human bladder epithelial cells  (ATCC)

Journal: Oncology Letters

Article Title: Cytotoxic, apoptotic and genotoxic effects of thymoquinone-oxime derivative on gastric cancer cells: An in vitro study

doi: 10.3892/ol.2026.15462

Figure Lengend Snippet: Effect of TQ-ox on apoptosis in HGEpiCs and AGS cells. Statistical significance was analyzed using one-way analysis of variance with Tukey's post hoc test. **P<0.01 and ***P<0.001 vs. control. Representative fluorescence microscopy images of acridine orange/ethidium bromide-stained cells showing live (green) and apoptotic (red/orange) cells in the control and 40 µM TQ-ox treated AGS groups. A total of ~50 cells were analyzed per condition. Scale bar, 100 µm. HGEpiC, human gastric epithelial cell; TQ-ox, thymoquinone-oxime.

Article Snippet: Primary HGEpiCs were obtained from Innoprot (cat. no. P10778).

Techniques: Control, Fluorescence, Microscopy, Staining

Journal: Oncology Letters

Article Title: Cytotoxic, apoptotic and genotoxic effects of thymoquinone-oxime derivative on gastric cancer cells: An in vitro study

doi: 10.3892/ol.2026.15462

Figure Lengend Snippet: Effect of TQ-ox on DNA damage in HGEpiCs and AGS cells following 24 h of TQ-ox treatment (5–40 µM). Statistical significance was analyzed using one-way analysis of variance with Tukey's post hoc test. **P<0.01 and ***P<0.001 vs. control. Representative fluorescence microscopy images showing nuclei (control) and comet tails (40 µM TQ-ox-treated cells), indicating fragmented DNA. A total of ~50 cells were analyzed per condition. Scale bar, 200 µm. HGEpiC, human gastric epithelial cell; TQ-ox, thymoquinone-oxime.

Article Snippet: Primary HGEpiCs were obtained from Innoprot (cat. no. P10778).

Techniques: Control, Fluorescence, Microscopy

Journal: Neoplasia (New York, N.Y.)

Article Title: Multi-omics profiling reveals microenvironmental remodeling as a key driver of house dust mite-induced lung cancer progression

doi: 10.1016/j.neo.2026.101275

Figure Lengend Snippet: HDM d oes not have mutagenic effects in human and mouse lung epithelial cell lines i n v itro . A) Dose-response curves of HDM treatment in BEAS-2B and LLC cells. Cell viability is shown relative to vehicle control (PBS; % of control). Calculated IC 50 values are indicated. B) Experimental setup for HDM exposure and duplex sequencing. BEAS-2B and LLC cells were treated with either HDM (200 µg/mL for BEAS-2B; 400 µg/mL for LLC) or vehicle (VEH; PBS), expanded across multiple passages, and subsequently subjected to genomic sequencing. C) Comparison of mutational burden between samples treated with either HDM (purple) or VEH (blue), shown as somatic mutations per megabase (Mb) of coding DNA. D) Mutational spectra of BEAS-2B and LLC cells treated with HDM compared to VEH controls. Mutations are classified into the six base substitution categories and displayed in SBS96 format. The experiments were performed in triplicate (A) or singlicate (B-D).

Article Snippet: Human bronchial epithelial cells (BEAS-2B) were purchased in 2018 from ATCC (Cat. No CRL-9609).

Techniques: Control, Sequencing, Genomic Sequencing, Comparison

Journal: The Journal of Biological Chemistry

Article Title: A high-throughput screen for nucleolar function reveals a role for the signaling protein, SPRR3, in ribosome biogenesis

