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Figure 5. Interference with <t>endogenous</t> <t>HMGB1</t> expression increases the sensitivity of HeLa cells to cisplatin. (A) HMGB1 protein expression levels were detected by western blotting in cytoplasmic and nuclear extracts from HeLa cells transfected with HMGB1 <t>shRNA</t> or NC shRNA, and incubated with/without 10 µg/ml cisplatin for 24 h. β‑Tubulin was used as a cytoplasmic marker and lamin B1 as a nuclear marker. (B) Growth inhibition rates were determined by MTT assay in HeLa and HeLa/DDP cells transfected with HMGB1 shRNA or NC shRNA, and incubated with 10 µg/ml cisplatin for 24, 48 and 72 h. **P<0.01, with comparisons indicated by brackets. HMGB1, high mobility group box 1 protein; ctrl, control; shRNA, short hairpin RNA; NC, negative control.
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Figure 5. Interference with <t>endogenous</t> <t>HMGB1</t> expression increases the sensitivity of HeLa cells to cisplatin. (A) HMGB1 protein expression levels were detected by western blotting in cytoplasmic and nuclear extracts from HeLa cells transfected with HMGB1 <t>shRNA</t> or NC shRNA, and incubated with/without 10 µg/ml cisplatin for 24 h. β‑Tubulin was used as a cytoplasmic marker and lamin B1 as a nuclear marker. (B) Growth inhibition rates were determined by MTT assay in HeLa and HeLa/DDP cells transfected with HMGB1 shRNA or NC shRNA, and incubated with 10 µg/ml cisplatin for 24, 48 and 72 h. **P<0.01, with comparisons indicated by brackets. HMGB1, high mobility group box 1 protein; ctrl, control; shRNA, short hairpin RNA; NC, negative control.
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Figure 5. Interference with <t>endogenous</t> <t>HMGB1</t> expression increases the sensitivity of HeLa cells to cisplatin. (A) HMGB1 protein expression levels were detected by western blotting in cytoplasmic and nuclear extracts from HeLa cells transfected with HMGB1 <t>shRNA</t> or NC shRNA, and incubated with/without 10 µg/ml cisplatin for 24 h. β‑Tubulin was used as a cytoplasmic marker and lamin B1 as a nuclear marker. (B) Growth inhibition rates were determined by MTT assay in HeLa and HeLa/DDP cells transfected with HMGB1 shRNA or NC shRNA, and incubated with 10 µg/ml cisplatin for 24, 48 and 72 h. **P<0.01, with comparisons indicated by brackets. HMGB1, high mobility group box 1 protein; ctrl, control; shRNA, short hairpin RNA; NC, negative control.
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Figure 5. Interference with <t>endogenous</t> <t>HMGB1</t> expression increases the sensitivity of HeLa cells to cisplatin. (A) HMGB1 protein expression levels were detected by western blotting in cytoplasmic and nuclear extracts from HeLa cells transfected with HMGB1 <t>shRNA</t> or NC shRNA, and incubated with/without 10 µg/ml cisplatin for 24 h. β‑Tubulin was used as a cytoplasmic marker and lamin B1 as a nuclear marker. (B) Growth inhibition rates were determined by MTT assay in HeLa and HeLa/DDP cells transfected with HMGB1 shRNA or NC shRNA, and incubated with 10 µg/ml cisplatin for 24, 48 and 72 h. **P<0.01, with comparisons indicated by brackets. HMGB1, high mobility group box 1 protein; ctrl, control; shRNA, short hairpin RNA; NC, negative control.
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Figure 5. Interference with <t>endogenous</t> <t>HMGB1</t> expression increases the sensitivity of HeLa cells to cisplatin. (A) HMGB1 protein expression levels were detected by western blotting in cytoplasmic and nuclear extracts from HeLa cells transfected with HMGB1 <t>shRNA</t> or NC shRNA, and incubated with/without 10 µg/ml cisplatin for 24 h. β‑Tubulin was used as a cytoplasmic marker and lamin B1 as a nuclear marker. (B) Growth inhibition rates were determined by MTT assay in HeLa and HeLa/DDP cells transfected with HMGB1 shRNA or NC shRNA, and incubated with 10 µg/ml cisplatin for 24, 48 and 72 h. **P<0.01, with comparisons indicated by brackets. HMGB1, high mobility group box 1 protein; ctrl, control; shRNA, short hairpin RNA; NC, negative control.
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OriGene adenoviral vector control
Effect of <t>adenoviral</t> catalase (Ad.CAT) gene transfection on REST protein expression in AVG neurons from T2DM. Raw images (top panel) and quantitative data (bottom panel) representing the REST protein levels in AVG neurons from all groups of rats, analyzed by reverse-phase protein microarray. Black dots represent each individual data point. N = 12 measurements from 6 rats/group. Data are means ± SEM. One-way ANOVA with post-hoc Bonferroni test was used to assess statistical significance. * p < 0.05 vs. sham; # p < 0.05 vs. T2DM.
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Effect of <t>adenoviral</t> catalase (Ad.CAT) gene transfection on REST protein expression in AVG neurons from T2DM. Raw images (top panel) and quantitative data (bottom panel) representing the REST protein levels in AVG neurons from all groups of rats, analyzed by reverse-phase protein microarray. Black dots represent each individual data point. N = 12 measurements from 6 rats/group. Data are means ± SEM. One-way ANOVA with post-hoc Bonferroni test was used to assess statistical significance. * p < 0.05 vs. sham; # p < 0.05 vs. T2DM.
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Effect of <t>adenoviral</t> catalase (Ad.CAT) gene transfection on REST protein expression in AVG neurons from T2DM. Raw images (top panel) and quantitative data (bottom panel) representing the REST protein levels in AVG neurons from all groups of rats, analyzed by reverse-phase protein microarray. Black dots represent each individual data point. N = 12 measurements from 6 rats/group. Data are means ± SEM. One-way ANOVA with post-hoc Bonferroni test was used to assess statistical significance. * p < 0.05 vs. sham; # p < 0.05 vs. T2DM.
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Effect of <t>adenoviral</t> catalase (Ad.CAT) gene transfection on REST protein expression in AVG neurons from T2DM. Raw images (top panel) and quantitative data (bottom panel) representing the REST protein levels in AVG neurons from all groups of rats, analyzed by reverse-phase protein microarray. Black dots represent each individual data point. N = 12 measurements from 6 rats/group. Data are means ± SEM. One-way ANOVA with post-hoc Bonferroni test was used to assess statistical significance. * p < 0.05 vs. sham; # p < 0.05 vs. T2DM.
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Image Search Results


