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ATCC 143b

FR6 promotes cytosolic and in vivo delivery of fluorous tagged peptides. ( a ) Cellular uptake of unmodified peptide, FPep, FR6/peptide, or FR6/FPep in HeLa cells visualized by confocal microscopy after 6 h incubation. The concentration of peptides was 5 μM. ( b ) Quantification of intracellular delivery efficiency of HeLa cells incubated with FITC FKLA or FR6/ FITC FKLA at different concentrations for 6 h (n = 3). The concentration of FR6 was 5 μM. ( c ) The LDH release of <t>143B</t> cells treated with PBS, FR6, KLA, FKLA, FR6/KLA, or FR6/FKLA for 24 h, respectively. The concentration of KLA, FKLA, and FR6 was 2.5 μM. ( d ) The apoptosis of 143B cells treated with FR6, KLA, FKLA, FR6/KLA, or FR6/FKLA for 24 h, respectively. The concentration of KLA, FKLA, and FR6 was 5 μM. ( e ) Confocal images of 3D tumor spheroids treated with different peptides for 12 h. The concentration of FITC KLA, FITC FKLA, and FR6 was 5 μM. ( f ) Schematic diagram of the in vivo therapy procedure. ( g ) Tumor progression curves following treatment with PBS, FR6, FKLA, or FR6/FKLA, respectively. Tumor images ( h ) and tumor weights ( i ) of mice treated with different samples.

143b, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1514 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 99 stars, based on 1514 article reviews

143b - by Bioz Stars, 2026-03

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1) Product Images from "Fluorous oligoarginines as supra-enhancers for intracellular and transdermal peptide delivery"

Article Title: Fluorous oligoarginines as supra-enhancers for intracellular and transdermal peptide delivery

Journal: Bioactive Materials

doi: 10.1016/j.bioactmat.2025.12.027

Figure Legend Snippet: FR6 promotes cytosolic and in vivo delivery of fluorous tagged peptides. ( a ) Cellular uptake of unmodified peptide, FPep, FR6/peptide, or FR6/FPep in HeLa cells visualized by confocal microscopy after 6 h incubation. The concentration of peptides was 5 μM. ( b ) Quantification of intracellular delivery efficiency of HeLa cells incubated with FITC FKLA or FR6/ FITC FKLA at different concentrations for 6 h (n = 3). The concentration of FR6 was 5 μM. ( c ) The LDH release of 143B cells treated with PBS, FR6, KLA, FKLA, FR6/KLA, or FR6/FKLA for 24 h, respectively. The concentration of KLA, FKLA, and FR6 was 2.5 μM. ( d ) The apoptosis of 143B cells treated with FR6, KLA, FKLA, FR6/KLA, or FR6/FKLA for 24 h, respectively. The concentration of KLA, FKLA, and FR6 was 5 μM. ( e ) Confocal images of 3D tumor spheroids treated with different peptides for 12 h. The concentration of FITC KLA, FITC FKLA, and FR6 was 5 μM. ( f ) Schematic diagram of the in vivo therapy procedure. ( g ) Tumor progression curves following treatment with PBS, FR6, FKLA, or FR6/FKLA, respectively. Tumor images ( h ) and tumor weights ( i ) of mice treated with different samples.

Techniques Used: In Vivo, Confocal Microscopy, Incubation, Concentration Assay

Image Search Results

Journal: Bioactive Materials

Article Title: Fluorous oligoarginines as supra-enhancers for intracellular and transdermal peptide delivery

doi: 10.1016/j.bioactmat.2025.12.027

Figure Lengend Snippet: FR6 promotes cytosolic and in vivo delivery of fluorous tagged peptides. ( a ) Cellular uptake of unmodified peptide, FPep, FR6/peptide, or FR6/FPep in HeLa cells visualized by confocal microscopy after 6 h incubation. The concentration of peptides was 5 μM. ( b ) Quantification of intracellular delivery efficiency of HeLa cells incubated with FITC FKLA or FR6/ FITC FKLA at different concentrations for 6 h (n = 3). The concentration of FR6 was 5 μM. ( c ) The LDH release of 143B cells treated with PBS, FR6, KLA, FKLA, FR6/KLA, or FR6/FKLA for 24 h, respectively. The concentration of KLA, FKLA, and FR6 was 2.5 μM. ( d ) The apoptosis of 143B cells treated with FR6, KLA, FKLA, FR6/KLA, or FR6/FKLA for 24 h, respectively. The concentration of KLA, FKLA, and FR6 was 5 μM. ( e ) Confocal images of 3D tumor spheroids treated with different peptides for 12 h. The concentration of FITC KLA, FITC FKLA, and FR6 was 5 μM. ( f ) Schematic diagram of the in vivo therapy procedure. ( g ) Tumor progression curves following treatment with PBS, FR6, FKLA, or FR6/FKLA, respectively. Tumor images ( h ) and tumor weights ( i ) of mice treated with different samples.

