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ATCC t24 human bladder cancer cells

Betulinic acid (BA) enhances tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL)-mediated cytotoxicity in <t>T24</t> human bladder cancer cells. T24 cells were treated with the indicated concentrations of BA and TRAIL alone or in combination for 24 h. (A, B) After treatment, cell viability was assessed via 3′-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay. (C) Morphological changes in the cells treated with BA and TRAIL alone or in combination were observed under an inverted microscope. (D, E) After 4′,6-diamidino-2-phenylindole (DAPI) staining, nuclear morphological changes were observed under a fluorescence microscope (D), and the frequency of cells with chromatin condensation and fragmentation was determined (E). (F, G) Flow cytometry was performed after propidium iodide (PI) staining. Representative histograms (F) and the frequency of cells in the sub-G1 phase (G) are shown. * p <0.05, ** p <0.01, and *** p <0.001 vs. control cells; ### p <0.001 vs. BA-treated cells (n=3).

T24 Human Bladder Cancer Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 98/100, based on 2678 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Combination Therapy with Betulinic Acid and TRAIL Increases ROS-Dependent Cytotoxicity and Inhibits PI3K/Akt Signaling in Human Bladder Cancer Cells"

Article Title: Combination Therapy with Betulinic Acid and TRAIL Increases ROS-Dependent Cytotoxicity and Inhibits PI3K/Akt Signaling in Human Bladder Cancer Cells

Journal: Biomolecules & Therapeutics

doi: 10.4062/biomolther.2026.035

Betulinic acid (BA) enhances tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL)-mediated cytotoxicity in T24 human bladder cancer cells. T24 cells were treated with the indicated concentrations of BA and TRAIL alone or in combination for 24 h. (A, B) After treatment, cell viability was assessed via 3′-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay. (C) Morphological changes in the cells treated with BA and TRAIL alone or in combination were observed under an inverted microscope. (D, E) After 4′,6-diamidino-2-phenylindole (DAPI) staining, nuclear morphological changes were observed under a fluorescence microscope (D), and the frequency of cells with chromatin condensation and fragmentation was determined (E). (F, G) Flow cytometry was performed after propidium iodide (PI) staining. Representative histograms (F) and the frequency of cells in the sub-G1 phase (G) are shown. * p <0.05, ** p <0.01, and *** p <0.001 vs. control cells; ### p <0.001 vs. BA-treated cells (n=3).

Figure Legend Snippet: Betulinic acid (BA) enhances tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL)-mediated cytotoxicity in T24 human bladder cancer cells. T24 cells were treated with the indicated concentrations of BA and TRAIL alone or in combination for 24 h. (A, B) After treatment, cell viability was assessed via 3′-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay. (C) Morphological changes in the cells treated with BA and TRAIL alone or in combination were observed under an inverted microscope. (D, E) After 4′,6-diamidino-2-phenylindole (DAPI) staining, nuclear morphological changes were observed under a fluorescence microscope (D), and the frequency of cells with chromatin condensation and fragmentation was determined (E). (F, G) Flow cytometry was performed after propidium iodide (PI) staining. Representative histograms (F) and the frequency of cells in the sub-G1 phase (G) are shown. * p <0.05, ** p <0.01, and *** p <0.001 vs. control cells; ### p <0.001 vs. BA-treated cells (n=3).

Techniques Used: MTT Assay, Inverted Microscopy, Staining, Fluorescence, Microscopy, Flow Cytometry, Control

Combination treatment with BA and TRAIL increases reactive oxygen species (ROS) production and decreases ATP levels in T24 human bladder cancer cells. T24 cells were treated with BA and TRAIL alone or in combination and cultured for 30 min (A-C) or 24 h (D). (A, B) After treatment, the cells were stained with 2′,7′-dichlorofluorescein diacetate (DCF-DA) and analyzed via flow cytometry. Representative histograms (A) and the frequency of DCF-positive cells (B) are shown. (C) Representative fluorescence images of the cells stained with DCF-DA, indicating ROS production, were captured via fluorescence microscopy. (D) Intracellular ATP levels were measured using an ATP assay kit. * p <0.05 and ** p <0.01 vs. control cells; ### p <0.001 vs. BA-treated cells (n=3).

Figure Legend Snippet: Combination treatment with BA and TRAIL increases reactive oxygen species (ROS) production and decreases ATP levels in T24 human bladder cancer cells. T24 cells were treated with BA and TRAIL alone or in combination and cultured for 30 min (A-C) or 24 h (D). (A, B) After treatment, the cells were stained with 2′,7′-dichlorofluorescein diacetate (DCF-DA) and analyzed via flow cytometry. Representative histograms (A) and the frequency of DCF-positive cells (B) are shown. (C) Representative fluorescence images of the cells stained with DCF-DA, indicating ROS production, were captured via fluorescence microscopy. (D) Intracellular ATP levels were measured using an ATP assay kit. * p <0.05 and ** p <0.01 vs. control cells; ### p <0.001 vs. BA-treated cells (n=3).

