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ATCC human neuroblastoma nb cell lines sk n be 2 c
$(A) General Synthesis of QW-5–70. i). 60% NaH, SEMCl, THF, 0–25 °C; ii). n-BuLi, 3,4,5-trimethoxybenzaldehyde, THF, −78 °C; iii). Dess-Martin, CH 2 Cl 2 , r.t.; iv)1-(phenylsulfonyl)-4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)-1H-indazole, Pd(PPh 3 ) 4 , Na 2 CO 3 , 1,4-dioxane/H 2 O (v/v = 2/1), reflux; v). Pd(OAC) 2 , PPh 3 , K 2 CO 3 , n-butanol, reflux; vi). 37% HCl, MeOH, reflux. (B) QW-5–70 induced tubulin depolymerization. Colchicine and paclitaxel were included as reference compounds. (C) SPR sensorgrams of QW-5–70 and colchicine binding to tubulin. (mean ± SEM, n = 3) (D) EBI competition assays. The upper β-tubulin band represents native β-tubulin, while the lower band corresponds to the EBI–β-tubulin adduct. GAPDH served as a loading control. (E) Immunoblot analysis of soluble and polymerized β-tubulin in PC-3 cells following treatment with QW-5–70, colchicine, or paclitaxel (20 nM). Cells were fractionated into soluble and polymerized tubulin pools, which were analyzed by immunoblotting. Ponceau S staining and GAPDH were used as loading controls for polymerized and soluble fractions, respectively. Quantification of polymerized β-tubulin expressed as a percentage of total β-tubulin (soluble + polymerized). (mean ± SEM, n=3). (F) Representative immunofluorescence images of interphase and mitotic <t>SK-N-BE(2)-C,</t> NB-1691, and PC-3 cells treated with QW-5–70 (2 nM and 5 nM) for 24 h. Microtubules were stained with anti-α-tubulin antibodies (red), and nuclei were counterstained with DAPI (blue). Scale bar = 50 μm (n=3). (G) High-resolution X-ray crystal structure of the sT2R complex with QW-5–70. Left panel: detailed interactions of QW-5–70 (green sticks) within the colchicine-binding site are shown. Bound water molecules are represented as red spheres, and hydrogen bonds are indicated by dashed magenta lines. The electron density for QW-5–70 is shown as a blue mesh; the final 2Fo-Fc map is contoured at 1.0 σ. Middle panel: detailed interactions of colchicine (light-brown sticks) binding to sT2R (PDB 6XER) for comparison. Right panel: superposition of sT2R complexes with QW-5–70 and colchicine sT2R (colored grey) complexes, highlighting the relative inhibitor binding positions and differing conformations of the α-T5 and β-T7 loops.$
Human Neuroblastoma Nb Cell Lines Sk N Be 2 C, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 446 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "QW-5-70 targets the colchicine site and demonstrates antitumor activity in P-gp–overexpressing cancer models"

Article Title: QW-5-70 targets the colchicine site and demonstrates antitumor activity in P-gp–overexpressing cancer models

