phospho ampk α1  (Bioss)

Journal: Cells

Article Title: Pifithrin-µ Induces Stress Granule Formation, Regulates Cell Survival, and Rewires Cellular Signaling

doi: 10.3390/cells13110885

Figure Lengend Snippet: Source of primary antibodies and the dilutions for Western blotting or immunolocalization. NA, not applicable.

Article Snippet: p-AMPK-α1/2 , Cell Signaling , #2535 , 1:2000 , NA.

Techniques: Western Blot

Journal: Cells

Article Title: Pifithrin-µ Induces Stress Granule Formation, Regulates Cell Survival, and Rewires Cellular Signaling

doi: 10.3390/cells13110885

Figure Lengend Snippet: PFT-µ diminishes the phosphorylation of AMPK on T172. Cells were incubated with vehicle (V) or PFT-µ for the hours [h] depicted. Crude extracts were evaluated for the phosphorylation of AMPK on T172 (p-AMPK). The same samples were also probed with antibodies against total AMPK (t-AMPK) and actin. The molecular mass of marker proteins in kD is indicated at the right margin. ECL signals were quantified for three independent experiments. Data were normalized to vehicle controls for each time point. Bars show average + SEM for each datapoint. Statistical evaluation was performed with one-way ANOVA combined with Bonferroni post hoc analysis. Changes were assessed relative to the vehicle control; ***, p < 0.001. AU, arbitrary units.

Article Snippet: p-AMPK-α1/2 , Cell Signaling , #2535 , 1:2000 , NA.

Techniques: Phospho-proteomics, Incubation, Marker, Control

Journal: PLoS ONE

Article Title: Sestrin2 Modulates AMPK Subunit Expression and Its Response to Ionizing Radiation in Breast Cancer Cells

doi: 10.1371/journal.pone.0032035

Figure Lengend Snippet: ( A ) MCF7 cells were plated into a 10 cm dish and grown until fully confluent. The cells were then lysed with lysis buffer and immunoprecipitation was preformed with the indicated AMPK subunit antibodies. These samples were then subjected to western blotting with AMPK subunit antibodies. A representative immunoblot from 3 independent experiments is shown. ( B ) Cells were transfected with 1 µg empty Flag vector (−) or 1 µg Sesn2F (+). Forty eight hours later the cells were lysed and immunoprecipitation was preformed with an anti-Flag antibody. The samples were then subjected to western blotting with the indicated antibodies. ( C ) MCF7 cells were treated with 1 µg empty Flag vector (−) or 1 µg Sesn2F (+). Forty eight hours later the cells were lysed and subjected to western blotting with the indicated phosphorylated AMPK antibodies. ( D ) The results from ( C ) were quantitated and expressed as the mean and SE from 3 independent experiments (* = P<0.05 and ** = P<0.01 compared to control).

Article Snippet: Antibodies against LKB1, phospho-AMPK α-subunit-(Thr172), phospho-AMPK α1-subunit-(Ser485), phospho-AMPK β-subunit-(Ser108), phospho-Acetly-CoA-Carboxylase (P-ACC), AMPKα1–2, AMPKβ1–2, AMPKγ1–3, phosphor-mTOR, phospho-p70-S6K, actin, and HRP-conjugated anti-rabbit secondary antibody were purchased from Cell Signalling (Mississauga, ON, Canada).

Techniques: Lysis, Immunoprecipitation, Western Blot, Transfection, Plasmid Preparation

Journal: PLoS ONE

Article Title: Sestrin2 Modulates AMPK Subunit Expression and Its Response to Ionizing Radiation in Breast Cancer Cells

doi: 10.1371/journal.pone.0032035

Figure Lengend Snippet: In response to genotoxic stress (IR), SESN2 is enhanced and leads to the formation of an active LKB1/AMPKα1β1γ1 complex. SESN2 may stabilize the AMPK complex, or transcriptionally regulate AMPK and enhance its expression. Both SESN2 and AMPK may then coordinate mTOR suppression, which translates into enhanced IR-induced cancer cell killing.

Article Snippet: Antibodies against LKB1, phospho-AMPK α-subunit-(Thr172), phospho-AMPK α1-subunit-(Ser485), phospho-AMPK β-subunit-(Ser108), phospho-Acetly-CoA-Carboxylase (P-ACC), AMPKα1–2, AMPKβ1–2, AMPKγ1–3, phosphor-mTOR, phospho-p70-S6K, actin, and HRP-conjugated anti-rabbit secondary antibody were purchased from Cell Signalling (Mississauga, ON, Canada).

Techniques: Expressing

Journal: Metabolism: clinical and experimental

Article Title: Serum metabolomics analysis reveals increased lipid catabolism in mildly hyperbilirubinemic Gilbert's syndrome individuals.

doi: 10.1016/j.metabol.2021.154913

Figure Lengend Snippet: Fig. 4. AMPK, PPARα, PGC1α and lipid catabolism. The figure presents the % increase of AMPK, PPARα and PGC-1α measured in PBMCs of GS vs. control individuals, as previously published by Mölzer et al. [22] and correlation coefficients (r) between UCB, AMPK; PPARα and PGC-1 α. The table shows correlations coefficients and p-values of AMPK (blue), PGC1α (orange), PPARα (green) and UCB (yellow) with their downstream lipid metabolites in the whole study population using Pearson or Spearman-Rho. Significant correlations are in bold type, t = trend.

Article Snippet: The following antibody set-up was used: rabbit anti-human monoclonal to AMPK α1 (phos-T183) and AMPKα2 (phos-T172) (ab133448, Abcam) and secondary antibody: goat anti-rabbit IgG H & L AlexaFluor 488 (ab150077, Abcam); rabbit anti-human polyclonal to PgC1α PE-labelled (orb124814, Biorbyt) and rabbit anti-human polyclonal to PPARα (phos-Ser12) FITClabelled (bs-4055R-FITC, Bioss).

Techniques: Control