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MedChemExpress pi3k akt signaling pathways
Influence of LX-2 Cells on MDA-MB-231 Cells through CCL5. Note: ( A ) Schematic representation of the cell experiment process; ( B ) CCK-8 experiment assessing changes in cell proliferation in each group; 100 µL of conditioned medium (CM) per well; ( C ) Scratch assay examining cell migration ability in each group with statistical analysis (scale bar: 100 μm); 2 mL of CM per well; ( D ) Transwell assay measuring cell invasion ability in each group (scale bar: 50 μm); 200 µL of CM per well; ( E ) WB analysis of EMT marker proteins E-cadherin, N-cadherin, and Vimentin, <t>and</t> <t>PI3K-AKT</t> pathway protein expression changes; 2 mL of CM per well. CM: condition medium.* P < 0.05, with all cell experiments repeated three times
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Influence of LX-2 Cells on MDA-MB-231 Cells through CCL5. Note: ( A ) Schematic representation of the cell experiment process; ( B ) CCK-8 experiment assessing changes in cell proliferation in each group; 100 µL of conditioned medium (CM) per well; ( C ) Scratch assay examining cell migration ability in each group with statistical analysis (scale bar: 100 μm); 2 mL of CM per well; ( D ) Transwell assay measuring cell invasion ability in each group (scale bar: 50 μm); 200 µL of CM per well; ( E ) WB analysis of EMT marker proteins E-cadherin, N-cadherin, and Vimentin, <t>and</t> <t>PI3K-AKT</t> pathway protein expression changes; 2 mL of CM per well. CM: condition medium.* P < 0.05, with all cell experiments repeated three times
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Influence of LX-2 Cells on MDA-MB-231 Cells through CCL5. Note: ( A ) Schematic representation of the cell experiment process; ( B ) CCK-8 experiment assessing changes in cell proliferation in each group; 100 µL of conditioned medium (CM) per well; ( C ) Scratch assay examining cell migration ability in each group with statistical analysis (scale bar: 100 μm); 2 mL of CM per well; ( D ) Transwell assay measuring cell invasion ability in each group (scale bar: 50 μm); 200 µL of CM per well; ( E ) WB analysis of EMT marker proteins E-cadherin, N-cadherin, and Vimentin, <t>and</t> <t>PI3K-AKT</t> pathway protein expression changes; 2 mL of CM per well. CM: condition medium.* P < 0.05, with all cell experiments repeated three times
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MedChemExpress cells
Influence of LX-2 Cells on MDA-MB-231 Cells through CCL5. Note: ( A ) Schematic representation of the cell experiment process; ( B ) CCK-8 experiment assessing changes in cell proliferation in each group; 100 µL of conditioned medium (CM) per well; ( C ) Scratch assay examining cell migration ability in each group with statistical analysis (scale bar: 100 μm); 2 mL of CM per well; ( D ) Transwell assay measuring cell invasion ability in each group (scale bar: 50 μm); 200 µL of CM per well; ( E ) WB analysis of EMT marker proteins E-cadherin, N-cadherin, and Vimentin, <t>and</t> <t>PI3K-AKT</t> pathway protein expression changes; 2 mL of CM per well. CM: condition medium.* P < 0.05, with all cell experiments repeated three times
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MedChemExpress ccr5 antagonist maraviroc
Influence of LX-2 Cells on MDA-MB-231 Cells through CCL5. Note: ( A ) Schematic representation of the cell experiment process; ( B ) CCK-8 experiment assessing changes in cell proliferation in each group; 100 µL of conditioned medium (CM) per well; ( C ) Scratch assay examining cell migration ability in each group with statistical analysis (scale bar: 100 μm); 2 mL of CM per well; ( D ) Transwell assay measuring cell invasion ability in each group (scale bar: 50 μm); 200 µL of CM per well; ( E ) WB analysis of EMT marker proteins E-cadherin, N-cadherin, and Vimentin, <t>and</t> <t>PI3K-AKT</t> pathway protein expression changes; 2 mL of CM per well. CM: condition medium.* P < 0.05, with all cell experiments repeated three times
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SRGN deficiency reshapes the inflammatory secretome and transcriptional programs in human macrophages (A) Volcano plot of differentially secreted proteins between SRGN −/− and wild-type THP-1 macrophages under M1 polarization. Among 1,507 quantified proteins, 53 were significantly altered (adjusted p < 0.05), with serglycin being the most downregulated protein in knockout cells. (B) Validation of selected targets by RT-qPCR. SRGN −/− M1 macrophages showed significantly increased expression of IL6 and TNF and reduced expression of <t>CCL5</t> compared with wild-type cells (mean ± SEM; unpaired Student’s t test; p < 0.05, ∗ p < 0.01, and ∗∗∗ p < 0.0001; n = 4). (C) ELISA quantification of secreted cytokines in culture supernatants. SRGN −/− macrophages secreted significantly less TNF-α, CCL5, and IL-6 compared with wild-type macrophages ( n = 4), consistent with proteomics and RNA-seq data. (D) Transmission electron microscopy (TEM) images of THP-1 M0 and M1 macrophages. Scale bars, 5 μm. Vesicles were manually annotated and quantified in 10 cells per experimental group. The number of vesicles per cell and the percentage of cellular area occupied by vesicles were significantly reduced in both M0 and M1 SRGN −/− macrophages compared with wild-type macrophages. (E) Phagocytosis assay using fluorescently labeled bioparticles. SRGN −/− macrophages exhibited reduced phagocytic capacity under both M0 and M1 conditions (mean ± SEM; unpaired Student’s t test; p < 0.05 and ∗∗ p < 0.001; n = 6).
