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ATCC mcf10a wildtype cells

(A) Schematic of the spheroid morphogenesis assay. Single <t>MCF10A/HRAS</t> or MCF10A wild-type cells were cultured in a collagen IV/laminin-rich EHS(Engelbreth-Holm-Swarm) hydrogel to generate basoapically polarized spheroids after 10 days in culture (DiC). (B) Representative immunofluorescence micrographs show differences in basoapical polarization of MCF10A spheroids at 10 DiC depending on HRas activation status. BM (collagen IV, yellow), F-actin cytoskeleton (magenta), nuclei (DAPI, blue) and Golgi protein (GM130, green). (C) HRas activation confirmed by pERK immunofluorescence after 1 hour OHT or EtOH treatment. Representative immunofluorescence intensities of intracellular pERK protein (inverted grey scale) in MCF10A/HRAS spheroids treated with OHT or EtOH for 16 hours. SAC: secondary antibody control. Right, quantification of mean pERK intensity per spheroid (n ≥ 44; 3 independent experiments). Box: interquartile range; whiskers: 5th–95th percentiles; red dots: median. (D) Phase-contrast images show the invasive transition of spheroids (10 DiC) with cell transmigration into the EHS matrix after 65 hours of HRas activation with OHT. EtOH-treated HRas off controls remained non-invasive. Kolmogorov-Smirnov test was performed for the data in C; n.s.: p > 0.05; ****: p ≤ 0.0001. Scale bars: 20 µm (B); 50 μm (C). Position of focal plane used for imaging and analyses is indicated by red bar.

Mcf10a Wildtype Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 8014 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Oncogenic Ras-Src-cortactin signaling rewires actin-generated forces to drive basement membrane rupture and initiate breast cancer invasion"

Article Title: Oncogenic Ras-Src-cortactin signaling rewires actin-generated forces to drive basement membrane rupture and initiate breast cancer invasion

Journal: bioRxiv

doi: 10.64898/2026.04.15.717430

(A) Schematic of the spheroid morphogenesis assay. Single MCF10A/HRAS or MCF10A wild-type cells were cultured in a collagen IV/laminin-rich EHS(Engelbreth-Holm-Swarm) hydrogel to generate basoapically polarized spheroids after 10 days in culture (DiC). (B) Representative immunofluorescence micrographs show differences in basoapical polarization of MCF10A spheroids at 10 DiC depending on HRas activation status. BM (collagen IV, yellow), F-actin cytoskeleton (magenta), nuclei (DAPI, blue) and Golgi protein (GM130, green). (C) HRas activation confirmed by pERK immunofluorescence after 1 hour OHT or EtOH treatment. Representative immunofluorescence intensities of intracellular pERK protein (inverted grey scale) in MCF10A/HRAS spheroids treated with OHT or EtOH for 16 hours. SAC: secondary antibody control. Right, quantification of mean pERK intensity per spheroid (n ≥ 44; 3 independent experiments). Box: interquartile range; whiskers: 5th–95th percentiles; red dots: median. (D) Phase-contrast images show the invasive transition of spheroids (10 DiC) with cell transmigration into the EHS matrix after 65 hours of HRas activation with OHT. EtOH-treated HRas off controls remained non-invasive. Kolmogorov-Smirnov test was performed for the data in C; n.s.: p > 0.05; ****: p ≤ 0.0001. Scale bars: 20 µm (B); 50 μm (C). Position of focal plane used for imaging and analyses is indicated by red bar.