Article Snippet: HeLa, 143B, HEK293, RAW264.7, and NIH3T3 were sourced from ATCC.

Techniques: In Vivo, Confocal Microscopy, Incubation, Concentration Assay

(A) 143B cells (osteosarcoma) show greater proliferation than hFOB cells (osteoblast control cells) in both high (25 mM) and low (5.6 mM) glucose media in three replicate experiments. (B) Mitochondrial membrane potential of 143B cells was significantly decreased when glucose media was changed from 25 mM to 5.6 mM comparing with hFOB cells in three biological replicate experiments.. (C) Mitochondrial membrane potential of the osteosarcoma cells was surprisingly greater in high glucose but lower in low glucose media. (D) Cell viability of 143B cells normalized to hFOB cells in 5.6 mM glucose or 10 mM galactose medium. Only the 143B osteosarcoma cells had significantly reduced viability in galactose media compared to both hFOB cells in galactose and 143B cells in glucose. (E) Cell viability of 6 osteosarcoma cell lines (including 5 primary tumor derived lines: HOS, MG-63, Saos-2, SJSA-1, U2 OS, and one pulmonary metastasis derived line: 15454-307) grown in 5.6 mM glucose or 10 mM galactose medium. Significant reductions of cell viability to variable degrees were seen in galactose conditions for all cell lines except HOS. Three biological replicate experiments per condition. All boxplots show the median of the data, the boxes mark the limits of the second and third quartiles and the whiskers the smallest and largest values no more than 1.5 times +/- the interquartile range. Points outside that range are considered “outlying” and are plotted individually. Differences between the groups were tested with ANOVA with a post-hoc Tukey test while controlling for biological replicates.

Journal: bioRxiv

Article Title: In vitro modeling of nutritional and mitochondria-targeted therapies for osteosarcoma

doi: 10.64898/2026.02.19.706776

Figure Lengend Snippet: (A) 143B cells (osteosarcoma) show greater proliferation than hFOB cells (osteoblast control cells) in both high (25 mM) and low (5.6 mM) glucose media in three replicate experiments. (B) Mitochondrial membrane potential of 143B cells was significantly decreased when glucose media was changed from 25 mM to 5.6 mM comparing with hFOB cells in three biological replicate experiments.. (C) Mitochondrial membrane potential of the osteosarcoma cells was surprisingly greater in high glucose but lower in low glucose media. (D) Cell viability of 143B cells normalized to hFOB cells in 5.6 mM glucose or 10 mM galactose medium. Only the 143B osteosarcoma cells had significantly reduced viability in galactose media compared to both hFOB cells in galactose and 143B cells in glucose. (E) Cell viability of 6 osteosarcoma cell lines (including 5 primary tumor derived lines: HOS, MG-63, Saos-2, SJSA-1, U2 OS, and one pulmonary metastasis derived line: 15454-307) grown in 5.6 mM glucose or 10 mM galactose medium. Significant reductions of cell viability to variable degrees were seen in galactose conditions for all cell lines except HOS. Three biological replicate experiments per condition. All boxplots show the median of the data, the boxes mark the limits of the second and third quartiles and the whiskers the smallest and largest values no more than 1.5 times +/- the interquartile range. Points outside that range are considered “outlying” and are plotted individually. Differences between the groups were tested with ANOVA with a post-hoc Tukey test while controlling for biological replicates.

Article Snippet: Authenticated human osteosarcoma cell lines were obtained: 143B (ATCC Cat# CRL-8303, RRID:CVCL_2270), HOS (ATCC Cat# CRL-1543, RRID:CVCL_0312), MG-63 (ATCC Cat# CRL-1427, RRID:CVCL_0426), Saos-2 (ATCC Cat# HTB-85, RRID:CVCL_0548), SJSA-1 (ATCC Cat# CRL-2098, RRID:CVCL_1697), U-2 OS (ATCC Cat# HTB-96, RRID:CVCL_0042) and osteoblast cell lines hFOB 1.19 ((ATCC Cat# CRL-3602, RRID:CVCL_3708), hFOB) and NHOst (Lonza Cat #: CC-2538).

Techniques: Control, Membrane, Derivative Assay

Differential expression, tested using DESeq2, and pathway analysis, tested using fgsea, is shown for 143B (A, B), HOS (C, D), MG-63 (E, F), Saos-2 (G, H), SJSA1 (I, J), U-2 OS (K, L) and osteosarcoma lung metastasis 15454-307 (M, N) osteosarcoma cell lines. Volcano plots display differential expression results with log2 fold change on the x-axis and negative log10 adjusted p-value on the y-axis (A, C, E, G, I, K, M). Bar plots detail the top five most up- and down-regulated pathways (B, D, F, H, J, L, N). Both significantly different points in the volcano plot and significant pathways in the bar plots are colored by cell line; non-statistically significant points or bars are shown in gray. Legends are grouped, with the legend applying to both the volcano plot and the bar plot of the same color.

