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Resistance exercise exceeds the benefits of endurance exercise in ameliorating metabolic dysfunction. Following 8 weeks of diet and exercise interventions, all mice were assessed for their metabolic function by GTT, ITT, and skeletal muscle response of Akt and <t>AS160</t> phosphorylation to injection of insulin measured by Western blot. (A–C) HOMA-IR taken after an overnight fast for baseline glucose and insulin. (D and E) GTT from 0–120 min and calculated AUC; colored * indicates significant difference from NC-SED. (F and G) ITT from 0–60 min and calculated AUC; colored * indicates significant difference from NC-SED. (H–N) pAkt stimulation, AS160 <t>S318,</t> and AS160 T642 in hindlimb muscles before and after insulin injection and the pre–post ∆ in phosphorylation. (O and P) Total and phosphorylated 4E-BP1. (Q–T) Western results for Raptor, COX4, LC3 II/I, and ubiquitin staining. Representative western blot images inset right. Data presented as mean ± standard error of the mean. Statistical analysis performed by analysis of variance between groups: * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001. NC-SED n : 8–16 (white); HFD-SED n : 8–18 (red); HFD-R EX n : 8–16 (blue); HFD-E EX n : 8–15 (green). 4E-BP1 = Eukaryotic translation initiation factor 4E binding protein; Akt = protein kinase B; AS160 = Akt substrate 160; COX4 = cytochrome c oxidase 4; CS = citrate sythase; E EX = endurance exercise; GAPDH = glyceraldehyde 3 phosphate dehydrogenase; GTT = glucose tolerance test; HFD = high fat diet; HOMA-IR = homeostatic model assessment for insulin resistance; iAUC = integrated area under the curve; ITT = insulin tolerance test; LC3 II/I = microtubule-associated protein light chain 3; NC = normal chow; pAkt = phospho-Akt; R EX = resistance exercise; SED = sedentary; Ub = ubiquitin.
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Resistance exercise exceeds the benefits of endurance exercise in ameliorating metabolic dysfunction. Following 8 weeks of diet and exercise interventions, all mice were assessed for their metabolic function by GTT, ITT, and skeletal muscle response of Akt and <t>AS160</t> phosphorylation to injection of insulin measured by Western blot. (A–C) HOMA-IR taken after an overnight fast for baseline glucose and insulin. (D and E) GTT from 0–120 min and calculated AUC; colored * indicates significant difference from NC-SED. (F and G) ITT from 0–60 min and calculated AUC; colored * indicates significant difference from NC-SED. (H–N) pAkt stimulation, AS160 <t>S318,</t> and AS160 T642 in hindlimb muscles before and after insulin injection and the pre–post ∆ in phosphorylation. (O and P) Total and phosphorylated 4E-BP1. (Q–T) Western results for Raptor, COX4, LC3 II/I, and ubiquitin staining. Representative western blot images inset right. Data presented as mean ± standard error of the mean. Statistical analysis performed by analysis of variance between groups: * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001. NC-SED n : 8–16 (white); HFD-SED n : 8–18 (red); HFD-R EX n : 8–16 (blue); HFD-E EX n : 8–15 (green). 4E-BP1 = Eukaryotic translation initiation factor 4E binding protein; Akt = protein kinase B; AS160 = Akt substrate 160; COX4 = cytochrome c oxidase 4; CS = citrate sythase; E EX = endurance exercise; GAPDH = glyceraldehyde 3 phosphate dehydrogenase; GTT = glucose tolerance test; HFD = high fat diet; HOMA-IR = homeostatic model assessment for insulin resistance; iAUC = integrated area under the curve; ITT = insulin tolerance test; LC3 II/I = microtubule-associated protein light chain 3; NC = normal chow; pAkt = phospho-Akt; R EX = resistance exercise; SED = sedentary; Ub = ubiquitin.
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Resistance exercise exceeds the benefits of endurance exercise in ameliorating metabolic dysfunction. Following 8 weeks of diet and exercise interventions, all mice were assessed for their metabolic function by GTT, ITT, and skeletal muscle response of Akt and <t>AS160</t> phosphorylation to injection of insulin measured by Western blot. (A–C) HOMA-IR taken after an overnight fast for baseline glucose and insulin. (D and E) GTT from 0–120 min and calculated AUC; colored * indicates significant difference from NC-SED. (F and G) ITT from 0–60 min and calculated AUC; colored * indicates significant difference from NC-SED. (H–N) pAkt stimulation, AS160 <t>S318,</t> and AS160 T642 in hindlimb muscles before and after insulin injection and the pre–post ∆ in phosphorylation. (O and P) Total and phosphorylated 4E-BP1. (Q–T) Western results for Raptor, COX4, LC3 II/I, and ubiquitin staining. Representative western blot images inset right. Data presented as mean ± standard error of the mean. Statistical analysis performed by analysis of variance between groups: * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001. NC-SED n : 8–16 (white); HFD-SED n : 8–18 (red); HFD-R EX n : 8–16 (blue); HFD-E EX n : 8–15 (green). 4E-BP1 = Eukaryotic translation initiation factor 4E binding protein; Akt = protein kinase B; AS160 = Akt substrate 160; COX4 = cytochrome c oxidase 4; CS = citrate sythase; E EX = endurance exercise; GAPDH = glyceraldehyde 3 phosphate dehydrogenase; GTT = glucose tolerance test; HFD = high fat diet; HOMA-IR = homeostatic model assessment for insulin resistance; iAUC = integrated area under the curve; ITT = insulin tolerance test; LC3 II/I = microtubule-associated protein light chain 3; NC = normal chow; pAkt = phospho-Akt; R EX = resistance exercise; SED = sedentary; Ub = ubiquitin.