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Multi Sciences (Lianke) Biotech Co Ltd ek3129
SRGN deficiency reshapes the inflammatory secretome and transcriptional programs in human macrophages (A) Volcano plot of differentially secreted proteins between SRGN −/− and wild-type THP-1 macrophages under M1 polarization. Among 1,507 quantified proteins, 53 were significantly altered (adjusted p < 0.05), with serglycin being the most downregulated protein in knockout cells. (B) Validation of selected targets by RT-qPCR. SRGN −/− M1 macrophages showed significantly increased expression of IL6 and TNF and reduced expression of <t>CCL5</t> compared with wild-type cells (mean ± SEM; unpaired Student’s t test; p < 0.05, ∗ p < 0.01, and ∗∗∗ p < 0.0001; n = 4). (C) ELISA quantification of secreted cytokines in culture supernatants. SRGN −/− macrophages secreted significantly less TNF-α, CCL5, and IL-6 compared with wild-type macrophages ( n = 4), consistent with proteomics and RNA-seq data. (D) Transmission electron microscopy (TEM) images of THP-1 M0 and M1 macrophages. Scale bars, 5 μm. Vesicles were manually annotated and quantified in 10 cells per experimental group. The number of vesicles per cell and the percentage of cellular area occupied by vesicles were significantly reduced in both M0 and M1 SRGN −/− macrophages compared with wild-type macrophages. (E) Phagocytosis assay using fluorescently labeled bioparticles. SRGN −/− macrophages exhibited reduced phagocytic capacity under both M0 and M1 conditions (mean ± SEM; unpaired Student’s t test; p < 0.05 and ∗∗ p < 0.001; n = 6).
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SRGN deficiency reshapes the inflammatory secretome and transcriptional programs in human macrophages (A) Volcano plot of differentially secreted proteins between SRGN −/− and wild-type THP-1 macrophages under M1 polarization. Among 1,507 quantified proteins, 53 were significantly altered (adjusted p < 0.05), with serglycin being the most downregulated protein in knockout cells. (B) Validation of selected targets by RT-qPCR. SRGN −/− M1 macrophages showed significantly increased expression of IL6 and TNF and reduced expression of <t>CCL5</t> compared with wild-type cells (mean ± SEM; unpaired Student’s t test; p < 0.05, ∗ p < 0.01, and ∗∗∗ p < 0.0001; n = 4). (C) ELISA quantification of secreted cytokines in culture supernatants. SRGN −/− macrophages secreted significantly less TNF-α, CCL5, and IL-6 compared with wild-type macrophages ( n = 4), consistent with proteomics and RNA-seq data. (D) Transmission electron microscopy (TEM) images of THP-1 M0 and M1 macrophages. Scale bars, 5 μm. Vesicles were manually annotated and quantified in 10 cells per experimental group. The number of vesicles per cell and the percentage of cellular area occupied by vesicles were significantly reduced in both M0 and M1 SRGN −/− macrophages compared with wild-type macrophages. (E) Phagocytosis assay using fluorescently labeled bioparticles. SRGN −/− macrophages exhibited reduced phagocytic capacity under both M0 and M1 conditions (mean ± SEM; unpaired Student’s t test; p < 0.05 and ∗∗ p < 0.001; n = 6).
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Multi Sciences (Lianke) Biotech Co Ltd ccl5
SRGN deficiency reshapes the inflammatory secretome and transcriptional programs in human macrophages (A) Volcano plot of differentially secreted proteins between SRGN −/− and wild-type THP-1 macrophages under M1 polarization. Among 1,507 quantified proteins, 53 were significantly altered (adjusted p < 0.05), with serglycin being the most downregulated protein in knockout cells. (B) Validation of selected targets by RT-qPCR. SRGN −/− M1 macrophages showed significantly increased expression of IL6 and TNF and reduced expression of <t>CCL5</t> compared with wild-type cells (mean ± SEM; unpaired Student’s t test; p < 0.05, ∗ p < 0.01, and ∗∗∗ p < 0.0001; n = 4). (C) ELISA quantification of secreted cytokines in culture supernatants. SRGN −/− macrophages secreted significantly less TNF-α, CCL5, and IL-6 compared with wild-type macrophages ( n = 4), consistent with proteomics and RNA-seq data. (D) Transmission electron microscopy (TEM) images of THP-1 M0 and M1 macrophages. Scale bars, 5 μm. Vesicles were manually annotated and quantified in 10 cells per experimental group. The number of vesicles per cell and the percentage of cellular area occupied by vesicles were significantly reduced in both M0 and M1 SRGN −/− macrophages compared with wild-type macrophages. (E) Phagocytosis assay using fluorescently labeled bioparticles. SRGN −/− macrophages exhibited reduced phagocytic capacity under both M0 and M1 conditions (mean ± SEM; unpaired Student’s t test; p < 0.05 and ∗∗ p < 0.001; n = 6).
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Image Search Results


