Fig 2: Overexpression of ATG7 reversed the effects of exosomal H19 knockdown on erlotinib resistance in NSCLC cells. HCC827 and A549 cells were treated with exosome or exosome+si-H19, and HCC827/ER and A549/ER cells were transfected with si-H19 or si-19+ATG7. (A and B) The level of ATG7 was detected by Western blot in HCC827 and A549 cells treated with exosome or exosome+si-H19. (C and D) The level of ATG7 was detected by Western blot in HCC827/ER and A549/ER cells transfected with si-H19 or or si-19+ATG7. (E and F) The IC50 value of erlotinib was detected for HCC827/ER and A549/ER cells by cell viability assay. (G and H) Proliferation of HCC827/ER and A549/ER cells were determined by MTT assay. (I and J) Migration and invasion of HCC827/ER and A549/ER cells were assessed by transwell assay. (K and L) The protein levels of MMP2 and MMP9 were detected by Western blot in HCC827/ER and A549/ER cells. *P<0.05.

Fig 3: DNA damage, ATM, p38, and JNK are implicated in the induction of Mmp2 mRNA.(A) HaCaT keratinocytes were treated with DMSO or 5 μM camptothecin (CPT) for 24 hours. Mmp2 mRNA was measured by RT-qPCR and normalized to Hprt1 and DMSO-treated samples (n = 3). (B) HaCaT keratinocytes were treated with PBS or 1 mM H2O2 for 24 hours. Mmp2 mRNA was measured by RT-qPCR and normalized to Hprt1 and PBS-treated samples (n = 3). (C) HaCaT keratinocytes were irradiated with 200 mJ/cm2 UVB and subsequently treated with DMSO, 10 μM CH-223191, 50 ng/mL vitamin B12, or 20 ng/mL FA for 24 hours. Protein levels of γH2AX and β-Actin were measured by Western blot. (D and F) HaCaT keratinocytes were transfected with siNC or siATM and irradiated with UVB. Cells were lysed 24 hours later for analysis. (D) Mmp2 mRNA was measured by RT-qPCR and normalized to Hprt1 and siNC-transfected samples (n = 3). (F) Protein levels of MMP2, phosphorylated SP1 (Thr-278 and Thr-739 residues), and β-Actin were measured by Western blot. (E) HaCaT keratinocytes were irradiated with UVB and treated with DMSO, 50 μM PD98059 (ERK inhibitor), 10 μM SB203580 (p38 inhibitor), or 25 μM SP600125 (JNK inhibitor) for 24 hours. Mmp2 mRNA was measured by RT-qPCR and normalized to Hprt1 and DMSO-treated samples (n = 3). Data are means ± SEM. P values were calculated by unpaired 2-tailed Student’s t test and 1-way ANOVA. *P < 0.05, ***P < 0.001.

Fig 4: HDAC8 regulates the migration of MM cells. (A) Cells were transfected with si-NC or si-HDAC1-1 or -2 for 24 h, the protein expression of HDAC1 was checked, si-HDAC1-1 was used for subsequent experiments. (B) Wound healing assay for cells transfected with si-NC or si-HDAC1 for 24 h. (C) U266 and (D) RPMI8226 cells were transfected with si-NC or si-HDAC1 for 24 h, the mRNA expression of MMP2, MMP9 and E-Cad was evaluated. (E) U266 cells were transfected with si-NC or si-HDAC1 for 24 h, the protein expression of MMP2, MMP9 and E-Cad was determined and quantitatively analyzed. Data are presented as the mean ± SD of three independent experiments. **P<0.01. HDAC1, histone deactylase 1; MM, multiple myeloma; si, small interfering; NC, negative control; E-Cad, E-Cadherin.

Fig 5: Circ_0010235 silencing augmented the anticancer activity of 2‐MeOE2 in vivo. (a) Tumor volume was monitored. (b) Tumor weight was examined after 23 days inoculation. (c, d) The expression levels of circ_0010235 and miR‐34a‐5p were measured by quantitative reverse transcription‐polymerase chain reaction (qRT‐PCR) in resected xenograft tumor tissues. (e) The protein levels of NFAT5 were measured by western blot assay in resected xenograft tumor tissues. (f) The expression levels of NFAT5, Ki67 and MMP2 in the collected xenograft tumors were estimated by immunohistochemistry (IHC) assay. *p < 0.05, **p < 0.01, ***p < 0.001 and ****p < 0.0001.