pkm2 inhibitor shikonin  (MedChemExpress)

Journal: Frontiers in Immunology

Article Title: GDF15 orchestrates mitochondrial-immune crosstalk via SMAD7-HIF-1α-PKM2 cascade to attenuate septic liver injury

doi: 10.3389/fimmu.2025.1712741

Figure Lengend Snippet: GDF15 preserves mitochondrial homeostasis in LPS-stimulated macrophages through dual regulation of SMAD7 and PKM2 pathways. (A) HIF-1α and SMAD7 expression in RAW264.7 macrophages across conditions: Untreated, LPS, LPS with rAAV8-mGdf15 overexpression (LPS+GDF15), and LPS with GDF15 knockdown (si-GDF15). β-actin: loading control.(HIF-1α suppression and SMAD7 induction by GDF15.) (B) Cytosolic and nuclear PKM2 protein levels. Lamin B1 (nuclear) and α-tubulin (cytosolic) markers validate fractionation efficiency. Study groups and individual replicates are identified in the figure key.(PKM2 subcellular redistribution modulated by GDF15.) (C) Immunofluorescence of PKM2 (red) and nuclei (DAPI, blue). Arrows indicate nuclear PKM2 accumulation. Scale bar: 15 μm.(Nuclear PKM2 enrichment upon LPS challenge mitigated by GDF15 and exacerbated by GDF15 knockdown.).

Article Snippet: Pharmacological agents included: HIF-1α inhibitor BAY 87-2243 [MedChemExpress, CAS 1227158-85-1; a potent and selective inhibitor of mitochondrial complex I that effectively suppresses HIF-1α protein accumulation under normoxic and hypoxic conditions ( )], PKM2 inhibitor Shikonin [MedChemExpress, CAS 54952-43-1; a specific inhibitor that binds to the PKM2 subunit, suppressing its enzymatic activity and nuclear translocation, with well-documented anti-inflammatory effects ( )], and SMAD7 activator Asiaticoside (MedChemExpress, 16830-15-2; a triterpenoid compound known to upregulate SMAD7 expression and ameliorate inflammation in macrophage models ( )).

Techniques: Expressing, Over Expression, Knockdown, Control, Fractionation, Immunofluorescence

Journal: Frontiers in Immunology

Article Title: GDF15 orchestrates mitochondrial-immune crosstalk via SMAD7-HIF-1α-PKM2 cascade to attenuate septic liver injury

doi: 10.3389/fimmu.2025.1712741

Figure Lengend Snippet: HIF-1α and PKM2 are critical effectors of GDF15-driven mitochondrial protection and anti-inflammatory responses. (A) HIF-1α inhibition by BAY 87-2243 (5 μM, 24 h). β-actin: loading control.(Pharmacological HIF-1α blockade.) (B) PKM2 inhibition by Shikonin (2 μM, 24 h). β-actin: loading control.(PKM2 activity suppression.) (C) UQCRC1 recovery in LPS-injured macrophages treated with: GDF15 overexpression, HIF-1α inhibitor (BAY), or PKM2 inhibitor (Shikonin). β-actin: loading control.(Mitochondrial complex III rescue via HIF-1α/PKM2 inhibition mirrors GDF15 effects.) (D) Inflammatory (TNF-α, IL-6) and metabolic (lactate) markers in cell supernatant (n = 5). Study groups and individual replicates are identified in the figure key. ***p < 0.001.(HIF-1α/PKM2 targeting replicates GDF15-mediated anti-inflammatory and metabolic homeostasis.) (E) UQCRC1 expression under GDF15 loss-of-function: si-GDF15 alone vs. combined with BAY 87–2243 or Shikonin. β-actin: loading control. Study groups and individual replicates are identified in the figure key.(Mitochondrial rescue in GDF15-deficient macrophages requires HIF-1α/PKM2 inhibition.) (F) Supernatant cytokines and lactate in si-GDF15 macrophages with/without inhibitors (n = 5). ***p < 0.001. (Inflammation reversal in GDF15-knockdown macrophages depends on HIF-1α/PKM2 blockade.).