KEY RESOURCES TABLE

Journal: Cell stem cell

Article Title: TFAP2C- and p63-Dependent Networks Sequentially Rearrange Chromatin Landscapes to Drive Human Epidermal Lineage Commitment

doi: 10.1016/j.stem.2018.12.012

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: Scrambled negative control non-effective shRNA , Origene , Cat #TR30021.

Techniques: Purification, Recombinant, Knock-Out, Blocking Assay, Plasmid Preparation, Cloning, One Step RT-PCR, SYBR Green Assay, Magnetic Beads, Staining, Sequencing, CRISPR, Negative Control, shRNA, Expressing, Software

Figure 5. Interference with endogenous HMGB1 expression increases the sensitivity of HeLa cells to cisplatin. (A) HMGB1 protein expression levels were detected by western blotting in cytoplasmic and nuclear extracts from HeLa cells transfected with HMGB1 shRNA or NC shRNA, and incubated with/without 10 µg/ml cisplatin for 24 h. β‑Tubulin was used as a cytoplasmic marker and lamin B1 as a nuclear marker. (B) Growth inhibition rates were determined by MTT assay in HeLa and HeLa/DDP cells transfected with HMGB1 shRNA or NC shRNA, and incubated with 10 µg/ml cisplatin for 24, 48 and 72 h. **P<0.01, with comparisons indicated by brackets. HMGB1, high mobility group box 1 protein; ctrl, control; shRNA, short hairpin RNA; NC, negative control.