doi: 10.1016/j.jbc.2026.111132

Figure Lengend Snippet: siSPRR3 depletion results in a reduction in the number of nucleoli per nucleus in MCF10A cells. A , siSPRR3 depletion with siGENOME siRNAs reduces the number of nucleoli per nucleus. Images and histograms from a genome-wide screen using Dharmacon/Horizon siGENOME siRNAs . The images show nuclei (Hoechst, blue ) and nucleoli (anti-fibrillarin, red ) after 72 h of treatment with the negative control (siGFP), positive control (siUTP4), or siSPRR3 siRNAs. Histograms show the distribution of cells that have the indicated number of nucleoli per nucleus. Light grey shows the distribution for the negative control, black shows the test condition, and dark grey shows overlap of the two frequencies. B , siSPRR3 depletion with siON-TARGET (siONT) SMARTPool siRNA reduces the number of nucleoli per nucleus. The images show nuclei and nucleoli after 72 h of treatment with the negative control (non-targeting siRNA, siNT), positive control (siUTP4), or siSPRR3 siRNAs. The shading in the histograms is as in A ). The data were collected across four replicates which are pooled in the histogram. C , siSPRR3 depletion with individual siONT SMARTPool siRNAs (deconvolution) reduces the number of nucleoli per nucleus. The images show nuclei and nucleoli after 72 h of treatment with the negative control (siNT), positive control (siNOL11), or representative siSPRR3 individual siRNAs (SPRR3-si1 and SPRR3-si2). The shading in the histograms is as in ( A ). The histograms include all three replicates pooled. The table summarizes each of four individual siONT SMARTPool siRNAs, showing that a reduction in nucleolar number correlates with a loss in cell viability. D , siSPRR3 (custom subpool of SPRR3-si1 and SPRR3-si2) reduces SPRR3 mRNA levels in MCF10A cells. RT-qPCR data of SPRR3 mRNA demonstrating knockdown after 72 h. The data were normalized to 7SL RNA abundance, then to siNT for comparison using the ΔΔC T method. The mean ± SEM are shown alongside individual data points, colored by replicate. E , siSPRR3 (custom subpool of SPRR3-si1 and SPRR3-si2) reduces SPRR3 protein levels in MCF10A cells. Western blot of SPRR3 protein demonstrating decreased levels after 72 h. Protein levels were normalized to total protein (trichloroethanol total protein stain), then to siNT. The mean ± SEM are shown alongside individual data points, colored by replicate. This sample was run on the same Western blot as in . After imaging total protein on the membrane, the blot was cut between 10 to 15 kD markers to stain separately for SPRR3 ( E , above) or RPS28 . Data in ( D and E ) were analyzed by unpaired two-sided Welch's t -tests in GraphPad Prism. ∗, p < 0.05; ∗∗∗, p < 0.001.

Article Snippet: Human MCF10A breast epithelial cells (#CRL-10317, American Type Culture Collection) were cultured in DMEM/nutrient mixture F-12 (Gibco 11330032) with 5% horse serum (Gibco 16050122), 20 ng/ml epidermal growth factor (Peprotech AF1005), 0.5 μg/ml hydrocortisone (MilliporeSigma H0135), 100 ng/ml cholera toxin (MilliporeSigma C8052), and 10 μg/ml insulin (MilliporeSigma I1882).

Techniques: Genome Wide, Negative Control, Positive Control, Quantitative RT-PCR, Knockdown, Comparison, Western Blot, Staining, Imaging, Membrane

Journal: The Journal of Biological Chemistry

Article Title: A high-throughput screen for nucleolar function reveals a role for the signaling protein, SPRR3, in ribosome biogenesis

doi: 10.1016/j.jbc.2026.111132

Figure Lengend Snippet: SPRR3 depletion reduces pre-rRNA transcription. A , schematic of the major steps in ribosome biogenesis in human cells. B , SPRR3 depletion inhibits nucleolar rRNA biogenesis. Representative images and quantification of control or SPRR3-depleted MCF10A cells (siONT SMARTpool) following anti-fibrillarin (FBL) staining and 5-EU incorporation. Scale bars are 10 μm. siNT is a non-targeting negative control siRNA. siPOLR1A is a positive control targeting the RNAPI subunit, POLR1A. The overall mean percent inhibition ± SEM is shown for each treatment, with each dot representing one well. Each well in the siSPRR3 condition represents a separate day of testing and control datapoints are distributed across the three testing days. 0% inhibition is determined by the mean value of siNT, and 100% inhibition is set to the mean value of the siPOLR1A positive control. C , RT-qPCR analysis shows decreased 47S/45S pre-rRNA levels upon SPRR3 depletion in MCF10A cells. The mean ± SEM are shown alongside individual data points, colored by replicate. The data were normalized to 7SL RNA abundance, then to siNT for comparison using the ΔΔC T method. D , dual-luciferase reporter assay shows RNAPI promoter activity is reduced after SPRR3 depletion. The mean ± SEM are shown alongside individual data points, colored by replicate. The controls in these data have also been published in , without the inclusion of siSPRR3. All the data in this figure were analyzed by ordinary one-way ANOVA with multiple comparisons against siNT and Holm-Šídák correction in GraphPad Prism. ∗, p < 0.05; ∗∗, p < 0.01; ∗∗∗, p < 0.001.