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Resistance exercise exceeds the benefits of endurance exercise in ameliorating metabolic dysfunction. Following 8 weeks of diet and exercise interventions, all mice were assessed for their metabolic function by GTT, ITT, and skeletal muscle response of Akt and <t>AS160</t> phosphorylation to injection of insulin measured by Western blot. (A–C) HOMA-IR taken after an overnight fast for baseline glucose and insulin. (D and E) GTT from 0–120 min and calculated AUC; colored * indicates significant difference from NC-SED. (F and G) ITT from 0–60 min and calculated AUC; colored * indicates significant difference from NC-SED. (H–N) pAkt stimulation, AS160 <t>S318,</t> and AS160 T642 in hindlimb muscles before and after insulin injection and the pre–post ∆ in phosphorylation. (O and P) Total and phosphorylated 4E-BP1. (Q–T) Western results for Raptor, COX4, LC3 II/I, and ubiquitin staining. Representative western blot images inset right. Data presented as mean ± standard error of the mean. Statistical analysis performed by analysis of variance between groups: * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001. NC-SED n : 8–16 (white); HFD-SED n : 8–18 (red); HFD-R EX n : 8–16 (blue); HFD-E EX n : 8–15 (green). 4E-BP1 = Eukaryotic translation initiation factor 4E binding protein; Akt = protein kinase B; AS160 = Akt substrate 160; COX4 = cytochrome c oxidase 4; CS = citrate sythase; E EX = endurance exercise; GAPDH = glyceraldehyde 3 phosphate dehydrogenase; GTT = glucose tolerance test; HFD = high fat diet; HOMA-IR = homeostatic model assessment for insulin resistance; iAUC = integrated area under the curve; ITT = insulin tolerance test; LC3 II/I = microtubule-associated protein light chain 3; NC = normal chow; pAkt = phospho-Akt; R EX = resistance exercise; SED = sedentary; Ub = ubiquitin.
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Resistance exercise exceeds the benefits of endurance exercise in ameliorating metabolic dysfunction. Following 8 weeks of diet and exercise interventions, all mice were assessed for their metabolic function by GTT, ITT, and skeletal muscle response of Akt and <t>AS160</t> phosphorylation to injection of insulin measured by Western blot. (A–C) HOMA-IR taken after an overnight fast for baseline glucose and insulin. (D and E) GTT from 0–120 min and calculated AUC; colored * indicates significant difference from NC-SED. (F and G) ITT from 0–60 min and calculated AUC; colored * indicates significant difference from NC-SED. (H–N) pAkt stimulation, AS160 <t>S318,</t> and AS160 T642 in hindlimb muscles before and after insulin injection and the pre–post ∆ in phosphorylation. (O and P) Total and phosphorylated 4E-BP1. (Q–T) Western results for Raptor, COX4, LC3 II/I, and ubiquitin staining. Representative western blot images inset right. Data presented as mean ± standard error of the mean. Statistical analysis performed by analysis of variance between groups: * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001. NC-SED n : 8–16 (white); HFD-SED n : 8–18 (red); HFD-R EX n : 8–16 (blue); HFD-E EX n : 8–15 (green). 4E-BP1 = Eukaryotic translation initiation factor 4E binding protein; Akt = protein kinase B; AS160 = Akt substrate 160; COX4 = cytochrome c oxidase 4; CS = citrate sythase; E EX = endurance exercise; GAPDH = glyceraldehyde 3 phosphate dehydrogenase; GTT = glucose tolerance test; HFD = high fat diet; HOMA-IR = homeostatic model assessment for insulin resistance; iAUC = integrated area under the curve; ITT = insulin tolerance test; LC3 II/I = microtubule-associated protein light chain 3; NC = normal chow; pAkt = phospho-Akt; R EX = resistance exercise; SED = sedentary; Ub = ubiquitin.
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GRB1 suppresses pancreatic cancer progression by targeting <t>the</t> <t>PI3K–AKT</t> signaling pathway. (A) GO enrichment analysis of GRB1–PDAC overlapping targets showing enrichment in kinase regulation and phosphatidylinositol signaling. (B) KEGG enrichment highlighting the PI3K–AKT pathway as the key signaling axis. (C) Western blot showing decreased phosphorylation of PI3K and AKT in GRB1‐treated tumor and liver metastasis tissues. (D, E) Molecular docking and visualization demonstrating stable binding of GRB1 to AKT1 and PIK3CA with strong binding energies. Data are presented as mean ± SEM. ns, no significance; * p < 0.01, ** p < 0.001, *** p < 0.0001.
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Image Search Results


