Sentences with phrase «mtor signaling proteins»

A and B, adenovirus - mediated overexpression of Ser473p - AKT up - regulates mTOR signaling proteins.

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.

A and B, phosphorylation and subcellular localization of mTOR signaling proteins in ALCL cell lines.

Inhibition of the PI3K / AKT pathway down - regulates mTOR signaling proteins.

Activation status of mTOR signaling proteins in ALCL cell tumors tumors.

The phosphorylation status of all mTOR signaling proteins was determined as negative, positive, and strongly positive (+ +) depending on the presence and staining intensity of signal (Table 1).

Not exact matches

A rapalog inhibits the mTOR protein by preventing it from activating some signals,» she says.

When the mitochondrial translation rate increases, the mTOR signaling pathway is activated, which causes the increase in the cytoplasmic protein translation rate to counteract pressure from the increased mitochondrial translation, thus representing a new evolutionary adaptation mechanism.

Here, we provide evidence that mTOR signaling phosphoproteins, including mTOR, eukaryotic initiation factor 4E — binding protein - 1, p70S6K, and ribosomal protein S6, are highly phosphorylated in ALK + ALCL cell lines and tumors.

mTOR is a regulatory protein that controls growth, metabolism and protein turnover which integrates signals from the cell and from the environment to sense nutrient and energy conditions.

Using DOS and small - molecule screening, Schreiber helped illuminate many cellular pathways, including the nutrient - response signaling network involving TOR proteins in yeast and mTOR in mammalian cells.

At the cellular level, p53 can either induce senescence or, of major interest here, inhibit senescence by controlling both reactive oxygen species (ROS) levels and a signaling pathway mediated by protein kinases AMPK and mammalian target of rapamycin (mTOR).

Abbreviations: ASC, apoptosis - associated speck - like protein containing a caspase - recruitment domain; ATM, adipose - tissue - resident macrophage; BAT, brown adipose tissue; CCR2, CC chemokine receptor 2; CHOP, C / EBP (CCAAT / enhancer - binding protein)- homologous protein; DHA, docosahexaenoic acid; EPA, eicosapentaenoic acid; ER, endoplasmic reticulum; GPCR, G - protein - coupled receptor; HIF, hypoxia - inducible factor; IFNγ, interferon γ; IKK, inhibitor of nuclear factor κB kinase; IL, interleukin; IRS - 1, insulin receptor substrate - 1; JNK, c - Jun N - terminal kinase; LDL, low - density lipoprotein; Ldlr, LDL receptor; LXR, liver X receptor; MCP - 1, monocyte chemoattractant protein 1; miRNA, microRNA; mTOR, mammalian target of rapamycin; NAFLD, non-alcoholic fatty liver disease; NF - κB, nuclear factor κB; NLRP3, NLR (nucleotide - binding - domain - and leucine - rich - repeat - containing) family, pyrin - domain - containing 3; oxLDL, oxidized LDL; PKR, double - stranded RNA - dependent protein kinase; PPAR, peroxisome - proliferator - activated receptor; STAT6, signal transducer and activator of transcription 6; SVF, stromal vascular fraction; TLR, Toll - like receptor; TNFα, tumour necrosis factor α; UPR, unfolded protein response; WAT, white adipose tissue