Journal: Molecular cancer therapeutics

doi: 10.1158/1535-7163.MCT-25-1013

$(A) General Synthesis of QW-5–70. i). 60% NaH, SEMCl, THF, 0–25 °C; ii). n-BuLi, 3,4,5-trimethoxybenzaldehyde, THF, −78 °C; iii). Dess-Martin, CH 2 Cl 2 , r.t.; iv)1-(phenylsulfonyl)-4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)-1H-indazole, Pd(PPh 3 ) 4 , Na 2 CO 3 , 1,4-dioxane/H 2 O (v/v = 2/1), reflux; v). Pd(OAC) 2 , PPh 3 , K 2 CO 3 , n-butanol, reflux; vi). 37% HCl, MeOH, reflux. (B) QW-5–70 induced tubulin depolymerization. Colchicine and paclitaxel were included as reference compounds. (C) SPR sensorgrams of QW-5–70 and colchicine binding to tubulin. (mean ± SEM, n = 3) (D) EBI competition assays. The upper β-tubulin band represents native β-tubulin, while the lower band corresponds to the EBI–β-tubulin adduct. GAPDH served as a loading control. (E) Immunoblot analysis of soluble and polymerized β-tubulin in PC-3 cells following treatment with QW-5–70, colchicine, or paclitaxel (20 nM). Cells were fractionated into soluble and polymerized tubulin pools, which were analyzed by immunoblotting. Ponceau S staining and GAPDH were used as loading controls for polymerized and soluble fractions, respectively. Quantification of polymerized β-tubulin expressed as a percentage of total β-tubulin (soluble + polymerized). (mean ± SEM, n=3). (F) Representative immunofluorescence images of interphase and mitotic SK-N-BE(2)-C, NB-1691, and PC-3 cells treated with QW-5–70 (2 nM and 5 nM) for 24 h. Microtubules were stained with anti-α-tubulin antibodies (red), and nuclei were counterstained with DAPI (blue). Scale bar = 50 μm (n=3). (G) High-resolution X-ray crystal structure of the sT2R complex with QW-5–70. Left panel: detailed interactions of QW-5–70 (green sticks) within the colchicine-binding site are shown. Bound water molecules are represented as red spheres, and hydrogen bonds are indicated by dashed magenta lines. The electron density for QW-5–70 is shown as a blue mesh; the final 2Fo-Fc map is contoured at 1.0 σ. Middle panel: detailed interactions of colchicine (light-brown sticks) binding to sT2R (PDB 6XER) for comparison. Right panel: superposition of sT2R complexes with QW-5–70 and colchicine sT2R (colored grey) complexes, highlighting the relative inhibitor binding positions and differing conformations of the α-T5 and β-T7 loops.$
Figure Legend Snippet: (A) General Synthesis of QW-5–70. i). 60% NaH, SEMCl, THF, 0–25 °C; ii). n-BuLi, 3,4,5-trimethoxybenzaldehyde, THF, −78 °C; iii). Dess-Martin, CH 2 Cl 2 , r.t.; iv)1-(phenylsulfonyl)-4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)-1H-indazole, Pd(PPh 3 ) 4 , Na 2 CO 3 , 1,4-dioxane/H 2 O (v/v = 2/1), reflux; v). Pd(OAC) 2 , PPh 3 , K 2 CO 3 , n-butanol, reflux; vi). 37% HCl, MeOH, reflux. (B) QW-5–70 induced tubulin depolymerization. Colchicine and paclitaxel were included as reference compounds. (C) SPR sensorgrams of QW-5–70 and colchicine binding to tubulin. (mean ± SEM, n = 3) (D) EBI competition assays. The upper β-tubulin band represents native β-tubulin, while the lower band corresponds to the EBI–β-tubulin adduct. GAPDH served as a loading control. (E) Immunoblot analysis of soluble and polymerized β-tubulin in PC-3 cells following treatment with QW-5–70, colchicine, or paclitaxel (20 nM). Cells were fractionated into soluble and polymerized tubulin pools, which were analyzed by immunoblotting. Ponceau S staining and GAPDH were used as loading controls for polymerized and soluble fractions, respectively. Quantification of polymerized β-tubulin expressed as a percentage of total β-tubulin (soluble + polymerized). (mean ± SEM, n=3). (F) Representative immunofluorescence images of interphase and mitotic SK-N-BE(2)-C, NB-1691, and PC-3 cells treated with QW-5–70 (2 nM and 5 nM) for 24 h. Microtubules were stained with anti-α-tubulin antibodies (red), and nuclei were counterstained with DAPI (blue). Scale bar = 50 μm (n=3). (G) High-resolution X-ray crystal structure of the sT2R complex with QW-5–70. Left panel: detailed interactions of QW-5–70 (green sticks) within the colchicine-binding site are shown. Bound water molecules are represented as red spheres, and hydrogen bonds are indicated by dashed magenta lines. The electron density for QW-5–70 is shown as a blue mesh; the final 2Fo-Fc map is contoured at 1.0 σ. Middle panel: detailed interactions of colchicine (light-brown sticks) binding to sT2R (PDB 6XER) for comparison. Right panel: superposition of sT2R complexes with QW-5–70 and colchicine sT2R (colored grey) complexes, highlighting the relative inhibitor binding positions and differing conformations of the α-T5 and β-T7 loops.