Techniques Used: Cell Culture, Staining, Flow Cytometry, Fluorescence, Microscopy, ATP Assay, Control

$Combination treatment with BA and TRAIL increases mitochondrial damage and induces changes in the expression levels of Bcl-2 family proteins in T24 human bladder cancer cells. T24 cells were treated with BA and TRAIL alone or in combination and cultured for 24 h. (A, B) After treatment, the cells were stained with 5,5′,6,6′-tetrachloro-1,1′,3,3′-tetramethylbenzimidazolyl carbocyanine iodide (JC-1) and analyzed via flow cytometry. Representative histograms (A) and the frequency of cells with JC-1 monomers (B), indicating mitochondrial membrane potential (MMP) loss, are shown. * p <0.05 vs. control cells; ### p <0.001 vs. BA-treated cells (n=3). (C, D) Mitochondrial and cytosolic fractions were isolated from the cells (C), total protein was extracted (D), and immunoblotting was performed using antibodies against target proteins. Cytochrome c oxidase (COX IV) and β-actin were used as loading controls for the two fractions, respectively.$
Figure Legend Snippet: Combination treatment with BA and TRAIL increases mitochondrial damage and induces changes in the expression levels of Bcl-2 family proteins in T24 human bladder cancer cells. T24 cells were treated with BA and TRAIL alone or in combination and cultured for 24 h. (A, B) After treatment, the cells were stained with 5,5′,6,6′-tetrachloro-1,1′,3,3′-tetramethylbenzimidazolyl carbocyanine iodide (JC-1) and analyzed via flow cytometry. Representative histograms (A) and the frequency of cells with JC-1 monomers (B), indicating mitochondrial membrane potential (MMP) loss, are shown. * p <0.05 vs. control cells; ### p <0.001 vs. BA-treated cells (n=3). (C, D) Mitochondrial and cytosolic fractions were isolated from the cells (C), total protein was extracted (D), and immunoblotting was performed using antibodies against target proteins. Cytochrome c oxidase (COX IV) and β-actin were used as loading controls for the two fractions, respectively.

Techniques Used: Expressing, Cell Culture, Staining, Flow Cytometry, Membrane, Control, Isolation, Western Blot

Combination treatment with BA and TRAIL activates the caspase-dependent extrinsic and intrinsic apoptotic pathways in T24 human bladder cancer cells. T24 cells were either directly co-treated with BA and TRAIL or pretreated with z-VAD-fmk for 1 h before co-treatment with BA and TRAIL and cultured for 24 h. (A) Total protein was extracted, and immunoblotting analysis was performed using antibodies against target proteins. (B) Caspase activity was examined using caspase assay kits. (C, D) After DAPI staining, nuclear morphological changes were observed under a fluorescence microscope (C), and the frequency of cells with chromatin condensation and fragmentation was determined (D). (E, F) Flow cytometry was performed after PI staining. Representative histograms (E) and the frequency of cells in the sub-G1 phase (F) are shown. ** p <0.01 and *** p <0.001 vs. control cells; ### p <0.001 vs. BA and TRAIL co-treated cells (n=3).

Figure Legend Snippet: Combination treatment with BA and TRAIL activates the caspase-dependent extrinsic and intrinsic apoptotic pathways in T24 human bladder cancer cells. T24 cells were either directly co-treated with BA and TRAIL or pretreated with z-VAD-fmk for 1 h before co-treatment with BA and TRAIL and cultured for 24 h. (A) Total protein was extracted, and immunoblotting analysis was performed using antibodies against target proteins. (B) Caspase activity was examined using caspase assay kits. (C, D) After DAPI staining, nuclear morphological changes were observed under a fluorescence microscope (C), and the frequency of cells with chromatin condensation and fragmentation was determined (D). (E, F) Flow cytometry was performed after PI staining. Representative histograms (E) and the frequency of cells in the sub-G1 phase (F) are shown. ** p <0.01 and *** p <0.001 vs. control cells; ### p <0.001 vs. BA and TRAIL co-treated cells (n=3).

Techniques Used: Cell Culture, Western Blot, Activity Assay, Caspase Assay, Staining, Fluorescence, Microscopy, Flow Cytometry, Control

Combination treatment with BA and TRAIL inhibits activation of the phosphoinositide 3-kinase (PI3K)/Akt pathway in T24 human bladder cancer cells. T24 cells were either directly co-treated with BA and TRAIL or pretreated with LY294002 for 1 h before co-treatment with BA and TRAIL and cultured for 24 h. (A) Total cellular proteins were isolated from the cells, and phosphorylation levels of PI3K and Akt were determined via immunoblotting. (B, C) After DAPI staining, nuclear morphological changes were observed under a fluorescence microscope (B), and the frequency of cells with chromatin condensation and fragmentation was determined (C). (D, E) Flow cytometry was performed after PI staining. Representative histograms (D) and the frequency of cells in the sub-G1 phase (E) are shown. (F) Cell viability was assessed via MTT assay. *** p <0.001 vs. control cells; ### p <0.001 vs. BA and TRAIL co-treated cells (n=3).

Figure Legend Snippet: Combination treatment with BA and TRAIL inhibits activation of the phosphoinositide 3-kinase (PI3K)/Akt pathway in T24 human bladder cancer cells. T24 cells were either directly co-treated with BA and TRAIL or pretreated with LY294002 for 1 h before co-treatment with BA and TRAIL and cultured for 24 h. (A) Total cellular proteins were isolated from the cells, and phosphorylation levels of PI3K and Akt were determined via immunoblotting. (B, C) After DAPI staining, nuclear morphological changes were observed under a fluorescence microscope (B), and the frequency of cells with chromatin condensation and fragmentation was determined (C). (D, E) Flow cytometry was performed after PI staining. Representative histograms (D) and the frequency of cells in the sub-G1 phase (E) are shown. (F) Cell viability was assessed via MTT assay. *** p <0.001 vs. control cells; ### p <0.001 vs. BA and TRAIL co-treated cells (n=3).

