Journal: bioRxiv

Article Title: Elimination of senescent cells with senolytic host-directed therapy reduces tuberculosis progression in mice

doi: 10.1101/2025.03.28.645957

Figure Lengend Snippet: (a) Schematics of the experimental strategy to measure senescence markers (p21, p16 and SA-βGal activity) and SASP cytokines levels in mice lungs at 10 and 20 days p.i. Day 1 CFU= 55. (b) %p21+p16+ and (c) %SA-βGal+ (CellEvent Senescence green+) cells out of all live lung (uninfected and Mtb- infected mice) and Spleen ( Mtb- infected mice) cells at 10 days p.i. as determined by multicolor flow cytometry. (d) %p21+p16+ and (e) %SA-βGal+ cells out of different lung-cell types at 10 days p.i., as determined by multicolor flow cytometry. Gating for p16⁺, p21⁺, and SA-βGal⁺ events for each cell type were established using reference cells from Mtb -infected WT B6 mice (set at 1 %). (AMs: Alveolar macrophages, IMs: Interstitial macrophages) (f) Normalized concentration of SASP-cytokines in lung homogenates at 20 dpi and 4 wpi as measured by a LEGENDplex™ Mouse Inflammation Panel (13-plex). The data are means ± SEM. Each data point represents a mouse (n=11-12). (two-way ANOVA with Tukey’s (b-e) or Dunnett’s (f) multiple comparisons test).

Article Snippet: The PVDF membranes were blocked using 5% Blotting-grade blocker (Bio-Rad; 1706404) in TBST buffer-Tris-buffered saline (Quality Biological; 351086101)+ 0.1% Tween 20 (Sigma; P2287) for 1-2 hour and incubated overnight at 4°C with the primary antibodies from Mouse Reactive Senescence Marker Antibody Sampler Kit (Cell Signaling Technology-78551)-Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb (1: 1000 dilution), Lamin B1 (E6M5T) Rabbit mAb (1: 1000 dilution), HMGB1 (D3E5) Rabbit mAb (1: 1000 dilution), p16 INK4A (E5F3Y) Rabbit mAb (1: 1000 dilution) and β-Actin (D6A8) Rabbit mAb (Cell Signaling Technology; 8457) (1:5000 dilution).

Techniques: Activity Assay, Infection, Flow Cytometry, Concentration Assay

Journal: bioRxiv

Article Title: Elimination of senescent cells with senolytic host-directed therapy reduces tuberculosis progression in mice

doi: 10.1101/2025.03.28.645957

Figure Lengend Snippet: (a) Representative H&E-stained images of Mtb -infected mice lungs treated with Vehicle or drugs, and respective ImageJ-based quantification. Yellow arrow indicates necrotic granuloma in Vehicle treated B6.Sst1S mice at 5 wpi. The data are means ± SEM. Each data point represents a mouse. Statistical analysis between two groups was done by unpaired two-tailed Student’s t test. Square represents necrotic granuloma formation in the lung. (b) Representative γH2A.X-Immunohistochemistry images of mice after lungs vehicle/ drugs treatment, and respective Violin plots to show ImageJ quantification of γH2A.X-stained area. Each data point represents a mouse. Statistical analysis between two groups was done by unpaired two-tailed Student’s t test. (c) %p21+βGal+ and %p16+βGal+ subpopulation observed in all live lung cells of Mtb -infected mice (n= 5-8). The data are means ± SEM. Each data point represents a mouse. Statistical analysis was calculated by two-way ANOVA with Dunnett’s multiple comparisons test. Bubble plot to show %p21+βGal+ and %p16+βGal+ subpopulation in different lung cell types in Mtb -infected (d) B6.Sst1S mice (n= 8) and (e) WT B6 old mice (n= 5) at indicated time point and treatment groups. The size of the bubble indicates %subpopulation out of all of particular cell types and color is adjusted p values relative to Veh group. Statistics are calculated by one-way ANOVA with Tukey’s multiple comparisons test ( p > 0.15: ns).