Figure Legend Snippet: (A) Schematic of the spheroid morphogenesis assay. Single MCF10A/HRAS or MCF10A wild-type cells were cultured in a collagen IV/laminin-rich EHS(Engelbreth-Holm-Swarm) hydrogel to generate basoapically polarized spheroids after 10 days in culture (DiC). (B) Representative immunofluorescence micrographs show differences in basoapical polarization of MCF10A spheroids at 10 DiC depending on HRas activation status. BM (collagen IV, yellow), F-actin cytoskeleton (magenta), nuclei (DAPI, blue) and Golgi protein (GM130, green). (C) HRas activation confirmed by pERK immunofluorescence after 1 hour OHT or EtOH treatment. Representative immunofluorescence intensities of intracellular pERK protein (inverted grey scale) in MCF10A/HRAS spheroids treated with OHT or EtOH for 16 hours. SAC: secondary antibody control. Right, quantification of mean pERK intensity per spheroid (n ≥ 44; 3 independent experiments). Box: interquartile range; whiskers: 5th–95th percentiles; red dots: median. (D) Phase-contrast images show the invasive transition of spheroids (10 DiC) with cell transmigration into the EHS matrix after 65 hours of HRas activation with OHT. EtOH-treated HRas off controls remained non-invasive. Kolmogorov-Smirnov test was performed for the data in C; n.s.: p > 0.05; ****: p ≤ 0.0001. Scale bars: 20 µm (B); 50 μm (C). Position of focal plane used for imaging and analyses is indicated by red bar.

Techniques Used: Cell Culture, Immunofluorescence, Activation Assay, Control, Transmigration Assay, Imaging

(A) Scheme of BM disruption and cell invasion assay. MCF10A/HRAS spheroids (10 DiC) were isolated from EHS matrix and placed on elastomeric substrates (16 kPa, functionalized with EHS proteins) to count events of local BM rupture and cell transmigration. Mechanical BM stress exertion by breast spheroids at time point of invasion onset was measured by traction force microscopy (TFM): Surface-coupled fluorescent fiducial microbeads were used to track tangential surface deformations from which strain energies were calculated as measure for cell force-generated BM stress. (B) In spheroids, the outer basal cell layer is covered by a BM which itself is in contact to the underlying substrate. Images show the BM integrity of a representative HRas on sample, fixed and stained after adhering (1 hour) to the elastomeric substrate. Collagen IV (yellow), laminin-332 (cyan) and F-actin cytoskeleton (magenta). Zoom in highlights in vivo -like layering of the endogenous BM. (C) Representative sequence of phase-contrast images illustrates the first appearance of protrusive cell bodies (also shown as zoom in), marking onset of BM disruption and cell transmigration. This was counted as a positive event of invasion. (D) Cumulative distribution of BM disruption time, depending on HRas induction on 16 kPa substrates (n ≥ 79 spheroids of ≥ 3 independent experiments). (E) Cumulative distribution of BM disruption time in spheroids treated with blebbistatin for myosin II inhibition and additionally with marimastat for MMP inhibition after HRas induction on stiff 16 kPa substrates (n ≥ 69 spheroids of ≥ 3 independent experiments). (F) Scatter plot shows individual invasion onset time points for the sample conditions analyzed in (D and E) (median and 95% confidence interval (CI)). (G) Calculated strain energies (SE) exerted by individual spheroids at onsets of BM disruption, depending on HRas activation and actomyosin inhibition, (cf. D and E). Representative maps of cell-induced traction stresses per condition from which SE were calculated. Scatter plot: median with 95% CI (n ≥ 48 from 3 independent experiments). Kruskal-Wallis test with Dunn’s multiple comparison test was performed for the data in D and E; n.s.: p > 0.05; *: p ≤ 0.05; **: p ≤ 0.01; ***: p ≤ 0.001; ****: p ≤ 0.0001. Scale bars: 20 µm (B, C and G).