Techniques Used: Activation Assay, Cell Culture, Isolation, Phospho-proteomics, Western Blot, Staining, Fluorescence, Microscopy, Flow Cytometry, MTT Assay, Control

Combination treatment with BA and TRAIL increases apoptosis in T24 human bladder cancer cells in an ROS-dependent manner. T24 cells were pretreated with N-acetyl-l-cysteine (NAC) 1 h before combination treatment with BA and TRAIL and cultured for 24 h. (A, B) Total protein was extracted and analyzed via immunoblotting using antibodies against target proteins. β-actin was used as a loading control. (C) Caspase-3 activity was measured using a caspase-3 assay kit. (D, E) After DAPI staining, nuclear morphological changes were observed under a fluorescence microscope (D), and the frequency of cells with chromatin condensation and fragmentation was determined (E). (F, G) Flow cytometry was performed after PI staining. Representative histograms (F) and the frequency of cells in the sub-G1 phase (G) are shown. (H) Cell viability was assessed via MTT assay. *** p <0.001 vs. control cells; ### p <0.001 vs. BA and TRAIL co-treated cells (n=3).

Figure Legend Snippet: Combination treatment with BA and TRAIL increases apoptosis in T24 human bladder cancer cells in an ROS-dependent manner. T24 cells were pretreated with N-acetyl-l-cysteine (NAC) 1 h before combination treatment with BA and TRAIL and cultured for 24 h. (A, B) Total protein was extracted and analyzed via immunoblotting using antibodies against target proteins. β-actin was used as a loading control. (C) Caspase-3 activity was measured using a caspase-3 assay kit. (D, E) After DAPI staining, nuclear morphological changes were observed under a fluorescence microscope (D), and the frequency of cells with chromatin condensation and fragmentation was determined (E). (F, G) Flow cytometry was performed after PI staining. Representative histograms (F) and the frequency of cells in the sub-G1 phase (G) are shown. (H) Cell viability was assessed via MTT assay. *** p <0.001 vs. control cells; ### p <0.001 vs. BA and TRAIL co-treated cells (n=3).

Techniques Used: Cell Culture, Western Blot, Control, Activity Assay, Caspase-3 Assay, Staining, Fluorescence, Microscopy, Flow Cytometry, MTT Assay

Schematic diagram of cytotoxicity induction in betulinic acid and TRAIL co-treated T24 human bladder cancer cells. TRAIL, tumor necrosis factor-related apoptosis-inducing ligand; PI3K, phosphoinositide 3-kinase; NAC, N-acetyl-l-cysteine; MMP, mitochondrial membrane potential; FADD, Fas-associated death domain; tBid, truncation of BH3-interacting domain death agonist; PARP, poly(ADP-ribose) polymerase.

Figure Legend Snippet: Schematic diagram of cytotoxicity induction in betulinic acid and TRAIL co-treated T24 human bladder cancer cells. TRAIL, tumor necrosis factor-related apoptosis-inducing ligand; PI3K, phosphoinositide 3-kinase; NAC, N-acetyl-l-cysteine; MMP, mitochondrial membrane potential; FADD, Fas-associated death domain; tBid, truncation of BH3-interacting domain death agonist; PARP, poly(ADP-ribose) polymerase.

Techniques Used: Membrane

Image Search Results

Journal: Biomolecules & Therapeutics

Article Title: Combination Therapy with Betulinic Acid and TRAIL Increases ROS-Dependent Cytotoxicity and Inhibits PI3K/Akt Signaling in Human Bladder Cancer Cells

doi: 10.4062/biomolther.2026.035

Figure Lengend Snippet: Betulinic acid (BA) enhances tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL)-mediated cytotoxicity in T24 human bladder cancer cells. T24 cells were treated with the indicated concentrations of BA and TRAIL alone or in combination for 24 h. (A, B) After treatment, cell viability was assessed via 3′-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay. (C) Morphological changes in the cells treated with BA and TRAIL alone or in combination were observed under an inverted microscope. (D, E) After 4′,6-diamidino-2-phenylindole (DAPI) staining, nuclear morphological changes were observed under a fluorescence microscope (D), and the frequency of cells with chromatin condensation and fragmentation was determined (E). (F, G) Flow cytometry was performed after propidium iodide (PI) staining. Representative histograms (F) and the frequency of cells in the sub-G1 phase (G) are shown. * p <0.05, ** p <0.01, and *** p <0.001 vs. control cells; ### p <0.001 vs. BA-treated cells (n=3).

Article Snippet: T24 human bladder cancer cells obtained from the American Type Culture Collection (Manassas, VA, USA) were cultured as previously described ( Kim et al. , 2021 ).

Techniques: MTT Assay, Inverted Microscopy, Staining, Fluorescence, Microscopy, Flow Cytometry, Control

Journal: Biomolecules & Therapeutics

Article Title: Combination Therapy with Betulinic Acid and TRAIL Increases ROS-Dependent Cytotoxicity and Inhibits PI3K/Akt Signaling in Human Bladder Cancer Cells

doi: 10.4062/biomolther.2026.035

Figure Lengend Snippet: Combination treatment with BA and TRAIL increases reactive oxygen species (ROS) production and decreases ATP levels in T24 human bladder cancer cells. T24 cells were treated with BA and TRAIL alone or in combination and cultured for 30 min (A-C) or 24 h (D). (A, B) After treatment, the cells were stained with 2′,7′-dichlorofluorescein diacetate (DCF-DA) and analyzed via flow cytometry. Representative histograms (A) and the frequency of DCF-positive cells (B) are shown. (C) Representative fluorescence images of the cells stained with DCF-DA, indicating ROS production, were captured via fluorescence microscopy. (D) Intracellular ATP levels were measured using an ATP assay kit. * p <0.05 and ** p <0.01 vs. control cells; ### p <0.001 vs. BA-treated cells (n=3).