Article Snippet: Pharmacological agents included: HIF-1α inhibitor BAY 87-2243 [MedChemExpress, CAS 1227158-85-1; a potent and selective inhibitor of mitochondrial complex I that effectively suppresses HIF-1α protein accumulation under normoxic and hypoxic conditions ( )], PKM2 inhibitor Shikonin [MedChemExpress, CAS 54952-43-1; a specific inhibitor that binds to the PKM2 subunit, suppressing its enzymatic activity and nuclear translocation, with well-documented anti-inflammatory effects ( )], and SMAD7 activator Asiaticoside (MedChemExpress, 16830-15-2; a triterpenoid compound known to upregulate SMAD7 expression and ameliorate inflammation in macrophage models ( )).

Techniques: Inhibition, Control, Activity Assay, Over Expression, Expressing, Knockdown

Journal: bioRxiv

Article Title: LncRNA YIYA enhances pancreatic cancer proliferation under high-glucose conditions through RAS–PKM2–mediated metabolic reprogramming that reinforces the Warburg phenotype

doi: 10.1101/2025.10.30.685546

Figure Lengend Snippet: (a) Relative change in Oxygen consumption rate (OCR) post-YIYA knockdown in MIA PaCa-2 cells grown under HG conditions. (b) Relative change in the ATP levels post-YIYA knockdown in MIA PaCa-2 cells grown under HG conditions. (c) Relative mRNA expression of GLUT1 upon YIYA inhibition in MIA PaCa-2 cells grown under HG conditions. (d) Relative fold change in glucose uptake post-YIYA inhibition in MIA PaCa-2 cells grown under HG conditions. (e) Immunofluorescence images representing PKM2 expression and localization in MIA PaCa-2 cells grown under NG or HG conditions (Scale Bar: 20 µm). (f) Immunoblot images representing PKM2 expression in MIA PaCa-2 cells grown under NG or HG. (g) Relative mRNA expression of LDH in MIA PaCa-2 cells grown under NG or HG. (h) Relative mRNA expression of MPC in MIA PaCa-2 cells grown under NG or HG. (i) Relative mRNA expression of PKM2 in HG cultured MIA PaCa-2 cells upon YIYA inhibition. (j) Immunoblot images representing PKM2 expression in MIA PaCa-2 cells grown under HG upon YIYA inhibition. (k) Relative fold change in extracellular lactate concentration in HG cultured MIA PaCa-2 cells upon YIYA inhibition. The glucose concentration used for NG is 5.5 mM, and for HG is 25 mM. The final concentration of siRNA used for transfection was 40 nM. Unless otherwise specified, treatments were carried out for 48 h. For quantitative comparisons, bar graphs representing gene expression or protein levels were normalized to the respective housekeeping gene or loading control (either GAPDH or β-actin). Fold change values shown in the graphs are expressed relative to the control, which was set to 1. All results are presented as mean ± SD from at least three independent experiments (n = 3). For comparisons involving multiple groups across varying concentrations and/or time points, two-way ANOVA followed by Tukey’s multiple comparisons post-test was performed. Statistical significance is indicated as (*) p < 0.05, (**) p<0.01, and (***) p < 0.001 versus the control. For pairwise comparisons between two groups, unpaired t-tests were applied.

Article Snippet: KRAS inhibitor (HY-130149), AKT inhibitor (HY-10115), Protein A/G magnetic beads (HY-K0202), and PKM2 inhibitor (HY-103617) were procured from MedChemExpress.

