorylation as well as reduced Akt phosphorylation in skeletal muscles in response to exogenous insulin stimulation.
WT PDCD5 competitively inhibited interaction between histone deacetylase 3 (HDAC3) and AKT, but PDCD5(L6R), an HDAC3-binding-deficient mutant, did not. Knockdown of PDCD5 accelerated HDAC3-AKT interaction, AKT and eNOS phosphorylation, and nitric oxide (NO) production
both NAD and NADH significantly increased the intracellular ATP levels of BV2 microglia, which were attenuated by SIRT2 siRNA, the SIRT2 inhibitor AGK2, and the phosphatidylinositol 3-kinase/Akt inhibitor LY294002. Results suggested that SIRT2 mediates the NAD-induced and NADH-induced increase in Akt phosphorylation in BV2 microglia.
CYP2E1-induced oxidative stress may be responsible for ethanol-induced suppression of Akt phosphorylation and pharmacological modulation of Akt in liver may be an effective strategy for the treatment of ethanol-induced fatty liver.
The metabolic defects of cycG mutant animals are abrogated by a concomitant loss of Wdb, CycG presumably influences Akt1 activity at the PP2A nexus; Well rounded (Wrd), another B' subunit of PP2A in Drosophila, binds CycG similar to Wdb, and that its loss ameliorates some, but not all, of the metabolic defects of cycG 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.
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 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.
Regeneration of Drosophila sensory neuron axons and dendrites is regulated by the Akt pathway involving Pten and microRNA bantam.
Overexpression of Akt enhanced Sindbis virus replication.
Perturbation of the Akt/Gsk3-beta signalling pathway is common to Drosophila expressing expanded untranslated CAG, CUG and AUUCU repeat RNAs.
dAkt activation under wild-type conditions is defined by feedback inhibition that depends on TOR Complex 1
Studies indicate that knockdown of dGirdin in the Drosophila wing imaginal disc cells resulted in reduction of cell size and this was enhanced by half reduction of the Akt gene dose.
dS6K activity is dependent on the Drosophila homologue of the phosphoinositide-dependent protein kinase 1, dPDK1, demonstrating that both dPDK1, as well as dTOR, mediated dS6K activation is phosphatidylinositide-3,4,5-trisphosphate (PIP3)-independent.
A mutation in the pleckstrin homology (PH) domain of Akt that reduces its affinity for PIP3 sufficed to rescue the lethality of flies devoid of PTEN activity.
stimulates growth by phosphorylating the tuberous sclerosis complex 2 (Tsc2) tumour suppressor and inhibiting formation of a Tsc1-Tsc2 complex
cell growth control by PTEN and it's ability to regulate known cell size regulators involved in protein translation (review)
In Drosophila cells, Drosophila protein kinase B is required for the activation of Drosophila p70 ribosomal S6 protein kinase by insulin.
InR regulates cell growth and proliferation through the dAkt pathway.
The role of the PI3K/Akt/mTOR pathway in inflammatory regulation is independent of the activation of TLRs/NF-kappaB. Cross-talk between PI3K/Akt/mTOR and TLRs/NF-kappaB signaling pathways promote inflammation.
Thus, activation of STAT3 and inactivation of AKT signaling are involved in structural regression of the corpus luteum.
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 accumulation and subsequent ovarian E2 production.
Caveolin-1 scaffolding domain residue phenylalanine 92 modulates Akt signaling
TG2 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.
The current study was designed to determine mechanisms underlying 20-hydroxyeicosatetraenoic acid -stimulated nitric oxide (NO) release, and particularly the role of NADPH oxidase, reactive oxygen species, and PI3-kinase in stimulated NO release.
PI3K/Akt and p53 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 activation in endothelial cells
Losartan metabolite stimulates eNOS phosphorylation and suppresses tumor necrosis factor alpha-induced endothelial cell apoptosis by activating AKT1.
prostaglandin F2alpha phosphorylates TSC2 and activates mTOR and ribosomal protein S6 kinase signaling in an AKT-independent manner
Results suggest that the mitogenic response to FGF-2 in vivo in the corneal endothelial layer may be inhibited by TGF-beta2-induced suppression of the PI3-kinase/AKT signaling pathway.
These results suggest that bGPR40 mediates LCFA signaling in mammary epithelial cells and thereby plays an important role in cell proliferation and survival.
Data show that laminar shear stress stimulates vascular smooth muscle cell apoptosis via the Akt pathway.
The intracellular mechanism of action of CART in regulation of FSH-induced MAPK signaling.
AMPK and AKT are both downstream of PI3K and that AKT activation is partially dependent on AMPK. The interrelationship between AMPK and AKT, although known to be individually important in mediating VEGF activation of eNOS, is clearly characterized.
These findings highlight novel and essential roles of PFKFB4 activity in later stages of neural crest (NC) development that are wired into the NC gene regulatory network.
Once inside in proximal tubule cells, glucose is diverted to the hexosamine biosynthetic pathway increasing O-GlcNAcylation of several intracellular proteins, including PKB.
Studied the effects of microRNA-27a on myogenin expression and the Akt/FoxO1 signal pathway during porcine myoblast differentiation. Overexpression of miR-27a suppressed myogenin expression during porcine myoblast differentiation, whereas inhibition of miR-27a promoted the mRNA and protein expression levels of myogenin; overexpression of miR-27a decreased the level of P-Akt/Akt and increased the protein level of FoxO1.
SCF 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 is the sensor that determines whether cells will be protected or injured by albumin; 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
Akt signaling in porcine patellofemoral joint cartilage is dependent upon frequency of loading, cartilage zone, and the time interval between loading and cartilage harvest.
in VSMCs exposed to hyperglycemia, IGF-I stimulation of Shc facilitates the transfer of Grb2 to p85 resulting in enhanced PI3K activation and AKT phosphorylation leading to enhanced cell proliferation and migration
There was no correlation of infarct size with expression or phosphorylation of AKT in ischemic postconditioning.
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, which further represses the activity of K(+) channel 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-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.
Potassium transport and gene expression in A. thaliana deficient at this site.
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+)-dependent manner, connecting the Ca(2+) signal to K(+) uptake through activation of a K(+) channel.
AtAKT1 mediates K+ absorption at high concentrations, and remains active in the presence of NH4+ although activity is reduced.
AtKC1-AKT1 channels in Arabidopsis roots facilitate growth under K+-limiting conditions
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.
Modulation of pptr-1 affects insulin/IGF-1 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 350.
Exogenous AKT was transcribed, and AKT was overexpressed, inducing the phosphorylation of p70S6K (Thr389) and 4E-BP1 (Thr37/46) in goat fetal fibroblasts.
findings suggested that the expressions of the cardiac CACNA1C were under the CLOCK-BMAL1 regulation, probably through the PI3K-Akt signal pathway
This study has identified Akt as a novel intracellular pathway required for neural crest differentiation.
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
, Akt kinase
, dAkt kinase
, protein kinase B
, related to PKA to PKC protein kinases
, related to the A and C kinases
, actin, cytoplasmic 1
, gamma non-muscle 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