Figure Legend Snippet: (A) Scheme of BM disruption and cell invasion assay. MCF10A/HRAS spheroids (10 DiC) were isolated from EHS matrix and placed on elastomeric substrates (16 kPa, functionalized with EHS proteins) to count events of local BM rupture and cell transmigration. Mechanical BM stress exertion by breast spheroids at time point of invasion onset was measured by traction force microscopy (TFM): Surface-coupled fluorescent fiducial microbeads were used to track tangential surface deformations from which strain energies were calculated as measure for cell force-generated BM stress. (B) In spheroids, the outer basal cell layer is covered by a BM which itself is in contact to the underlying substrate. Images show the BM integrity of a representative HRas on sample, fixed and stained after adhering (1 hour) to the elastomeric substrate. Collagen IV (yellow), laminin-332 (cyan) and F-actin cytoskeleton (magenta). Zoom in highlights in vivo -like layering of the endogenous BM. (C) Representative sequence of phase-contrast images illustrates the first appearance of protrusive cell bodies (also shown as zoom in), marking onset of BM disruption and cell transmigration. This was counted as a positive event of invasion. (D) Cumulative distribution of BM disruption time, depending on HRas induction on 16 kPa substrates (n ≥ 79 spheroids of ≥ 3 independent experiments). (E) Cumulative distribution of BM disruption time in spheroids treated with blebbistatin for myosin II inhibition and additionally with marimastat for MMP inhibition after HRas induction on stiff 16 kPa substrates (n ≥ 69 spheroids of ≥ 3 independent experiments). (F) Scatter plot shows individual invasion onset time points for the sample conditions analyzed in (D and E) (median and 95% confidence interval (CI)). (G) Calculated strain energies (SE) exerted by individual spheroids at onsets of BM disruption, depending on HRas activation and actomyosin inhibition, (cf. D and E). Representative maps of cell-induced traction stresses per condition from which SE were calculated. Scatter plot: median with 95% CI (n ≥ 48 from 3 independent experiments). Kruskal-Wallis test with Dunn’s multiple comparison test was performed for the data in D and E; n.s.: p > 0.05; *: p ≤ 0.05; **: p ≤ 0.01; ***: p ≤ 0.001; ****: p ≤ 0.0001. Scale bars: 20 µm (B, C and G).

Techniques Used: Disruption, Invasion Assay, Isolation, Transmigration Assay, Microscopy, Generated, Staining, In Vivo, Sequencing, Inhibition, Activation Assay, Comparison

(A) Representative images of MT1-MMP (inversed grey scale) staining of MCF10A/HRas spheroids incubated with 1 µM OHT or EtOH (HRas off control) for 16 hours, and the secondary antibody control (SAC) to measure unspecific background signals. (B) Quantification of fluorescence intensities of MT1-MMP staining (n = 60 and n = 30 for SAC from three and two individual staining experiments, respectively). Scatter plot includes median and 95% CI. Mann-Whitney-U-test was performed for the data (n.s.: p > 0.05). Scale bars: 20 µm. Position of focal plane used for imaging and analyses is indicated by red bar.

Figure Legend Snippet: (A) Representative images of MT1-MMP (inversed grey scale) staining of MCF10A/HRas spheroids incubated with 1 µM OHT or EtOH (HRas off control) for 16 hours, and the secondary antibody control (SAC) to measure unspecific background signals. (B) Quantification of fluorescence intensities of MT1-MMP staining (n = 60 and n = 30 for SAC from three and two individual staining experiments, respectively). Scatter plot includes median and 95% CI. Mann-Whitney-U-test was performed for the data (n.s.: p > 0.05). Scale bars: 20 µm. Position of focal plane used for imaging and analyses is indicated by red bar.

Techniques Used: Staining, Incubation, Control, Fluorescence, MANN-WHITNEY, Imaging

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Journal: bioRxiv

Article Title: Oncogenic Ras-Src-cortactin signaling rewires actin-generated forces to drive basement membrane rupture and initiate breast cancer invasion