Article Snippet: T24 human bladder cancer cells obtained from the American Type Culture Collection (Manassas, VA, USA) were cultured as previously described ( Kim et al. , 2021 ).

Techniques: Cell Culture, Staining, Flow Cytometry, Fluorescence, Microscopy, ATP Assay, Control

Journal: Biomolecules & Therapeutics

Article Title: Combination Therapy with Betulinic Acid and TRAIL Increases ROS-Dependent Cytotoxicity and Inhibits PI3K/Akt Signaling in Human Bladder Cancer Cells

doi: 10.4062/biomolther.2026.035

Figure Lengend Snippet: Combination treatment with BA and TRAIL increases mitochondrial damage and induces changes in the expression levels of Bcl-2 family proteins in T24 human bladder cancer cells. T24 cells were treated with BA and TRAIL alone or in combination and cultured for 24 h. (A, B) After treatment, the cells were stained with 5,5′,6,6′-tetrachloro-1,1′,3,3′-tetramethylbenzimidazolyl carbocyanine iodide (JC-1) and analyzed via flow cytometry. Representative histograms (A) and the frequency of cells with JC-1 monomers (B), indicating mitochondrial membrane potential (MMP) loss, are shown. * p <0.05 vs. control cells; ### p <0.001 vs. BA-treated cells (n=3). (C, D) Mitochondrial and cytosolic fractions were isolated from the cells (C), total protein was extracted (D), and immunoblotting was performed using antibodies against target proteins. Cytochrome c oxidase (COX IV) and β-actin were used as loading controls for the two fractions, respectively.

Article Snippet: T24 human bladder cancer cells obtained from the American Type Culture Collection (Manassas, VA, USA) were cultured as previously described ( Kim et al. , 2021 ).

Techniques: Expressing, Cell Culture, Staining, Flow Cytometry, Membrane, Control, Isolation, Western Blot

Journal: Biomolecules & Therapeutics

Article Title: Combination Therapy with Betulinic Acid and TRAIL Increases ROS-Dependent Cytotoxicity and Inhibits PI3K/Akt Signaling in Human Bladder Cancer Cells

doi: 10.4062/biomolther.2026.035

Figure Lengend Snippet: Combination treatment with BA and TRAIL activates the caspase-dependent extrinsic and intrinsic apoptotic pathways in T24 human bladder cancer cells. T24 cells were either directly co-treated with BA and TRAIL or pretreated with z-VAD-fmk for 1 h before co-treatment with BA and TRAIL and cultured for 24 h. (A) Total protein was extracted, and immunoblotting analysis was performed using antibodies against target proteins. (B) Caspase activity was examined using caspase assay kits. (C, D) After DAPI staining, nuclear morphological changes were observed under a fluorescence microscope (C), and the frequency of cells with chromatin condensation and fragmentation was determined (D). (E, F) Flow cytometry was performed after PI staining. Representative histograms (E) and the frequency of cells in the sub-G1 phase (F) are shown. ** p <0.01 and *** p <0.001 vs. control cells; ### p <0.001 vs. BA and TRAIL co-treated cells (n=3).

Article Snippet: T24 human bladder cancer cells obtained from the American Type Culture Collection (Manassas, VA, USA) were cultured as previously described ( Kim et al. , 2021 ).

Techniques: Cell Culture, Western Blot, Activity Assay, Caspase Assay, Staining, Fluorescence, Microscopy, Flow Cytometry, Control

Journal: Biomolecules & Therapeutics

Article Title: Combination Therapy with Betulinic Acid and TRAIL Increases ROS-Dependent Cytotoxicity and Inhibits PI3K/Akt Signaling in Human Bladder Cancer Cells

doi: 10.4062/biomolther.2026.035

Figure Lengend Snippet: Combination treatment with BA and TRAIL inhibits activation of the phosphoinositide 3-kinase (PI3K)/Akt pathway in T24 human bladder cancer cells. T24 cells were either directly co-treated with BA and TRAIL or pretreated with LY294002 for 1 h before co-treatment with BA and TRAIL and cultured for 24 h. (A) Total cellular proteins were isolated from the cells, and phosphorylation levels of PI3K and Akt were determined via immunoblotting. (B, C) After DAPI staining, nuclear morphological changes were observed under a fluorescence microscope (B), and the frequency of cells with chromatin condensation and fragmentation was determined (C). (D, E) Flow cytometry was performed after PI staining. Representative histograms (D) and the frequency of cells in the sub-G1 phase (E) are shown. (F) Cell viability was assessed via MTT assay. *** p <0.001 vs. control cells; ### p <0.001 vs. BA and TRAIL co-treated cells (n=3).

Article Snippet: T24 human bladder cancer cells obtained from the American Type Culture Collection (Manassas, VA, USA) were cultured as previously described ( Kim et al. , 2021 ).