Journal: bioRxiv

Article Title: In vitro modeling of nutritional and mitochondria-targeted therapies for osteosarcoma

doi: 10.64898/2026.02.19.706776

Figure Lengend Snippet: Differential expression, tested using DESeq2, and pathway analysis, tested using fgsea, is shown for 143B (A, B), HOS (C, D), MG-63 (E, F), Saos-2 (G, H), SJSA1 (I, J), U-2 OS (K, L) and osteosarcoma lung metastasis 15454-307 (M, N) osteosarcoma cell lines. Volcano plots display differential expression results with log2 fold change on the x-axis and negative log10 adjusted p-value on the y-axis (A, C, E, G, I, K, M). Bar plots detail the top five most up- and down-regulated pathways (B, D, F, H, J, L, N). Both significantly different points in the volcano plot and significant pathways in the bar plots are colored by cell line; non-statistically significant points or bars are shown in gray. Legends are grouped, with the legend applying to both the volcano plot and the bar plot of the same color.

Techniques: Quantitative Proteomics

Cell viability of (A) healthy osteoblasts hFOB, (B) primary osteosarcomas 143B and (C) MG-63, and (D) lung metastasis 15454-307 treated with 5 µM cycloheximide. Cell viability of (E) healthy osteoblasts NHOst, (F) healthy fibroblasts Q2148, and osteosarcomas (G) MG-63 or (H) 15454-307 treated with metformin, ONC201, or ONC206 in 5.6 mM glucose DMEM-10% FBS medium for 72 h. Cell viability of the same control cells and osteosarcoma cells, (I) hFOB, (J) NHOst, (K) Q2148, (L) 143B, (M) MG-63, (N) 15454-307 treated with 1.5 µM ONC201, or 0.15 µM ONC206 in 17 mM glucose DMEM-10%FBS medium for 72 h. Cell viability was tested using ANOVA with a post-hoc Tukey test for all comparisons. Box plots identify the median second and third quartiles and the whiskers extend to the smallest and largest values no more than 1.5 times +/- the interquartile range. Points outside that range are considered “outlying” and are plotted individually.

Journal: bioRxiv

Article Title: In vitro modeling of nutritional and mitochondria-targeted therapies for osteosarcoma

doi: 10.64898/2026.02.19.706776

Figure Lengend Snippet: Cell viability of (A) healthy osteoblasts hFOB, (B) primary osteosarcomas 143B and (C) MG-63, and (D) lung metastasis 15454-307 treated with 5 µM cycloheximide. Cell viability of (E) healthy osteoblasts NHOst, (F) healthy fibroblasts Q2148, and osteosarcomas (G) MG-63 or (H) 15454-307 treated with metformin, ONC201, or ONC206 in 5.6 mM glucose DMEM-10% FBS medium for 72 h. Cell viability of the same control cells and osteosarcoma cells, (I) hFOB, (J) NHOst, (K) Q2148, (L) 143B, (M) MG-63, (N) 15454-307 treated with 1.5 µM ONC201, or 0.15 µM ONC206 in 17 mM glucose DMEM-10%FBS medium for 72 h. Cell viability was tested using ANOVA with a post-hoc Tukey test for all comparisons. Box plots identify the median second and third quartiles and the whiskers extend to the smallest and largest values no more than 1.5 times +/- the interquartile range. Points outside that range are considered “outlying” and are plotted individually.

Techniques: Control

2500 cells per well were seeded in 96 well plates with DMEM 10% FBS 12.5 mM glucose medium, and, after culturing overnight, the media was removed and replaced with the same medium with or without 25 nM antimycin A (AA) alone or with 2 mM dichloroacetate (DCA) alone or with a combination of the same concentrations of AA and DCA in (A) healthy osteoblast hFOB cells, (B) primary osteosarcoma 143B or (C) MG63 cells. (D-G) Cells were treated with a combination of 2.5 µM ONC201 (201) and 0.25 µM ONC206 (206), either with just the two-drug treatment or with the addition of 2 mM DCA, or 2 mM metformin (met) in 200 µL medium per well in (D) hFOB, (E) 143B, (F) MG-63 or (G) 15454-307 cells. (H-K) Cells were also treated with a combination of 2.5 µM ONC201, 2 mM DCA, and 2 mM met in 200 µL medium per well in (H) hFOB, (I) 143B, (J) MG-63 or (K) 15454-307 cells. After cells were cultured for 6 days, then MTT cell viability assays were performed with n = 3 biological replicate experiments. Cell viability was tested using ANOVA with a post-hoc Tukey test for all comparisons. Box plots identify the median second and third quartiles and the whiskers extend to the smallest and largest values no more than 1.5 times +/- the interquartile range. Points outside that range are considered “outlying” and are plotted individually.