Techniques Used: Binding Assay, Reflux, Control, Western Blot, Staining, Immunofluorescence, Comparison

(A) Representative images and quantification of colony formation in BE2C/VCR cells treated with QW-5–70, vincristine, or colchicine (1–5 nM). (B) Colony formation assays in PC-3/TxR cells treated with QW-5–70, paclitaxel, or colchicine (1–5 nM). Colony area is expressed as mean ± SEM relative to vehicle control (n = 5). (C) Transwell migration of BE2C/VCR (left) and PC-3/TxR (right) cells after 24 h treatment with vincristine or paclitaxel (5 nM) or QW-5–70 (2 or 5 nM). (D) Transwell migration of BE2C/VCR (left) and PC-3/TxR (right) cells treated with QW-5–70 (0.5–5 nM) for 24 h. Migration area is expressed as mean ± SEM relative to control (n = 5). Scale bar = 100 μm. (E) Immunoblot analysis of P-gp expression in SK-N-BE(2)-C and BE2C/VCR cells. (F) Viability of BE2C/VCR cells treated with QW-5–70 or vincristine (0.1 nM–3 μM) in the absence or presence of verapamil (10 μM) for 72 h (MTS assay; n = 4). (G) Intracellular concentrations of QW-5–70 and vincristine in parental SK-N-BE(2)-C and BE2C/VCR cells following 50 nM, 2 h treatment, with or without tariquidar (1 μM), quantified by LC–MS/MS (n = 3). (H) Immunoblot analysis of P-gp expression in PC-3 and PC-3/TxR cells. (I) Cell viability of PC-3/TxR cells treated with QW-5–70 or paclitaxel (0.1 nM–3 μM) in the absence or presence of verapamil (10 μM) for 72 h (MTS assay; n = 4). (J) Intracellular concentrations of QW-5–70 and paclitaxel in PC-3 and PC-3/TxR cells under the same conditions as panel G, quantified by LC–MS/MS (n = 3). (K) Immunoblot analysis of P-gp expression in PC-3/TxR cells following transfection with scrambled control or si-P-gp. GAPDH served as a loading control. (L) Viability of QW-5–70 and paclitaxel in PC-3/TxR, PC-3/TxR-scramble, and PC-3/TxR-si-P-gp cells (MTS assay; n=4).

Figure Legend Snippet: (A) Representative images and quantification of colony formation in BE2C/VCR cells treated with QW-5–70, vincristine, or colchicine (1–5 nM). (B) Colony formation assays in PC-3/TxR cells treated with QW-5–70, paclitaxel, or colchicine (1–5 nM). Colony area is expressed as mean ± SEM relative to vehicle control (n = 5). (C) Transwell migration of BE2C/VCR (left) and PC-3/TxR (right) cells after 24 h treatment with vincristine or paclitaxel (5 nM) or QW-5–70 (2 or 5 nM). (D) Transwell migration of BE2C/VCR (left) and PC-3/TxR (right) cells treated with QW-5–70 (0.5–5 nM) for 24 h. Migration area is expressed as mean ± SEM relative to control (n = 5). Scale bar = 100 μm. (E) Immunoblot analysis of P-gp expression in SK-N-BE(2)-C and BE2C/VCR cells. (F) Viability of BE2C/VCR cells treated with QW-5–70 or vincristine (0.1 nM–3 μM) in the absence or presence of verapamil (10 μM) for 72 h (MTS assay; n = 4). (G) Intracellular concentrations of QW-5–70 and vincristine in parental SK-N-BE(2)-C and BE2C/VCR cells following 50 nM, 2 h treatment, with or without tariquidar (1 μM), quantified by LC–MS/MS (n = 3). (H) Immunoblot analysis of P-gp expression in PC-3 and PC-3/TxR cells. (I) Cell viability of PC-3/TxR cells treated with QW-5–70 or paclitaxel (0.1 nM–3 μM) in the absence or presence of verapamil (10 μM) for 72 h (MTS assay; n = 4). (J) Intracellular concentrations of QW-5–70 and paclitaxel in PC-3 and PC-3/TxR cells under the same conditions as panel G, quantified by LC–MS/MS (n = 3). (K) Immunoblot analysis of P-gp expression in PC-3/TxR cells following transfection with scrambled control or si-P-gp. GAPDH served as a loading control. (L) Viability of QW-5–70 and paclitaxel in PC-3/TxR, PC-3/TxR-scramble, and PC-3/TxR-si-P-gp cells (MTS assay; n=4).