Techniques: Activation Assay, Cell Culture, Isolation, Phospho-proteomics, Western Blot, Staining, Fluorescence, Microscopy, Flow Cytometry, MTT Assay, Control

Journal: Biomolecules & Therapeutics

Article Title: Combination Therapy with Betulinic Acid and TRAIL Increases ROS-Dependent Cytotoxicity and Inhibits PI3K/Akt Signaling in Human Bladder Cancer Cells

doi: 10.4062/biomolther.2026.035

Figure Lengend Snippet: Combination treatment with BA and TRAIL increases apoptosis in T24 human bladder cancer cells in an ROS-dependent manner. T24 cells were pretreated with N-acetyl-l-cysteine (NAC) 1 h before combination treatment with BA and TRAIL and cultured for 24 h. (A, B) Total protein was extracted and analyzed via immunoblotting using antibodies against target proteins. β-actin was used as a loading control. (C) Caspase-3 activity was measured using a caspase-3 assay kit. (D, E) After DAPI staining, nuclear morphological changes were observed under a fluorescence microscope (D), and the frequency of cells with chromatin condensation and fragmentation was determined (E). (F, G) Flow cytometry was performed after PI staining. Representative histograms (F) and the frequency of cells in the sub-G1 phase (G) are shown. (H) Cell viability was assessed via MTT assay. *** p <0.001 vs. control cells; ### p <0.001 vs. BA and TRAIL co-treated cells (n=3).

Article Snippet: T24 human bladder cancer cells obtained from the American Type Culture Collection (Manassas, VA, USA) were cultured as previously described ( Kim et al. , 2021 ).

Techniques: Cell Culture, Western Blot, Control, Activity Assay, Caspase-3 Assay, Staining, Fluorescence, Microscopy, Flow Cytometry, MTT Assay

Journal: Biomolecules & Therapeutics

Article Title: Combination Therapy with Betulinic Acid and TRAIL Increases ROS-Dependent Cytotoxicity and Inhibits PI3K/Akt Signaling in Human Bladder Cancer Cells

doi: 10.4062/biomolther.2026.035

Figure Lengend Snippet: Schematic diagram of cytotoxicity induction in betulinic acid and TRAIL co-treated T24 human bladder cancer cells. TRAIL, tumor necrosis factor-related apoptosis-inducing ligand; PI3K, phosphoinositide 3-kinase; NAC, N-acetyl-l-cysteine; MMP, mitochondrial membrane potential; FADD, Fas-associated death domain; tBid, truncation of BH3-interacting domain death agonist; PARP, poly(ADP-ribose) polymerase.

Article Snippet: T24 human bladder cancer cells obtained from the American Type Culture Collection (Manassas, VA, USA) were cultured as previously described ( Kim et al. , 2021 ).

Techniques: Membrane

Mechanical pressure enhances mechano‐sensitivity of urinary epithelial cells. (A) The scheme of mechanical pressure model in vitro. B) CCK‐8 assay of SV‐HUC, T24, 253J cells exposed on gradient pressure. (C) CCK‐8 assay of cells exposed on 40 cmH 2 O pressure for different times. (D) EdU assay of cells exposed on 40 cmH 2 O pressure for 12 h. (E) F‐Actin staining of SV‐HUC, T24, 253J cells exposed on 40 cm H 2 O pressure for 12 h. (F) The quantitative analysis of EdU assay. (G) The quantitative analysis of nucleo‐cytoplasmic ratio. (H) Expression level of Piezo1/ITGB1/YAP/α‐SMA in cells exposed on gradient pressure. (I) Wound closure assay of SV‐HUC cells exposed on gradient pressure for 24, 48 h. (J) The quantitative analysis of wound closure assay in SV‐HUC cells. (K) The quantitative analysis of wound closure assay in T24 cells. (L) TEM image of SV‐HUC cell exposed on 40 cm H 2 O pressure. (M) The detection process of nanoindentation before and after HP for 2 h. N) Detection of Young's modulus in T24 cells using nanoindentation before and after HP for 2 h. (O) The quantitative analysis of Z position and Young's modulus detection. All data are presented as the Mean ± SD ( n = 3). * p < 0.05, ** p < 0.01, and *** p < 0.001. ns, no significant difference.

Journal: Advanced Science

Article Title: Piezo1 Channel Mediates Mechanically Programmable Drug Delivery to Potentiate Intravesical Chemotherapy

doi: 10.1002/advs.202522936

Figure Lengend Snippet: Mechanical pressure enhances mechano‐sensitivity of urinary epithelial cells. (A) The scheme of mechanical pressure model in vitro. B) CCK‐8 assay of SV‐HUC, T24, 253J cells exposed on gradient pressure. (C) CCK‐8 assay of cells exposed on 40 cmH 2 O pressure for different times. (D) EdU assay of cells exposed on 40 cmH 2 O pressure for 12 h. (E) F‐Actin staining of SV‐HUC, T24, 253J cells exposed on 40 cm H 2 O pressure for 12 h. (F) The quantitative analysis of EdU assay. (G) The quantitative analysis of nucleo‐cytoplasmic ratio. (H) Expression level of Piezo1/ITGB1/YAP/α‐SMA in cells exposed on gradient pressure. (I) Wound closure assay of SV‐HUC cells exposed on gradient pressure for 24, 48 h. (J) The quantitative analysis of wound closure assay in SV‐HUC cells. (K) The quantitative analysis of wound closure assay in T24 cells. (L) TEM image of SV‐HUC cell exposed on 40 cm H 2 O pressure. (M) The detection process of nanoindentation before and after HP for 2 h. N) Detection of Young's modulus in T24 cells using nanoindentation before and after HP for 2 h. (O) The quantitative analysis of Z position and Young's modulus detection. All data are presented as the Mean ± SD ( n = 3). * p < 0.05, ** p < 0.01, and *** p < 0.001. ns, no significant difference.

Article Snippet: The human bladder cancer cell lines T24, 253J, and the normal control cell SV‐HUC, which was the SV‐40 immortalized human uroepithelial cell line, were obtained from the American Type Culture Collection (ATCC, USA).