Journal: bioRxiv

Article Title: In vitro modeling of nutritional and mitochondria-targeted therapies for osteosarcoma

doi: 10.64898/2026.02.19.706776

Figure Lengend Snippet: 2500 cells per well were seeded in 96 well plates with DMEM 10% FBS 12.5 mM glucose medium, and, after culturing overnight, the media was removed and replaced with the same medium with or without 25 nM antimycin A (AA) alone or with 2 mM dichloroacetate (DCA) alone or with a combination of the same concentrations of AA and DCA in (A) healthy osteoblast hFOB cells, (B) primary osteosarcoma 143B or (C) MG63 cells. (D-G) Cells were treated with a combination of 2.5 µM ONC201 (201) and 0.25 µM ONC206 (206), either with just the two-drug treatment or with the addition of 2 mM DCA, or 2 mM metformin (met) in 200 µL medium per well in (D) hFOB, (E) 143B, (F) MG-63 or (G) 15454-307 cells. (H-K) Cells were also treated with a combination of 2.5 µM ONC201, 2 mM DCA, and 2 mM met in 200 µL medium per well in (H) hFOB, (I) 143B, (J) MG-63 or (K) 15454-307 cells. After cells were cultured for 6 days, then MTT cell viability assays were performed with n = 3 biological replicate experiments. Cell viability was tested using ANOVA with a post-hoc Tukey test for all comparisons. Box plots identify the median second and third quartiles and the whiskers extend to the smallest and largest values no more than 1.5 times +/- the interquartile range. Points outside that range are considered “outlying” and are plotted individually.

Techniques: Cell Culture

(A-B) Looking at pediatric cancers with Clp alterations, (A) 1.15% of osteosarcomas have ClpP alterations and (B) 9.20% of osteosarcomas have ClpX alterations. Cancers are given on the x-axis with the y-axis the percentage of alterations across all patients in either (A) ClpP or (B) ClpX. Color indicates the alteration type. (C-E) 90% confluent hFOB or 143B cells in 100 mm Petri dishes were treated with increasing doses of ONC201 or ONC206 indicated in 5.6 mM glucose DMEM, after 24 h, cells were collected and lysed in RIPA buffer. (C) Western immunoblots following SDS-PAGE (immunoblots for ClpP and ClpX are in supplemental figure S4) were imaged with anti-ClpP o r ClpX and anti-CS antibodies, resulting band intensities for the untreated and highest dose of each drug were analyzed by ImageJ, normalized to CS and relative to hFOB for ClpP (D) and ClpX (E) . (F) The differential expression results from 143B cells treated with ONC201 or ONC206 were used to evaluate the overlap in expression changes using an UpSet plot, where the bars show the number of genes changed and a single dot underneath for ONC201 and ONC206, respectively, and the line showing the number of significantly differentially expressed genes in common with both treatments. Pathway analysis, done with over-representation analysis (ORA) in WebGestaltR, on gene expression changes unique to (G) ONC201 alone, (H) ONC206 alone, (I) or common to both versions of the drug. Pathway analysis bar plots give the top five most up- and down-regulated pathways colored by treatment type with non-statistically significant pathways in gray (G-I) .

Journal: bioRxiv

Article Title: In vitro modeling of nutritional and mitochondria-targeted therapies for osteosarcoma

doi: 10.64898/2026.02.19.706776

Figure Lengend Snippet: (A-B) Looking at pediatric cancers with Clp alterations, (A) 1.15% of osteosarcomas have ClpP alterations and (B) 9.20% of osteosarcomas have ClpX alterations. Cancers are given on the x-axis with the y-axis the percentage of alterations across all patients in either (A) ClpP or (B) ClpX. Color indicates the alteration type. (C-E) 90% confluent hFOB or 143B cells in 100 mm Petri dishes were treated with increasing doses of ONC201 or ONC206 indicated in 5.6 mM glucose DMEM, after 24 h, cells were collected and lysed in RIPA buffer. (C) Western immunoblots following SDS-PAGE (immunoblots for ClpP and ClpX are in supplemental figure S4) were imaged with anti-ClpP o r ClpX and anti-CS antibodies, resulting band intensities for the untreated and highest dose of each drug were analyzed by ImageJ, normalized to CS and relative to hFOB for ClpP (D) and ClpX (E) . (F) The differential expression results from 143B cells treated with ONC201 or ONC206 were used to evaluate the overlap in expression changes using an UpSet plot, where the bars show the number of genes changed and a single dot underneath for ONC201 and ONC206, respectively, and the line showing the number of significantly differentially expressed genes in common with both treatments. Pathway analysis, done with over-representation analysis (ORA) in WebGestaltR, on gene expression changes unique to (G) ONC201 alone, (H) ONC206 alone, (I) or common to both versions of the drug. Pathway analysis bar plots give the top five most up- and down-regulated pathways colored by treatment type with non-statistically significant pathways in gray (G-I) .