Article Snippet: Human MCF10A breast epithelial cells (#CRL-10317, American Type Culture Collection) were cultured in DMEM/nutrient mixture F-12 (Gibco 11330032) with 5% horse serum (Gibco 16050122), 20 ng/ml epidermal growth factor (Peprotech AF1005), 0.5 μg/ml hydrocortisone (MilliporeSigma H0135), 100 ng/ml cholera toxin (MilliporeSigma C8052), and 10 μg/ml insulin (MilliporeSigma I1882).

Techniques: Control, Staining, Negative Control, Positive Control, Inhibition, Quantitative RT-PCR, Comparison, Luciferase, Reporter Assay, Activity Assay

Journal: The Journal of Biological Chemistry

Article Title: A high-throughput screen for nucleolar function reveals a role for the signaling protein, SPRR3, in ribosome biogenesis

doi: 10.1016/j.jbc.2026.111132

Figure Lengend Snippet: SPRR3 depletion causes reduced global translation (protein synthesis). A , representative image and quantification of puromycin incorporation shows reduced translation after SPRR3 depletion in MCF10A cells. α-puromycin shows puromycin incorporation as a proxy for global protein synthesis. Total protein is the trichloroethanol total protein stain loading control. Images were quantified with Bio-Rad Image Lab. The mean ± SEM are shown alongside individual data points, colored by replicate. siRPL4 is the positive control. Data were normalized to a non-targeting siRNA (siNT), then graphed and analyzed by ordinary one-way ANOVA with multiple comparisons against siNT and Holm-Šídák correction in GraphPad Prism. ∗∗∗, p < 0.001. The control data in this puromycin Western blot have also been published in without the SPRR3 data. B , summary table describing the effects of SPRR3 depletion on ribosome biogenesis and the nucleolus. SPRR3 depletion reduces nucleolar number, nucleolar rRNA biogenesis (5-EU incorporation assay), pre-rRNA transcript levels (RT-qPCR of 47S/45S rRNA), rDNA promoter activity (luciferase reporter assay), and global protein synthesis (puromycin incorporation assay). SPRR3 depletion was found to have no effect on the ratio of 18S to 28S rRNA nor to produce changes in pre-rRNA northern blots, indicating that SPRR3 does not affect rRNA processing. Taken together, this suggests that SPRR3 plays a role in pre-rRNA transcription and nucleolar rRNA biogenesis that is essential to the normal translational activity of ribosomes.

Article Snippet: Human MCF10A breast epithelial cells (#CRL-10317, American Type Culture Collection) were cultured in DMEM/nutrient mixture F-12 (Gibco 11330032) with 5% horse serum (Gibco 16050122), 20 ng/ml epidermal growth factor (Peprotech AF1005), 0.5 μg/ml hydrocortisone (MilliporeSigma H0135), 100 ng/ml cholera toxin (MilliporeSigma C8052), and 10 μg/ml insulin (MilliporeSigma I1882).

Techniques: Staining, Control, Positive Control, Western Blot, Quantitative RT-PCR, Activity Assay, Luciferase, Reporter Assay, Northern Blot

Journal: The Journal of Biological Chemistry

Article Title: A high-throughput screen for nucleolar function reveals a role for the signaling protein, SPRR3, in ribosome biogenesis