Techniques: Knockdown, Expressing, Inhibition, Immunofluorescence, Western Blot, Cell Culture, Concentration Assay, Transfection, Gene Expression, Control

Journal: bioRxiv

Article Title: LncRNA YIYA enhances pancreatic cancer proliferation under high-glucose conditions through RAS–PKM2–mediated metabolic reprogramming that reinforces the Warburg phenotype

doi: 10.1101/2025.10.30.685546

Figure Lengend Snippet: (a) Relative mRNA and (b) protein expression of KRAS upon YIYA inhibition in MIA PaCa-2 cells grown under HG conditions. (c) Interaction of lncRNA YIYA with KRAS protein in MIA PaCa-2 cells grown under HG conditions, as analyzed using RIP-qPCR (KRAS was immunoprecipitated using a specific antibody, and the associated RNA was analyzed by qPCR). IgG served as a control. RIP-qPCR illustration prepared with Biorender software. (d) Change in mRNA expression of PKM2 upon KRAS inhibition (KRASi; Adagrasib dose∼100 nM) in MIA PaCa-2 cells grown under HG conditions. (e) Immunoblot images representing PKM2 protein expression in MIA PaCa-2 cells grown under HG upon KRAS inhibition (Adagrasib dose∼100 nM). (f) Interaction of PKM2 protein with KRAS protein in MIA PaCa-2 cells grown under NG or HG conditions, as analyzed using CO-IP (KRAS was immunoprecipitated using a specific antibody, and the precipitated complexes were analyzed by SDS–PAGE followed by immunoblotting with a PKM2 antibody.) (g) Interaction of lncRNA YIYA with PKM2 protein in MIA PaCa-2 cells grown under HG conditions, as analyzed using RIP-qPCR (PKM2 was immunoprecipitated using a specific antibody, and the associated RNA was analyzed by qPCR). IgG served as a control. (h) Immunoblot images representing KRAS protein expression in MIA PaCa-2 cells grown under HG upon YIYA inhibition and autophagy inhibition (CQ∼10 μM). The glucose concentration used for NG is 5.5 mM, and for HG is 25 mM. The final concentration of siRNA used for transfection was 40 nM. Unless otherwise specified, treatments were carried out for 48 h. For quantitative comparisons, bar graphs representing gene expression or protein levels were normalized to the respective housekeeping gene or loading control (either GAPDH or β-actin). Fold change values shown in the graphs are expressed relative to the control, which was set to 1. All results are presented as mean ± SD from at least three independent experiments (n = 3). For comparisons involving multiple groups across varying concentrations and/or time points, two-way ANOVA followed by Tukey’s multiple comparisons post-test was performed. Statistical significance is indicated as (*) p < 0.05, (**) p<0.01, and (***) p < 0.001 versus the control. For pairwise comparisons between two groups, unpaired t-tests were applied.

Article Snippet: KRAS inhibitor (HY-130149), AKT inhibitor (HY-10115), Protein A/G magnetic beads (HY-K0202), and PKM2 inhibitor (HY-103617) were procured from MedChemExpress.

Techniques: Expressing, Inhibition, Immunoprecipitation, Control, Software, Western Blot, Co-Immunoprecipitation Assay, SDS Page, Concentration Assay, Transfection, Gene Expression

Journal: bioRxiv

Article Title: A PKM2-YAP reciprocal repartitioning modulates invasion of breast cancer cells

doi: 10.1101/2025.07.10.664113

Figure Lengend Snippet: (A) Representative confocal photomicrographs of breast cancer MDA-MB-231 cells grown on 0.4 kPa (top row of micrographs) and 20 kPa (bottom row of micrographs) polyacrylamide hydrogels coated with Collagen I and observed after 24Lh of culture with staining for DNA (white using DAPI, left panel) and F-actin (green using phalloidin, right panel (n□= 3). Scale bar: 20□μm and graphs showing cell area (left) and aspect ratio (right) of individual MDA-MB-231 cells grown on 0.4 kPa and 20 kPa hydrogels (n□= 3, N□= 30 single cells). (B) Epifluorescence photomicrographs of RFP-labelled MDA-MB-231 cells with their migration tracks for 3 hours, 0.4 kPa (left) and 20 kPa (right) and scatter plot graph depicting migration speed (n=3, N=20). See also Video S1, S2. (C) Graph measuring fold change of extracellular lactate (top left), extracellular pyruvate (top right), intracellular lactate (bottom left), intracellular pyruvate (bottom right) between 0.4 kPa and 20 kPa hydrogels. (D) Representative confocal photomicrographs of MDA-MB-231 cells grown on 0.4 kPa (top row of micrographs) and 20 kPa (bottom row of micrographs) polyacrylamide hydrogels coated with Collagen I and observed after 24□h of culture with staining for DNA (white using DAPI, left panel), PKM2 (Red, middle panel) and F-actin (green, right panel). (n□= 3). Scale bar: 20□μm and scatter plot graph depicting nucleus/cytoplasm ratio of PKM2 (n=3, N=30) (See Figure S1 for a schematic depiction of how nuclear and cytoplasmic boundaries were delineated and the ratio of the PKM2 levels calculated). (E) Schematic depiction of matrix stiffness-driven phenotypic changes and PKM2 subcellular localization. Error bars denote mean□±□SEM. Unpaired Student’s□ t □test was performed for statistical significance (* P □≤ 0.05, ** P □≤ 0.01, *** P □< 0.001, **** P □< 0.0001).