Techniques: In Vitro, CCK-8 Assay, EdU Assay, Staining, Expressing, Wound Closure Assay

Mechanical pressure amplifies calcium influx via Piezo1/ITGB1‐mediated membrane tension. (A) RNA expression level of Piezo1/ITGB1 in cells exposed on mechanical pressure. (B) Protein expression level of Piezo1/ITGB1 in cells exposed on hydrostatic pressure. (C) The heatmap of differentially expressed genes (DEGs) in T24 cells from RNA sequencing. (D) Go analysis of DEGs in T24 cells from RNA sequencing. E) KEGG analysis of DEGs in T24 cells from RNA sequencing. (F) The flow cytometry result of intracellular calcium flux in T24 and SV‐HUC cells exposed on hydrostatic pressure for 0, 0.5, 1, 2, and 4 h using Fluo‐4AM probe. (G) The flow cytometry result of intracellular calcium flux in T24 cells exposed on hydrostatic pressure with Piezo1 agonists or inhibitors. (H) The image of intracellular calcium flux in T24 cells exposed on hydrostatic pressure with agonists or inhibitors using Fluo‐4AM probe. (I) Expression level of Piezo1/ITGB1 signal of cells exposed on pressure with agonists or inhibitors. (J) Membrane tension through fluorescence lifetime imaging (FLIM) in T24 cells exposed on pressure for 2 h. All data are presented as the Mean ± SD ( n = 3). * p < 0.05, ** p < 0.01, and *** p < 0.001. ns, no significant difference.

Journal: Advanced Science

Article Title: Piezo1 Channel Mediates Mechanically Programmable Drug Delivery to Potentiate Intravesical Chemotherapy

doi: 10.1002/advs.202522936

Figure Lengend Snippet: Mechanical pressure amplifies calcium influx via Piezo1/ITGB1‐mediated membrane tension. (A) RNA expression level of Piezo1/ITGB1 in cells exposed on mechanical pressure. (B) Protein expression level of Piezo1/ITGB1 in cells exposed on hydrostatic pressure. (C) The heatmap of differentially expressed genes (DEGs) in T24 cells from RNA sequencing. (D) Go analysis of DEGs in T24 cells from RNA sequencing. E) KEGG analysis of DEGs in T24 cells from RNA sequencing. (F) The flow cytometry result of intracellular calcium flux in T24 and SV‐HUC cells exposed on hydrostatic pressure for 0, 0.5, 1, 2, and 4 h using Fluo‐4AM probe. (G) The flow cytometry result of intracellular calcium flux in T24 cells exposed on hydrostatic pressure with Piezo1 agonists or inhibitors. (H) The image of intracellular calcium flux in T24 cells exposed on hydrostatic pressure with agonists or inhibitors using Fluo‐4AM probe. (I) Expression level of Piezo1/ITGB1 signal of cells exposed on pressure with agonists or inhibitors. (J) Membrane tension through fluorescence lifetime imaging (FLIM) in T24 cells exposed on pressure for 2 h. All data are presented as the Mean ± SD ( n = 3). * p < 0.05, ** p < 0.01, and *** p < 0.001. ns, no significant difference.

Techniques: Membrane, RNA Expression, Expressing, RNA Sequencing, Flow Cytometry, Fluorescence, Imaging

Mechanical pressure enhances DOX accumulation in tumor. (A) Proliferation assay of SV‐HUC, T24, 253J cells exposed on 40 cm H 2 O pressure and different concentrations of DOX. (B) The uptake efficiency of DOX in cells exposed on HP from flow cytometry. (C) The quantitative analysis of the apoptosis rate of cells induced by DOX and HP from flow cytometry. D)The quantitative result of DOX uptake efficiency from flow cytometry using a series of endocytic inhibitors. (E) DOX uptake efficiency of T24 cells exposed on DOX from flow cytometry using a series of endocytic inhibitors. (F) DOX uptake efficiency of T24 cells exposed on DOX and HP from flow cytometry using a series of endocytic inhibitors. (G) DOX accumulation in tumor spheres exposed on HP and different concentrations of DOX. H) Immunofluorescence of Piezo1/ITGB1 in tumor spheres exposed on HP and DOX. I) The quantitative analysis of DOX intensity in tumor spheres treated with different concentrations of DOX. J) The quantitative analysis of Piezo1 and ITGB1 expression levels in tumor spheres. K) The quantitative analysis of DOX accumulation in tumor spheres treated with DOX and HP. All data are presented as the Mean ± SD ( n = 3). * p < 0.05, ** p < 0.01, and *** p < 0.001. ns, no significant difference.

Journal: Advanced Science

Article Title: Piezo1 Channel Mediates Mechanically Programmable Drug Delivery to Potentiate Intravesical Chemotherapy

doi: 10.1002/advs.202522936

Figure Lengend Snippet: Mechanical pressure enhances DOX accumulation in tumor. (A) Proliferation assay of SV‐HUC, T24, 253J cells exposed on 40 cm H 2 O pressure and different concentrations of DOX. (B) The uptake efficiency of DOX in cells exposed on HP from flow cytometry. (C) The quantitative analysis of the apoptosis rate of cells induced by DOX and HP from flow cytometry. D)The quantitative result of DOX uptake efficiency from flow cytometry using a series of endocytic inhibitors. (E) DOX uptake efficiency of T24 cells exposed on DOX from flow cytometry using a series of endocytic inhibitors. (F) DOX uptake efficiency of T24 cells exposed on DOX and HP from flow cytometry using a series of endocytic inhibitors. (G) DOX accumulation in tumor spheres exposed on HP and different concentrations of DOX. H) Immunofluorescence of Piezo1/ITGB1 in tumor spheres exposed on HP and DOX. I) The quantitative analysis of DOX intensity in tumor spheres treated with different concentrations of DOX. J) The quantitative analysis of Piezo1 and ITGB1 expression levels in tumor spheres. K) The quantitative analysis of DOX accumulation in tumor spheres treated with DOX and HP. All data are presented as the Mean ± SD ( n = 3). * p < 0.05, ** p < 0.01, and *** p < 0.001. ns, no significant difference.