Resistance exercise exceeds the benefits of endurance exercise in ameliorating metabolic dysfunction. Following 8 weeks of diet and exercise interventions, all mice were assessed for their metabolic function by GTT, ITT, and skeletal muscle response of Akt and AS160 phosphorylation to injection of insulin measured by Western blot. (A–C) HOMA-IR taken after an overnight fast for baseline glucose and insulin. (D and E) GTT from 0–120 min and calculated AUC; colored * indicates significant difference from NC-SED. (F and G) ITT from 0–60 min and calculated AUC; colored * indicates significant difference from NC-SED. (H–N) pAkt stimulation, AS160 S318, and AS160 T642 in hindlimb muscles before and after insulin injection and the pre–post ∆ in phosphorylation. (O and P) Total and phosphorylated 4E-BP1. (Q–T) Western results for Raptor, COX4, LC3 II/I, and ubiquitin staining. Representative western blot images inset right. Data presented as mean ± standard error of the mean. Statistical analysis performed by analysis of variance between groups: * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001. NC-SED n : 8–16 (white); HFD-SED n : 8–18 (red); HFD-R EX n : 8–16 (blue); HFD-E EX n : 8–15 (green). 4E-BP1 = Eukaryotic translation initiation factor 4E binding protein; Akt = protein kinase B; AS160 = Akt substrate 160; COX4 = cytochrome c oxidase 4; CS = citrate sythase; E EX = endurance exercise; GAPDH = glyceraldehyde 3 phosphate dehydrogenase; GTT = glucose tolerance test; HFD = high fat diet; HOMA-IR = homeostatic model assessment for insulin resistance; iAUC = integrated area under the curve; ITT = insulin tolerance test; LC3 II/I = microtubule-associated protein light chain 3; NC = normal chow; pAkt = phospho-Akt; R EX = resistance exercise; SED = sedentary; Ub = ubiquitin.