Techniques: Western Blot, SDS Page, Quantitative Proteomics, Expressing, Gene Expression

Activation of autophagy in chemotherapy‐treated HOS‐143B cells. (A) Dose response curve for cisplatin treatment. (B) Dose response curve for doxorubicin hydrochloride treatment. The HOS‐143B cells were dosed with either cisplatin or doxorubicin hydrochloride in increasing concentrations up to 200 or 20 μM, respectively. (C) Western blotting images of LC3‐I, LC3‐II, p62, and β‐actin protein levels in 5 μM cisplatin‐treated or 0.75 μM doxorubicin hydrochloride‐treated HOS‐143B cells. Untreated HOS‐143B cells served as the control. β‐actin is used as an internal control. Graphical representation of fold changes in protein levels (D) LC3‐II:LC3‐I and (E) p62 protein levels in cisplatin‐treated and doxorubicin hydrochloride‐treated HOS‐143B cells relative to the control. (F) FITC‐LC3 and DAPI immunofluorescence images of HOS‐143B cells treated with cisplatin (10 μM) or doxorubicin hydrochloride (1 μM) for 48 h. Data are expressed as mean ± SD. For all data n = 3 cell culture replicates run in triplicate; * p ≤ 0.05.

Journal: Cancer Medicine

Article Title: Inhibition of Autophagy Reveals ATR Protein Kinase as a Key Mediator of Cisplatin Sensitivity in Osteosarcoma

doi: 10.1002/cam4.71658

Figure Lengend Snippet: Activation of autophagy in chemotherapy‐treated HOS‐143B cells. (A) Dose response curve for cisplatin treatment. (B) Dose response curve for doxorubicin hydrochloride treatment. The HOS‐143B cells were dosed with either cisplatin or doxorubicin hydrochloride in increasing concentrations up to 200 or 20 μM, respectively. (C) Western blotting images of LC3‐I, LC3‐II, p62, and β‐actin protein levels in 5 μM cisplatin‐treated or 0.75 μM doxorubicin hydrochloride‐treated HOS‐143B cells. Untreated HOS‐143B cells served as the control. β‐actin is used as an internal control. Graphical representation of fold changes in protein levels (D) LC3‐II:LC3‐I and (E) p62 protein levels in cisplatin‐treated and doxorubicin hydrochloride‐treated HOS‐143B cells relative to the control. (F) FITC‐LC3 and DAPI immunofluorescence images of HOS‐143B cells treated with cisplatin (10 μM) or doxorubicin hydrochloride (1 μM) for 48 h. Data are expressed as mean ± SD. For all data n = 3 cell culture replicates run in triplicate; * p ≤ 0.05.

Article Snippet: HOS‐143B (ATCC, CRL‐8303, authenticated) cells were cultured in 1× DMEM + GlutaMAX (ThermoFisher Scientific) supplemented with 10% FBS (ThermoFisher Scientific), 1% non‐essential amino acids (ThermoFisher Scientific), 1% sodium pyruvate (ThermoFisher Scientific), and 1% penicillin–streptomycin (ThermoFisher Scientific).

Techniques: Activation Assay, Western Blot, Control, Immunofluorescence, Cell Culture

KO of ATG7 by CRISPR/Cas9 ablates autophagy in HOS‐143B cells. (Ai) Schematic illustration of the binding site of TrueGuide sgRNA on Exon 11 of ATG7 gene. The sgRNA guides the Cas9 endonuclease to the target site for enzymatic double stranded cleavage ( ThermoFisher.com ). (Aii) Gel electrophoresis of PCR product for the cleavage assay shows a 36% reduction of ATG7 expression in the pooled cell population following ATG7 KO. (B) qRT‐PCR relative expression of ATG7 normalized to GAPDH in ATG7 −/− , NTC and WT HOS‐143B cells following single cell clonal isolation for constitutive knockout of ATG7. (C) Western blotting images of ATG7, LC3‐I, LC3‐II, p62, ATG5‐ATG12, ATG5 and β‐actin protein levels in ATG7 −/− , NTC and WT HOS‐143B cells following single cell clonal isolation for constitutive knockout of ATG7 . Graphical representation of fold changes in relative protein levels of (D) ATG7, (E) LC3‐II:LC3‐I, (F) p62, (G) ATG5‐ATG12, (H) ATG5 in ATG7 −/− and NTC compared to the WT HOS‐143B cells. Data are expressed as mean ± SD. For all data n = 3 biological replicates run in triplicate; **** p < 0.0001; *** p < 0.001; ** p < 0.01 (One‐way ANOVA).