Techniques: Proliferation Assay, Flow Cytometry, Immunofluorescence, Expressing

Mechanical pressure enhances tumor apoptosis induced by chemical drugs. (A) Western blotting results of Piezo1/ITGB1 expression level in five matched pairs of bladder normal and tumor tissues. (B) CCK‐8 assay of T24 cell exposed on 40 cm H 2 O pressure and different concentrations of MMC. (C) Immunofluorescence of Piezo1/ITGB1 in SV‐HUC cells exposed on HP and DOX. (D) The quantitative analysis of Piezo1/ITGB1 expression and DOX nuclear accumulation in SV‐HUC cells. (E) Immunofluorescence of Piezo1/ITGB1 in T24 cells exposed on HP and DOX. (F) The quantitative analysis of Piezo1/ITGB1 expression and DOX nuclear accumulation in T24 cells. (G,H) Expression level of mechanical axis and apoptosis proteins in cells treated with DOX and mechanical pressure. (I) Expression level of apoptosis proteins in T24 cells treated with MMC and mechanical pressure.

Journal: Advanced Science

Article Title: Piezo1 Channel Mediates Mechanically Programmable Drug Delivery to Potentiate Intravesical Chemotherapy

doi: 10.1002/advs.202522936

Figure Lengend Snippet: Mechanical pressure enhances tumor apoptosis induced by chemical drugs. (A) Western blotting results of Piezo1/ITGB1 expression level in five matched pairs of bladder normal and tumor tissues. (B) CCK‐8 assay of T24 cell exposed on 40 cm H 2 O pressure and different concentrations of MMC. (C) Immunofluorescence of Piezo1/ITGB1 in SV‐HUC cells exposed on HP and DOX. (D) The quantitative analysis of Piezo1/ITGB1 expression and DOX nuclear accumulation in SV‐HUC cells. (E) Immunofluorescence of Piezo1/ITGB1 in T24 cells exposed on HP and DOX. (F) The quantitative analysis of Piezo1/ITGB1 expression and DOX nuclear accumulation in T24 cells. (G,H) Expression level of mechanical axis and apoptosis proteins in cells treated with DOX and mechanical pressure. (I) Expression level of apoptosis proteins in T24 cells treated with MMC and mechanical pressure.

Techniques: Western Blot, Expressing, CCK-8 Assay, Immunofluorescence

Piezo1 mediates mechanical potentiation of chemotherapeutic efficacy. (A) Proliferation assay of overexpressed cells exposed on HP and different concentrations of DOX. (B) Expression level of the mechanical pathway and apoptosis proteins in cells treated with DOX and HP. (C) The apoptosis rate induced by DOX and HP from flow cytometry. (D) The quantitative analysis of apoptosis rate from flow cytometry. (E) The flow cytometry result of DOX accumulation in T24 cells exposed on HP with Piezo1 agonists or inhibitors. (F) Expression level of the mechanical pathway and apoptosis proteins in Sh‐Piezo1 cells treated with DOX and HP. (G) The flow cytometry result of DOX accumulation in Sh‐Piezo1 cells exposed on HP. (H) The flow cytometry result of DOX uptake in T24 cells treated with YAP‐specific inhibitor verteporfin. All data are presented as the Mean ± SD ( n = 3). * p < 0.05, ** p < 0.01, and *** p < 0.001. ns, no significant difference.

Journal: Advanced Science

Article Title: Piezo1 Channel Mediates Mechanically Programmable Drug Delivery to Potentiate Intravesical Chemotherapy

doi: 10.1002/advs.202522936

Figure Lengend Snippet: Piezo1 mediates mechanical potentiation of chemotherapeutic efficacy. (A) Proliferation assay of overexpressed cells exposed on HP and different concentrations of DOX. (B) Expression level of the mechanical pathway and apoptosis proteins in cells treated with DOX and HP. (C) The apoptosis rate induced by DOX and HP from flow cytometry. (D) The quantitative analysis of apoptosis rate from flow cytometry. (E) The flow cytometry result of DOX accumulation in T24 cells exposed on HP with Piezo1 agonists or inhibitors. (F) Expression level of the mechanical pathway and apoptosis proteins in Sh‐Piezo1 cells treated with DOX and HP. (G) The flow cytometry result of DOX accumulation in Sh‐Piezo1 cells exposed on HP. (H) The flow cytometry result of DOX uptake in T24 cells treated with YAP‐specific inhibitor verteporfin. All data are presented as the Mean ± SD ( n = 3). * p < 0.05, ** p < 0.01, and *** p < 0.001. ns, no significant difference.

Techniques: Proliferation Assay, Expressing, Flow Cytometry

Representative haematoxylin–eosin (HE)-stained sections of SV-HUC-1 and T24 spheroids prepared by cryosectioning ( A-F ) and paraffin embedding (G-L) . A necrotic core (indicated by asterisks, A-B , D-E , G-H , J-K ) is visible in most cross sections, except those obtained from peripheral regions. Scale bars: 500 µm (A, D, G, J), 100 µm (B, E, H, K), 50 µm (C, F, I, L).