Article Snippet: The PVDF membranes were blocked using 5% Blotting-grade blocker (Bio-Rad; 1706404) in TBST buffer-Tris-buffered saline (Quality Biological; 351086101)+ 0.1% Tween 20 (Sigma; P2287) for 1-2 hour and incubated overnight at 4°C with the primary antibodies from Mouse Reactive Senescence Marker Antibody Sampler Kit (Cell Signaling Technology-78551)-Phospho-Histone H2A.X (Ser139) (20E3) Rabbit mAb (1: 1000 dilution), Lamin B1 (E6M5T) Rabbit mAb (1: 1000 dilution), HMGB1 (D3E5) Rabbit mAb (1: 1000 dilution), p16 INK4A (E5F3Y) Rabbit mAb (1: 1000 dilution) and β-Actin (D6A8) Rabbit mAb (Cell Signaling Technology; 8457) (1:5000 dilution).

Techniques: Staining, Infection, Two Tailed Test, Immunohistochemistry

Journal: The Journal of clinical endocrinology and metabolism

Article Title: Inactivation of the p16 tumor suppressor gene in adrenocortical tumors.

doi: 10.1210/jcem.84.8.5877

Figure Lengend Snippet: FIG. 4. a, Adrenocortical carcinoma showing a nearly complete neg- ative p16 nuclear immunostaining (frozen tissue; magnification, 3250); b, adrenocortical adenoma with unreactive nuclei and adja- cent normal tissue intensely positive (paraffin-embedded tissue; mag- nification, 325).

Article Snippet: Endogenous peroxidase was blocked with 0.3% hydrogen peroxide for 30 min. Tissues were incubated overnight at 4 C with the primary antibody anti-p16 (F-12, Santa Cruz Biotechnology, Inc.) diluted 1:250.

Techniques: Immunostaining

Journal: Oncology reports

Article Title: Radiosensitization of esophageal carcinoma cells by knockdown of HMGB1 expression.

doi: 10.3892/or.2018.6923

Figure Lengend Snippet: Figure 4. Suppression of HMGB1 increases the apoptosis rates of esophageal carcinoma cells after IR in vitro and affects the generation of apoptosis‑related proteins. (A) The apoptotic rate was calculated as the sum of B2 and B4. As the results revealed, compared with the NC group, silencing of HMGB1 sensitized ECA109 and TE13 cells to apoptosis both with 6 Gy radiation (A, lower images) and without (A, upper images). (B) After transfection with HMGB1‑shRNA, the expression of Bcl‑2 was attenuated, while the expression of Bax and caspase‑9 was increased in ECA109 and TE13 cells. (C) HMGB1‑shRNA and irradia- tion induced G0/G1 arrest in ESCC cells. (D) The results of flow cytometry revealed that the percentages of G0/G1‑phase cells in the HMGB1‑shRNA groups were significantly higher compared to those of the NC groups before IR, and the HMGB1‑shRNA group percentages significantly increased after irradiation. (E) In the HMGB1‑shRNA group, the expression of cyclin D1 and CDK4 was attenuated, while the expression of p16 was increased. Additionally, irradiation inhibited cyclin D1 and CDK4 expression in esophageal tumor cells. A comparison with the NC group is symbolized by an asterisk *P<0.05; and a comparison with the corresponding non‑irradiated group is symbolized by triangle ▲▲P<0.01. HMGB1, high mobility group box 1; IR, irradiation.

Article Snippet: The relevant antibodies were anti-HMGB1 (dilution 1:10,000; cat. no. ab79823), anti-γH2AX (di lut ion 1:1,000; cat. no. ab26350; Abcam), anti-MMP-2 (dilution 1:1,000; cat. no. 10373-2-AP), anti-MMP-9 (dilution 1:1,000; cat. no. 10375-2-AP), anti-p16 (cat. no. 10883-1-AP), anti-caspase-9 (dilution 1:1,000; cat. no. 10380-1-AP), anti-Bcl-2 (dilution 1:2,000; cat. no. 12789-1-AP), anti-CDK4 (dilution 1:2,000; cat. no. 11026-1-AP), anti-cyclin D1 (dilution 1:5,000; cat. no. 60186-1-lg), anti-Bax (dilution 1:5,000; cat. no. 50599-2-lg; ProteinTech Group, Inc., Chicago, IL, USA) and anti-β-actin (dilution 1:10,000; cat. no. AP0060; Bioworld Technology, Inc., St. Louis Park, MN, USA).