doi: 10.1016/j.jbc.2026.111132

Figure Lengend Snippet: SPRR3 depletion causes the nucleolar stress response in MCF10A and A549 cells. A , schematic of the nucleolar stress response in human cells. Disruption of ribosome biogenesis causes accumulation of free 5S RNP which inhibits the ubiquitin ligase MDM2, leading to accumulation of TP53 and increased transcription of CDKN1A . B , TP53 stabilization after SPRR3 depletion in MCF10A cells. Representative images and quantification of TP53 Western blots after 72h of treatment with siSPRR3. siNOL11 was used as a positive control. TP53 levels were normalized to total protein (trichloroethanol stain), then siNT. C , CDKN1A mRNA levels are elevated after SPRR3 depletion in MCF10A cells. After 72 h of siSPRR3 treatment, CDKN1A mRNA transcript levels were detected with RT-qPCR using primers for CDKN1A mRNA. siNOL11 was used as a positive control. These data were normalized to 7SL RNA abundance, then to siNT for comparison using the ΔΔC T method. D , siSPRR3 reduces SPRR3 mRNA levels in A549 cells. After 72 h of siSPRR3 treatment, SPRR3 transcript levels were detected by RT-qPCR. The data were normalized as in ( C ). E , siSPRR3 reduces SPRR3 protein levels in A549 cells. After 72 h of treatment with siSPRR3, SPRR3 protein levels were detected by Western blot. SPRR3 levels were normalized as in ( B ). F , SPRR3 depletion lowers 47S/45S pre-rRNA levels in A549 cells. Primers to the 5′ ETS of the 47S/45S rRNA were used to detect pre-rRNA levels after 72h of treatment with siSPRR3. siNOL11 was used as a positive control. The data were normalized as in ( C and D ). G , TP53 stabilization after SPRR3 knockdown in A549 cells. Representative images and quantification of TP53 Western blots after 48h or 72h of treatment with siSPRR3 are shown. Protein levels were normalized as in ( B and E ). H , CDKN1A levels are elevated after SPRR3 depletion in A549 cells. After 72 h of treatment with siSPRR3, CDKN1A transcript levels were detected with RT-qPCR using primers for CDKN1A mRNA. siNOL11 was used as a positive control. Data were normalized as in ( C ). The mean ± SEM are shown alongside individual data points. For graphs with two conditions, data were analyzed by unpaired two-sided Welch's t -tests in GraphPad Prism. For graphs with more than two conditions, data were analyzed by ordinary one-way ANOVA with multiple comparisons against siNT and Holm-Šídák correction in GraphPad Prism. ∗, p < 0.05; ∗∗, p < 0.01; ∗∗∗, p < 0.001.

Article Snippet: Human MCF10A breast epithelial cells (#CRL-10317, American Type Culture Collection) were cultured in DMEM/nutrient mixture F-12 (Gibco 11330032) with 5% horse serum (Gibco 16050122), 20 ng/ml epidermal growth factor (Peprotech AF1005), 0.5 μg/ml hydrocortisone (MilliporeSigma H0135), 100 ng/ml cholera toxin (MilliporeSigma C8052), and 10 μg/ml insulin (MilliporeSigma I1882).

Techniques: Disruption, Ubiquitin Proteomics, Western Blot, Positive Control, Staining, Quantitative RT-PCR, Comparison, Knockdown

Journal: The Journal of Biological Chemistry

Article Title: A high-throughput screen for nucleolar function reveals a role for the signaling protein, SPRR3, in ribosome biogenesis

doi: 10.1016/j.jbc.2026.111132

Figure Lengend Snippet: SPRR3 drives AKT phosphorylation and maintains POLR1A levels. A , AKT phosphorylation at serine 473 (pAKT) is decreased after a 72h SPRR3 depletion in MCF10A cells. Representative images and quantification are shown for pAKT, total AKT, and total protein (measured by trichloroethanol stain). Blots were probed for pAKT, then stripped and re-probed for total AKT. Signal was measured in Bio-Rad Image Lab. pAKT levels were normalized to total protein and total AKT. Total AKT was normalized to total protein, ensuring no significant difference in overall AKT levels upon SPRR3 depletion. B , phosphorylated AKT (pAKT) levels are decreased after 72h SPRR3 depletion in A549 cells. Representative images and quantification are shown for pAKT, total AKT, and total protein (measured by trichloroethanol stain). C , POLR1A levels are decreased upon 72h SPRR3 depletion. Representative image of Western blotting and quantification of POLR1A levels in MCF10A cells. siPOLR1A was used as a positive control. D , summary of effects of siSPRR3 depletion that we have confirmed in both MCF10A cells and A549 cells. For all graphs in this figure, the mean ± SEM are shown alongside individual data points. Data were analyzed by unpaired two-sided Welch's t -tests in GraphPad Prism. ∗, p < 0.05; ∗∗, p < 0.01; ∗∗∗, p < 0.001; ns, not significant.

Article Snippet: Human MCF10A breast epithelial cells (#CRL-10317, American Type Culture Collection) were cultured in DMEM/nutrient mixture F-12 (Gibco 11330032) with 5% horse serum (Gibco 16050122), 20 ng/ml epidermal growth factor (Peprotech AF1005), 0.5 μg/ml hydrocortisone (MilliporeSigma H0135), 100 ng/ml cholera toxin (MilliporeSigma C8052), and 10 μg/ml insulin (MilliporeSigma I1882).

