LncRNA HIF1A-AS2 accelerates malignant phenotypes of renal carcinoma by modulating miR-30a-5p/SOX4 axis as a ceRNA

Abstract

Objective: Several reports have proposed that lncRNAs, as potential biomarkers, participate in the progression and growth of malignant tumors. HIF1A-AS2 is a novel lncRNA and potential biomarker, involved in the genesis and development of carcinomas. However, the molecular mechanism of HIF1A-AS2 in renal carcinoma is unclear. Methods: The relative expression levels of HIF1A-AS2 and miR-30a-5p were detected using RT-qPCR in renal carcinoma tissues and cell lines. Using loss-of-function and overexpression, the biological effects of HIF1A-AS2 and miR-30a-5p in kidney carcinoma progression were characterized. Dual luciferase reporter gene analysis and Western blot were used to detect the potential mechanism of HIF1A-AS2 in renal carcinomas. Results: HIF1A-AS2 was upregulated in kidney carcinoma tissues when compared with para-carcinoma tissues (P < 0.05). In addition, tumor size, tumor node mestastasis stage and differentiation were identified as being closely associated with HIF1A-AS2 expression (P < 0.05). Knockdown or overexpression of HIF1A-AS2 either restrained or promoted the malignant phenotype and WNT/β-catenin signaling in renal carcinoma cells (P < 0.05). MiR-30a-5p was downregulated in renal cancers and partially reversed HIF1A-AS2 functions in malignant renal tumor cells. HIF1A-AS2 acted as a microRNA sponge that actively regulated the relative expression of SOX4 in sponging miR-30a-5p and subsequently increased the malignant phenotypes of renal carcinomas. HIF1A-AS2 showed a carcinogenic effect and miR-30a-5p acted as an antagonist of the anti-oncogene effects in the pathogenesis of renal carcinomas. Conclusions:The HIF1A-AS2-miR-30a-5p-SOX4 axis was associated with the malignant progression and development of renal carcinoma. The relative expression of HIF1A-AS2 was negatively correlated with the expression of miR-30a-5p, and was closely correlated with SOX4 mRNA levels in renal cancers.

Long Noncoding RNA Hotair Promotes the Progression and Immune Escape in Laryngeal Squamous Cell Carcinoma through MicroRNA-30a/GRP78/PD-L1 Axis

“…The aberrant activity of Hotair can occur at different levels, such as regulating chromatin status and transcriptional silencing as a molecular scaffold or control gene expression by sponging to miRNAs [ 12 ]. hsa-miR-30a-5p acts as a negative regulator of tumor proliferation and migration [ 33 – 35 ] and has been reported to play a role in many diseases, such as gastric cancer [ 35 ], hepatocellular cancer [ 34 ], and renal cancer [ 33 ]. Furthermore, many lncRNAs have been reported to act as ceRNAs of hsa-miR-30a-5p [ 33 – 35 ], including Hotair [ 10 ].…”

“…hsa-miR-30a-5p acts as a negative regulator of tumor proliferation and migration [ 33 – 35 ] and has been reported to play a role in many diseases, such as gastric cancer [ 35 ], hepatocellular cancer [ 34 ], and renal cancer [ 33 ]. Furthermore, many lncRNAs have been reported to act as ceRNAs of hsa-miR-30a-5p [ 33 – 35 ], including Hotair [ 10 ]. However, Hotair, a ceRNA of hsa-miR-30a-5p, has only been reported in gastric cancer [ 10 ], and there are no reports on these effects in LSCC.…”

LAPTM4B promotes the progression of bladder cancer by stimulating cell proliferation and invasion

“…Some gene mutations, such as in osteopontin and CTLA4, result in the development of bladder cancer, which can be used as potential targets for treatment ( 25 ). In addition, a variety of new therapeutic targets, such as proteins or long non-coding RNA, have been discovered, which provide significant convenience for the study of tumor mechanism and treatment ( 26 – 28 ). In the present study, LAPTM4B, a regulator of multiple types of tumor ( 10 – 12 , 29 , 30 ), was associated with the progression of bladder cancer.…”

Temozolomide abrogates the aggressiveness of urothelial carcinoma cells by enhancing senescence and depleting the side population

“…After transferring the supernatant into a new tube, the protein concentration was measured using a detergent-compatible protein assay reagent (Bio-Rad Laboratories, Inc.). Gel electrophoresis, membrane transfer and blocking, and antibody binding were performed as described previously ( 28 , 32 ). Proteins (25 µg protein/lane) were loaded and separated on 10 or 15% SDS-PAGE gels.…”