Our study revealed that this lncRNA SNHG12/SP1/CDCA3 axis promoted RCC progression and sunitinib resistance, which could provide a new therapeutic target for sunitinib-resistant RCC. valuetumour-node-metastasis, small nucleolar RNA host gene 12, clear cell renal cell carcinoma. Table 2 Univariate and multivariate analyses of SNHG12 mRNA level and patient survival. valuevaluealgorithm was used. this study, we found SNHG12 was highly expressed in RCC tissues and in sunitinib-resistant RCC cells and was associated with a poor clinical prognosis. SNHG12 promoted RCC proliferation, migration, invasion and sunitinib resistance via CDCA3 in vitro. Mechanically, SNHG12 bound to SP1 and prevented the ubiquitylation-dependent proteolysis of SP1. Stabilised SP1 bound to a specific region in the promoter of CDCA3 and increased CDCA3 expression. Furthermore, in vivo experiments showed that SNHG12 increased tumour growth and that knocking down SNHG12 could reverse RCC sunitinib resistance. Our study revealed that this lncRNA SNHG12/SP1/CDCA3 axis promoted RCC progression and sunitinib resistance, which could provide a new therapeutic target for sunitinib-resistant RCC. valuetumour-node-metastasis, small nucleolar RNA host gene 12, clear cell renal cell carcinoma. Table 2 Univariate and multivariate analyses of SNHG12 mRNA level and patient survival. valuevaluealgorithm was used. Interestingly, the conversation strength between SNHG12 and SP1 was relatively higher, and potential binding sequences were predicted (Supplementary Fig. 7a, b). Thus, we mainly focused on SP1. Next, we confirmed the expression promoting effect of SP1 on CDCA3 in RCC cells at the mRNA and protein levels (Fig. 6a, b and Supplementary Fig. 7c). Encouraged by this observation, we predicted the binding sites of SP1 in the CDCA3 promoter with JASPAR (Fig. ?(Fig.6c),6c), and seven potential positions were identified. To validate the exact sites, a chromatin immunoprecipitation (ChIP) assay was performed. In both 786-O and ACHN cells, a strong enrichment between position E2 and anti-SP1 antibody was observed (Fig. ?(Fig.6d6d and Supplementary Fig. 7d). Furthermore, we constructed a CDCA3 promoter E2-wild-type (WT) GV238 vector and a CDCA3 promoter E2-mutant (MUT) GV238 vector. Luciferase activity analysis Tenapanor showed that this luciferase activity of the vector made up of the WT CDCA3 promoter could be promoted by SP1 overexpression in 293T cells (Fig. ?(Fig.6e6e). Open in a separate window Fig. 6 SNHG12 bound to and stabilised SP1, which activated CDCA3 transcription.a qRT-PCR for mRNA levels of SP1 and CDCA3 in transfected ACHN cells. b western blot assays for protein levels of SP1 and CDCA3 in transfected ACHN and 786-O cells. c The predicted positions of putative SP1 binding motif in ?2000-bp human CDCA3 promoter. d ChIP-PCR assays were performed to show direct binding of SP1 to CDCA3 promoter regions in ACHN cells. e Luciferase reporter assays were performed by co-transfecting the wild type CDCA3 promoter or fragment E2-mutant CDCA3 promoter with SP1 overexpression vector or blank vector in 293T cells. f Anti-SP1 RIP-PCR assays were performed in ACHN and 786-O cells to show SP1 directly bound to SNHG12. g qRT-PCR and western blot for mRNA and protein levels of SP1 in transfected RCC cells. h, i SP1 protein levels were measured by western blot in RCC cells after transfected sh SNHG12 or SNHG12 overexpression vector and treated with cycloheximide (CHX) for a certain period of time. j Cells with SNHG12 knockdown were treated with vehicle (DMSO), MG132 (20?nM) or chloroquine (50?nM) for 24?h. Western blot assays were applied to show SP1 protein levels. k Immunoprecipitation with an anti-SP1 antibody were performed in SNHG12 knockdown or overexpression RCC Tenapanor cells, and analysed by western blotting with an anti-ubiquitin antibody. *test or paired Students test, receiver operator characteristic curve, Pearson 2 test, Cox regression analysis, linear regression and KaplanCMeier curve with log-rank test were conducted as indicated. Significance was decided at P?0.05. Supplementary information Supplementary Tables(21K, docx) Supplementary Physique 1(720K, tif) Supplementary Physique 2(1.1M, tif) Supplementary Physique 3(2.2M, tif) Supplementary Physique 4(5.4M, tif) Supplementary Physique 5(1.6M, tif) Supplementary Physique 6(1.2M, tif) Supplementary Physique 7(1.3M, Tenapanor tif) Supplementary Physique legends(16K, docx) Acknowledgements This study was supported by the National Key R&D Program of China (grant nos. 2017YFB1303100), the National Natural Science Foundation of China (grant nos. 81672524, 81672528 and 81874090), the Hubei Provincial Natural Rabbit polyclonal to ATF2 Science Foundation of China (grant no. 2018CFA038), the Impartial Innovation Foundation of Huazhong University of Science and Technology (grant no. 118530309), the Clinical Research Physician Program of Tongji Medical College, Huazhong University of Science and Technology (grant no. 5001530015) and the Integrated Innovation Team for Major Human Disease Program of Tongji Medical College, Huazhong University of Science and Technology. Conflict of interest The authors declare that they have no conflict of interest. Footnotes Edited by G. Calin Publishers note Springer Nature remains neutral with regard to jurisdictional claims in published maps and.
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