Techniques Used: Activity Assay, Expressing, Control, Migration, Western Blot, MTS Assay, Liquid Chromatography with Mass Spectroscopy, Transfection

(A) Cell-cycle distribution of SK-N-BE(2)-C, NB-1691, and PC-3/TxR cells treated with QW-5–70 (2 or 5 nM) for 24 h, analyzed by flow cytometry (n=3). (B, C) Immunoblot analysis of cell-cycle–related proteins (phospho-histone H3 (Ser10), histone H3, cyclin B1, phospho-CDK1 (Thr161), and CDK1) in parental (SK-N-BE(2)-C, NB-1691) and resistant (BE2C/VCR, PC-3/TxR) cells treated with QW-5–70 (2 or 5 nM) for 24 h. (D, E) Immunoblot analysis of apoptosis-related proteins (cCas9, cCas3, PARP, cPARP, p-BCL2 (Ser70), and BCL2) in the same cell lines following 24 h treatment. GAPDH served as a loading control.

Figure Legend Snippet: (A) Cell-cycle distribution of SK-N-BE(2)-C, NB-1691, and PC-3/TxR cells treated with QW-5–70 (2 or 5 nM) for 24 h, analyzed by flow cytometry (n=3). (B, C) Immunoblot analysis of cell-cycle–related proteins (phospho-histone H3 (Ser10), histone H3, cyclin B1, phospho-CDK1 (Thr161), and CDK1) in parental (SK-N-BE(2)-C, NB-1691) and resistant (BE2C/VCR, PC-3/TxR) cells treated with QW-5–70 (2 or 5 nM) for 24 h. (D, E) Immunoblot analysis of apoptosis-related proteins (cCas9, cCas3, PARP, cPARP, p-BCL2 (Ser70), and BCL2) in the same cell lines following 24 h treatment. GAPDH served as a loading control.

Techniques Used: Flow Cytometry, Western Blot, Control

(A) SK-N-BE(2)-c cells were treated with five doses of QW-5–70 (0.125 to 2 nM) in combination with five doses of DFMO (10–1000 μM). Cell viability was assessed using the MTS assay (n=4). (B) CI–Fa analysis of the QW-5–70 and DFMO combination. CI values were calculated using the Chou–Talalay median-effect method for five experimentally tested dose pairs at their corresponding Fa values. CI < 1, CI = 1, and CI > 1 indicate synergistic, additive, and antagonistic interactions, respectively. (C) SK-N-BE(2)-c cells were treated with five doses of QW-5–70 (0.125 to 2 nM) in combination with five doses of MLN8237 (1–100 nM). Cell viability was assessed using the MTS assay (n=4). (D) SK-N-BE(2)-C cells were treated with 1 nM QW-5–70 in combination with either DFMO (300 μM, top) or MLN8237 (30 nM, bottom) as indicated. Cell lysates were analyzed by immunoblotting for cPARP as a marker of apoptosis, with GAPDH used as a loading control. (E) Representative colony formation images of SK-N-BE(2)-C cells treated with the same combination. Colony formations were quantified and expressed as mean ± SEM relative to vehicle (set to 100%) (n=5).

