title: hnRNPK-regulated PTOV1-AS1 modulates heme oxygenase-1 expression via miR-1207-5p.
abstract: Antisense transcripts were initially identified as transcriptional noise, but have since been reported to play an important role in the quality control of miRNA functions. In this report, we tested the hypothesis that heterogeneous nuclear ribonucleoprotein K (hnRNPK) regulates miRNA function via competitive endogenous RNAs, such as pseudogenes, long non-coding RNAs, and antisense transcripts. Based on analyses of RNA sequencing data, the knockdown of hnRNPK decreased the antisense PTOV1-AS1 transcript which harbors five binding sites for miR-1207-5p. We identified heme oxygenase-1 (HO-1) mRNA as a novel target of miR-1207-5p by western blotting and Ago2 immunoprecipitation. The knockdown of hnRNPK or PTOV1-AS1 suppressed HO-1 expression by increasing the enrichment of HO-1 mRNA in miR-1207-5p-mediated miRISC. Downregulation of HO-1 by a miR-1207-5p mimic or knockdown of hnRNPK and PTOV1-AS1 inhibited the proliferation and clonogenic ability of HeLa cells. Taken together, our results demonstrate that hnRNPKregulated PTOV1-AS1 modulates HO-1 expression via miR- 1207-5p. [BMB Reports 2017; 50(4): 220-225].
authors.affiliation: Department of Health Sciences and Technology, Samsung Advanced Institute for Health Sciences and Technology, Sungkyunkwan University, Seoul 06351, Korea.
authors.forename: Chang Hoon
authors.initials: CH
authors.lastname: Shin
authors.affiliation: Soonchunhyang Institute of Medi-bio Science (SIMS), Soonchunhyang University, Cheonan 31151, Korea.
authors.forename: Seongho
authors.initials: S
authors.lastname: Ryu
authors.affiliation: Department of Health Sciences and Technology, Samsung Advanced Institute for Health Sciences and Technology, Sungkyunkwan University, Seoul 06351, Korea; Institute for Future Medicine, Samsung Medical Center, Seoul 06351, Korea.
authors.forename: Hyeon Ho
authors.initials: HH
authors.lastname: Kim
mesh_terms: D000070416:Antagomirs / Q000378:metabolism; D060565:Argonaute Proteins / Q000378:metabolism; D001665:Binding Sites; D014408:Biomarkers, Tumor / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D049109:Cell Proliferation; D015536:Down-Regulation; D006367:HeLa Cells; D051547:Heme Oxygenase-1 / Q000235:genetics* / Q000378:metabolism*; D034641:Heterogeneous-Nuclear Ribonucleoprotein K / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D047468:Immunoprecipitation; D035683:MicroRNAs / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D009363:Neoplasm Proteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D034622:RNA Interference; D012333:RNA, Messenger / Q000378:metabolism; D034741:RNA, Small Interfering / Q000378:metabolism; D048868:Adaptor Proteins, Signal Transducing
chemical_list: D000070416:Antagomirs; D060565:Argonaute Proteins; D014408:Biomarkers, Tumor; D051547:Heme Oxygenase-1; D034641:Heterogeneous-Nuclear Ribonucleoprotein K; D035683:MicroRNAs; D009363:Neoplasm Proteins; D012333:RNA, Messenger; D034741:RNA, Small Interfering; C575047:MIRN1207 microRNA, human; C425183:PTOV1 protein, human; D048868:Adaptor Proteins, Signal Transducing