cell lines op9 cells riken brc rbc1124 hela cells atcc ccl  (ATCC)

Journal: Scientific Reports

Article Title: The C16orf87 protein is a subunit of the MIER corepressor complex controlling embryonic development and cell migration

doi: 10.1038/s41598-026-50740-7

Figure Lengend Snippet: C16orf87 partially mediates HDAC1 and MIER1 protein interactions. ( A ) C16orf87 interacts with the HDAC and MIER proteins. Volcano plot of the IP-MS experiment showing identified proteins interacting with the Flag-C16orf87 protein in HeLa cells. An adjusted P -value cut-off of 0.05 and a log2 fold change cut-off of 2 were used. Data are shown from a biological triplicate experiment. ( B ) Lack of C16orf87 does not change HDAC and MIER protein accumulation. Soluble Panc-01 WT (WT) and Panc-01 KO (KO) whole-cell lysates were analyzed by WB with the indicated antibodies. ( C ) C16orf87 partially mediates HDAC1 and MIER1 interaction. Co-immunoprecipitation of Flag-HDAC1 from siRNA (siC16 and siScr) and pcDNA3-Flag-HDAC1-transfected HeLa cells. Isolated proteins were analyzed by WB with the indicated antibodies. An arrowhead indicates the migration of the MIER1 protein isoforms, whereas an asterisk indicates the migration of the C16orf87 isoforms. ( D ) HDAC1 interacts weakly with C16orf87 in vitro. GST (as a control) and GST-HDAC1 pull-down with bacterially purified 8 × His-tagged C16orf87(Wt, 5 × C > A, 1–130, and 5 × C > A/1–130) proteins. An asterisk indicates a degradation product/partially translated GST-HDAC1. Proteins were detected with the anti-His and anti-GST antibodies.

Article Snippet: Human pancreatic cancer cell lines Panc-01 (ATCC, CRL-1469) and MiaPaCa-2 (ATCC, CRL-1420), mouse skeletal muscle cell line C2C12 (ATCC, CRL-1772), and human cervical cancer cell line HeLa S3 (ATCC, CCL-2.2) were used in this study.

Techniques: Protein-Protein interactions, Immunoprecipitation, Transfection, Isolation, Migration, In Vitro, Control, Purification

Journal: International Journal of Molecular Sciences

Article Title: Anticancer Activity of the Antimicrobial Myristoylated Peptide Myr-B in HeLa Cells: Cytotoxic, Membrane-Disruptive and Proteomic Insights

doi: 10.3390/ijms27093918

Figure Lengend Snippet: The cytotoxic effect of N-myristoylated peptides against human cervical cancer HeLa cells. Cell viability was assessed using MTT assay for HeLa cell line after 3 h and 24 h of incubation with N-myristoylated Myr-A ( a ), Myr-B ( b ) and Myr-C ( c ) peptides and corresponding non-myristoylated Pep-A ( d ), Pep-B ( e ) and Pep-C ( f ) ones. Data are expressed as a percentage of viable cells in the presence of different peptide concentrations (2.5–50 µM) compared to untreated HeLa cells (negative control). Positive control represents cells treated with 2% NaN 3 . Untreated cells serve as negative control. All experiments were performed using two independent replicates, each with at least three repeats. Statistical significance was assessed using one-way ANOVA followed by Dunnett’s post hoc test (GraphPad Prism 11.0). Difference from the negative control was considered statistically significant as follows: * adjusted p -value < 0.05; ** p -value < 0.01; *** p -value < 0.001; **** p -value < 0.0001.

Article Snippet: The human cervical cancer HeLa cell line (ATCC CCL-2) was cultured under the same conditions (37 °C, 5% CO 2 ), but in Roswell Park Memorial Institute (RPMI) 1640 medium supplemented with 10% ( v / v ) FBS, 1% ( w / v ) glutamine, 1% ( w / v ) penicillin–streptomycin, and 0.2% ( w / v ) NaHCO 3 [ ].