doi: 10.64898/2026.04.15.717430

Figure Lengend Snippet: (A) Schematic of the spheroid morphogenesis assay. Single MCF10A/HRAS or MCF10A wild-type cells were cultured in a collagen IV/laminin-rich EHS(Engelbreth-Holm-Swarm) hydrogel to generate basoapically polarized spheroids after 10 days in culture (DiC). (B) Representative immunofluorescence micrographs show differences in basoapical polarization of MCF10A spheroids at 10 DiC depending on HRas activation status. BM (collagen IV, yellow), F-actin cytoskeleton (magenta), nuclei (DAPI, blue) and Golgi protein (GM130, green). (C) HRas activation confirmed by pERK immunofluorescence after 1 hour OHT or EtOH treatment. Representative immunofluorescence intensities of intracellular pERK protein (inverted grey scale) in MCF10A/HRAS spheroids treated with OHT or EtOH for 16 hours. SAC: secondary antibody control. Right, quantification of mean pERK intensity per spheroid (n ≥ 44; 3 independent experiments). Box: interquartile range; whiskers: 5th–95th percentiles; red dots: median. (D) Phase-contrast images show the invasive transition of spheroids (10 DiC) with cell transmigration into the EHS matrix after 65 hours of HRas activation with OHT. EtOH-treated HRas off controls remained non-invasive. Kolmogorov-Smirnov test was performed for the data in C; n.s.: p > 0.05; ****: p ≤ 0.0001. Scale bars: 20 µm (B); 50 μm (C). Position of focal plane used for imaging and analyses is indicated by red bar.

Article Snippet: MCF10A wildtype cells (purchased from ATCC), MCF10A_ER:HRas G12V and MCF10A_HRas G12V cells described in and kindly provided by Buzz Baum were maintained in culture dishes under standard culture conditions (37 °C, 5% CO 2 ) in DMEM/F12 growth medium (ThermoFisher Scientific) containing 5% horse serum (ThermoFisher Scientific) or steroid hormone free horse serum (c.c.pro) (in all experiments from onwards), 0.5 μg/mL hydrocortisone, 100 ng/mL cholera toxin, 20 ng/mL EGF, 10 μg/mL insulin (all Sigma Aldrich), 100 U/mL penicillin and 100 μg/mL streptomycin (both ThermoFisher Scientific).

Techniques: Cell Culture, Immunofluorescence, Activation Assay, Control, Transmigration Assay, Imaging

Journal: bioRxiv

Article Title: Oncogenic Ras-Src-cortactin signaling rewires actin-generated forces to drive basement membrane rupture and initiate breast cancer invasion

doi: 10.64898/2026.04.15.717430

Figure Lengend Snippet: (A) Scheme of BM disruption and cell invasion assay. MCF10A/HRAS spheroids (10 DiC) were isolated from EHS matrix and placed on elastomeric substrates (16 kPa, functionalized with EHS proteins) to count events of local BM rupture and cell transmigration. Mechanical BM stress exertion by breast spheroids at time point of invasion onset was measured by traction force microscopy (TFM): Surface-coupled fluorescent fiducial microbeads were used to track tangential surface deformations from which strain energies were calculated as measure for cell force-generated BM stress. (B) In spheroids, the outer basal cell layer is covered by a BM which itself is in contact to the underlying substrate. Images show the BM integrity of a representative HRas on sample, fixed and stained after adhering (1 hour) to the elastomeric substrate. Collagen IV (yellow), laminin-332 (cyan) and F-actin cytoskeleton (magenta). Zoom in highlights in vivo -like layering of the endogenous BM. (C) Representative sequence of phase-contrast images illustrates the first appearance of protrusive cell bodies (also shown as zoom in), marking onset of BM disruption and cell transmigration. This was counted as a positive event of invasion. (D) Cumulative distribution of BM disruption time, depending on HRas induction on 16 kPa substrates (n ≥ 79 spheroids of ≥ 3 independent experiments). (E) Cumulative distribution of BM disruption time in spheroids treated with blebbistatin for myosin II inhibition and additionally with marimastat for MMP inhibition after HRas induction on stiff 16 kPa substrates (n ≥ 69 spheroids of ≥ 3 independent experiments). (F) Scatter plot shows individual invasion onset time points for the sample conditions analyzed in (D and E) (median and 95% confidence interval (CI)). (G) Calculated strain energies (SE) exerted by individual spheroids at onsets of BM disruption, depending on HRas activation and actomyosin inhibition, (cf. D and E). Representative maps of cell-induced traction stresses per condition from which SE were calculated. Scatter plot: median with 95% CI (n ≥ 48 from 3 independent experiments). Kruskal-Wallis test with Dunn’s multiple comparison test was performed for the data in D and E; n.s.: p > 0.05; *: p ≤ 0.05; **: p ≤ 0.01; ***: p ≤ 0.001; ****: p ≤ 0.0001. Scale bars: 20 µm (B, C and G).