Journal: Cancer Medicine

Article Title: Inhibition of Autophagy Reveals ATR Protein Kinase as a Key Mediator of Cisplatin Sensitivity in Osteosarcoma

doi: 10.1002/cam4.71658

Figure Lengend Snippet: KO of ATG7 by CRISPR/Cas9 ablates autophagy in HOS‐143B cells. (Ai) Schematic illustration of the binding site of TrueGuide sgRNA on Exon 11 of ATG7 gene. The sgRNA guides the Cas9 endonuclease to the target site for enzymatic double stranded cleavage ( ThermoFisher.com ). (Aii) Gel electrophoresis of PCR product for the cleavage assay shows a 36% reduction of ATG7 expression in the pooled cell population following ATG7 KO. (B) qRT‐PCR relative expression of ATG7 normalized to GAPDH in ATG7 −/− , NTC and WT HOS‐143B cells following single cell clonal isolation for constitutive knockout of ATG7. (C) Western blotting images of ATG7, LC3‐I, LC3‐II, p62, ATG5‐ATG12, ATG5 and β‐actin protein levels in ATG7 −/− , NTC and WT HOS‐143B cells following single cell clonal isolation for constitutive knockout of ATG7 . Graphical representation of fold changes in relative protein levels of (D) ATG7, (E) LC3‐II:LC3‐I, (F) p62, (G) ATG5‐ATG12, (H) ATG5 in ATG7 −/− and NTC compared to the WT HOS‐143B cells. Data are expressed as mean ± SD. For all data n = 3 biological replicates run in triplicate; **** p < 0.0001; *** p < 0.001; ** p < 0.01 (One‐way ANOVA).

Techniques: CRISPR, Binding Assay, Nucleic Acid Electrophoresis, Cleavage Assay, Expressing, Quantitative RT-PCR, Single Cell, Isolation, Knock-Out, Western Blot

Chemosensitivity and migration of ATG7 knockout HOS‐143B cells. (A) Western blotting images of LC3‐I, LC3‐II, p62 and β‐actin protein levels in ATG7 −/− , NTC and WT HOS‐143B cells treated with 5 μM of cisplatin or 0.75 μM of doxorubicin hydrochloride. Untreated cells served as the control. To assess chemosensitivity, ATG7 −/− , NTC and WT HOS‐143B cells were dosed with DOX and CIS in increasing concentrations up to 200 μM and 20 μM, respectively. (B) The dose response curve for DOX treatment. (C) Graphical representation of IC 50 of DOX. (D) The dose response curve for CIS treatment. (E) Graphical representation of IC 50 of CIS. To assess migration, a scratch assay was carried out and migratory distance was measured after 48 h of incubation. (F) Graphical representation of migratory distance (μm) of ATG7 −/− , NTC and WT HOS‐143B, in DOX or CIS‐treated and untreated conditions. Data are expressed as mean ± SD. For all data n = 3 biological replicates run in triplicate; ** p < 0.01; * p < 0.05 (One‐way ANOVA).

Journal: Cancer Medicine

Article Title: Inhibition of Autophagy Reveals ATR Protein Kinase as a Key Mediator of Cisplatin Sensitivity in Osteosarcoma

doi: 10.1002/cam4.71658

Figure Lengend Snippet: Chemosensitivity and migration of ATG7 knockout HOS‐143B cells. (A) Western blotting images of LC3‐I, LC3‐II, p62 and β‐actin protein levels in ATG7 −/− , NTC and WT HOS‐143B cells treated with 5 μM of cisplatin or 0.75 μM of doxorubicin hydrochloride. Untreated cells served as the control. To assess chemosensitivity, ATG7 −/− , NTC and WT HOS‐143B cells were dosed with DOX and CIS in increasing concentrations up to 200 μM and 20 μM, respectively. (B) The dose response curve for DOX treatment. (C) Graphical representation of IC 50 of DOX. (D) The dose response curve for CIS treatment. (E) Graphical representation of IC 50 of CIS. To assess migration, a scratch assay was carried out and migratory distance was measured after 48 h of incubation. (F) Graphical representation of migratory distance (μm) of ATG7 −/− , NTC and WT HOS‐143B, in DOX or CIS‐treated and untreated conditions. Data are expressed as mean ± SD. For all data n = 3 biological replicates run in triplicate; ** p < 0.01; * p < 0.05 (One‐way ANOVA).