Abbreviations: Aβ, amyloid β - peptide; AD, Alzheimer's disease; ALS, amyotrophic lateral sclerosis; Ambra1, activating molecule in Beclin -1-regulated autophagy; AMPK, AMP - activated protein kinase; APP, amyloid precursor protein; AR, androgen receptor; Atg, autophagy - related; AV, autophagic vacuole; Bcl, B - cell lymphoma; BH3, Bcl - 2 homology 3; CaMKKβ, Ca2 + - dependent protein kinase kinase β; CHMP2B, charged multivesicular body protein 2B; CMA, chaperone - mediated autophagy; 2 ′ 5 ′ ddA, 2 ′, 5 ′ - dideoxyadenosine; deptor, DEP - domain containing mTOR - interacting protein; DRPLA, dentatorubral pallidoluysian atrophy; 4E - BP1, translation initiation factor 4E - binding protein - 1; Epac, exchange protein directly activated by cAMP; ER, endoplasmic reticulum; ERK1 / 2, extracellular - signal - regulated kinase 1/2; ESCRT, endosomal sorting complex required for transport; FAD, familial AD; FDA, U.S. Food and Drug Administration; FIP200, focal adhesion kinase family - interacting protein of 200 kDa; FoxO3, forkhead box O3; FTD, frontotemporal dementia; FTD3, FTD linked to chromosome 3; GAP, GTPase - activating protein; GR, guanidine retinoid; GSK3, glycogen synthase kinase 3; HD, Huntington's disease; hiPSC, human induced pluripotent stem cell; hVps, mammalian vacuolar protein sorting homologue; IKK, inhibitor of nuclear factor κB kinase; IMPase, inositol monophosphatase; IP3R, Ins (1,4,5) P3 receptor; I1R, imidazoline - 1 receptor; JNK1, c - Jun N - terminal kinase 1; LC3, light chain 3; LD, Lafora disease; L - NAME, NG - nitro - L - arginine methyl ester; LRRK2, leucine - rich repeat kinase 2; MIPS, myo - inositol -1-phosphate synthase; mLST8, mammalian lethal with SEC13 protein 8; MND, motor neuron disease; mTOR, mammalian target of rapamycin; mTORC, mTOR complex; MVB, multivesicular body; NAC, N - acetylcysteine; NBR1, neighbour of BRCA1 gene 1; NOS, nitric oxide synthase; p70S6K, ribosomal protein S6 kinase - 1; PD, Parkinson's disease; PDK1, phosphoinositide - dependent kinase 1; PE, phosphatidylethanolamine; PI3K, phosphoinositide 3 - kinase; PI3KC1a, class Ia PI3K; PI3KC3, class III PI3K; PI3KK, PI3K - related protein kinase; PINK1, PTEN - induced kinase 1; PKA, protein kinase A; PLC, phospholipase C; polyQ, polyglutamine; PS, presenilin; PTEN, phosphatase and tensin homologue deleted from chromosome 10; Rag, Ras - related GTP - binding protein; raptor, regulatory - associated protein of mTOR; Rheb, Ras homologue enriched in brain; rictor, rapamycin - insensitive companion of mTOR; SBMA, spinobulbar muscular atrophy; SCA, spinocerebellar ataxia; SLC, solute carrier; SMER, small - molecule enhancer of rapamycin; SMIR, small - molecule inhibitor of rapamycin; SNARE, N - ethylmaleimide - sensitive factor - attachment protein receptor; SOD1, copper / zinc superoxide dismutase 1; TFEB, transcription factor EB; TOR, target of rapamycin; TSC, tuberous sclerosis complex; ULK1, UNC -51-like kinase 1; UVRAG, UV irradiation resistance - associated gene; VAMP, vesicle - associated membrane protein; v - ATPase, vacuolar H + - ATPase; Vps, vacuolar protein sorting

There is also another mechanism by which cellular amino acid nutrition impacts on mTOR signalling; this involves the amino acids generated within the lysosomes by intracellular protein degradation and autophagosomal digestion [23,24].

The augmented anabolic response to amino acids and insulin was shown to be due to an increased activation of the mTOR / p70S6K signalling pathway, which is considered an integral control point for muscle protein anabolism and muscle cell growth.

mTOR is the signal that says, «Let's make some protein!»

Eating too much protein can also activate your body's most important signaling pathway — mTOR, or the mammalian target of rapamycin — and boost your risk of cancer.

Insulin and leptin receptor resistance from too many net carbs and activation of the mTOR metabolic signaling pathway by too much protein.

Akt stimulates glucose uptake, glycogen synthesis, and protein synthesis via Akt / mTOR and Akt / GSK -3 β signaling networks and inhibits apoptosis and protein degradation in skeletal muscle by inactivating FoxO transcription factors leading to increased lean mass.

mTOR integrates signals from insulin, nutrients (amino acids or dietary protein) and the fuel gauge of the cell, AMPK (all energy including fats) to determine whether the cell should divide and grow, or involute and become dormant.