Figure Legend Snippet: (A) SK-N-BE(2)-c cells were treated with five doses of QW-5–70 (0.125 to 2 nM) in combination with five doses of DFMO (10–1000 μM). Cell viability was assessed using the MTS assay (n=4). (B) CI–Fa analysis of the QW-5–70 and DFMO combination. CI values were calculated using the Chou–Talalay median-effect method for five experimentally tested dose pairs at their corresponding Fa values. CI < 1, CI = 1, and CI > 1 indicate synergistic, additive, and antagonistic interactions, respectively. (C) SK-N-BE(2)-c cells were treated with five doses of QW-5–70 (0.125 to 2 nM) in combination with five doses of MLN8237 (1–100 nM). Cell viability was assessed using the MTS assay (n=4). (D) SK-N-BE(2)-C cells were treated with 1 nM QW-5–70 in combination with either DFMO (300 μM, top) or MLN8237 (30 nM, bottom) as indicated. Cell lysates were analyzed by immunoblotting for cPARP as a marker of apoptosis, with GAPDH used as a loading control. (E) Representative colony formation images of SK-N-BE(2)-C cells treated with the same combination. Colony formations were quantified and expressed as mean ± SEM relative to vehicle (set to 100%) (n=5).

Techniques Used: Activity Assay, MTS Assay, Western Blot, Marker, Control

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Journal: Molecular cancer therapeutics

Article Title: QW-5-70 targets the colchicine site and demonstrates antitumor activity in P-gp–overexpressing cancer models

doi: 10.1158/1535-7163.MCT-25-1013

Figure Lengend Snippet: (A) General Synthesis of QW-5–70. i). 60% NaH, SEMCl, THF, 0–25 °C; ii). n-BuLi, 3,4,5-trimethoxybenzaldehyde, THF, −78 °C; iii). Dess-Martin, CH 2 Cl 2 , r.t.; iv)1-(phenylsulfonyl)-4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)-1H-indazole, Pd(PPh 3 ) 4 , Na 2 CO 3 , 1,4-dioxane/H 2 O (v/v = 2/1), reflux; v). Pd(OAC) 2 , PPh 3 , K 2 CO 3 , n-butanol, reflux; vi). 37% HCl, MeOH, reflux. (B) QW-5–70 induced tubulin depolymerization. Colchicine and paclitaxel were included as reference compounds. (C) SPR sensorgrams of QW-5–70 and colchicine binding to tubulin. (mean ± SEM, n = 3) (D) EBI competition assays. The upper β-tubulin band represents native β-tubulin, while the lower band corresponds to the EBI–β-tubulin adduct. GAPDH served as a loading control. (E) Immunoblot analysis of soluble and polymerized β-tubulin in PC-3 cells following treatment with QW-5–70, colchicine, or paclitaxel (20 nM). Cells were fractionated into soluble and polymerized tubulin pools, which were analyzed by immunoblotting. Ponceau S staining and GAPDH were used as loading controls for polymerized and soluble fractions, respectively. Quantification of polymerized β-tubulin expressed as a percentage of total β-tubulin (soluble + polymerized). (mean ± SEM, n=3). (F) Representative immunofluorescence images of interphase and mitotic SK-N-BE(2)-C, NB-1691, and PC-3 cells treated with QW-5–70 (2 nM and 5 nM) for 24 h. Microtubules were stained with anti-α-tubulin antibodies (red), and nuclei were counterstained with DAPI (blue). Scale bar = 50 μm (n=3). (G) High-resolution X-ray crystal structure of the sT2R complex with QW-5–70. Left panel: detailed interactions of QW-5–70 (green sticks) within the colchicine-binding site are shown. Bound water molecules are represented as red spheres, and hydrogen bonds are indicated by dashed magenta lines. The electron density for QW-5–70 is shown as a blue mesh; the final 2Fo-Fc map is contoured at 1.0 σ. Middle panel: detailed interactions of colchicine (light-brown sticks) binding to sT2R (PDB 6XER) for comparison. Right panel: superposition of sT2R complexes with QW-5–70 and colchicine sT2R (colored grey) complexes, highlighting the relative inhibitor binding positions and differing conformations of the α-T5 and β-T7 loops.

