Fig 2: Long noncoding RNA LINC00336 inhibits ferroptosis in lung cancer by functioning as a competing endogenous RNA. LSH induces ELAVL1 expression through the inactivation of p53 and ELAVL1 enhances LINC00336 levels through transcriptional regulation by interacting with LINC00336. Then, LINC00336 absorbs MIR6852 as a ceRNA, which increases the mRNA level of CBS, stimulating cell proliferation, colony formation, and tumor formation, and inhibiting ferroptosis in lung cancer

Fig 3: p38 inhibition effects on HuR expression and regulation in U937 monocytic cells.Full length HuR (36 kDa) and HuR cleavage products (CP1; 24 kDa and CP2; 8 kDa) in LPS-stimulated (A) and Salmonella enteritidis-infected (B) p38 inhibitor- or negative control for p38 inhibition-treated U937 Mock, B27g, H9F and E45M cells at 5 h time point (SB90; p38 inhibitor SB202190 and SB74; control for p38 inhibition SB202474) Expression of HuR was determined by SDS-PAGE and Western blotting. HSPA8 was used as a loading control. Results from densitometric analysis of five independent experiments are shown in diagram. See Materials and Methods for details. * = P-value =0.06 for HuR and † = P-value =0.06 for CP2 versus untreated sample at the respective cell line.

Fig 4: LINC00336 interacts with RNA-binding protein ELAVL1. a The LINC00336-interacting proteins were annotated with their Log10 ratio in H358 and PC9 cell lysate. b Immunoblot analysis of LINC00336-binding protein ELAVL1 in H358 and PC9 cells. c Levels of LINC00336 binding to ELAVL1 relative to control IgG derived from three experiments conducted on H358 and PC9 cells. d The predicted secondary structure of LINC00336. e RNA pull-down analysis of ELAVL1 pulldown by in vitro-transcribed biotinylated LINC00336 (wild-type vs. domain truncation mutants). f The domain structure of ELAVL1 and the three Flag-tag ELAVL1 constructs used for mapping. g IB analysis of FLAG-tagged ELAVL1 truncations retrieved by biotinylated LINC00336. h RIP assays show the association between the ELAVL1 RRM domain and LINC00336. i N134S, R136K, and V139G mutants of ELAVL1 impair binding with LINC00336. j Computational modeling results show multiple binding sites for LINC00336 on ELAVL1. The green region is the binding site for LINC00336. Data are shown as the mean ± SEM; n = 3 independent experiments, two-tailed Student’s t-test: ns nonsignificant (p > 0.05), *P < 0.05, **P < 0.01, ***P < 0.001

Fig 5: Western blot analysis of SIRT1 (a) and HuR (b) and representative images of immunoreactive bands (c). Data are presented as means ± SEM of densitometric analysis of immunoreactive bands normalised to internal reference protein (GAPDH). Statistical analysis by one-way ANOVA, followed by the Tukey HSD test. #p < 0.05 vs D1, ##p < 0.01 vs D1; + p < 0.05 vs PM D1, + + p < 0.05 vs PM D1