IndraLab
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"For ovine conceptus development during implantation and placentation, integrin activation by SPP1 binding and arginine are proposed to stimulate remodeling of trophectoderm for elongation and adherence to uterine LE/sGE via cytoskeletal reorganization that facilitates cell motility, stabilizes adhesion, and collectively activates MTOR signaling pathways mediated by protein kinase b-alpha (AKT1), tuberous sclerosis 1 and 2 (TSC1 and TSC2) and MTORC1 (cell proliferation and mRNA translation), as well as mTORC2 (cell migration, cell survival and cytoskeletal organization) in trophectoderm cells."
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"The benzimidazole anthelmintics usually decreased signaling proteins related to cell proliferation and survival, such as phosphorylated (p) HER2/3, PI3K and protein kinase B (AKT), rapidly accelerated fibrosarcoma (a family of three serine/threonine specific protein kinases) (RAF)/MEK/ERK, mTOR, and Ki-67."
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"AKT, protein kinase B alpha; ER, endoplasmic reticulum; IKKβ, I-kappa-B kinase beta; IKKɛ, I-kappa-B kinase epsilon; IRS1/2, insulin receptor substrate 1; ISRE, interferon-stimulated response element; MAVS, mitochondrial antiviral signaling protein; mTOR, mechanistic target of rapamycin; NF-κB, nuclear factor kappa-light-chain-enhancer of activated B cells; PI-3K, phosphoinositide-3-kinase; STAT1/2/3/4/5/6, signal transducer and activator of transcription 1/2/2/4/5/6; STING, stimulator of interferon genes; TBK1, TANK-binding kinase 1.Fig."
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"This protein will degrade Cell Division Control Protein 2 (CDC2), resulting in cell arrest in the G2-M phase.63 AKT1 inhibition can also inhibit the activity of proteins that play an important role in cell proliferation such, as Mammalian Target of Rapamycin (mTOR), IkB Kinase (IKK), and Cyclin D1, and increase the activity of antiproliferative proteins such as Glycogen Synthase Kinase 3 Betha (GSK3β) and Forkhead box protein O1 (FOXO1).64When overexpressed, CDK4 causes uncontrolled cell growth and proliferation."
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"Phosphorylated Akt1 (pAkt1) indirectly activates mechanistic target of rapamycin (mTOR) by phosphorylating TSC1/2 complex, the inhibitory regulator of mTOR, thereby activating mTOR pathway that culminates in phosphorylation of 4EBP1 at Thr46/47 and S6K at Thr389, both important regulators of cap-dependent protein translation ( xref )."
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"Note: AKT, protein kinase B; COX-1, cyclooxygenase-1; cPLA2, cytoplasmic phospholipase A2; EIF2α, eukaryotic initiation factor 2 alpha; ER, endoplasmic reticulum; HK-2 cells, human kidney 2 cells; MAPK, mitogen-activated protein kinase; mitoROS, mitochondrial reactive oxygen species; mTOR, mitogen-activated protein kinase; PS-MPs, polystyrene microplastics; ROS, reactive oxygen species."
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"Although mTOR was activated in PIK3CA mutant cells when deprived of glutamine (XREF_SUPPLEMENTARY), our data suggest that the activation of mTOR does not determine glutamine sensitivity in these cells, because the overexpression of myristoylated AKT1 increased mTOR activity in the PIK3CA WT in the absence of glutamine (XREF_SUPPLEMENTARY)."
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"Phosphoinositide 3-kinase (PI3K), pyruvate dehydrogenase kinase (PDK), and protein kinase B (PKB; Akt) activation induced by growth factors (GFs) activate the mammalian target of the rapamycin (mechanistic target of rapamycin kinase; mTOR) pathway, which results in elevated HIF-1α transcriptional activity [6]."
| PMC
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"Phosphorylated Akt1 indirectly activates mTOR by phosphorylating TSC1/2 (tuberous sclerosis protein complex 1/2) complex, which is a negative regulator of mTOR there by activating the pathway to phosphorylate 4EBP1 (eukaryotic initiation factor 4E- binding protein-1) at Thr46/47, S6K (p70 Ribosomal S6 kinase) at Thr389 both are important in initiating protein translation downstream (Fig. xref D)."
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"Although mTOR signaling in the hypothalamus regulates food intake and absence of S6 K enhances insulin sensitivity and protects against diet- and age related obesity, our findings in Akt1 null mice fed a high-fat diet suggest that Akt, rather than mTOR, is the critical mediator of vascular senescence because mTOR activity was increased to a similar extent by a high-fat diet in WT and Akt1 null mice."