Article Snippet: Human neuroblastoma (NB) cell lines (SK-N-BE(2)-C, RRID: CVCL_0529; NB-1691, RRID: CVCL_5628; SK-N-BE(2), RRID: CVCL_0528; SiMa, RRID: CVCL_1695; IMR-32, RRID: CVCL_0346) and prostate cancer cell lines (PC-3, RRID: CVCL_0035; 22Rv1, RRID: CVCL_1045) were originally obtained from ATCC in 2019.

Techniques: Binding Assay, Reflux, Control, Western Blot, Staining, Immunofluorescence, Comparison

Journal: Molecular cancer therapeutics

Article Title: QW-5-70 targets the colchicine site and demonstrates antitumor activity in P-gp–overexpressing cancer models

doi: 10.1158/1535-7163.MCT-25-1013

Figure Lengend Snippet: (A) Representative images and quantification of colony formation in BE2C/VCR cells treated with QW-5–70, vincristine, or colchicine (1–5 nM). (B) Colony formation assays in PC-3/TxR cells treated with QW-5–70, paclitaxel, or colchicine (1–5 nM). Colony area is expressed as mean ± SEM relative to vehicle control (n = 5). (C) Transwell migration of BE2C/VCR (left) and PC-3/TxR (right) cells after 24 h treatment with vincristine or paclitaxel (5 nM) or QW-5–70 (2 or 5 nM). (D) Transwell migration of BE2C/VCR (left) and PC-3/TxR (right) cells treated with QW-5–70 (0.5–5 nM) for 24 h. Migration area is expressed as mean ± SEM relative to control (n = 5). Scale bar = 100 μm. (E) Immunoblot analysis of P-gp expression in SK-N-BE(2)-C and BE2C/VCR cells. (F) Viability of BE2C/VCR cells treated with QW-5–70 or vincristine (0.1 nM–3 μM) in the absence or presence of verapamil (10 μM) for 72 h (MTS assay; n = 4). (G) Intracellular concentrations of QW-5–70 and vincristine in parental SK-N-BE(2)-C and BE2C/VCR cells following 50 nM, 2 h treatment, with or without tariquidar (1 μM), quantified by LC–MS/MS (n = 3). (H) Immunoblot analysis of P-gp expression in PC-3 and PC-3/TxR cells. (I) Cell viability of PC-3/TxR cells treated with QW-5–70 or paclitaxel (0.1 nM–3 μM) in the absence or presence of verapamil (10 μM) for 72 h (MTS assay; n = 4). (J) Intracellular concentrations of QW-5–70 and paclitaxel in PC-3 and PC-3/TxR cells under the same conditions as panel G, quantified by LC–MS/MS (n = 3). (K) Immunoblot analysis of P-gp expression in PC-3/TxR cells following transfection with scrambled control or si-P-gp. GAPDH served as a loading control. (L) Viability of QW-5–70 and paclitaxel in PC-3/TxR, PC-3/TxR-scramble, and PC-3/TxR-si-P-gp cells (MTS assay; n=4).

Techniques: Activity Assay, Expressing, Control, Migration, Western Blot, MTS Assay, Liquid Chromatography with Mass Spectroscopy, Transfection

Journal: Molecular cancer therapeutics

Article Title: QW-5-70 targets the colchicine site and demonstrates antitumor activity in P-gp–overexpressing cancer models

doi: 10.1158/1535-7163.MCT-25-1013

Figure Lengend Snippet: (A) Cell-cycle distribution of SK-N-BE(2)-C, NB-1691, and PC-3/TxR cells treated with QW-5–70 (2 or 5 nM) for 24 h, analyzed by flow cytometry (n=3). (B, C) Immunoblot analysis of cell-cycle–related proteins (phospho-histone H3 (Ser10), histone H3, cyclin B1, phospho-CDK1 (Thr161), and CDK1) in parental (SK-N-BE(2)-C, NB-1691) and resistant (BE2C/VCR, PC-3/TxR) cells treated with QW-5–70 (2 or 5 nM) for 24 h. (D, E) Immunoblot analysis of apoptosis-related proteins (cCas9, cCas3, PARP, cPARP, p-BCL2 (Ser70), and BCL2) in the same cell lines following 24 h treatment. GAPDH served as a loading control.