Techniques: In Vitro, Transfection, Expressing, Flow Cytometry, Irradiation, Comparison

Journal: BMC molecular and cell biology

Article Title: LEP O-GlcNAcylation inactivates NF-κB pathway by suppressing LEP protein level and thus mediates cellular senescence and osteogenic differentiation in mouse mesenchymal stem cells.

doi: 10.1186/s12860-024-00523-7

Figure Lengend Snippet: Fig. 2 Etoposide increased LEP expression and promotes cellular senescence in C3H10T1/2 cells (A) The expression of LEP was measured using qPCR. (B and C) Cellular senescence was assessed by β-galactosidase staining. (D and E) qPCR was performed to measure the expression of aging markers p21 and p16. (F) The protein levels of p21 and p16 were evaluated by western blot

Article Snippet: The primary antibodies used in this study were as follows: anti-p21 (1/1000, ab109520, Abcam), anti-p16 (1/1000, #80772, CellSignaling, Danvers, MA, USA), anti-ALP (1/1000, ab307726, Abcam), anti-COL1A1 (1/1000, ab34710, Abcam), antiRUNX2 (1/1000, ab236639, Abcam), anti-p65 (1/1000, ab32536, Abcam), anti-p-p65 (1/1000, ab76302, Abcam), anti-OGT (1/1000, ab96718), anti-OGA (1/5000, ab124807), anti-LEP (1/1000, ab16227, Abcam), antiGAPDH (1/10000, ab181602, Abcam), anti-Lamin B (1/10000, ab133741, Abcam) and anti-O-GlcNAc (1: 1000, MA1-072, Thermo Scientific, Waltham, MA, USA).

Techniques: Expressing, Staining, Western Blot

Journal: BMC molecular and cell biology

Article Title: LEP O-GlcNAcylation inactivates NF-κB pathway by suppressing LEP protein level and thus mediates cellular senescence and osteogenic differentiation in mouse mesenchymal stem cells.

doi: 10.1186/s12860-024-00523-7

Figure Lengend Snippet: Fig. 3 LEP knockdown inhibited etoposide-induced cellular senescence in C3H10T1/2 cells (A) The expression of LEP was measured using qPCR. (B and C) Cellular senescence was assessed by β-galactosidase staining. (D and E) qPCR was performed to measure the expression of aging markers p21 and p16. (F) The protein levels of p21 and p16 were evaluated by western blot

Article Snippet: The primary antibodies used in this study were as follows: anti-p21 (1/1000, ab109520, Abcam), anti-p16 (1/1000, #80772, CellSignaling, Danvers, MA, USA), anti-ALP (1/1000, ab307726, Abcam), anti-COL1A1 (1/1000, ab34710, Abcam), antiRUNX2 (1/1000, ab236639, Abcam), anti-p65 (1/1000, ab32536, Abcam), anti-p-p65 (1/1000, ab76302, Abcam), anti-OGT (1/1000, ab96718), anti-OGA (1/5000, ab124807), anti-LEP (1/1000, ab16227, Abcam), antiGAPDH (1/10000, ab181602, Abcam), anti-Lamin B (1/10000, ab133741, Abcam) and anti-O-GlcNAc (1: 1000, MA1-072, Thermo Scientific, Waltham, MA, USA).

Techniques: Knockdown, Expressing, Staining, Western Blot

Journal: Cells

Article Title: Artesunate Inhibits the Cell Growth in Colorectal Cancer by Promoting ROS-Dependent Cell Senescence and Autophagy

doi: 10.3390/cells11162472

Figure Lengend Snippet: Artesunate caused excessive mitochondrial ROS to induce cell senescence and inhibit cell proliferation. ( A ) Artesunate arrested cell cycle at G0/G1 phase in SW480 and HCT116. Cells were seeded in 6-well plates. Once attached, cells were maintained in FBS-free medium for about 16~24 h. Afterwards, cell were treated with artesunate (1, 2, and 4 μM in medium containing 10% FBS) for 72 h and then harvested for PI staining to analyze cell cycle by flow cytometry. ( B ) Artesunate induced cell senescence in SW480 and HCT116. Cells were seeded in 6-well plates and treated with artesunate (1, 2, and 4 μM) for 72 h. Cell senescence was represented via SA-β-gal activity, which was assayed using a SA-β-gal staining kit after artesunate treatment. ( C ) Artesunate treatment downregulated the protein levels of CDK 2/4/6 and upregulated the protein levels of CDKIs, p16, and p21 in SW480 and HCT116. Cells were seeded in 60 mm dishes and treated with artesunate (1, 2, and 4 μM) for 72 h. Then, cells were lysed with RIPA to extract total protein. The protein levels were measured by western blotting. The gray values of protein blots were evaluated by Image J. Relative protein expression was normalized to β-actin. ( D ) NAC attenuated the effect of artesunate on protein expression of p16 in SW480 and HCT116. NAC was used at a concentration of 2 mM and added alone or together with artesunate (4 μM) for 72 h. * p < 0.05, ** p < 0.01, and *** p < 0.001 vs. Ctrl. ### p < 0.001 vs. cells treated with artesunate alone. Data were shown as mean ± SD.