Journal: Journal of Sport and Health Science

Article Title: Weightlifting outperforms voluntary wheel running for improving adiposity and insulin sensitivity in obese mice

doi: 10.1016/j.jshs.2025.101100

Figure Lengend Snippet: Resistance exercise exceeds the benefits of endurance exercise in ameliorating metabolic dysfunction. Following 8 weeks of diet and exercise interventions, all mice were assessed for their metabolic function by GTT, ITT, and skeletal muscle response of Akt and AS160 phosphorylation to injection of insulin measured by Western blot. (A–C) HOMA-IR taken after an overnight fast for baseline glucose and insulin. (D and E) GTT from 0–120 min and calculated AUC; colored * indicates significant difference from NC-SED. (F and G) ITT from 0–60 min and calculated AUC; colored * indicates significant difference from NC-SED. (H–N) pAkt stimulation, AS160 S318, and AS160 T642 in hindlimb muscles before and after insulin injection and the pre–post ∆ in phosphorylation. (O and P) Total and phosphorylated 4E-BP1. (Q–T) Western results for Raptor, COX4, LC3 II/I, and ubiquitin staining. Representative western blot images inset right. Data presented as mean ± standard error of the mean. Statistical analysis performed by analysis of variance between groups: * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001. NC-SED n : 8–16 (white); HFD-SED n : 8–18 (red); HFD-R EX n : 8–16 (blue); HFD-E EX n : 8–15 (green). 4E-BP1 = Eukaryotic translation initiation factor 4E binding protein; Akt = protein kinase B; AS160 = Akt substrate 160; COX4 = cytochrome c oxidase 4; CS = citrate sythase; E EX = endurance exercise; GAPDH = glyceraldehyde 3 phosphate dehydrogenase; GTT = glucose tolerance test; HFD = high fat diet; HOMA-IR = homeostatic model assessment for insulin resistance; iAUC = integrated area under the curve; ITT = insulin tolerance test; LC3 II/I = microtubule-associated protein light chain 3; NC = normal chow; pAkt = phospho-Akt; R EX = resistance exercise; SED = sedentary; Ub = ubiquitin.

Article Snippet: Primary antibodies used for analysis were from Cell Signaling Technologies (Danvers, MA, USA) and diluted 1:1000 unless otherwise stated as follows: protein kinase B (Akt; 1:500; #4691; Cell Signaling Technologies), phospho-Akt (pAkt) S473 (1:500; #9271; Cell Signaling Technologies), Ubiquitin (#3933; Cell Signaling Technologies), microtubule-associated protein light chain 3 (LC3 II/I; #4018; Cell Signaling Technologies), cytochrome c oxidase subunit 4(COX4; #11967; Cell Signaling Technologies), Akt substrate 160 (AS160 S318; #8619; Cell Signaling Technologies), AS160 T642 (#8881; Cell Signaling Technologies), eukaryotic translation initiation factor 4E binding protein (4E-BP1; #9452; Cell Signaling Technologies), and glyceraldehyde 3 phosphate dehydrogenase (GAPDH; #2118; Cell Signaling Technologies).