Techniques: Flow Cytometry, Western Blot, Control

Journal: Molecular cancer therapeutics

Article Title: QW-5-70 targets the colchicine site and demonstrates antitumor activity in P-gp–overexpressing cancer models

doi: 10.1158/1535-7163.MCT-25-1013

Figure Lengend Snippet: (A) SK-N-BE(2)-c cells were treated with five doses of QW-5–70 (0.125 to 2 nM) in combination with five doses of DFMO (10–1000 μM). Cell viability was assessed using the MTS assay (n=4). (B) CI–Fa analysis of the QW-5–70 and DFMO combination. CI values were calculated using the Chou–Talalay median-effect method for five experimentally tested dose pairs at their corresponding Fa values. CI < 1, CI = 1, and CI > 1 indicate synergistic, additive, and antagonistic interactions, respectively. (C) SK-N-BE(2)-c cells were treated with five doses of QW-5–70 (0.125 to 2 nM) in combination with five doses of MLN8237 (1–100 nM). Cell viability was assessed using the MTS assay (n=4). (D) SK-N-BE(2)-C cells were treated with 1 nM QW-5–70 in combination with either DFMO (300 μM, top) or MLN8237 (30 nM, bottom) as indicated. Cell lysates were analyzed by immunoblotting for cPARP as a marker of apoptosis, with GAPDH used as a loading control. (E) Representative colony formation images of SK-N-BE(2)-C cells treated with the same combination. Colony formations were quantified and expressed as mean ± SEM relative to vehicle (set to 100%) (n=5).

Techniques: Activity Assay, MTS Assay, Western Blot, Marker, Control

FKA treatment suppresses the proliferative and clone-forming abilities of NB cells. A The structure of FKA. B HUVECs were treated with 0, 12.5, 25, 50 μM FKA for 48 h. The viability of HUVECs was detected by CCK-8 assay. C Human NB cell line (SK-N-SH) was treated with 0, 12.5, 25, 50 μM FKA for 48 h. The viability of SK-N-SH cells was detected by CCK-8 assay. D SK-N-SH cells were treated with 0, 12.5, 25, 50 μM FKA for 48 h. The clone-forming ability of SK-N-SH cells was detected by colony formation assay. *** p < 0.001

Journal: Discover Oncology

Article Title: Flavokawain A suppresses the malignant progression of neuroblastoma in vitro depending on inactivation of ERK/VEGF/MMPs signaling pathway

doi: 10.1007/s12672-024-01568-y

Figure Lengend Snippet: FKA treatment suppresses the proliferative and clone-forming abilities of NB cells. A The structure of FKA. B HUVECs were treated with 0, 12.5, 25, 50 μM FKA for 48 h. The viability of HUVECs was detected by CCK-8 assay. C Human NB cell line (SK-N-SH) was treated with 0, 12.5, 25, 50 μM FKA for 48 h. The viability of SK-N-SH cells was detected by CCK-8 assay. D SK-N-SH cells were treated with 0, 12.5, 25, 50 μM FKA for 48 h. The clone-forming ability of SK-N-SH cells was detected by colony formation assay. *** p < 0.001

Article Snippet: Human NB cell line (SK-N-SH) and human umbilical vein endothelial cells (HUVECs) purchased from iCell Bioscience (Shanghai, China) were cultured in DMEM (Gibco, CA, USA) supplemented with 10% FBS and 1% penicillin–streptomycin at 37 °C in a humidified incubator containing 5% CO 2 .

Techniques: CCK-8 Assay, Colony Assay