Techniques: Phospho-proteomics, Staining, Western Blot, Positive Control

Journal: Physiological Reports

Article Title: Effects of cAMP and CFTR modulation on apical fluid pH in human airway Calu‐3 cells

doi: 10.14814/phy2.70747

Figure Lengend Snippet: Concentration‐response analysis of cAMP elevating agents on apical fluid pH. Human airway epithelial (Calu‐3) cells were exposed to cAMP elevating agent (a and b) forskolin and (c and d) isoproterenol in the basolateral (bottom) compartment for 3 h at various concentrations. (a and c) A dose–response curve for measured apical fluid pH is depicted and (b and d) comparisons between treatment groups were performed. Data presented as means ± SD ( n = 4–5, FSK; n = 5, ISO). A one‐way ANOVA with subsequent multiple comparisons was used for statistical analysis. **** p ≤ 0.0001.

Article Snippet: The human airway epithelial cell line Calu‐3 (male, age 25) (ATCC, HTB‐55), derived from lung adenocarcinoma tissue, was cultured in Alpha‐Minimum Essential medium (α‐MEM) (Corning, 10‐022‐CV) supplemented with 10% fetal bovine serum (VWR, 080‐450), 1% HEPES (Corning, 25‐060‐CI), and 1% penicillin–streptomycin (VWR, 97063‐708) at 37°C and 5% CO 2 for both submerged and air‐liquid interface (ALI) culture conditions.

Techniques: Concentration Assay

Journal: Physiological Reports

Article Title: Effects of cAMP and CFTR modulation on apical fluid pH in human airway Calu‐3 cells

doi: 10.14814/phy2.70747

Figure Lengend Snippet: Control experiment in Ringer's solution to validate drug‐induced pH changes in the absence of cells. Various combinations of cAMP elevating agents forskolin (0.1 μM) and isoproterenol (0.01 μM), CFTR potentiator VX‐770 (1 μM), PDE‐4 inhibitor roflumilast (1 μM), and ABCC4 inhibitor MK‐571 (10 μM) were administered to the basolateral (bottom) compartment for 3 h to evaluate the change in pH in the absence of human airway epithelial (Calu‐3) cells. Data presented as means ± SD ( n = 3). A one‐way ANOVA with subsequent multiple comparisons was used for statistical analysis.

Article Snippet: The human airway epithelial cell line Calu‐3 (male, age 25) (ATCC, HTB‐55), derived from lung adenocarcinoma tissue, was cultured in Alpha‐Minimum Essential medium (α‐MEM) (Corning, 10‐022‐CV) supplemented with 10% fetal bovine serum (VWR, 080‐450), 1% HEPES (Corning, 25‐060‐CI), and 1% penicillin–streptomycin (VWR, 97063‐708) at 37°C and 5% CO 2 for both submerged and air‐liquid interface (ALI) culture conditions.

Techniques: Control

Journal: Physiological Reports

Article Title: Effects of cAMP and CFTR modulation on apical fluid pH in human airway Calu‐3 cells

doi: 10.14814/phy2.70747

Figure Lengend Snippet: Effect of various pharmacological interventions on apical fluid pH. Human airway epithelial (Calu‐3) cells were exposed to various combinations of cAMP elevating agents forskolin (0.1 μM) and isoproterenol (0.01 μM), CFTR potentiator VX‐770 (1 μM), PDE‐4 inhibitor roflumilast (1 μM), and ABCC4 inhibitor MK‐571 (10 μM) to the basolateral (bottom) compartment for 3 h. Measured apical fluid pH is depicted and comparisons between treatment groups were performed. Data presented as means ± SD ( n = 7). A two‐way ANOVA with subsequent multiple comparisons was used for statistical analysis. **** p ≤ 0.0001; #### p ≤ 0.0001.

Article Snippet: The human airway epithelial cell line Calu‐3 (male, age 25) (ATCC, HTB‐55), derived from lung adenocarcinoma tissue, was cultured in Alpha‐Minimum Essential medium (α‐MEM) (Corning, 10‐022‐CV) supplemented with 10% fetal bovine serum (VWR, 080‐450), 1% HEPES (Corning, 25‐060‐CI), and 1% penicillin–streptomycin (VWR, 97063‐708) at 37°C and 5% CO 2 for both submerged and air‐liquid interface (ALI) culture conditions.