Techniques: Migration, Knock-Out, Western Blot, Control, Wound Healing Assay, Incubation

Chemosensitivity of HOS‐143B cells following co‐administration with ATMi/ATRi. (A) Image showing the relative levels of phospho‐p53 (S15; boxed) in ATG7 −/− and NTC HOS‐143B cells. (B) Graphical representation of relative phosphorylation of p53 (S15). For the dose response assay, HOS‐143B cells were dosed with CIS or DOX in increasing concentrations up to 200 μM or 10 μM respectively alongside 1 μM of either ATMi/KU‐60019 or ATRi/VE‐821. (C) Dose response curve for DOX with/without 1 μM ATMi/ATRi. (D) Graphical representation of IC 50 of DOX with/without 1 μM ATMi/ATRi. (E) Dose response curve for CIS with/without 1 μM ATMi/ATRi. (F) Graphical representation of IC 50 values of CIS with/without 1 μM ATMi/ATRi. (G) Dose response curve of CIS combined with/without ATRi A–D. (H) Graphical representation of IC 50 values of CIS with/without ATRi A–D. VE‐821/ATRi A, BAY1895344/ATRi B, AZD6738/ATRi C and AZ20/ATRi D. 1 μM of ATRi A, ATRi C and ATRi D and 0.1 μM of ATRi B. Data are expressed as mean ± SD. For all data n = 3 biological replicates run in triplicate; ** p < 0.01; * p < 0.05 (two‐sample t ‐test vs. control).

Journal: Cancer Medicine

Article Title: Inhibition of Autophagy Reveals ATR Protein Kinase as a Key Mediator of Cisplatin Sensitivity in Osteosarcoma

doi: 10.1002/cam4.71658

Figure Lengend Snippet: Chemosensitivity of HOS‐143B cells following co‐administration with ATMi/ATRi. (A) Image showing the relative levels of phospho‐p53 (S15; boxed) in ATG7 −/− and NTC HOS‐143B cells. (B) Graphical representation of relative phosphorylation of p53 (S15). For the dose response assay, HOS‐143B cells were dosed with CIS or DOX in increasing concentrations up to 200 μM or 10 μM respectively alongside 1 μM of either ATMi/KU‐60019 or ATRi/VE‐821. (C) Dose response curve for DOX with/without 1 μM ATMi/ATRi. (D) Graphical representation of IC 50 of DOX with/without 1 μM ATMi/ATRi. (E) Dose response curve for CIS with/without 1 μM ATMi/ATRi. (F) Graphical representation of IC 50 values of CIS with/without 1 μM ATMi/ATRi. (G) Dose response curve of CIS combined with/without ATRi A–D. (H) Graphical representation of IC 50 values of CIS with/without ATRi A–D. VE‐821/ATRi A, BAY1895344/ATRi B, AZD6738/ATRi C and AZ20/ATRi D. 1 μM of ATRi A, ATRi C and ATRi D and 0.1 μM of ATRi B. Data are expressed as mean ± SD. For all data n = 3 biological replicates run in triplicate; ** p < 0.01; * p < 0.05 (two‐sample t ‐test vs. control).

Techniques: Phospho-proteomics, Control

Pharmacological inhibition of ATR enhanced apoptosis and blocked p53 phosphorylation and autophagy. (A) Annexin V/PI staining of HOS‐143B cells with/without 5 μM CIS and/or 0.01 μM ATRi, BAY‐1895344. Quadrant guide: Lower left = live cells; Lower right, early apoptosis; Upper left, necrosis; Upper right, late apoptosis. (B) Percentage of the live, early and late apoptotic and necrotic cell population. (C) Statistical analysis of live, early and late apoptotic and necrotic cell population. (D) Western blotting images of total p53, phospho‐p53 and β‐actin protein levels in HOS‐143B cells treated with either 5 μM CIS or 0.01 μM ATRi, or a combination of both. Untreated cells served as the control. Graphical representation of fold changes in protein levels of (E) Total p53 and (F) phospho‐p53 relative to the control. (G) Western blotting images of ATG7, LC3‐I, LC3‐II, and β‐actin protein levels in HOS‐143B cells treated with either 5 μM CIS or 0.01 μM ATRi, or a combination of both. Untreated cells served as the control. Graphical representation of fold changes in protein levels of (H) ATG7 (I) LC3‐II:LC3‐I, and (J) p62 relative to the control. Data are expressed as mean ± SD. For all data n = 3 biological replicates run in triplicate; **** p < 0.0001; *** p < 0.001; ** p < 0.01; * p ≤ 0.05 (flow cytometry: One‐way ANOVA; Western blot: two‐sample t ‐test vs. control).