Techniques: Phospho-proteomics, Injection, Western Blot, Muscles, Ubiquitin Proteomics, Staining, Binding Assay

Journal: Advanced Science

Article Title: Fc‐Dependent Targeting of the GAS6–MERTK Axis With Monoclonal and Bispecific Antibodies Overcomes Drug Resistance Across EGFR Mutations in Exons 19, 20, and 21

doi: 10.1002/advs.78290

Figure Lengend Snippet:

Article Snippet: pAKT1 (Ser473) , 4060 , Cell Signaling Technology (CST) , AB_329825.

Techniques: Cell-Signaling

GRB1 suppresses pancreatic cancer progression by targeting the PI3K–AKT signaling pathway. (A) GO enrichment analysis of GRB1–PDAC overlapping targets showing enrichment in kinase regulation and phosphatidylinositol signaling. (B) KEGG enrichment highlighting the PI3K–AKT pathway as the key signaling axis. (C) Western blot showing decreased phosphorylation of PI3K and AKT in GRB1‐treated tumor and liver metastasis tissues. (D, E) Molecular docking and visualization demonstrating stable binding of GRB1 to AKT1 and PIK3CA with strong binding energies. Data are presented as mean ± SEM. ns, no significance; * p < 0.01, ** p < 0.001, *** p < 0.0001.

Journal: Food Science & Nutrition

Article Title: Ginsenoside Rb1 From the Functional Food Panax ginseng Suppresses Pancreatic Cancer Progression via Macrophage Reprogramming Through the PI3K ‐ AKT Pathway

doi: 10.1002/fsn3.72468

Figure Lengend Snippet: GRB1 suppresses pancreatic cancer progression by targeting the PI3K–AKT signaling pathway. (A) GO enrichment analysis of GRB1–PDAC overlapping targets showing enrichment in kinase regulation and phosphatidylinositol signaling. (B) KEGG enrichment highlighting the PI3K–AKT pathway as the key signaling axis. (C) Western blot showing decreased phosphorylation of PI3K and AKT in GRB1‐treated tumor and liver metastasis tissues. (D, E) Molecular docking and visualization demonstrating stable binding of GRB1 to AKT1 and PIK3CA with strong binding energies. Data are presented as mean ± SEM. ns, no significance; * p < 0.01, ** p < 0.001, *** p < 0.0001.

Article Snippet: Gemcitabine (Solarbio, China, G8970), Ginsenoside Rb1 (Macklin, Shanghai, G742231), Mouse Ki67 (Abclonal, China, A20018); CK19 (Abclonal, China, A25546); SOX2 (Abclonal, China, A19118); Vimentin (Abclonal, China, A19607); Zeb‐1 (Abclonal, China, A5600); E‐cadherin (Abcam, USA, ab40772); AKT (Abclonal, China, AP0637); P‐AKT (Abclonal, China, AP0637); PI3K (Abclonal, China, A27717); P‐PI3K (Abclonal, China, A27717); GAPDH (Abclonal, China, A19056); CD45 (BioLegend, USA, 103106); CD3 (BioLegend, USA, 100219); CD11b (BioLegend, USA, 101224); CD206 (Abclonal, China, A21014); CD206 (BioLegend, USA, 141721); CD163 (BioLegend, USA, 155327); ARG1 (BioLegend, USA, 165804); CD86 (BioLegend, USA, 105013); M‐CSF (MCE, USA, HY‐ P70488 ); IL4 (MCE, USA, HY‐139092); PMA (MCE, USA, HY‐18739); collagenase Type IV (Sigma, USA, C5138); deoxyribonuclease I (Thermo, USA, EN0521); Matrigel (Corning, USA, 354234); Organoid culture medium (Omabio, China, OM12).