Influence of LX-2 Cells on MDA-MB-231 Cells through CCL5. Note: ( A ) Schematic representation of the cell experiment process; ( B ) CCK-8 experiment assessing changes in cell proliferation in each group; 100 µL of conditioned medium (CM) per well; ( C ) Scratch assay examining cell migration ability in each group with statistical analysis (scale bar: 100 μm); 2 mL of CM per well; ( D ) Transwell assay measuring cell invasion ability in each group (scale bar: 50 μm); 200 µL of CM per well; ( E ) WB analysis of EMT marker proteins E-cadherin, N-cadherin, and Vimentin, and PI3K-AKT pathway protein expression changes; 2 mL of CM per well. CM: condition medium.* P < 0.05, with all cell experiments repeated three times

Journal: Cancer Cell International

Article Title: Targeting the CCL5/CCR5-PI3K-AKT axis suppresses hepatic stellate cell-induced breast cancer metastasis

doi: 10.1186/s12935-026-04295-2

Figure Lengend Snippet: Influence of LX-2 Cells on MDA-MB-231 Cells through CCL5. Note: ( A ) Schematic representation of the cell experiment process; ( B ) CCK-8 experiment assessing changes in cell proliferation in each group; 100 µL of conditioned medium (CM) per well; ( C ) Scratch assay examining cell migration ability in each group with statistical analysis (scale bar: 100 μm); 2 mL of CM per well; ( D ) Transwell assay measuring cell invasion ability in each group (scale bar: 50 μm); 200 µL of CM per well; ( E ) WB analysis of EMT marker proteins E-cadherin, N-cadherin, and Vimentin, and PI3K-AKT pathway protein expression changes; 2 mL of CM per well. CM: condition medium.* P < 0.05, with all cell experiments repeated three times

