c met kinase inhibitor  (Bristol Myers)

Journal: Experimental and Therapeutic Medicine

Article Title: Predominant control of PDGF/PDGF receptor signaling in the migration and proliferation of human adipose‑derived stem cells under culture conditions with a combination of growth factors

doi: 10.3892/etm.2024.12444

Figure Lengend Snippet: Pharmacological inhibition of hASC viability cultured with inhibitors of growth factor receptors. The cells were cultured in DMEM containing (A) PDGF-BB (20 ng/ml), (B) PDGF-BB (20 ng/ml)/VEGF (1 ng/ml) and (C) PDGF-BB (20 ng/ml)/HGF (1 ng/ml), without or with the indicated receptor inhibitors for 48 h. Cell viability was examined by Cell Counting Kit-8 assays. The inhibitors used were imatinib (5 µM), VEGFR tyrosine kinase inhibitor II (10 µM) and tivantinib (0.5 nM). Data are expressed as a percentage of the control value (no inhibitor) and as the mean ± SD (n=4). ** P<0.01 vs. no inhibitor. hASCs, human adipose-derived stem cells; PDGF, platelet-derived growth factor; VEGF, vascular endothelial growth factor; HGF, hepatocyte growth factor; VEGFR, VEGF receptor.

Article Snippet: VEGFR tyrosine kinase inhibitor II (a VEGFR inhibitor) and tivantinib [a MET proto-oncogene, receptor tyrosine kinase (c-Met) inhibitor] were purchased from Cayman Chemical Company.

Techniques: Inhibition, Cell Culture, Cell Counting, Derivative Assay

Journal: Investigational new drugs

Article Title: A novel bivalent anti-c-MET/PD-1 bispecific antibody exhibits potent cytotoxicity against c-MET/PD-L1-positive colorectal cancer.

doi: 10.1007/s10637-023-01381-4

Figure Lengend Snippet: Fig. 3 The anti-c-MET/PD-1 BsAb inhibits HGF-induced colorectal cancer cell migration and invasion. (A) c-MET and PD-L1 protein expression was detected in colon cancer cell lines by western blot analysis. (B) c-MET and PD-L1 protein expression was detected in exosomes isolated from colon cancer cell culture supernatants by west ern blot analysis. (C) Wound healing assay. Cancer cells were cultured to confluency in 24-well plates. A linear scrape wound was created using a sterile pipette tip and the cells were treated with the indicated concentrations of BsAb or JNJ38877605 and 100 ng/mL HGF for 24 h (original magnification, 100×). (D) Tumor invasion assay using a matrigel basement membrane matrix. Cancer cells were treated with the BsAb or JNJ38877605 for 24 h with 100 ng/mL HGF was added to the lower chamber. Data are presented as mean ± SD from three inde pendent experiments

Article Snippet: The c-MET kinase inhibitors JNJ38877605 was obtained from Selleckchem (S1114, Houston, TX, USA).

Techniques: Migration, Expressing, Western Blot, Isolation, Cell Culture, Wound Healing Assay, Sterility, Transferring, Invasion Assay, Membrane

Journal: Cell reports

Article Title: A cancer-associated METTL14 mutation induces aberrant m6A modification, affecting tumor growth.

doi: 10.1016/j.celrep.2023.112688

Figure Lengend Snippet: Figure 7. Mutant METTL14-mediated aber- rant m6A modifications destabilize c-MET mRNA (A) A GSEA was performed for the genes upregu- lated by c-MET between METTL14+/+ and METTL14Mu/Mu clones. The FDR q value is indi- cated in the panel. (B) The expression of c-MET mRNA relative to that of GAPDH mRNA was quantified by qPCR and is displayed as the mean ± SEM by setting the mean value of wild-type HEC108 cells (METTL14+/+) as one. Significant differences are indicated by as- terisks (Mann-Whitney U tests; *p < 0.05, ns, no significance). (C) Representative images of western blot analysis of c-MET expression in HEC108 cells of each ge- notype (left panel). The level of c-MET expression was quantified by normalizing it to that of GAPDH (right panel). Significant differences are indicated by asterisks (Mann-Whitney U tests; *p < 0.05, ns, no significance). (D) MeRIP-seq peaks identified in c-MET mRNA for each genotype are indicated with black boxes. Differential methylation sites analyzed by exome- Peak are indicated. (E) After transcription was inhibited by the addition of Act.D, the amount of remaining c-MET mRNA was quantified by qPCR 8 h after Act.D treatment. The amount of c-MET mRNA is displayed as the mean ± SEM by setting the initial amount for each genotype as 100%. Significant difference is indi- cated by an asterisk (Mann-Whitney U tests; *p < 0.05). (F) The effect of foretinib, a c-MET kinase inhibitor, on the expression levels of c-MET, phosphorylated c-MET, and c-Myc in each indicated clone was determined by western blotting. The expression of GAPDH is shown as a reference. (G) Cell viability of the indicated HEC108 clones was analyzed in the presence of foretinib. The cell viability without foretinib was set as one. Mu = R298P.

Article Snippet: HEC108-derived cells were seeded into 96-welled microplates in the presence of either the c-Myc-Max dimerization inhibitor 10058-F4 (ab145065; Abcam) or the ATP-competitive c-MET kinase inhibitor foretinib (GSK1363089, Selleck) at various concentrations.

Techniques: Mutagenesis, Clone Assay, Expressing, MANN-WHITNEY, Western Blot, Methylation

Journal: Drug safety

Article Title: Safety and Tolerability of c-MET Inhibitors in Cancer

doi: 10.1007/s40264-018-0780-x

Figure Lengend Snippet: Trials of interest across different tumor types and novel treatment combinations with approved c-MET inhibitors

Article Snippet: Small Molecule c-MET Kinase Inhibitors Capmatinib (INC280, Novartis, Basel, Switzerland) is a potent oral, ATP-competitive, class I c-MET inhibitor.

Techniques: Mutagenesis, Expressing, Activity Assay, Translocation Assay

Journal: Drug safety

Article Title: Safety and Tolerability of c-MET Inhibitors in Cancer

doi: 10.1007/s40264-018-0780-x

Figure Lengend Snippet: Summary of toxicity profiles of main novel c-MET inhibitors

Article Snippet: Small Molecule c-MET Kinase Inhibitors Capmatinib (INC280, Novartis, Basel, Switzerland) is a potent oral, ATP-competitive, class I c-MET inhibitor.

Techniques: Drug discovery, Bioprocessing, Biomarker Discovery, Mutagenesis