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"Western blot analysis was applied to measure the levels of NLRC5, microtubule-associated protein 1A/1B-light chain 3 type I (LC3I), LC3II, sequestosome 1 (p62), protein kinase B (AKT), phosphorylated Akt (pAKT), mammalian target of rapamycin (mTOR) and phosphorylated mTOR (pmTOR)."
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"Protein synthesis in skeletal muscle is mainly regulated by the PI3K–AKT ‘phosphoinositide‐3‐kinase’–‘AKT’ [‘protein kinase B’ (PKB)] pathway downstream of anabolic hormones phosphorylating mTORC (‘mammalian target of rapamycin complex’) and its downstream targets, leading to protein translation (Figure
2)."
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"Despite modulation of PRAS40, which regulates the mTOR containing TORC1 complex, mutational activation of PIK3CA or AKT1 did not consistently increase phosphorylation of mTOR at serine 2448 or phosphorylation of mTOR target proteins and their targets, including p70-ribosomal protein S6-kinase (p70S6K), eukaryotic elongation factor 4 binding protein 1 (EIF4EBP1), and ribosomal protein S6."
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"In Figures XREF_FIG, application of the phosphoinositide 3-kinase (PI 3-K) inhibitor LY294002 (10 muM) during treatment with either EPO (10 ng/ml) or Wnt1 (100 ng/ml) prevented EPO or Wnt1 from phosphorylating mTOR and p70S6K, illustrating that the PI 3-K and Akt1 pathways are necessary for EPO or Wnt1 to phosphorylate mTOR and p70S6K."
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"Upon activation through phosphorylation, pAkt promotes cell survival by inactivating the pro‐apoptotic proteins Bad, c‐Raf and caspase‐9 (Burgering & Bos, 1995; Cardone et al., 1998; Franke & Cantley, 1997; Zimmermann & Moelling, 1999) and activates mammalian target of rapamycin (mTOR) phosphorylation (Heinonen et al., 2008)."