Techniques: Analysis, Western Blot, Phospho-proteomics, Docking Assay, Binding Assay

Food‐derived bioactive compound GRB1 inhibits M2 macrophage polarization and pancreatic cancer progression via PI3K–AKT signaling. (A) Schematic of macrophage differentiation and co‐culture workflow. PBMCs or THP‐1 cells were induced to M2 macrophages with IL‐4, with or without GRB1 treatment. GRB1‐treated macrophages were co‐cultured with pancreatic cancer organoids or co‐injected with ASPC1 cells in vivo. (B) qRT–PCR showing reduced expression of M2 markers (CD206, TGFB1, CD115) after GRB1 treatment. (C) Western blot showing that GRB1 inhibited PI3K and AKT phosphorylation in macrophages. (D) Bright‐field images of organoids co‐cultured with control, M2, or GRB1‐treated M2 macrophages, showing reduced growth in the GRB1 group. (E–G) Representative liver images, H&E/IHC staining for CD163 and CD206, and quantification showing that GRB1 decreased M2 macrophage infiltration and liver metastases. Data are presented as mean ± SEM. ns, no significance; * p < 0.01, ** p < 0.001, *** p < 0.0001.

Journal: Food Science & Nutrition

Article Title: Ginsenoside Rb1 From the Functional Food Panax ginseng Suppresses Pancreatic Cancer Progression via Macrophage Reprogramming Through the PI3K ‐ AKT Pathway

doi: 10.1002/fsn3.72468

Figure Lengend Snippet: Food‐derived bioactive compound GRB1 inhibits M2 macrophage polarization and pancreatic cancer progression via PI3K–AKT signaling. (A) Schematic of macrophage differentiation and co‐culture workflow. PBMCs or THP‐1 cells were induced to M2 macrophages with IL‐4, with or without GRB1 treatment. GRB1‐treated macrophages were co‐cultured with pancreatic cancer organoids or co‐injected with ASPC1 cells in vivo. (B) qRT–PCR showing reduced expression of M2 markers (CD206, TGFB1, CD115) after GRB1 treatment. (C) Western blot showing that GRB1 inhibited PI3K and AKT phosphorylation in macrophages. (D) Bright‐field images of organoids co‐cultured with control, M2, or GRB1‐treated M2 macrophages, showing reduced growth in the GRB1 group. (E–G) Representative liver images, H&E/IHC staining for CD163 and CD206, and quantification showing that GRB1 decreased M2 macrophage infiltration and liver metastases. Data are presented as mean ± SEM. ns, no significance; * p < 0.01, ** p < 0.001, *** p < 0.0001.

Article Snippet: Gemcitabine (Solarbio, China, G8970), Ginsenoside Rb1 (Macklin, Shanghai, G742231), Mouse Ki67 (Abclonal, China, A20018); CK19 (Abclonal, China, A25546); SOX2 (Abclonal, China, A19118); Vimentin (Abclonal, China, A19607); Zeb‐1 (Abclonal, China, A5600); E‐cadherin (Abcam, USA, ab40772); AKT (Abclonal, China, AP0637); P‐AKT (Abclonal, China, AP0637); PI3K (Abclonal, China, A27717); P‐PI3K (Abclonal, China, A27717); GAPDH (Abclonal, China, A19056); CD45 (BioLegend, USA, 103106); CD3 (BioLegend, USA, 100219); CD11b (BioLegend, USA, 101224); CD206 (Abclonal, China, A21014); CD206 (BioLegend, USA, 141721); CD163 (BioLegend, USA, 155327); ARG1 (BioLegend, USA, 165804); CD86 (BioLegend, USA, 105013); M‐CSF (MCE, USA, HY‐ P70488 ); IL4 (MCE, USA, HY‐139092); PMA (MCE, USA, HY‐18739); collagenase Type IV (Sigma, USA, C5138); deoxyribonuclease I (Thermo, USA, EN0521); Matrigel (Corning, USA, 354234); Organoid culture medium (Omabio, China, OM12).

Techniques: Derivative Assay, Co-culture Assay, Cell Culture, Organoids, Injection, In Vivo, Quantitative RT-PCR, Expressing, Western Blot, Phospho-proteomics, Control, Immunohistochemistry