Journal: Cancer Medicine

Article Title: Inhibition of Autophagy Reveals ATR Protein Kinase as a Key Mediator of Cisplatin Sensitivity in Osteosarcoma

doi: 10.1002/cam4.71658

Figure Lengend Snippet: Pharmacological inhibition of ATR enhanced apoptosis and blocked p53 phosphorylation and autophagy. (A) Annexin V/PI staining of HOS‐143B cells with/without 5 μM CIS and/or 0.01 μM ATRi, BAY‐1895344. Quadrant guide: Lower left = live cells; Lower right, early apoptosis; Upper left, necrosis; Upper right, late apoptosis. (B) Percentage of the live, early and late apoptotic and necrotic cell population. (C) Statistical analysis of live, early and late apoptotic and necrotic cell population. (D) Western blotting images of total p53, phospho‐p53 and β‐actin protein levels in HOS‐143B cells treated with either 5 μM CIS or 0.01 μM ATRi, or a combination of both. Untreated cells served as the control. Graphical representation of fold changes in protein levels of (E) Total p53 and (F) phospho‐p53 relative to the control. (G) Western blotting images of ATG7, LC3‐I, LC3‐II, and β‐actin protein levels in HOS‐143B cells treated with either 5 μM CIS or 0.01 μM ATRi, or a combination of both. Untreated cells served as the control. Graphical representation of fold changes in protein levels of (H) ATG7 (I) LC3‐II:LC3‐I, and (J) p62 relative to the control. Data are expressed as mean ± SD. For all data n = 3 biological replicates run in triplicate; **** p < 0.0001; *** p < 0.001; ** p < 0.01; * p ≤ 0.05 (flow cytometry: One‐way ANOVA; Western blot: two‐sample t ‐test vs. control).

Techniques: Inhibition, Phospho-proteomics, Staining, Western Blot, Control, Flow Cytometry

K7M2 murine osteosarcoma cells and 143B human osteosarcoma cells are highly dependent on methionine in vitro. The EC 50 of methionine of K7M2 and 143B cells was determined by treating the cells with various concentrations of methionine for 96 h. Cell viability was measured using the WST-8 cell-viability reagent. Experiments were repeated three times, in triplicate. Data are shown as mean±standard deviation. The concentration axis is scaled in log2. EC 50 : Half-maximal effective concentration. Please see the Materials and Methods for details.

Journal: In Vivo

Article Title: Methionine Restriction Alone Induces T-cell-mediated Immunotherapy of Osteosarcoma in a Syngeneic Mouse Model

doi: 10.21873/invivo.14239

Figure Lengend Snippet: K7M2 murine osteosarcoma cells and 143B human osteosarcoma cells are highly dependent on methionine in vitro. The EC 50 of methionine of K7M2 and 143B cells was determined by treating the cells with various concentrations of methionine for 96 h. Cell viability was measured using the WST-8 cell-viability reagent. Experiments were repeated three times, in triplicate. Data are shown as mean±standard deviation. The concentration axis is scaled in log2. EC 50 : Half-maximal effective concentration. Please see the Materials and Methods for details.

Article Snippet: The K7M2 murine osteosarcoma cell line and 143B human osteosarcoma cell line were obtained from the American Type Culture Collection (Manassas, VA, USA).

Techniques: In Vitro, Standard Deviation, Concentration Assay

Expression of PD-L1 in K7M2 and 143B cells decreased with methionine-restricted (MR) medium. (A) The expression of PD-L1 was measured in K7M2 and 143B cells treated with the EC 50 of methionine as MR for 96 h. Western blotting was performed for analysis of PD-L1 in three independent samples. GAPDH was used as a loading control. (B) Quantitative comparisons of PD-L1 expression in 143B and K7M2 cells determined by western blot are shown as mean±standard deviation. EC 50 : Half-maximal effective concentration; MR: methionine restriction. *p<0.05. Please see the Materials and Methods for details.

Journal: In Vivo

Article Title: Methionine Restriction Alone Induces T-cell-mediated Immunotherapy of Osteosarcoma in a Syngeneic Mouse Model

doi: 10.21873/invivo.14239

Figure Lengend Snippet: Expression of PD-L1 in K7M2 and 143B cells decreased with methionine-restricted (MR) medium. (A) The expression of PD-L1 was measured in K7M2 and 143B cells treated with the EC 50 of methionine as MR for 96 h. Western blotting was performed for analysis of PD-L1 in three independent samples. GAPDH was used as a loading control. (B) Quantitative comparisons of PD-L1 expression in 143B and K7M2 cells determined by western blot are shown as mean±standard deviation. EC 50 : Half-maximal effective concentration; MR: methionine restriction. *p<0.05. Please see the Materials and Methods for details.

Article Snippet: The K7M2 murine osteosarcoma cell line and 143B human osteosarcoma cell line were obtained from the American Type Culture Collection (Manassas, VA, USA).

Techniques: Expressing, Western Blot, Control, Standard Deviation, Concentration Assay

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