Article Snippet: PKM2 cytoplasmic activator TEPP-46 (HY-18657, MedChemExpress), PKM2 inhibitor PKM2-IN-1 (HY-103617, MedChemExpress) and YAP inhibitor Verteporfin (HY-B0146, MedChemExpress) were used for the current study.

Techniques: Staining, Migration

Journal: bioRxiv

Article Title: A PKM2-YAP reciprocal repartitioning modulates invasion of breast cancer cells

doi: 10.1101/2025.07.10.664113

Figure Lengend Snippet: (A) Representative confocal photomicrographs of breast cancer MDA-MB-231 cells untreated (top row of micrographs) or treated with 40□μM TEPP-46, PKM2 cytoplasmic activator (second row from top) grown on 0.4 kPa (soft) hydrogels coated with Collagen I and observed after 24□h of culture with staining by□DNA (white using DAPI, left panel) and PKM2 (Red, right panel). (n□= 3). Scale bar: 20□μm. Scatter plot graph (right) depicting nucleus/cytoplasm ratio of PKM2 between untreated and 40□μM TEPP-46-treated MDA-MB-231 cells on 0.4 kPa hydrogels (n = 3, N = 30). (B) Representative confocal photomicrographs of breast cancer MDA-MB-231 cells untreated (top row of micrographs) or treated with 40□μM TEPP-46, PKM2 cytoplasmic activator (second row from top) grown on 0.4 kPa (soft) hydrogels coated with Collagen I and observed after 24□h of culture with staining by□DNA (white using DAPI, left panel) and F- actin (green using phalloidin, right panel (n□= 3). Scale bar: 20□μm. Graphs showing cell area (top) and aspect ratio (bottom) of individual MDA-MB-231 cells untreated and treated with 40□μM TEPP-46 on 0.4 kPa hydrogels (n□= 3, N□= 30 single cells). (C) Epifluorescence photomicrographs of RFP-labelled MDA-MB-231 cells with their migration tracks for 3 hours, control (top) and treated with 40□μM TEPP-46 (bottom) on 0.4 kPa hydrogels and scatter plot graph (right) depicting migration speed (n=3, N > 20). See also Video S3, S4. (D) schematic depiction of PKM2 activation-driven phenotypic alterations. Error bars denote mean□±□SEM. Unpaired Student’s□ t □test was performed for statistical significance (* P □≤ 0.05, ** P □≤ 0.01, *** P □< 0.001, **** P □< 0.0001).

Article Snippet: PKM2 cytoplasmic activator TEPP-46 (HY-18657, MedChemExpress), PKM2 inhibitor PKM2-IN-1 (HY-103617, MedChemExpress) and YAP inhibitor Verteporfin (HY-B0146, MedChemExpress) were used for the current study.