Article Snippet: CDK2, CDK4, CDK6, Cyclin D1, Cyclin E1, p21, Rb, phosphorylated-Rb, caspase 3, cleaved-caspase 3, PARP, cleaved-PARP, Bax, Bcl-2, BIP, PERK, IRE1α, CHOP, DR5, Beclin 1, LC3A/B, Atg3, Atg5, Atg7, and Atg12 primary antibodies for western blotting were purchased from Cell Signaling Technology Inc. (Danvers, MA, USA). p16 and phosphor-IRE1α primary antibodies for western blotting were purchased from Abcam (Cambridge, UK). p16, p21, and Cyclin D1 primary antibodies for immunohistochemistry and β-actin, XBP1S, and XBP1U primary antibodies for western blotting were purchased from Proteintech Group, Inc. (Manchester, UK).

Techniques: Staining, Flow Cytometry, Activity Assay, Western Blot, Expressing, Concentration Assay

Journal: Cells

Article Title: Artesunate Inhibits the Cell Growth in Colorectal Cancer by Promoting ROS-Dependent Cell Senescence and Autophagy

doi: 10.3390/cells11162472

Figure Lengend Snippet: Artesunate inhibited the growth of CT26-derived tumor in vivo. ( A ) Experimental timeline of CT26-derived tumor model in balb/c mice. Balb/c mice were injected CT-26 cells (1 × 10 5 cells for each mouse) subcutaneously to establish the CT26-derived tumor model. Tumor-loaded mice were gavaged with artesunate at 30 mg/kg or 60 mg/kg for 24 days. Body weights and tumor volumes were recorded every three days. ( B ) Curve of tumor volume. ( C ) Tumor weight. Tumor tissues were collected and weighted after treatment. ( D ) Immunohistochemical images of Ki67, Cyclin D1, p16, p21, LC3B, and p-IRE1α. Immunohistochemistry assay was performed using a SABC-POD staining kit. ( E ) Curve of body weight. ( F ) Organ indexes. Lung, heart, spleen, liver, and kidney were collected and weighted to calculate the organ indexes after treatment. * p < 0.05, *** p < 0.001 vs. Model group. Data were shown as mean ± SD.

Article Snippet: CDK2, CDK4, CDK6, Cyclin D1, Cyclin E1, p21, Rb, phosphorylated-Rb, caspase 3, cleaved-caspase 3, PARP, cleaved-PARP, Bax, Bcl-2, BIP, PERK, IRE1α, CHOP, DR5, Beclin 1, LC3A/B, Atg3, Atg5, Atg7, and Atg12 primary antibodies for western blotting were purchased from Cell Signaling Technology Inc. (Danvers, MA, USA). p16 and phosphor-IRE1α primary antibodies for western blotting were purchased from Abcam (Cambridge, UK). p16, p21, and Cyclin D1 primary antibodies for immunohistochemistry and β-actin, XBP1S, and XBP1U primary antibodies for western blotting were purchased from Proteintech Group, Inc. (Manchester, UK).

Techniques: Derivative Assay, In Vivo, Injection, Immunohistochemical staining, Immunohistochemistry, Staining

Journal: mBio

Article Title: Genome-Wide siRNA Screen Identifies Complementary Signaling Pathways Involved in Listeria Infection and Reveals Different Actin Nucleation Mechanisms during Listeria Cell Invasion and Actin Comet Tail Formation

doi: 10.1128/mBio.00598-15

Figure Lengend Snippet: Contributions of the different subunits of the Arp2/3 complex to Listeria invasion. Subunits of the Arp2/3 complex were knocked down by siRNA transfection of HeLa cells either individually (A) or in combination (B). One hour after infection with Listeria , cells were washed with gentamicin in order to kill extracellular bacteria, and Listeria entry was measured by counting CFU. Bars represent the mean and standard error of the mean (SEM) from 3 experiments. Significant differences (Student’s t test) from the scramble treatments are indicated as ** ( P < 0.01) and * ( P < 0.05). (C) HeLa cells infected with Listeria for 10 min were stained for actin (red) and the Arp2/3 complex subunit p20 (left panel, green) or p16 (right panel, green). Bars, 5 µm.