Article Snippet: To investigate the impact of the CCL5, CCR5, and PI3K-AKT signaling pathways on BC cells, during the cell culture process, cells were treated with 10 ng/ml CCL5 (MCE, HY-P7282), 100 nM CCR5 antagonist Maraviroc (MCE, HY-13004), and 500 nM of the PI3K inhibitor BKM120 (MCE, HY-70063) were added to the culture medium [ ].

Techniques: CCK-8 Assay, Wound Healing Assay, Migration, Transwell Assay, Marker, Expressing

Impact of CCR5 and PI3K-AKT Pathway Inhibition on MDA-MB-231 Cells. Note: ( A ) CCK-8 experiment evaluating changes in cell proliferation in each group; ( B ) Scratch assay assessing cell migration ability in each group with statistical representation (scale bar: 100 μm); ( C ) Transwell assay measuring cell invasion ability in each group (scale bar: 50 μm); ( D ) WB analysis of EMT marker proteins E-cadherin, N-cadherin, and Vimentin, and PI3K-AKT pathway protein expression changes. * P < 0.05, with all cell experiments repeated three times

Journal: Cancer Cell International

Article Title: Targeting the CCL5/CCR5-PI3K-AKT axis suppresses hepatic stellate cell-induced breast cancer metastasis

doi: 10.1186/s12935-026-04295-2

Figure Lengend Snippet: Impact of CCR5 and PI3K-AKT Pathway Inhibition on MDA-MB-231 Cells. Note: ( A ) CCK-8 experiment evaluating changes in cell proliferation in each group; ( B ) Scratch assay assessing cell migration ability in each group with statistical representation (scale bar: 100 μm); ( C ) Transwell assay measuring cell invasion ability in each group (scale bar: 50 μm); ( D ) WB analysis of EMT marker proteins E-cadherin, N-cadherin, and Vimentin, and PI3K-AKT pathway protein expression changes. * P < 0.05, with all cell experiments repeated three times

Article Snippet: To investigate the impact of the CCL5, CCR5, and PI3K-AKT signaling pathways on BC cells, during the cell culture process, cells were treated with 10 ng/ml CCL5 (MCE, HY-P7282), 100 nM CCR5 antagonist Maraviroc (MCE, HY-13004), and 500 nM of the PI3K inhibitor BKM120 (MCE, HY-70063) were added to the culture medium [ ].

Techniques: Inhibition, CCK-8 Assay, Wound Healing Assay, Migration, Transwell Assay, Marker, Expressing

CCL5 Derived from HSCs Activates the PI3K-AKT Pathway through the CCL5/CCR5 Axis to Promote the Invasion and Metastasis of Breast Cancer Cells

Journal: Cancer Cell International

Article Title: Targeting the CCL5/CCR5-PI3K-AKT axis suppresses hepatic stellate cell-induced breast cancer metastasis

doi: 10.1186/s12935-026-04295-2

Figure Lengend Snippet: CCL5 Derived from HSCs Activates the PI3K-AKT Pathway through the CCL5/CCR5 Axis to Promote the Invasion and Metastasis of Breast Cancer Cells

Article Snippet: To investigate the impact of the CCL5, CCR5, and PI3K-AKT signaling pathways on BC cells, during the cell culture process, cells were treated with 10 ng/ml CCL5 (MCE, HY-P7282), 100 nM CCR5 antagonist Maraviroc (MCE, HY-13004), and 500 nM of the PI3K inhibitor BKM120 (MCE, HY-70063) were added to the culture medium [ ].