Techniques: Staining, Migration, Control, Activation Assay

Journal: bioRxiv

Article Title: A PKM2-YAP reciprocal repartitioning modulates invasion of breast cancer cells

doi: 10.1101/2025.07.10.664113

Figure Lengend Snippet: Decreased MDA-MB-231 breast cancer cell migration on stiff matrices upon PKM2 inhibition. (A) Representative confocal photomicrographs of breast cancer MDA-MB-231 cells untreated (top row of micrographs) or treated with 1.5LμM PKM2-IN-1, PKM2 inhibitor (second row from top) grown on 20 kPa (stiff) hydrogels coated with Collagen I and observed after 24□h of culture with staining by□DNA (white using DAPI, left panel) and PKM2 (Red, right panel). (n□= 3). Scale bar: 20□μm. Scatter plot graph (right) depicting nucleus/cytoplasm ratio of PKM2 between untreated and 1.5□μM PKM2-IN-1 treated MDA- MB-231 cells on 20 kPa hydrogels (n=3, N=30). (B) Representative confocal photomicrographs of breast cancer MDA-MB-231 cells untreated (top row of micrographs) or treated with 1.5□μM PKM2-IN-1 (second row from top) grown on 20 kPa (stiff) hydrogels coated with Collagen I and observed after 24□h of culture with staining by□DNA (white using DAPI, left panel) and F-actin (green using phalloidin, right panel (n□= 3). Scale bar: 20□μm. Graphs showing total cell area (right top) and aspect ratio (right bottom) of individual MDA-MB-231 cells untreated and treated with 1.5□μM PKM2-IN-1 on 20 kPa hydrogels (n□= 3, N = 30 single cells). (C) Epifluorescence photomicrographs of RFP- labelled MDA-MB-231 cells with their migration tracks for 3 hours, control (left) and treated with 1.5□μM PKM2-IN-1 (right) on 20 kPa hydrogels and scatter plot graph (right most) depicting migration speed (n=3, N > 20). See also Video S5, S6. (D) Graph measuring fold change of extracellular lactate (top left), extracellular pyruvate (top right), intracellular lactate (bottom left), intracellular pyruvate (bottom right) between untreated and 2□μM PKM2-IN-1 treated MDA-MB-231 cells on 20 kPa hydrogels (n=3). (E) Schematic depiction of alterations of traits under PKM2 inhibition. Error bars denote mean□±□SEM. Unpaired Student’s□ t □test was performed for statistical significance (* P □≤ 0.05, ** P □≤ 0.01, *** P □< 0.001, **** P □< 0.0001).

Article Snippet: PKM2 cytoplasmic activator TEPP-46 (HY-18657, MedChemExpress), PKM2 inhibitor PKM2-IN-1 (HY-103617, MedChemExpress) and YAP inhibitor Verteporfin (HY-B0146, MedChemExpress) were used for the current study.

Techniques: Migration, Inhibition, Staining, Control

Journal: bioRxiv

Article Title: A PKM2-YAP reciprocal repartitioning modulates invasion of breast cancer cells

doi: 10.1101/2025.07.10.664113

Figure Lengend Snippet: (A) Representative confocal photomicrographs of breast cancer MDA-MB-231 cells grown on 0.4 kPa (top row of micrographs) and 20 kPa (bottom row of micrographs) polyacrylamide hydrogels coated with Collagen I and observed after 24□h of culture with staining for DNA (white using DAPI, left panel) and YAP (red, right panel). Yellow dotted areas represent nuclear area (n□= 3). Scale bar: 10□μm. Adjacent scatter plot graph depicting nucleus/cytoplasm ratio of YAP between MDA-MB-231 grown on 0.4 kPa and 20 kPa hydrogels (n = 3, n > 50). (B) Representative confocal photomicrographs of breast cancer MDA-MB-231 cells untreated (top row of micrographs) or treated with 40□μM TEPP-46, PKM2 cytoplasmic activator (second row from top) grown on 0.4 kPa (soft) hydrogels coated with Collagen I and observed after 24□h of culture with staining by□DNA (white using DAPI, left panel) and YAP (Red, right panel). Yellow dotted areas represent nuclear area (n□= 3). Scale bar: 10□μm. Adjacent scatter plot graph depicting nucleus/cytoplasm ratio of YAP between untreated and 40□μM TEPP-46 treated MDA-MB-231 cells on 0.4 kPa hydrogels (n = 3, N > 25). (C) Schematic depiction of YAP localization after PKM2 activation in soft gels. Error bars denote mean□±□SEM. Unpaired Student’s□ t □test was performed for statistical significance (* P □≤ 0.05, ** P □≤ 0.01, *** P □< 0.001, **** P □< 0.0001).