Article Snippet: For staining at bacterial entry sites of individual Arp2/3 subunits (rabbit polyclonal anti-p20 antibody [Santa Cruz sc-68394] or mouse monoclonal anti-p16 antibody [Santa Cruz sc-166760]) or for SPIRE2 (rabbit polyclonal AP54024PU-N; Acris GmbH), cells were infected at an MOI of 25 and fixed 10 min postinfection; for staining of Arp2/3 subunits at actin comet tails, cells were infected at an MOI of 5 and fixed 6 h postinfection.

Techniques: Transfection, Infection, Bacteria, Staining

Journal: mBio

Article Title: Genome-Wide siRNA Screen Identifies Complementary Signaling Pathways Involved in Listeria Infection and Reveals Different Actin Nucleation Mechanisms during Listeria Cell Invasion and Actin Comet Tail Formation

doi: 10.1128/mBio.00598-15

Figure Lengend Snippet: Contributions of the different subunits of the Arp2/3 complex to actin comet tail formation by Listeria . (A) Examples of images from validation experiments for actin and Listeria upon inactivation of each subunit of the Arp2/3 complex. Bar, 5 µm (B) Percentage of Listeria cells displaying long actin tails, short tails, full actin clouds, partial clouds, or no actin association upon inactivation of Arp2, Arp3, p41 (both subunits simultaneously), p34, p21, p20, and p16. Bars represent the means from 4 experiments. (C) HeLa cells infected with Listeria for 6 h and stained for actin (red) and for the Arp2/3 complex subunit p20 (left panel, green) or p16 (right panel, green). Bars, 5 µm; insert bar left, 2 µm; insert bar right, 1 µm.

Article Snippet: For staining at bacterial entry sites of individual Arp2/3 subunits (rabbit polyclonal anti-p20 antibody [Santa Cruz sc-68394] or mouse monoclonal anti-p16 antibody [Santa Cruz sc-166760]) or for SPIRE2 (rabbit polyclonal AP54024PU-N; Acris GmbH), cells were infected at an MOI of 25 and fixed 10 min postinfection; for staining of Arp2/3 subunits at actin comet tails, cells were infected at an MOI of 5 and fixed 6 h postinfection.

Techniques: Biomarker Discovery, Infection, Staining

Journal: Journal of orthopaedic research : official publication of the Orthopaedic Research Society

Article Title: Involvement of ERCC1 in the Pathogenesis of Osteoarthritis Through the Modulation of Apoptosis and Cellular Senescence

doi: 10.1002/jor.22656

Figure Lengend Snippet: Effect of ERCC1 inhibition on cellular senescence in HC under IL-1β stimulation. (A) Plotted is the average of SA-β-gal-positive cells. Error bars indicate the SD (***p < 0.001). (B) Shown is a representative image of an immunoblot measuring the expression levels of p16 and IL-6 in HC. Quantification of the expression ratios of p16(C) and IL-6 (D) to β-actin were calculated. Error bars indicate the SD. *p < 0.05, ***p < 0.001, not significant (NS).

Article Snippet: 20 , 21 The following antibodies were used: rabbit anti-human ERCC1, rabbit anti-human p16, rabbit anti-human cleaved poly (ADP-ribose) polymerase (PARP; all from Cell Signaling), rabbit anti-human matrix metallopeptidase (MMP)13, rabbit anti-human IL-6 (both from Abcam, Cambridge, England), mouse anti-human collagen type II, alpha 1 (COL2A1; Millipore, Billerica, MA), HRP-conjugated goat anti-rabbit IgG, and HRP-conjugated goat anti-mouse IgG (both from Cell Signaling).