Techniques:

Journal: Physiological Reports

Article Title: Effects of cAMP and CFTR modulation on apical fluid pH in human airway Calu‐3 cells

doi: 10.14814/phy2.70747

Figure Lengend Snippet: CFTR inhibitors administered in the apical or basolateral compartment do not impact apical fluid pH. Human airway epithelial (Calu‐3) cells were exposed to CFTR inhibitors (a and c) CFTRinh‐172 and (b and d) GlyH‐101 in the apical (a and b, top) or basolateral (c and d, bottom) compartment for 3 h at various concentrations. cAMP elevating agent forskolin (0.1 μM) was used as a positive control and comparisons between treatment groups were performed. Data presented as means ± SD ( n = 5). A one‐way ANOVA with subsequent multiple comparisons was used for statistical analysis.

Article Snippet: The human airway epithelial cell line Calu‐3 (male, age 25) (ATCC, HTB‐55), derived from lung adenocarcinoma tissue, was cultured in Alpha‐Minimum Essential medium (α‐MEM) (Corning, 10‐022‐CV) supplemented with 10% fetal bovine serum (VWR, 080‐450), 1% HEPES (Corning, 25‐060‐CI), and 1% penicillin–streptomycin (VWR, 97063‐708) at 37°C and 5% CO 2 for both submerged and air‐liquid interface (ALI) culture conditions.

Techniques: Positive Control

Journal: Physiological Reports

Article Title: Effects of cAMP and CFTR modulation on apical fluid pH in human airway Calu‐3 cells

doi: 10.14814/phy2.70747

Figure Lengend Snippet: Effect of cAMP elevating agents FSK and ISO post‐CFTR inhibition on apical fluid pH. Human airway epithelial (Calu‐3) cells were pre‐treated with CFTR inhibitors (a) CFTRinh‐172 (10 μM) and (b) GlyH‐101 (10 μM) to the apical (top) compartment for 30 min prior to treatment with cAMP elevating agents forskolin (0.1 μM) and isoproterenol (0.01 μM) to the basolateral (bottom) compartment for 3 h. Measured apical fluid pH is depicted and comparisons between treatment groups were performed. Data presented as means ± SD ( n = 4). A one‐way ANOVA with subsequent multiple comparisons was used for statistical analysis.

Article Snippet: The human airway epithelial cell line Calu‐3 (male, age 25) (ATCC, HTB‐55), derived from lung adenocarcinoma tissue, was cultured in Alpha‐Minimum Essential medium (α‐MEM) (Corning, 10‐022‐CV) supplemented with 10% fetal bovine serum (VWR, 080‐450), 1% HEPES (Corning, 25‐060‐CI), and 1% penicillin–streptomycin (VWR, 97063‐708) at 37°C and 5% CO 2 for both submerged and air‐liquid interface (ALI) culture conditions.

Techniques: Inhibition

Journal: Physiological Reports

Article Title: Effects of cAMP and CFTR modulation on apical fluid pH in human airway Calu‐3 cells

doi: 10.14814/phy2.70747

Figure Lengend Snippet: Effect of CFTR potentiator VX‐770 post‐CFTR inhibition on apical fluid pH. Human airway epithelial (Calu‐3) cells were pre‐treated with CFTR inhibitors (a) CFTRinh‐172 (10 μM) and (b) GlyH‐101 (10 μM) to the apical (top) compartment for 30 min prior to treatment with CFTR potentiator VX‐770 (1 μM) to the basolateral (bottom) compartment for 3 h. Measured apical fluid pH is depicted and comparisons between treatment groups were performed. Data presented as means ± SD ( n = 4). A one‐way ANOVA with subsequent multiple comparisons was used for statistical analysis.

Article Snippet: The human airway epithelial cell line Calu‐3 (male, age 25) (ATCC, HTB‐55), derived from lung adenocarcinoma tissue, was cultured in Alpha‐Minimum Essential medium (α‐MEM) (Corning, 10‐022‐CV) supplemented with 10% fetal bovine serum (VWR, 080‐450), 1% HEPES (Corning, 25‐060‐CI), and 1% penicillin–streptomycin (VWR, 97063‐708) at 37°C and 5% CO 2 for both submerged and air‐liquid interface (ALI) culture conditions.

Techniques: Inhibition