Fig 1: PTEN may regulate autophagy by allowing for a bypass of PTEN/PRAS40 signaling in TSC2-/- cells and influence cell proliferation. PTEN could suppress the activation of mTOR and promote autophagy not only by inhibiting Akt/Rheb/mTOR pathway, but also by activating the PTEN/PRAS40 pathway.
Fig 2: mTORC1 gene expression (a), protein content (b), and phosphorylation (c) are linearly correlated with mammalian longevity. Pearson correlations were performed between gene expression, protein content or phosphorylation, and longevity. Linear regression was applied when significant relationships were found. R2(mtor) = 0.1; R2(rptor) = 0.40; R2(mTOR) < 0.1; R2(Raptor) = 0.14; R2(PRAS40) = 0.22; R2(mTORSer2448/mTOR) = 0.27; R2(PRAS40Thr246/PRAS40) = 0.40. Minimum signification level was set at p < 0.05. Gene expression, and protein content and phosphorylation were log-transformed to accomplish the assumptions of normality
Fig 3: The autophagy levels and related molecular pathways assessed in TSC2-/- MEFs that received VO-OHpic treatment. (A) Western blot assays of LC3, p-PTEN and p-PRAS40 in TSC2-/- MEFs, with or without VO-OHpic treatment. Quantitative analysis of (B) LC3-I and (C) LC3-II expression levels in TSC2-/- MEFs, with or without VO-OHpic treatment. Quantitative analysis of (D) p-PTEN/PTEN and (E) p-PRAS40/PRAS40 relative expression levels in TSC2-/- MEFs, with or without VO-OHpic treatment. *P<0.05, **P<0.01 and ***P<0.001. VO-OHpic, hydroxyl(oxo)vanadium 3-hydroxypiridine-2-carboxylic acid; +V, VO-OHpic treatment; MEF, murine embryonic fibroblasts; p, phosphorylated; TSC, tuberous sclerosis complex; LC3, human microtubule-associated protein 1 light chain 3; PRAS40, proline-rich Akt substrate 40 kDa.
Supplier Page from Abcam for Anti-PRAS40 (phospho T246) antibody [EPR6262-107]