Journal: Molecular medicine reports

Article Title: Inhibiting the cytoplasmic location of HMGB1 reverses cisplatin resistance in human cervical cancer cells.

doi: 10.3892/mmr.2016.6003

Figure Lengend Snippet: Figure 5. Interference with endogenous HMGB1 expression increases the sensitivity of HeLa cells to cisplatin. (A) HMGB1 protein expression levels were detected by western blotting in cytoplasmic and nuclear extracts from HeLa cells transfected with HMGB1 shRNA or NC shRNA, and incubated with/without 10 µg/ml cisplatin for 24 h. β‑Tubulin was used as a cytoplasmic marker and lamin B1 as a nuclear marker. (B) Growth inhibition rates were determined by MTT assay in HeLa and HeLa/DDP cells transfected with HMGB1 shRNA or NC shRNA, and incubated with 10 µg/ml cisplatin for 24, 48 and 72 h. **P<0.01, with comparisons indicated by brackets. HMGB1, high mobility group box 1 protein; ctrl, control; shRNA, short hairpin RNA; NC, negative control.

Article Snippet: The human HMGB1 short hairpin (sh) RNAs (cat. no. TG316576) and negative control (NC) shRNA (cat. no. TR30013) were obtained from OriGene Technologies, Inc. (Rockville, MD, USA).

Techniques: Expressing, Western Blot, Transfection, shRNA, Incubation, Marker, Inhibition, MTT Assay, Control, Negative Control

Figure 6. Transfection with HMGB1 induces cell apoptosis in HeLa cells. HeLa cells were transfected with HMGB1 shRNA or NC shRNA and treated with 10 µg/ml of cisplatin for 48 h. (A) Cell apoptosis was detected by an Annexin V‑PI dual staining analysis, **P<0.01 (B). Expression levels of apoptosis‑related proteins were detected by western blot analysis of whole cell lysates. β‑actin was used as an internal control (C). HMGB1, high mobility group box protein 1; shRNA, short hairpin RNA; NC, negative control; ctrl, control; PI, propidium iodide; PARP, poly ADP ribose polymerase.

Journal: Molecular medicine reports

Article Title: Inhibiting the cytoplasmic location of HMGB1 reverses cisplatin resistance in human cervical cancer cells.

doi: 10.3892/mmr.2016.6003

Figure Lengend Snippet: Figure 6. Transfection with HMGB1 induces cell apoptosis in HeLa cells. HeLa cells were transfected with HMGB1 shRNA or NC shRNA and treated with 10 µg/ml of cisplatin for 48 h. (A) Cell apoptosis was detected by an Annexin V‑PI dual staining analysis, **P<0.01 (B). Expression levels of apoptosis‑related proteins were detected by western blot analysis of whole cell lysates. β‑actin was used as an internal control (C). HMGB1, high mobility group box protein 1; shRNA, short hairpin RNA; NC, negative control; ctrl, control; PI, propidium iodide; PARP, poly ADP ribose polymerase.

Article Snippet: The human HMGB1 short hairpin (sh) RNAs (cat. no. TG316576) and negative control (NC) shRNA (cat. no. TR30013) were obtained from OriGene Technologies, Inc. (Rockville, MD, USA).

Techniques: Transfection, shRNA, Staining, Expressing, Western Blot, Control, Negative Control

Figure 7. Cell autophagy induced by HMGB1 treatment in HeLa cells is mediated by the ERK1/2 pathway. Western blot analysis of LC3‑I, LC3‑II, p62, ERK1/2 and p‑ERK1/2 protein levels was performed in (A) 24 h serum‑starved HeLa cells, treated with 100 µg/ml rhHMGB1 or 100 µg/ml BSA for 48 h, and (B) HeLa cells transfected with NC shRNA and HMGB1 shRNA. β‑actin was used as a loading control. HMGB1, high mobility group box protein 1; ERK1/2, extracellular signal‑related kinases 1 and 2; LC3, microtubule associated protein 1 light chain 3; shRNA, short hairpin RNA; NC, negative control; p62, nucleoporin p62; p, phosphorylated; BSA, bovine serum albumin; rh, recombinant human.