Techniques: Inhibition, Western Blot, Expressing

Journal: BMC cancer

Article Title: ARPC5 acts as a potential prognostic biomarker that is associated with cell proliferation, migration and immune infiltrate in gliomas.

doi: 10.1186/s12885-023-11433-w

Figure Lengend Snippet: Fig. 1 Abnormally high expression of ARPC5 in glioma. (A) Differential expression of ARPC5 in various tumor types was analyzed based on the TIMER online website. (B) The distinct upregulation of ARPC5 in glioma was demonstrated in GEPIA online website. (C) Box plot based on the expression of ARPC5 in the GSE2223 (Glioma = 50, Normal = 4). (D) Box plot based on the expression of ARPC5 in the GSE29796 (Glioma = 52, Normal = 20). (E) Box plot based on the expression of ARPC5 in the GSE116520 (Glioma = 34, Normal = 8). (F) Box plot based on the protein expression of ARPC5 in the CPTAC samples (Glioma = 99, Normal = 10). (G) ARPC5 protein expression was detected in cerebral cortex (Patient id: 1582), low grade glioma (Patient id: 3365), and high-grade glioma (Patient id: 3251) tissues from HPA dataset. (H) Representative images of ARPC5 expression in glioma and its surrounding tissues. *p < 0.05, **p < 0.01, ***p < 0.001

Article Snippet: Glioma tissue samples and glioma chip ZLBraG180sur01 were incubated with ARPC5 antibody (16717-1-AP, proteintech, Wuhan, China) and CD3 antibody (17617-1-AP, proteintech, Wuhan, China).

Techniques: Expressing, Quantitative Proteomics

Journal: BMC cancer

Article Title: ARPC5 acts as a potential prognostic biomarker that is associated with cell proliferation, migration and immune infiltrate in gliomas.

doi: 10.1186/s12885-023-11433-w

Figure Lengend Snippet: Fig. 2 Correlation between different status of ARPC5 expression and prognosis of glioma patients. (A) Survival analysis of ARPC5 in CGGA database. (B) ROC curve analysis of ARPC5 at 1, 3, and 5 years in CGGA database. (C) Survival analysis of ARPC5 in TCGA database. (D) ROC curve analysis of ARPC5 at 1, 3, and 5 years in TCGA database. Survival analysis of the signature in patients stratified by grade (E, F), gender (G, H), age (I, J), IDH mutation status (K, L), 1p/19q codeletion status (M, N), and MGMTp methylation status (O, P) in CGGA database

Article Snippet: Glioma tissue samples and glioma chip ZLBraG180sur01 were incubated with ARPC5 antibody (16717-1-AP, proteintech, Wuhan, China) and CD3 antibody (17617-1-AP, proteintech, Wuhan, China).

Techniques: Expressing, Mutagenesis, Methylation

Journal: BMC cancer

Article Title: ARPC5 acts as a potential prognostic biomarker that is associated with cell proliferation, migration and immune infiltrate in gliomas.

doi: 10.1186/s12885-023-11433-w

Figure Lengend Snippet: Fig. 3 Prognostic significance of ARPC5 and its association with drug sensitivity in glioma. (A) Univariate regression analysis of prognosis in CGGA data base. (B) Multivariate analysis of prognosis in CGGA database. (C) The nomogram to predict the association between ARPC5 expression and OS was de veloped using the CGGA dataset. (D) The calibration curve for the nomogram-predicted OS. ARPC5 affects the sensitivity to 5-fluorouracil (E), bleomycin (F), etoposide (G), crizotinib (H), sorafenib (I), and erlotinib (J)

Article Snippet: Glioma tissue samples and glioma chip ZLBraG180sur01 were incubated with ARPC5 antibody (16717-1-AP, proteintech, Wuhan, China) and CD3 antibody (17617-1-AP, proteintech, Wuhan, China).

Techniques: Expressing

Journal: BMC cancer

Article Title: ARPC5 acts as a potential prognostic biomarker that is associated with cell proliferation, migration and immune infiltrate in gliomas.

doi: 10.1186/s12885-023-11433-w

Figure Lengend Snippet: Fig. 4 Enrichment analysis identifies ARPC5-associated signaling pathways. (A) Heatmap for DEGs generated by compare the difference of ARPC5 ex pression in glioma from the CGGA dataset. (B) Volcano plots illustrated all DEGs. Barplot showing the GO (C) and KEGG (D) analysis for ARPC5 in glioma. (E) GO functional annotation of ARPC5 in glioma from GSEA. (F) KEGG pathway analysis of ARPC5 in glioma from GSEA.

Article Snippet: Glioma tissue samples and glioma chip ZLBraG180sur01 were incubated with ARPC5 antibody (16717-1-AP, proteintech, Wuhan, China) and CD3 antibody (17617-1-AP, proteintech, Wuhan, China).