Techniques: MTT Assay, Incubation, Negative Control, Positive Control

Journal: International Journal of Molecular Sciences

Article Title: Anticancer Activity of the Antimicrobial Myristoylated Peptide Myr-B in HeLa Cells: Cytotoxic, Membrane-Disruptive and Proteomic Insights

doi: 10.3390/ijms27093918

Figure Lengend Snippet: Evaluation of Myr-B peptide-induced death of human cervical cancer HeLa ( a ) and colon cancer Caco-2 ( b ) cells. Cell membrane integrity was assessed through lactate dehydrogenase (LDH) release from untreated HeLa or Caco-2 cells (negative control) after 3 h exposure of HeLa and Caco-2 cells to their respective IC 50 doses of Myr-B peptide (38 μM and 50 μM, respectively) and from HeLa or Caco-2 cells treated with a lysis solution to release all LDH (positive control). The exposure to Pep-B was carried out under the same conditions as the corresponding treatment with the Myr-B peptide for each cancer cell line. Statistical significance was assessed using one-way ANOVA followed by Dunnett’s post hoc test (GraphPad Prism 11.0). Difference from the negative control was considered statistically significant as follows: * adjusted p -value < 0.05; *** p -value < 0.001; **** p -value < 0.0001.

Article Snippet: The human cervical cancer HeLa cell line (ATCC CCL-2) was cultured under the same conditions (37 °C, 5% CO 2 ), but in Roswell Park Memorial Institute (RPMI) 1640 medium supplemented with 10% ( v / v ) FBS, 1% ( w / v ) glutamine, 1% ( w / v ) penicillin–streptomycin, and 0.2% ( w / v ) NaHCO 3 [ ].

Techniques: Membrane, Negative Control, Lysis, Positive Control

Journal: International Journal of Molecular Sciences

Article Title: Anticancer Activity of the Antimicrobial Myristoylated Peptide Myr-B in HeLa Cells: Cytotoxic, Membrane-Disruptive and Proteomic Insights

doi: 10.3390/ijms27093918

Figure Lengend Snippet: Scanning electron microscopy (SEM) analysis of Myr-B peptide-induced effects on human cervical cancer HeLa cells. SEM micrographs (acquired and processed using JEOL inTouchScope Interface software, https://www.jeol.com/products/scientific/sem/JSM-IT510.php , access date: 23 April 2026) of untreated HeLa cells (negative control) ( a , b ), HeLa cells after 3 h exposure to 38 μM Myr-B ( c , d ) and 38 μM Pep-B ( e , f ) and HeLa cells treated with 2% NaN 3 (positive control) ( g , h ). Magnification and scale bars = ( a – d ) 1500× and 10 μm, respectively; ( e – h ) 10,000× and 1 μm, respectively.

Article Snippet: The human cervical cancer HeLa cell line (ATCC CCL-2) was cultured under the same conditions (37 °C, 5% CO 2 ), but in Roswell Park Memorial Institute (RPMI) 1640 medium supplemented with 10% ( v / v ) FBS, 1% ( w / v ) glutamine, 1% ( w / v ) penicillin–streptomycin, and 0.2% ( w / v ) NaHCO 3 [ ].

Techniques: Electron Microscopy, Software, Negative Control, Positive Control

Journal: International Journal of Molecular Sciences

Article Title: Anticancer Activity of the Antimicrobial Myristoylated Peptide Myr-B in HeLa Cells: Cytotoxic, Membrane-Disruptive and Proteomic Insights

doi: 10.3390/ijms27093918

Figure Lengend Snippet: Proteomic analysis of human cervical cancer HeLa cells treated with Myr-B and Pep-B peptides. Biplot of PLS-DA showing group separation and the top 20 feature loadings contributing to the variance along the principal components were obtained using MetaboAnalyst 6.0 ( a ). The selected proteins were clustered in a heatmap according to their LFQ values in the three experimental conditions; boxes were used to highlight different abundance patterns in Myr-B and Pep-B samples ( b ). Volcano plot analysis was performed with GraphPad Prism 11.0 using multiple unpaired t -tests with Welch correction to identify differentially regulated proteins, with a relative PPI network and functional enrichment determined using Metascape for the Myr-B vs. CTRL ( c , d ), Pep-B vs. CTRL ( e , f ) and Myr-B vs. Pep-B ( g , h ) comparisons, respectively. Differential proteins were selected with a difference cutoff ± 0.2 and −log10 p -value > 2.

Article Snippet: The human cervical cancer HeLa cell line (ATCC CCL-2) was cultured under the same conditions (37 °C, 5% CO 2 ), but in Roswell Park Memorial Institute (RPMI) 1640 medium supplemented with 10% ( v / v ) FBS, 1% ( w / v ) glutamine, 1% ( w / v ) penicillin–streptomycin, and 0.2% ( w / v ) NaHCO 3 [ ].

Techniques: Functional Assay