Techniques: Disruption, Invasion Assay, Isolation, Transmigration Assay, Microscopy, Generated, Staining, In Vivo, Sequencing, Inhibition, Activation Assay, Comparison

Journal: bioRxiv

Article Title: Oncogenic Ras-Src-cortactin signaling rewires actin-generated forces to drive basement membrane rupture and initiate breast cancer invasion

doi: 10.64898/2026.04.15.717430

Figure Lengend Snippet: (A) Representative images of MT1-MMP (inversed grey scale) staining of MCF10A/HRas spheroids incubated with 1 µM OHT or EtOH (HRas off control) for 16 hours, and the secondary antibody control (SAC) to measure unspecific background signals. (B) Quantification of fluorescence intensities of MT1-MMP staining (n = 60 and n = 30 for SAC from three and two individual staining experiments, respectively). Scatter plot includes median and 95% CI. Mann-Whitney-U-test was performed for the data (n.s.: p > 0.05). Scale bars: 20 µm. Position of focal plane used for imaging and analyses is indicated by red bar.

Techniques: Staining, Incubation, Control, Fluorescence, MANN-WHITNEY, Imaging

(A) Background-corrected FRET ratio traces for MCF10A cells expressing NLS-ZapCV2. Addition of ZnCl 2 for 30 min results in an increase in labile Zn 2+ from 150 pM to 75 nM. Addition of the Zn 2+ chelator TPA followed by the addition of Zn 2+ and pyrithione at 75 min allows for calibration of the sensor and subsequent quantification of labile Zn 2+ . (B) Quantification of Zn 2+ at rest and at the time point of ATAC-seq. (C) Pseudo-colored ratio images of representative cells at the indicated points. (D) FRET ratio traces of MCF10A cells treated with TPA to deplete labile Zn 2+ , followed by calibration. (E) Quantification of Zn 2+ at rest. The asterisk indicates that Zn 2+ cannot be accurately quantified because it is at the lower detection limit of the sensor. Zn 2+ is estimated to be ∼1 pM. (F) Pseudo-colored ratio images of representative cells at the indicated points. Each trace represents a single cell in the field of view. Lookup table values refer to the FRET ratio (background-corrected FRET channel/background-corrected CFP channel). Scale bar = 20 μm.

Journal: Life Science Alliance

Article Title: Cellular zinc status alters chromatin accessibility and binding of p53 to DNA

doi: 10.26508/lsa.202402638

Figure Lengend Snippet: (A) Background-corrected FRET ratio traces for MCF10A cells expressing NLS-ZapCV2. Addition of ZnCl 2 for 30 min results in an increase in labile Zn 2+ from 150 pM to 75 nM. Addition of the Zn 2+ chelator TPA followed by the addition of Zn 2+ and pyrithione at 75 min allows for calibration of the sensor and subsequent quantification of labile Zn 2+ . (B) Quantification of Zn 2+ at rest and at the time point of ATAC-seq. (C) Pseudo-colored ratio images of representative cells at the indicated points. (D) FRET ratio traces of MCF10A cells treated with TPA to deplete labile Zn 2+ , followed by calibration. (E) Quantification of Zn 2+ at rest. The asterisk indicates that Zn 2+ cannot be accurately quantified because it is at the lower detection limit of the sensor. Zn 2+ is estimated to be ∼1 pM. (F) Pseudo-colored ratio images of representative cells at the indicated points. Each trace represents a single cell in the field of view. Lookup table values refer to the FRET ratio (background-corrected FRET channel/background-corrected CFP channel). Scale bar = 20 μm.