The resulting increase in free amino acid concentrations activates the serine / threonine kinases, Akt1 and Akt2, which mobilize the signaling protein mTOR (the mammalian target of rapamycin), which then suppresses autophagic activity.

\ u003cbr \ u003e \ u003cbr \ u003e \ u003cstrong \ u003eGaspari Nutrition SizeOn ¨ Max Performance Benefits: \ u003c\ / strong \ u003e \ u003c\ / p \ u003e \ n \ u003cul \ u003e \ n \ u003cli \ u003eSpeeds up Protein Synthesis \ u0026amp; Muscle Force Recovery \ u003c\ / li \ u003e \ n \ u003cli \ u003eHeightened Muscle Volume, Muscle Fiber Size, Cell Volume \ u0026amp; Plasma Amino Acid Levels \ u003c\ / li \ u003e \ n \ u003cli \ u003eIntensifies S6K1 and 4E - BP1 Signaling and Hypertrophic mTOR Pathway Conduction \ u003c\ / li \ u003e \ n \ u003cli \ u003eInitiates \ u0026amp; Maintains Myogenesis and Muscle Recovery While You Are Still Training \ u003c\ / li \ u003e \ n \ u003cli \ u003eTransports Vital Nutrients, Essential Minerals, and Growth Co-factors To Skeletal Muscle Tissue.

Leucine is both a component of muscle but also a potent signaling molecule for a protein called mTOR which, when activated, tells muscle cells to collect and store amino acids.

Leucine is the catalyst in signaling the mTOR pathway which activates protein synthesis.

Reactive oxygen species (ROS) are not universally bad, and one of their important functions is to signal the body to increase protein synthesis as part of the mTOR pathway.

The «typical» high - protein dietary recommendations promoted on BB websites lead to increased IGF1 and mTOR signalling which is not very healthy for an adult as these are growth factors that tend to grow things (e.g. cancer) that we are not looking forward to.

mTOR is extremely sensitive to Leucine and decreasing concentrations signal to mTOR that there is not enough dietary protein present to synthesize new skeletal muscle protein, so mTOR deactivates.

Increased Leucine levels signal to mTOR that there is enough dietary protein to synthesize new skeletal muscle protein, so mTOR «turns on» muscle growth.

For example, because long - term use of marijuana downregulates the expression and responsiveness of the CB1 receptor, in a manner similar to frequent blood sugar swings leading to insulin resistance, some say that THC may impair muscle building by interrupting the mTOR signaling pathway, which is important for protein synthesis.

It seems that both signaling muscle protein synthesis (MPS) and aging prematurely (as discussed in this and previous video) involve the leucine / mTOR connection.

Declining leucine levels signal mTOR that there's a lack of dietary protein present to synthesize new skeletal muscle protein, therefore disabling mTOR.

Upon ingesting increased concentrations of leucine, the elevated amino acid then signals mTOR that sufficient dietary protein exists, and switches on overall protein synthesis.

The discordant mTOR - p70S6K phosphorylation with protein only and protein feedings with alcohol is not unprecedented given we [8] and others [43] have shown that mTOR - S6K phosphorylation often parallels changes in MPS but does not always reflect either the magnitude or duration of the increased MPS signal in humans.

The first novel finding of this study was that mTOR signaling and rates of myofibrillar protein synthesis (MPS) following concurrent resistance, continuous and intermittent high - intensity exercise, designed to mimic the metabolic profile of many team sports, were impaired during the early (8 h) recovery phase by the ingestion of large amounts (1.5 g • kg − 1 BM) of alcohol.

AMP - activated protein kinase suppresses protein synthesis in rat skeletal muscle through down - regulated mammalian target of rapamycin (mTOR) signaling

Repression of protein synthesis and mTOR signaling in rat liver mediated by the AMPK activator aminoimidazole carboxamide ribonucleoside