Article Snippet: PKM2 cytoplasmic activator TEPP-46 (HY-18657, MedChemExpress), PKM2 inhibitor PKM2-IN-1 (HY-103617, MedChemExpress) and YAP inhibitor Verteporfin (HY-B0146, MedChemExpress) were used for the current study.

Techniques: Staining, Activation Assay

Journal: bioRxiv

Article Title: A PKM2-YAP reciprocal repartitioning modulates invasion of breast cancer cells

doi: 10.1101/2025.07.10.664113

Figure Lengend Snippet: (A) Representative confocal photomicrographs of breast cancer MDA-MB-231 cells untreated (top row of micrographs) or treated with 5□μM Verteporfin, YAP signalling inhibitor (second row from top) grown on 20 kPa (stiff) hydrogels coated with Collagen I and observed after 24□h of culture with staining by□DNA (white using DAPI, left panel) and F-actin (green using phalloidin, right panel (n□= 3). Scale bar: 20□μm. Graphs showing total cell area (top) and aspect ratio (second from top) of individual MDA-MB-231 cells untreated and treated with 5□μM Verteporfin on 20 kPa hydrogels (n□= 3, N□= 30 single cells). (B) Representative confocal photomicrographs of MDA-MB-231 cells untreated (top row of micrographs) or treated with 5□μM Verteporfin (second row from top) grown on 20 kPa (stiff) hydrogels coated with Collagen I and observed after 24□h of culture with staining by□DNA (white using DAPI, left panel) and PKM2 (Red, right panel) and adjacent scatter plot graph (right) depicting nucleus/cytoplasm ratio of PKM2 between untreated and 5□μM Verteporfin treated MDA-MB-231 cells on 20 kPa hydrogels (n=3, N=50). (n□= 3). Scale bar: 20□μm. (C) Epifluorescence photomicrographs of MDA-MB-231 cells with their migration tracks for 3 hours, control (left) and treated with 5□μM Verteporfin (right) on 20 kPa hydrogels and scatter plot graph (right) depicting migration speed (n=3, N > 20). See also Video S7, S8. (D) Graph measuring fold change of intracellular pyruvate (first from left), intracellular lactate (second from left), extracellular pyruvate (third from left), extracellular lactate (last from left) between untreated and 5□μM Verteporfin treated MDA-MB-231 cells on 20 kPa hydrogels (n=3). (E) Schematic depiction of PKM2-YAP reciprocal repartitioning. Error bars denote mean□±□SEM. Unpaired Student’s□ t □test was performed for statistical significance (* P □≤ 0.05, ** P □≤ 0.01, *** P □< 0.001, **** P □< 0.0001).

Article Snippet: PKM2 cytoplasmic activator TEPP-46 (HY-18657, MedChemExpress), PKM2 inhibitor PKM2-IN-1 (HY-103617, MedChemExpress) and YAP inhibitor Verteporfin (HY-B0146, MedChemExpress) were used for the current study.

Techniques: Staining, Migration, Control

Journal: bioRxiv

Article Title: A PKM2-YAP reciprocal repartitioning modulates invasion of breast cancer cells

doi: 10.1101/2025.07.10.664113

Figure Lengend Snippet: (A) Bright field micrographs taken at 0, 8, 16, and 24 h (top to bottom) from time-lapse videography of lrECM-coated clusters of MDA-MB-231 cells invading into surrounding Collagen I, control (left), treated with 5 μM PKM2-IN-1(middle) and treated with 5 μM Verteporfin (right). (B) Scatter plot graph depicting number of dispersed single cells in Collagen I normalized to the initial cluster size obtained from time lapse videography ( n = 3). Error bars denote mean ± SEM. One-way ANOVA with Tukey’s multiple comparison test was performed for statistical significance (* P ≤ 0.05, ** P ≤ 0.01, *** P < 0.001, **** P < 0.0001). See also Video S17, S18 and S19.