Article Snippet: Wildtype MCF10A cells (#CRL-10317; ATCC) were cultured at 5% CO 2 in DMEM/F12 (#11320033; Thermo Fisher Scientific) supplemented with 5% Horse Serum (#16050122; Thermo Fisher Scientific), 1% penicillin/streptomycin (#15070063; Thermo Fisher Scientific), 20 ng/ml EGF (#PHG0313; Thermo Fisher Scientific), 0.5 mg/ml hydrocortisone (#H0888; Sigma-Aldrich), 100 ng/ml Cholera toxin (#C8052; Sigma-Aldrich, and 10 μg/ml insulin (#12585014; Thermo Fisher Scientific).

Techniques: Expressing

(A) Barcode plots that show enrichment of the p 53 motif upon treatment of MCF10A cells with TPA (top). Addition of exogenous ZnCl 2 results in depletion of the same motif (bottom). The barcode plots represent each quartile (Q1–Q4) of the enrichment curves generated for the p53 motif. Red indicates more enrichment of the motif; yellow is less enrichment of the motif. (B) A subset of p53 binding sites from a ChIP-seq dataset ( GSM3378513 ) are differentially accessible depending on cellular Zn 2+ status. ATAC-seq reads were mapped to 2,164 ChIP-seq peaks and subjected to differential accessibility analysis using DESeq2. With TPA treatment, 62 peaks showed significant ( P adj ≤ 0.1) changes in accessibility (51 decreased, 11 increased). With ZnCl 2 treatment, seven peaks showed significant changes in accessibility (one increased, five decreased). Source data are available for this figure.

Journal: Life Science Alliance

Article Title: Cellular zinc status alters chromatin accessibility and binding of p53 to DNA

doi: 10.26508/lsa.202402638

Figure Lengend Snippet: (A) Barcode plots that show enrichment of the p 53 motif upon treatment of MCF10A cells with TPA (top). Addition of exogenous ZnCl 2 results in depletion of the same motif (bottom). The barcode plots represent each quartile (Q1–Q4) of the enrichment curves generated for the p53 motif. Red indicates more enrichment of the motif; yellow is less enrichment of the motif. (B) A subset of p53 binding sites from a ChIP-seq dataset ( GSM3378513 ) are differentially accessible depending on cellular Zn 2+ status. ATAC-seq reads were mapped to 2,164 ChIP-seq peaks and subjected to differential accessibility analysis using DESeq2. With TPA treatment, 62 peaks showed significant ( P adj ≤ 0.1) changes in accessibility (51 decreased, 11 increased). With ZnCl 2 treatment, seven peaks showed significant changes in accessibility (one increased, five decreased). Source data are available for this figure.

Techniques: Generated, Binding Assay, ChIP-sequencing

Also shown are the PRO-seq coverage tracks for MCF10A cells treated with 10 μM Nutlin-3A for 3 h ( GSE227931 ), the annotated region from the GSM3378513 p53 Nutlin-3A ChIP-seq dataset, and the predicted amplicon from ChIP-qPCR. (A, B, C, D, E, F) Coverage tracks as noted above for the (A) ERGIC1, (B) NFIB, (C) SFN, (D) EGR1, (E) PLD5, and (F) LRIG3-DT regions.

Journal: Life Science Alliance

Article Title: Cellular zinc status alters chromatin accessibility and binding of p53 to DNA

doi: 10.26508/lsa.202402638

Figure Lengend Snippet: Also shown are the PRO-seq coverage tracks for MCF10A cells treated with 10 μM Nutlin-3A for 3 h ( GSE227931 ), the annotated region from the GSM3378513 p53 Nutlin-3A ChIP-seq dataset, and the predicted amplicon from ChIP-qPCR. (A, B, C, D, E, F) Coverage tracks as noted above for the (A) ERGIC1, (B) NFIB, (C) SFN, (D) EGR1, (E) PLD5, and (F) LRIG3-DT regions.

Techniques: ChIP-sequencing, Amplification, ChIP-qPCR

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