Journal: PLOS One

Article Title: Integrated light and electron microscopy workflow for morphological, molecular and ultrastructural analysis of spheroids

doi: 10.1371/journal.pone.0342659

Figure Lengend Snippet: Representative haematoxylin–eosin (HE)-stained sections of SV-HUC-1 and T24 spheroids prepared by cryosectioning ( A-F ) and paraffin embedding (G-L) . A necrotic core (indicated by asterisks, A-B , D-E , G-H , J-K ) is visible in most cross sections, except those obtained from peripheral regions. Scale bars: 500 µm (A, D, G, J), 100 µm (B, E, H, K), 50 µm (C, F, I, L).

Article Snippet: Normal human urothelial SV-HUC-1 cells (CRL-9520) and muscle-invasive human bladder cancer urothelial T24 cells (HTB-4) were purchased from ATCC (Manassas, VA, United States) and cultured in a 1:1 mixture of A-DMEM medium (Gibco, Thermo Fisher Scientific, Waltham, MA, United States) and F12 (Sigma-Aldrich, St. Louis, MO, United States), supplemented with 5% fetal bovine serum (Invitrogen, Carlsbad, CA, United States) and 4 mM GlutaMAX (Gibco, Thermo Fisher Scientific, Waltham, MA, United States).

Techniques: Staining

Representative images of paraffin sections show E-cadherin (green) in the plasma membrane in cells of SV-HUC-1 spheroids ( A-a3 ) and N-cadherin (red) in the plasma membrane of T24 spheroids ( B-b3 ). Some SV-HUC-1 cells are also positive for N-cadherin (arrows, a2 and a3 ). Yellow insets (in A and B) are magnified (a1-a3 and b1-b3) and display individual and merged channels of E-cadherin, N-cadherin, and DAPI-stained nuclei. Scale bars: 100 µm (A, B) , 20 µm (a1-a3, b1-b3).

Journal: PLOS One

Article Title: Integrated light and electron microscopy workflow for morphological, molecular and ultrastructural analysis of spheroids

doi: 10.1371/journal.pone.0342659

Figure Lengend Snippet: Representative images of paraffin sections show E-cadherin (green) in the plasma membrane in cells of SV-HUC-1 spheroids ( A-a3 ) and N-cadherin (red) in the plasma membrane of T24 spheroids ( B-b3 ). Some SV-HUC-1 cells are also positive for N-cadherin (arrows, a2 and a3 ). Yellow insets (in A and B) are magnified (a1-a3 and b1-b3) and display individual and merged channels of E-cadherin, N-cadherin, and DAPI-stained nuclei. Scale bars: 100 µm (A, B) , 20 µm (a1-a3, b1-b3).

Techniques: Clinical Proteomics, Membrane, Staining

SV-HUC-1 (A) and T24 cells (C) form spheroids with a spherical morphology. (B) SV-HUC-1 cells are tightly attached to each other (arrows), and microvilli are seen on their surface. (D) T24 cells are loosely attached, displaying wider intercellular spaces (arrowheads) and have fewer microvilli. Scale bars: 100 µm (A, C) , 10 µm (B, D) .

Journal: PLOS One

Article Title: Integrated light and electron microscopy workflow for morphological, molecular and ultrastructural analysis of spheroids

doi: 10.1371/journal.pone.0342659

Figure Lengend Snippet: SV-HUC-1 (A) and T24 cells (C) form spheroids with a spherical morphology. (B) SV-HUC-1 cells are tightly attached to each other (arrows), and microvilli are seen on their surface. (D) T24 cells are loosely attached, displaying wider intercellular spaces (arrowheads) and have fewer microvilli. Scale bars: 100 µm (A, C) , 10 µm (B, D) .

Techniques:

Outermost cells in SV-HUC-1 spheroids display cuboidal morphology (A) , whereas T24 cells are more elongated (B) . The presence of cell junctions in the outermost cell layer of SV-HUC-1 (C) and T24 spheroid (D) (boxed regions) indicates a tight cellular network of the outermost cell layer. The central necrotic zone (asterisks) is filled with necrotic cells in SV-HUC-1 and T24 spheroids (E, F) , as clearly demonstrated on semithin sections (G, H) , prepared before ultrathin sectioning. Scale bars: 100 µm (G-H) , 10 µm (A-B) , 5 µm (E-F) , 1 µm (C-D) .

Journal: PLOS One

Article Title: Integrated light and electron microscopy workflow for morphological, molecular and ultrastructural analysis of spheroids

doi: 10.1371/journal.pone.0342659

Figure Lengend Snippet: Outermost cells in SV-HUC-1 spheroids display cuboidal morphology (A) , whereas T24 cells are more elongated (B) . The presence of cell junctions in the outermost cell layer of SV-HUC-1 (C) and T24 spheroid (D) (boxed regions) indicates a tight cellular network of the outermost cell layer. The central necrotic zone (asterisks) is filled with necrotic cells in SV-HUC-1 and T24 spheroids (E, F) , as clearly demonstrated on semithin sections (G, H) , prepared before ultrathin sectioning. Scale bars: 100 µm (G-H) , 10 µm (A-B) , 5 µm (E-F) , 1 µm (C-D) .

Techniques:

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1) Product Images from "Combination Therapy with Betulinic Acid and TRAIL Increases ROS-Dependent Cytotoxicity and Inhibits PI3K/Akt Signaling in Human Bladder Cancer Cells"

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