Article Snippet: PKM2 cytoplasmic activator TEPP-46 (HY-18657, MedChemExpress), PKM2 inhibitor PKM2-IN-1 (HY-103617, MedChemExpress) and YAP inhibitor Verteporfin (HY-B0146, MedChemExpress) were used for the current study.

Techniques: Control, Comparison

Journal: Lipids in health and disease

Article Title: SRT3025-loaded cell membrane hybrid liposomes (3025@ML) enhanced anti-tumor activity of Oxaliplatin via inhibiting pyruvate kinase M2 and fatty acid synthase.

doi: 10.1186/s12944-025-02431-x

Figure Lengend Snippet: Fig. 4 Compound 3K enhanced the anti-tumor activity of OXA and induced cell apoptosis by inhibiting PKM2 and FASN. CCK8 analysis confirmed that compound 3K inhibited cell viability of T24 cells and 5637 cells (A, B, and C). Compound 3K, OXA, and combination therapy treated T24 cells (D) and 5637 cells (D). Compound 3K decreased the accumulation of PKM2 and Bcl-2 and increased the expression of Bax and Cleaved Caspase-3. Quantitative analysis of the PKM2, FASN, Bax, Bcl-2, and Cleaved Caspase-3 proteins (E). 3K: compound 3K; *P<0.05

Article Snippet: Keywords Bladder cancer, SRT3025, Oxaliplatin, PKM2, FASN no. S8616), were purchased from Selleck Chemicals (Houston, USA).

Techniques: Activity Assay, Expressing

Journal: Lipids in health and disease

Article Title: SRT3025-loaded cell membrane hybrid liposomes (3025@ML) enhanced anti-tumor activity of Oxaliplatin via inhibiting pyruvate kinase M2 and fatty acid synthase.

doi: 10.1186/s12944-025-02431-x

Figure Lengend Snippet: Fig. 5 3025@ML enhanced anti-tumor activity of OXA. T24 cells and 5637 cells were treated with 3025@ML, OXA, or the com by reducing PKM2 and FASN bination to verify 3025@ML enhanced anti-tumor activity of OXA by CCK8 analysis (A and B) and trypan blue staining (C and D). This combination therapy significantly reduced cell viability and induced cell death. Annexin V/PI staining (E) supported combination therapy enhances the percentage of cell apoptosis. (F) Treating the cells with OXA or OXA + 3025@ML caused the downregulation of PKM2, AKT, and mTOR and the decrease of p-AKT and p-mTOR levels. (G) Quantitative analysis of the PKM2, FASN, p-AKT, and p-mTOR proteins. *P<0.05

Article Snippet: Keywords Bladder cancer, SRT3025, Oxaliplatin, PKM2, FASN no. S8616), were purchased from Selleck Chemicals (Houston, USA).

Techniques: Activity Assay, Staining

Journal: Lipids in health and disease

Article Title: SRT3025-loaded cell membrane hybrid liposomes (3025@ML) enhanced anti-tumor activity of Oxaliplatin via inhibiting pyruvate kinase M2 and fatty acid synthase.

doi: 10.1186/s12944-025-02431-x

Figure Lengend Snippet: Fig. 6 The anti-tumor activity of 3025@ML via lipid metabolism. PI3K: phosphatidylinositol 3-kinase; AKT: protein kinase B; mTOR: mammalian target of rapamycin; PKM2: pyruvate kinase M2; FASN: fatty acid synthase

Article Snippet: Keywords Bladder cancer, SRT3025, Oxaliplatin, PKM2, FASN no. S8616), were purchased from Selleck Chemicals (Houston, USA).

Techniques: Activity Assay