Techniques: Derivative Assay

SRGN deficiency reshapes the inflammatory secretome and transcriptional programs in human macrophages (A) Volcano plot of differentially secreted proteins between SRGN −/− and wild-type THP-1 macrophages under M1 polarization. Among 1,507 quantified proteins, 53 were significantly altered (adjusted p < 0.05), with serglycin being the most downregulated protein in knockout cells. (B) Validation of selected targets by RT-qPCR. SRGN −/− M1 macrophages showed significantly increased expression of IL6 and TNF and reduced expression of CCL5 compared with wild-type cells (mean ± SEM; unpaired Student’s t test; p < 0.05, ∗ p < 0.01, and ∗∗∗ p < 0.0001; n = 4). (C) ELISA quantification of secreted cytokines in culture supernatants. SRGN −/− macrophages secreted significantly less TNF-α, CCL5, and IL-6 compared with wild-type macrophages ( n = 4), consistent with proteomics and RNA-seq data. (D) Transmission electron microscopy (TEM) images of THP-1 M0 and M1 macrophages. Scale bars, 5 μm. Vesicles were manually annotated and quantified in 10 cells per experimental group. The number of vesicles per cell and the percentage of cellular area occupied by vesicles were significantly reduced in both M0 and M1 SRGN −/− macrophages compared with wild-type macrophages. (E) Phagocytosis assay using fluorescently labeled bioparticles. SRGN −/− macrophages exhibited reduced phagocytic capacity under both M0 and M1 conditions (mean ± SEM; unpaired Student’s t test; p < 0.05 and ∗∗ p < 0.001; n = 6).

Journal: iScience

Article Title: Serglycin modulates inflammation and metabolism in macrophages

doi: 10.1016/j.isci.2026.115235

Figure Lengend Snippet: SRGN deficiency reshapes the inflammatory secretome and transcriptional programs in human macrophages (A) Volcano plot of differentially secreted proteins between SRGN −/− and wild-type THP-1 macrophages under M1 polarization. Among 1,507 quantified proteins, 53 were significantly altered (adjusted p < 0.05), with serglycin being the most downregulated protein in knockout cells. (B) Validation of selected targets by RT-qPCR. SRGN −/− M1 macrophages showed significantly increased expression of IL6 and TNF and reduced expression of CCL5 compared with wild-type cells (mean ± SEM; unpaired Student’s t test; p < 0.05, ∗ p < 0.01, and ∗∗∗ p < 0.0001; n = 4). (C) ELISA quantification of secreted cytokines in culture supernatants. SRGN −/− macrophages secreted significantly less TNF-α, CCL5, and IL-6 compared with wild-type macrophages ( n = 4), consistent with proteomics and RNA-seq data. (D) Transmission electron microscopy (TEM) images of THP-1 M0 and M1 macrophages. Scale bars, 5 μm. Vesicles were manually annotated and quantified in 10 cells per experimental group. The number of vesicles per cell and the percentage of cellular area occupied by vesicles were significantly reduced in both M0 and M1 SRGN −/− macrophages compared with wild-type macrophages. (E) Phagocytosis assay using fluorescently labeled bioparticles. SRGN −/− macrophages exhibited reduced phagocytic capacity under both M0 and M1 conditions (mean ± SEM; unpaired Student’s t test; p < 0.05 and ∗∗ p < 0.001; n = 6).

Article Snippet: THP-1: cytokine levels were measured using ELISA kits from R&D Systems: CCL5 (Cat. No. DY278), IL6 (Cat. No. DY206), IL-1β (Cat. No. DY201), TGF-β (Cat. No. DY240; activation kit DY010), and TNF-α (Cat. No. DY210), following the manufacturer’s instructions.

Techniques: Knock-Out, Biomarker Discovery, Quantitative RT-PCR, Expressing, Enzyme-linked Immunosorbent Assay, RNA Sequencing, Transmission Assay, Electron Microscopy, Phagocytosis Assay, Labeling