Techniques: Protein-Protein interactions, Generated, Functional Assay

Journal: BMC cancer

Article Title: ARPC5 acts as a potential prognostic biomarker that is associated with cell proliferation, migration and immune infiltrate in gliomas.

doi: 10.1186/s12885-023-11433-w

Figure Lengend Snippet: Fig. 5 Investigations the expression of ARPC5 in glioma through single-cell analysis. (A) Through dimension reduction analysis of CGGA single-cell data, TSNE plot depicted that 6,148 cells were classified into 16 clusters. (B) The violin plot showed the expression of ARPC5 in each type of cluster. (C) Sixteen clusters were divided into 5 types of cells: astrocyte, macrophage, monocyte, epithelial and T cell. (D) The scatter plot shows the expression of ARPC5 in each cell

Article Snippet: Glioma tissue samples and glioma chip ZLBraG180sur01 were incubated with ARPC5 antibody (16717-1-AP, proteintech, Wuhan, China) and CD3 antibody (17617-1-AP, proteintech, Wuhan, China).

Techniques: Expressing, Single-cell Analysis

Journal: BMC cancer

Article Title: ARPC5 acts as a potential prognostic biomarker that is associated with cell proliferation, migration and immune infiltrate in gliomas.

doi: 10.1186/s12885-023-11433-w

Figure Lengend Snippet: Fig. 6 Correlations of ARPC5 expression with immunity-related indexes. (A) Violin plot showed the correlation between immune classification and tumor purity. The immune infiltration models of low- and high-ARPC5 were detected through ssGSEA methods in glioma from the TCGA database. (C) Violin plot showed the correlation between ARPC5 with stromal scores, immune scores, and ESTIMATE scores. (D) Lollipop showed the correlation between ARPC5 with infiltrating immune cells. Scatter plot showed the correlation between ARPC5 with TMB (E) and MSI (F). (G-J) Violin plot showed the correla tion between ARPC5 with immunotherapy

Article Snippet: Glioma tissue samples and glioma chip ZLBraG180sur01 were incubated with ARPC5 antibody (16717-1-AP, proteintech, Wuhan, China) and CD3 antibody (17617-1-AP, proteintech, Wuhan, China).

Techniques: Expressing

Journal: BMC cancer

Article Title: ARPC5 acts as a potential prognostic biomarker that is associated with cell proliferation, migration and immune infiltrate in gliomas.

doi: 10.1186/s12885-023-11433-w

Figure Lengend Snippet: Fig. 7 Effect of ARPC5 on the expression of CD3 and prognosis. (A) Representative images revealed the relationships between the ARPC5 expression and T cell marker CD3 in gliomas. (B) Survival analysis of ARPC5 in glioma chip ZL-BraG180sur01.

Article Snippet: Glioma tissue samples and glioma chip ZLBraG180sur01 were incubated with ARPC5 antibody (16717-1-AP, proteintech, Wuhan, China) and CD3 antibody (17617-1-AP, proteintech, Wuhan, China).

Techniques: Expressing, Marker

Journal: BMC cancer

Article Title: ARPC5 acts as a potential prognostic biomarker that is associated with cell proliferation, migration and immune infiltrate in gliomas.

doi: 10.1186/s12885-023-11433-w

Figure Lengend Snippet: Fig. 8 Effect of ARPC5 on the proliferation and migration of glioma cells. (A) The expression level of ARPC5 protein was detected in LN229 and U251 cells after shRNA interference, GAPDH was used to confirm equal protein loading. (B) RT-qPCR verified the expression efficiency of ARPC5 in LN229 and U251 cells after shRNA interference. Growth curve assessing the effect of ARPC5 on the proliferation of LN229 (C) and U251 (D) cells. (E) The representa tive image showed the clone formation ability of LN229 and U251 cells after transfection. (F) Transwell analysis was further used to examine the effect of ARPC5 on migration of LN229 and U251 cells, and the number of migrating cells was quantitatively analyzed. *p < 0.05, **p < 0.01, ***p < 0.001

Article Snippet: Glioma tissue samples and glioma chip ZLBraG180sur01 were incubated with ARPC5 antibody (16717-1-AP, proteintech, Wuhan, China) and CD3 antibody (17617-1-AP, proteintech, Wuhan, China).

Techniques: Migration, Expressing, shRNA, Quantitative RT-PCR, Transfection