Journal: Molecular medicine reports

Article Title: Inhibiting the cytoplasmic location of HMGB1 reverses cisplatin resistance in human cervical cancer cells.

doi: 10.3892/mmr.2016.6003

Figure Lengend Snippet: Figure 7. Cell autophagy induced by HMGB1 treatment in HeLa cells is mediated by the ERK1/2 pathway. Western blot analysis of LC3‑I, LC3‑II, p62, ERK1/2 and p‑ERK1/2 protein levels was performed in (A) 24 h serum‑starved HeLa cells, treated with 100 µg/ml rhHMGB1 or 100 µg/ml BSA for 48 h, and (B) HeLa cells transfected with NC shRNA and HMGB1 shRNA. β‑actin was used as a loading control. HMGB1, high mobility group box protein 1; ERK1/2, extracellular signal‑related kinases 1 and 2; LC3, microtubule associated protein 1 light chain 3; shRNA, short hairpin RNA; NC, negative control; p62, nucleoporin p62; p, phosphorylated; BSA, bovine serum albumin; rh, recombinant human.

Article Snippet: The human HMGB1 short hairpin (sh) RNAs (cat. no. TG316576) and negative control (NC) shRNA (cat. no. TR30013) were obtained from OriGene Technologies, Inc. (Rockville, MD, USA).

Techniques: Western Blot, Transfection, shRNA, Control, Negative Control, Recombinant

Effect of adenoviral catalase (Ad.CAT) gene transfection on REST protein expression in AVG neurons from T2DM. Raw images (top panel) and quantitative data (bottom panel) representing the REST protein levels in AVG neurons from all groups of rats, analyzed by reverse-phase protein microarray. Black dots represent each individual data point. N = 12 measurements from 6 rats/group. Data are means ± SEM. One-way ANOVA with post-hoc Bonferroni test was used to assess statistical significance. * p < 0.05 vs. sham; # p < 0.05 vs. T2DM.

Journal: Antioxidants

Article Title: Hydrogen Peroxide-Induced Re-Expression of Repressor Element 1-Silencing Transcription Factor Contributes to Cardiac Vagal Dysfunction in Type 2 Diabetes Mellitus

doi: 10.3390/antiox14050588

Figure Lengend Snippet: Effect of adenoviral catalase (Ad.CAT) gene transfection on REST protein expression in AVG neurons from T2DM. Raw images (top panel) and quantitative data (bottom panel) representing the REST protein levels in AVG neurons from all groups of rats, analyzed by reverse-phase protein microarray. Black dots represent each individual data point. N = 12 measurements from 6 rats/group. Data are means ± SEM. One-way ANOVA with post-hoc Bonferroni test was used to assess statistical significance. * p < 0.05 vs. sham; # p < 0.05 vs. T2DM.

Article Snippet: Under the microscope, 2 μL of saline, adenoviral catalase gene (Ad.CAT, 1 × 10 10 pfu/mL, University of Iowa, Iowa City, IA, USA), adenoviral vector control (Ad.Empty, 1 × 10 10 pfu/mL, University of Iowa, Iowa City, IA, USA), rat lentiviral REST shRNA (Lenti.REST shRNA, 29mer target-specific shRNA designed against multiple slice variants based on NM_031788 and NM_031788.1 , 1 × 10 7 TU/mL, CAT#: TL711581V, OriGene Technologies, Inc., Rockville, MD, USA), or lentiviral scrambled shRNA (Lenti.scrambled shRNA, lenti particles carrying a 29mer scrambled shRNA sequence cassette, 1 × 10 7 TU/mL, CAT#: TR30021V, OriGene Technologies, Inc., Rockville, MD, USA) was microinjected into the AVG by a glass micropipette connected to a WPI Nanoliter 2000 microinjector (World Precision Instruments, Sarasota, FL, USA).

Techniques: Transfection, Expressing, Microarray